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*** fulerene ***elNémo ID: 251228182850571820Job options:ID = 251228182850571820 JOBID = fulerene USERID = KS PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:
HEADER fulerene
HEADER DE NOVO PROTEIN 17-NOV-15 5ET3
TITLE CRYSTAL STRUCTURE OF DE NOVO DESIGNED FULLERENE ORGANIZING PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FULLERENE ORGANIZING PROTEIN (C60SOL-COP-3);
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 4 ORGANISM_TAXID: 32630
KEYWDS DE NOVO PROTEIN, FULLERENE, COMPLEX, HELICAL ASSEMBLY
EXPDTA X-RAY DIFFRACTION
AUTHOR K.-H.KIM,Y.H.KIM,R.ACHARYA,N.H.KIM,J.PAUL,G.GRIGORYAN,W.F.DEGRADO
REVDAT 3 08-NOV-23 5ET3 1 REMARK
REVDAT 2 25-DEC-19 5ET3 1 JRNL REMARK
REVDAT 1 04-MAY-16 5ET3 0
JRNL AUTH K.-H.KIM,D.-K.KO,Y.-T.KIM,N.H.KIM,J.PAUL,S.-Q.ZHANG,
JRNL AUTH 2 C.B.MURRAY,R.ACHARYA,W.F.DEGRADO,Y.H.KIM,G.GRIGORYAN
JRNL TITL PROTEIN-DIRECTED SELF-ASSEMBLY OF A FULLERENE CRYSTAL.
JRNL REF NAT COMMUN V. 7 11429 2016
JRNL REFN ESSN 2041-1723
JRNL PMID 27113637
JRNL DOI 10.1038/NCOMMS11429
REMARK 2
REMARK 2 RESOLUTION. 1.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_2306: ???
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.520
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 7487
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.040
REMARK 3 FREE R VALUE TEST SET COUNT : 752
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 15.3045 - 2.8532 0.81 1161 135 0.2570 0.2764
REMARK 3 2 2.8532 - 2.2671 0.99 1399 150 0.1985 0.2228
REMARK 3 3 2.2671 - 1.9812 1.00 1400 155 0.1947 0.2132
REMARK 3 4 1.9812 - 1.8003 1.00 1403 158 0.2060 0.2475
REMARK 3 5 1.8003 - 1.6715 0.98 1372 154 0.2141 0.2521
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.140
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 536
REMARK 3 ANGLE : 0.893 778
REMARK 3 CHIRALITY : 0.033 70
REMARK 3 PLANARITY : 0.222 81
REMARK 3 DIHEDRAL : 21.212 166
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 30 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.4210 40.8730 4.3230
REMARK 3 T TENSOR
REMARK 3 T11: 0.0837 T22: 0.1210
REMARK 3 T33: 0.1141 T12: 0.0355
REMARK 3 T13: 0.0319 T23: 0.0684
REMARK 3 L TENSOR
REMARK 3 L11: 1.8346 L22: 2.5477
REMARK 3 L33: 5.4979 L12: -0.1720
REMARK 3 L13: 1.0512 L23: -1.6405
REMARK 3 S TENSOR
REMARK 3 S11: 0.1284 S12: 0.0549 S13: 0.2451
REMARK 3 S21: 0.0067 S22: -0.0784 S23: -0.1052
REMARK 3 S31: -0.2886 S32: -0.2235 S33: 0.2840
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.4242 40.8829 6.3203
REMARK 3 T TENSOR
REMARK 3 T11: 0.0830 T22: 0.1131
REMARK 3 T33: 0.1202 T12: -0.0270
REMARK 3 T13: 0.0304 T23: -0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 2.0786 L22: 2.6851
REMARK 3 L33: 5.5269 L12: 0.0497
REMARK 3 L13: 1.1035 L23: 1.7197
REMARK 3 S TENSOR
REMARK 3 S11: 0.1036 S12: -0.0354 S13: 0.1369
REMARK 3 S21: -0.0869 S22: -0.0989 S23: 0.0519
REMARK 3 S31: -0.3586 S32: 0.1926 S33: 0.2743
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5ET3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215326.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7537
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.670
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 16.30
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 11.30
REMARK 200 R MERGE FOR SHELL (I) : 0.18800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3S0R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: THE 2 UL DROP CONSISTED OF A 1:1 V/V
REMARK 280 MIXTURE OF 8 MG/ML COMPLEX SOLUTION IN 25 MM TRIS PH 8.0 AND
REMARK 280 RESERVOIR SOLUTION CONSISTING OF 0.2 M AMMONIUM ACETATE, 0.1 M
REMARK 280 SODIUM CITRATE TRIBASIC DIHYDRATE PH 5.6, 30% W/V POLYETHYLENE
REMARK 280 GLYCOL 4,000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.52467
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 22.26233
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.52467
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 22.26233
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 72.99728
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 114 O HOH B 115 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 60C A 101
DBREF 5ET3 A 1 30 PDB 5ET3 5ET3 1 30
DBREF 5ET3 B 1 30 PDB 5ET3 5ET3 1 30
SEQRES 1 A 30 ALA GLU ALA GLU SER ALA LEU GLU TYR ALA GLN GLN ALA
SEQRES 2 A 30 LEU GLU LYS ALA GLN LEU ALA LEU GLN ALA ALA ARG GLN
SEQRES 3 A 30 ALA LEU LYS ALA
SEQRES 1 B 30 ALA GLU ALA GLU SER ALA LEU GLU TYR ALA GLN GLN ALA
SEQRES 2 B 30 LEU GLU LYS ALA GLN LEU ALA LEU GLN ALA ALA ARG GLN
SEQRES 3 B 30 ALA LEU LYS ALA
HET 60C A 101 60
HETNAM 60C (C_{60}-I_{H})[5,6]FULLERENE
HETSYN 60C BUCKMINSTERFULLERENE, BUCKYBALL
FORMUL 3 60C C60
FORMUL 4 HOH *29(H2 O)
HELIX 1 AA1 ALA A 1 ALA A 30 1 30
HELIX 2 AA2 GLU B 2 ALA B 30 1 29
SITE 1 AC1 8 SER A 5 ALA A 6 TYR A 9 LEU A 19
SITE 2 AC1 8 ALA B 6 TYR B 9 LEU B 19 ALA B 23
CRYST1 42.145 42.145 66.787 90.00 90.00 120.00 P 62 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.023728 0.013699 0.000000 0.00000
SCALE2 0.000000 0.027398 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014973 0.00000
ATOM 1 N ALA A 1 9.073 38.624 25.204 1.00 29.98 N
ANISOU 1 N ALA A 1 4879 3877 2635 -917 -792 81 N
ATOM 2 CA ALA A 1 9.528 37.206 25.236 1.00 32.66 C
ANISOU 2 CA ALA A 1 5017 4291 3103 -968 -838 217 C
ATOM 3 C ALA A 1 9.242 36.533 23.894 1.00 25.74 C
ANISOU 3 C ALA A 1 3948 3458 2372 -917 -774 295 C
ATOM 4 O ALA A 1 9.032 37.213 22.886 1.00 20.56 O
ANISOU 4 O ALA A 1 3276 2772 1763 -872 -729 265 O
ATOM 5 CB ALA A 1 8.851 36.458 26.377 1.00 33.17 C
ANISOU 5 CB ALA A 1 5120 4467 3017 -953 -785 231 C
ATOM 6 N GLU A 2 9.226 35.203 23.888 1.00 20.93 N
ANISOU 6 N GLU A 2 3220 2897 1835 -916 -768 389 N
ATOM 7 CA GLU A 2 9.105 34.439 22.651 1.00 19.54 C
ANISOU 7 CA GLU A 2 2897 2725 1803 -866 -728 457 C
ATOM 8 C GLU A 2 7.834 34.786 21.871 1.00 19.78 C
ANISOU 8 C GLU A 2 2904 2834 1777 -798 -592 433 C
ATOM 9 O GLU A 2 7.876 34.947 20.653 1.00 16.05 O
ANISOU 9 O GLU A 2 2351 2338 1410 -749 -567 451 O
ATOM 10 CB GLU A 2 9.135 32.936 22.951 1.00 19.71 C
ANISOU 10 CB GLU A 2 2878 2745 1866 -880 -748 535 C
ATOM 11 CG GLU A 2 10.518 32.392 23.310 1.00 25.10 C
ANISOU 11 CG GLU A 2 3542 3357 2637 -896 -872 590 C
ATOM 12 CD GLU A 2 10.972 32.764 24.712 1.00 29.16 C
ANISOU 12 CD GLU A 2 4152 3878 3047 -973 -951 575 C
ATOM 13 OE1 GLU A 2 10.117 33.123 25.547 1.00 28.05 O
ANISOU 13 OE1 GLU A 2 4114 3795 2748 -1005 -903 522 O
ATOM 14 OE2 GLU A 2 12.190 32.698 24.980 1.00 25.98 O1-
ANISOU 14 OE2 GLU A 2 3718 3442 2712 -991 -1061 619 O1-
ATOM 15 N ALA A 3 6.715 34.894 22.580 1.00 21.50 N
ANISOU 15 N ALA A 3 3173 3164 1832 -776 -489 405 N
ATOM 16 CA ALA A 3 5.438 35.216 21.950 1.00 19.99 C
ANISOU 16 CA ALA A 3 2922 3090 1584 -686 -333 403 C
ATOM 17 C ALA A 3 5.504 36.564 21.240 1.00 14.69 C
ANISOU 17 C ALA A 3 2283 2340 957 -575 -267 313 C
ATOM 18 O ALA A 3 5.056 36.698 20.101 1.00 17.92 O
ANISOU 18 O ALA A 3 2584 2757 1470 -495 -187 328 O
ATOM 19 CB ALA A 3 4.321 35.218 22.984 1.00 25.63 C
ANISOU 19 CB ALA A 3 3657 3961 2122 -645 -219 393 C
ATOM 20 N GLU A 4 6.064 37.559 21.919 1.00 21.98 N
ANISOU 20 N GLU A 4 3374 3160 1819 -570 -311 214 N
ATOM 21 CA GLU A 4 6.185 38.898 21.353 1.00 23.25 C
ANISOU 21 CA GLU A 4 3615 3184 2036 -473 -268 122 C
ATOM 22 C GLU A 4 7.091 38.896 20.127 1.00 18.10 C
ANISOU 22 C GLU A 4 2842 2419 1617 -518 -333 173 C
ATOM 23 O GLU A 4 6.772 39.509 19.108 1.00 16.74 O
ANISOU 23 O GLU A 4 2628 2203 1528 -420 -247 162 O
ATOM 24 CB GLU A 4 6.731 39.872 22.400 1.00 23.15 C
ANISOU 24 CB GLU A 4 3860 3041 1894 -509 -353 11 C
ATOM 25 CG GLU A 4 5.783 40.128 23.560 1.00 44.88 C
ANISOU 25 CG GLU A 4 6778 5899 4377 -403 -252 -67 C
ATOM 26 CD GLU A 4 6.383 41.039 24.613 1.00 64.90 C
ANISOU 26 CD GLU A 4 9628 8275 6755 -447 -363 -192 C
ATOM 27 OE1 GLU A 4 7.598 41.318 24.537 1.00 71.69 O
ANISOU 27 OE1 GLU A 4 10545 8967 7728 -619 -553 -190 O
ATOM 28 OE2 GLU A 4 5.639 41.476 25.516 1.00 73.47 O1-
ANISOU 28 OE2 GLU A 4 10907 9418 7591 -313 -265 -286 O1-
ATOM 29 N SER A 5 8.221 38.205 20.231 1.00 16.58 N
ANISOU 29 N SER A 5 2585 2198 1514 -650 -480 242 N
ATOM 30 CA SER A 5 9.175 38.127 19.131 1.00 15.54 C
ANISOU 30 CA SER A 5 2316 2007 1583 -674 -528 309 C
ATOM 31 C SER A 5 8.551 37.417 17.934 1.00 13.10 C
ANISOU 31 C SER A 5 1862 1761 1355 -574 -422 362 C
ATOM 32 O SER A 5 8.778 37.791 16.779 1.00 13.63 O
ANISOU 32 O SER A 5 1852 1785 1540 -522 -375 381 O
ATOM 33 CB SER A 5 10.446 37.404 19.575 1.00 16.81 C
ANISOU 33 CB SER A 5 2410 2175 1801 -791 -696 390 C
ATOM 34 OG SER A 5 11.120 38.139 20.583 1.00 20.84 O
ANISOU 34 OG SER A 5 3050 2625 2242 -917 -827 352 O
ATOM 35 N ALA A 6 7.747 36.402 18.226 1.00 12.22 N
ANISOU 35 N ALA A 6 1731 1752 1161 -568 -396 394 N
ATOM 36 CA ALA A 6 7.092 35.626 17.180 1.00 10.79 C
ANISOU 36 CA ALA A 6 1452 1622 1028 -514 -333 447 C
ATOM 37 C ALA A 6 6.101 36.487 16.408 1.00 14.04 C
ANISOU 37 C ALA A 6 1835 2066 1434 -408 -196 409 C
ATOM 38 O ALA A 6 6.032 36.412 15.181 1.00 11.60 O
ANISOU 38 O ALA A 6 1451 1741 1216 -352 -160 436 O
ATOM 39 CB ALA A 6 6.390 34.417 17.767 1.00 11.04 C
ANISOU 39 CB ALA A 6 1495 1747 954 -584 -361 507 C
ATOM 40 N LEU A 7 5.343 37.313 17.122 1.00 12.30 N
ANISOU 40 N LEU A 7 1686 1896 1093 -356 -120 349 N
ATOM 41 CA LEU A 7 4.334 38.139 16.465 1.00 12.44 C
ANISOU 41 CA LEU A 7 1674 1961 1092 -213 11 325 C
ATOM 42 C LEU A 7 4.991 39.250 15.673 1.00 13.81 C
ANISOU 42 C LEU A 7 1899 1971 1378 -155 15 284 C
ATOM 43 O LEU A 7 4.507 39.621 14.603 1.00 13.94 O
ANISOU 43 O LEU A 7 1855 1994 1448 -57 86 304 O
ATOM 44 CB LEU A 7 3.354 38.722 17.483 1.00 12.87 C
ANISOU 44 CB LEU A 7 1799 2127 964 -118 109 274 C
ATOM 45 CG LEU A 7 2.482 37.697 18.210 1.00 20.92 C
ANISOU 45 CG LEU A 7 2733 3367 1849 -181 136 349 C
ATOM 46 CD1 LEU A 7 1.427 38.445 18.983 1.00 20.19 C
ANISOU 46 CD1 LEU A 7 2673 3430 1568 -22 282 309 C
ATOM 47 CD2 LEU A 7 1.841 36.685 17.262 1.00 19.07 C
ANISOU 47 CD2 LEU A 7 2322 3249 1674 -245 131 466 C
ATOM 48 N GLU A 8 6.104 39.762 16.186 1.00 11.78 N
ANISOU 48 N GLU A 8 1750 1574 1151 -238 -78 245 N
ATOM 49 CA GLU A 8 6.848 40.798 15.483 1.00 13.55 C
ANISOU 49 CA GLU A 8 2027 1641 1482 -242 -100 237 C
ATOM 50 C GLU A 8 7.402 40.242 14.166 1.00 13.99 C
ANISOU 50 C GLU A 8 1915 1713 1687 -259 -101 329 C
ATOM 51 O GLU A 8 7.313 40.882 13.122 1.00 13.35 O
ANISOU 51 O GLU A 8 1818 1583 1671 -194 -44 350 O
ATOM 52 CB GLU A 8 7.980 41.339 16.360 1.00 17.99 C
ANISOU 52 CB GLU A 8 2722 2075 2038 -388 -236 206 C
ATOM 53 CG GLU A 8 8.703 42.536 15.757 1.00 29.92 C
ANISOU 53 CG GLU A 8 4316 3414 3639 -443 -279 214 C
ATOM 54 CD GLU A 8 9.694 43.174 16.716 1.00 41.41 C
ANISOU 54 CD GLU A 8 5935 4738 5061 -626 -443 186 C
ATOM 55 OE1 GLU A 8 9.667 42.839 17.920 1.00 45.88 O
ANISOU 55 OE1 GLU A 8 6592 5335 5506 -670 -507 131 O
ATOM 56 OE2 GLU A 8 10.500 44.012 16.262 1.00 46.55 O1-
ANISOU 56 OE2 GLU A 8 6629 5260 5797 -747 -520 232 O1-
ATOM 57 N TYR A 9 7.953 39.034 14.225 1.00 10.50 N
ANISOU 57 N TYR A 9 1370 1337 1281 -325 -165 385 N
ATOM 58 CA TYR A 9 8.486 38.360 13.048 1.00 10.58 C
ANISOU 58 CA TYR A 9 1251 1370 1398 -299 -157 461 C
ATOM 59 C TYR A 9 7.376 38.071 12.039 1.00 9.31 C
ANISOU 59 C TYR A 9 1053 1267 1216 -195 -63 468 C
ATOM 60 O TYR A 9 7.536 38.293 10.845 1.00 11.38 O
ANISOU 60 O TYR A 9 1268 1514 1541 -136 -15 502 O
ATOM 61 CB TYR A 9 9.187 37.068 13.482 1.00 11.08 C
ANISOU 61 CB TYR A 9 1264 1475 1472 -346 -250 507 C
ATOM 62 CG TYR A 9 9.652 36.152 12.374 1.00 9.19 C
ANISOU 62 CG TYR A 9 936 1258 1299 -268 -237 568 C
ATOM 63 CD1 TYR A 9 10.970 36.178 11.935 1.00 15.33 C
ANISOU 63 CD1 TYR A 9 1611 2043 2171 -251 -260 635 C
ATOM 64 CD2 TYR A 9 8.790 35.228 11.796 1.00 10.19 C
ANISOU 64 CD2 TYR A 9 1089 1406 1377 -211 -209 567 C
ATOM 65 CE1 TYR A 9 11.407 35.328 10.939 1.00 15.74 C
ANISOU 65 CE1 TYR A 9 1602 2124 2253 -128 -228 683 C
ATOM 66 CE2 TYR A 9 9.219 34.374 10.800 1.00 12.78 C
ANISOU 66 CE2 TYR A 9 1400 1723 1734 -120 -207 602 C
ATOM 67 CZ TYR A 9 10.527 34.424 10.377 1.00 14.51 C
ANISOU 67 CZ TYR A 9 1531 1949 2032 -53 -203 652 C
ATOM 68 OH TYR A 9 10.948 33.566 9.386 1.00 18.38 O
ANISOU 68 OH TYR A 9 2024 2436 2522 87 -179 679 O
ATOM 69 N ALA A 10 6.249 37.575 12.540 1.00 9.46 N
ANISOU 69 N ALA A 10 1086 1374 1133 -188 -44 451 N
ATOM 70 CA ALA A 10 5.102 37.263 11.698 1.00 9.93 C
ANISOU 70 CA ALA A 10 1092 1522 1158 -127 16 478 C
ATOM 71 C ALA A 10 4.636 38.505 10.950 1.00 11.37 C
ANISOU 71 C ALA A 10 1274 1686 1360 -13 105 464 C
ATOM 72 O ALA A 10 4.365 38.449 9.756 1.00 10.85 O
ANISOU 72 O ALA A 10 1161 1637 1324 40 133 502 O
ATOM 73 CB ALA A 10 3.970 36.694 12.543 1.00 10.64 C
ANISOU 73 CB ALA A 10 1167 1751 1126 -169 20 491 C
ATOM 74 N GLN A 11 4.561 39.626 11.663 1.00 10.61 N
ANISOU 74 N GLN A 11 1264 1536 1231 31 138 409 N
ATOM 75 CA GLN A 11 4.130 40.887 11.061 1.00 10.16 C
ANISOU 75 CA GLN A 11 1258 1421 1182 161 211 395 C
ATOM 76 C GLN A 11 5.108 41.335 9.976 1.00 11.85 C
ANISOU 76 C GLN A 11 1477 1513 1514 135 195 437 C
ATOM 77 O GLN A 11 4.701 41.803 8.911 1.00 13.10 O
ANISOU 77 O GLN A 11 1618 1667 1692 226 247 475 O
ATOM 78 CB GLN A 11 4.002 41.969 12.127 1.00 13.73 C
ANISOU 78 CB GLN A 11 1874 1787 1557 221 229 312 C
ATOM 79 CG GLN A 11 3.214 43.184 11.688 1.00 28.29 C
ANISOU 79 CG GLN A 11 3801 3581 3366 415 314 293 C
ATOM 80 CD GLN A 11 1.845 43.239 12.341 1.00 38.83 C
ANISOU 80 CD GLN A 11 5107 5090 4555 588 411 269 C
ATOM 81 OE1 GLN A 11 1.731 43.241 13.566 1.00 45.48 O
ANISOU 81 OE1 GLN A 11 6034 5961 5286 595 421 204 O
ATOM 82 NE2 GLN A 11 0.798 43.274 11.526 1.00 34.19 N
ANISOU 82 NE2 GLN A 11 4386 4650 3956 730 484 336 N
ATOM 83 N GLN A 12 6.397 41.174 10.243 1.00 10.47 N
ANISOU 83 N GLN A 12 1307 1264 1405 10 122 449 N
ATOM 84 CA GLN A 12 7.424 41.524 9.267 1.00 13.06 C
ANISOU 84 CA GLN A 12 1597 1528 1836 -33 117 519 C
ATOM 85 C GLN A 12 7.357 40.617 8.033 1.00 12.02 C
ANISOU 85 C GLN A 12 1350 1493 1725 26 159 578 C
ATOM 86 O GLN A 12 7.475 41.086 6.909 1.00 12.28 O
ANISOU 86 O GLN A 12 1368 1510 1790 71 209 632 O
ATOM 87 CB GLN A 12 8.808 41.455 9.914 1.00 13.03 C
ANISOU 87 CB GLN A 12 1575 1486 1891 -183 23 545 C
ATOM 88 CG GLN A 12 9.038 42.559 10.938 1.00 18.83 C
ANISOU 88 CG GLN A 12 2475 2083 2598 -275 -46 493 C
ATOM 89 CD GLN A 12 10.207 42.295 11.869 1.00 33.06 C
ANISOU 89 CD GLN A 12 4252 3884 4426 -445 -174 514 C
ATOM 90 OE1 GLN A 12 10.789 41.211 11.873 1.00 36.79 O
ANISOU 90 OE1 GLN A 12 4572 4472 4935 -463 -202 566 O
ATOM 91 NE2 GLN A 12 10.552 43.296 12.671 1.00 38.60 N
ANISOU 91 NE2 GLN A 12 5125 4446 5096 -564 -267 476 N
ATOM 92 N ALA A 13 7.147 39.322 8.251 1.00 11.24 N
ANISOU 92 N ALA A 13 1203 1478 1589 22 129 567 N
ATOM 93 CA ALA A 13 6.961 38.371 7.163 1.00 11.59 C
ANISOU 93 CA ALA A 13 1205 1582 1616 79 145 599 C
ATOM 94 C ALA A 13 5.752 38.719 6.292 1.00 11.74 C
ANISOU 94 C ALA A 13 1232 1645 1584 157 195 608 C
ATOM 95 O ALA A 13 5.827 38.639 5.068 1.00 10.30 O
ANISOU 95 O ALA A 13 1041 1472 1400 211 222 628 O
ATOM 96 CB ALA A 13 6.817 36.953 7.717 1.00 10.84 C
ANISOU 96 CB ALA A 13 1122 1524 1472 39 73 582 C
ATOM 97 N LEU A 14 4.651 39.114 6.920 1.00 10.31 N
ANISOU 97 N LEU A 14 1058 1511 1350 174 206 581 N
ATOM 98 CA LEU A 14 3.448 39.476 6.180 1.00 10.42 C
ANISOU 98 CA LEU A 14 1041 1604 1312 263 245 611 C
ATOM 99 C LEU A 14 3.667 40.757 5.370 1.00 11.16 C
ANISOU 99 C LEU A 14 1178 1613 1451 354 303 638 C
ATOM 100 O LEU A 14 3.173 40.860 4.252 1.00 11.65 O
ANISOU 100 O LEU A 14 1218 1718 1492 414 319 677 O
ATOM 101 CB LEU A 14 2.254 39.639 7.127 1.00 12.70 C
ANISOU 101 CB LEU A 14 1293 2009 1525 294 262 596 C
ATOM 102 CG LEU A 14 1.727 38.367 7.804 1.00 13.81 C
ANISOU 102 CG LEU A 14 1376 2274 1598 180 204 609 C
ATOM 103 CD1 LEU A 14 0.418 38.685 8.515 1.00 16.56 C
ANISOU 103 CD1 LEU A 14 1646 2786 1860 237 242 619 C
ATOM 104 CD2 LEU A 14 1.552 37.212 6.829 1.00 17.93 C
ANISOU 104 CD2 LEU A 14 1884 2816 2111 102 118 634 C
ATOM 105 N GLU A 15 4.406 41.713 5.930 1.00 10.71 N
ANISOU 105 N GLU A 15 1200 1424 1445 337 313 616 N
ATOM 106 CA GLU A 15 4.772 42.940 5.220 1.00 12.04 C
ANISOU 106 CA GLU A 15 1446 1472 1658 379 346 659 C
ATOM 107 C GLU A 15 5.525 42.607 3.934 1.00 13.34 C
ANISOU 107 C GLU A 15 1550 1663 1856 339 355 706 C
ATOM 108 O GLU A 15 5.258 43.185 2.869 1.00 12.96 O
ANISOU 108 O GLU A 15 1517 1614 1794 391 383 728 O
ATOM 109 CB GLU A 15 5.622 43.854 6.111 1.00 12.99 C
ANISOU 109 CB GLU A 15 1686 1428 1823 295 312 630 C
ATOM 110 CG GLU A 15 4.813 44.667 7.101 1.00 19.10 C
ANISOU 110 CG GLU A 15 2598 2131 2529 391 318 549 C
ATOM 111 CD GLU A 15 5.661 45.305 8.182 1.00 30.63 C
ANISOU 111 CD GLU A 15 4215 3424 4000 273 248 495 C
ATOM 112 OE1 GLU A 15 6.906 45.239 8.090 1.00 34.49 O
ANISOU 112 OE1 GLU A 15 4675 3863 4567 96 186 546 O
ATOM 113 OE2 GLU A 15 5.076 45.871 9.130 1.00 33.91 O1-
ANISOU 113 OE2 GLU A 15 4780 3774 4330 362 252 406 O1-
ATOM 114 N LYS A 16 6.441 41.648 4.038 1.00 11.33 N
ANISOU 114 N LYS A 16 1229 1449 1627 263 328 699 N
ATOM 115 CA LYS A 16 7.226 41.202 2.896 1.00 10.55 C
ANISOU 115 CA LYS A 16 1074 1399 1537 273 347 722 C
ATOM 116 C LYS A 16 6.327 40.542 1.854 1.00 11.65 C
ANISOU 116 C LYS A 16 1216 1614 1598 351 357 699 C
ATOM 117 O LYS A 16 6.483 40.778 0.656 1.00 11.45 O
ANISOU 117 O LYS A 16 1193 1605 1551 396 393 726 O
ATOM 118 CB LYS A 16 8.313 40.222 3.342 1.00 11.79 C
ANISOU 118 CB LYS A 16 1168 1589 1722 233 321 730 C
ATOM 119 CG LYS A 16 9.496 40.883 4.031 1.00 13.89 C
ANISOU 119 CG LYS A 16 1396 1814 2066 127 296 779 C
ATOM 120 CD LYS A 16 10.468 39.850 4.580 1.00 16.38 C
ANISOU 120 CD LYS A 16 1625 2192 2408 109 262 803 C
ATOM 121 CE LYS A 16 11.530 40.496 5.454 1.00 24.64 C
ANISOU 121 CE LYS A 16 2620 3217 3523 -32 200 847 C
ATOM 122 NZ LYS A 16 12.504 39.500 5.979 1.00 26.01 N1+
ANISOU 122 NZ LYS A 16 2686 3477 3722 -31 158 889 N1+
ATOM 123 N ALA A 17 5.384 39.718 2.307 1.00 10.24 N
ANISOU 123 N ALA A 17 1042 1484 1366 346 313 660 N
ATOM 124 CA ALA A 17 4.478 39.051 1.387 1.00 9.60 C
ANISOU 124 CA ALA A 17 977 1469 1202 372 286 649 C
ATOM 125 C ALA A 17 3.645 40.080 0.641 1.00 12.12 C
ANISOU 125 C ALA A 17 1292 1812 1503 430 318 680 C
ATOM 126 O ALA A 17 3.361 39.922 -0.540 1.00 12.37 O
ANISOU 126 O ALA A 17 1345 1874 1480 458 311 691 O
ATOM 127 CB ALA A 17 3.575 38.083 2.116 1.00 9.84 C
ANISOU 127 CB ALA A 17 1002 1555 1182 312 209 630 C
ATOM 128 N GLN A 18 3.256 41.141 1.341 1.00 10.70 N
ANISOU 128 N GLN A 18 1108 1607 1350 462 349 699 N
ATOM 129 CA GLN A 18 2.373 42.133 0.747 1.00 13.98 C
ANISOU 129 CA GLN A 18 1537 2041 1734 544 376 733 C
ATOM 130 C GLN A 18 3.068 42.928 -0.337 1.00 12.17 C
ANISOU 130 C GLN A 18 1360 1737 1528 560 409 764 C
ATOM 131 O GLN A 18 2.457 43.245 -1.359 1.00 11.65 O
ANISOU 131 O GLN A 18 1302 1710 1416 611 409 795 O
ATOM 132 CB GLN A 18 1.848 43.079 1.808 1.00 12.94 C
ANISOU 132 CB GLN A 18 1438 1874 1606 614 401 735 C
ATOM 133 CG GLN A 18 0.846 42.450 2.703 1.00 16.11 C
ANISOU 133 CG GLN A 18 1763 2408 1948 627 382 731 C
ATOM 134 CD GLN A 18 0.489 43.379 3.803 1.00 25.65 C
ANISOU 134 CD GLN A 18 3022 3575 3146 735 418 708 C
ATOM 135 OE1 GLN A 18 1.290 43.613 4.707 1.00 24.60 O
ANISOU 135 OE1 GLN A 18 2960 3322 3064 727 425 673 O
ATOM 136 NE2 GLN A 18 -0.700 43.959 3.726 1.00 24.16 N
ANISOU 136 NE2 GLN A 18 2814 3478 2888 853 440 725 N
ATOM 137 N LEU A 19 4.336 43.261 -0.123 1.00 10.76 N
ANISOU 137 N LEU A 19 1207 1466 1416 506 427 774 N
ATOM 138 CA LEU A 19 5.046 44.066 -1.112 1.00 12.81 C
ANISOU 138 CA LEU A 19 1503 1672 1692 499 455 832 C
ATOM 139 C LEU A 19 5.336 43.240 -2.362 1.00 13.64 C
ANISOU 139 C LEU A 19 1571 1867 1745 520 470 841 C
ATOM 140 O LEU A 19 5.260 43.762 -3.467 1.00 13.36 O
ANISOU 140 O LEU A 19 1568 1837 1673 553 490 890 O
ATOM 141 CB LEU A 19 6.329 44.669 -0.522 1.00 13.33 C
ANISOU 141 CB LEU A 19 1592 1638 1836 400 453 868 C
ATOM 142 CG LEU A 19 7.505 43.806 -0.065 1.00 15.24 C
ANISOU 142 CG LEU A 19 1747 1925 2121 327 448 866 C
ATOM 143 CD1 LEU A 19 8.463 43.550 -1.211 1.00 15.28 C
ANISOU 143 CD1 LEU A 19 1688 2005 2113 334 490 928 C
ATOM 144 CD2 LEU A 19 8.234 44.470 1.101 1.00 19.12 C
ANISOU 144 CD2 LEU A 19 2273 2311 2680 206 408 885 C
ATOM 145 N ALA A 20 5.641 41.952 -2.193 1.00 12.14 N
ANISOU 145 N ALA A 20 1344 1733 1537 513 456 798 N
ATOM 146 CA ALA A 20 5.814 41.056 -3.337 1.00 11.18 C
ANISOU 146 CA ALA A 20 1245 1672 1332 562 465 796 C
ATOM 147 C ALA A 20 4.494 40.864 -4.088 1.00 14.50 C
ANISOU 147 C ALA A 20 1713 2135 1661 585 415 781 C
ATOM 148 O ALA A 20 4.469 40.823 -5.321 1.00 15.26 O
ANISOU 148 O ALA A 20 1860 2258 1680 626 424 806 O
ATOM 149 CB ALA A 20 6.364 39.712 -2.879 1.00 12.88 C
ANISOU 149 CB ALA A 20 1459 1904 1528 564 453 753 C
ATOM 150 N LEU A 21 3.397 40.786 -3.343 1.00 12.30 N
ANISOU 150 N LEU A 21 1409 1878 1384 558 358 758 N
ATOM 151 CA LEU A 21 2.081 40.630 -3.948 1.00 11.47 C
ANISOU 151 CA LEU A 21 1311 1846 1203 566 290 773 C
ATOM 152 C LEU A 21 1.745 41.847 -4.811 1.00 14.82 C
ANISOU 152 C LEU A 21 1745 2269 1618 632 322 834 C
ATOM 153 O LEU A 21 1.173 41.711 -5.892 1.00 14.77 O
ANISOU 153 O LEU A 21 1772 2309 1530 647 276 862 O
ATOM 154 CB LEU A 21 1.014 40.445 -2.868 1.00 12.48 C
ANISOU 154 CB LEU A 21 1361 2039 1342 536 243 770 C
ATOM 155 CG LEU A 21 0.896 39.032 -2.292 1.00 21.12 C
ANISOU 155 CG LEU A 21 2465 3157 2403 440 161 731 C
ATOM 156 CD1 LEU A 21 -0.379 38.891 -1.476 1.00 19.28 C
ANISOU 156 CD1 LEU A 21 2123 3045 2159 397 111 763 C
ATOM 157 CD2 LEU A 21 0.941 37.995 -3.404 1.00 24.93 C
ANISOU 157 CD2 LEU A 21 3070 3623 2779 400 82 716 C
ATOM 158 N GLN A 22 2.104 43.034 -4.327 1.00 12.49 N
ANISOU 158 N GLN A 22 1448 1902 1396 660 383 860 N
ATOM 159 CA GLN A 22 1.838 44.277 -5.057 1.00 13.69 C
ANISOU 159 CA GLN A 22 1646 2016 1539 721 402 925 C
ATOM 160 C GLN A 22 2.652 44.337 -6.346 1.00 15.03 C
ANISOU 160 C GLN A 22 1867 2174 1671 712 428 967 C
ATOM 161 O GLN A 22 2.175 44.837 -7.372 1.00 17.10 O
ANISOU 161 O GLN A 22 2170 2453 1875 754 411 1022 O
ATOM 162 CB GLN A 22 2.144 45.500 -4.185 1.00 16.27 C
ANISOU 162 CB GLN A 22 2020 2221 1941 736 435 940 C
ATOM 163 CG GLN A 22 1.068 45.803 -3.150 1.00 20.28 C
ANISOU 163 CG GLN A 22 2511 2747 2447 807 422 916 C
ATOM 164 CD GLN A 22 -0.253 46.184 -3.793 1.00 27.15 C
ANISOU 164 CD GLN A 22 3357 3706 3253 913 397 960 C
ATOM 165 OE1 GLN A 22 -1.199 45.398 -3.808 1.00 38.40 O
ANISOU 165 OE1 GLN A 22 4680 5284 4628 917 362 961 O
ATOM 166 NE2 GLN A 22 -0.320 47.394 -4.332 1.00 31.78 N
ANISOU 166 NE2 GLN A 22 4037 4196 3841 988 399 1011 N
ATOM 167 N ALA A 23 3.880 43.837 -6.289 1.00 13.94 N
ANISOU 167 N ALA A 23 1719 2021 1556 670 471 953 N
ATOM 168 CA ALA A 23 4.705 43.706 -7.484 1.00 14.83 C
ANISOU 168 CA ALA A 23 1863 2161 1610 682 515 999 C
ATOM 169 C ALA A 23 4.034 42.770 -8.490 1.00 16.77 C
ANISOU 169 C ALA A 23 2163 2482 1726 720 469 972 C
ATOM 170 O ALA A 23 3.957 43.076 -9.676 1.00 16.40 O
ANISOU 170 O ALA A 23 2176 2460 1597 749 476 1024 O
ATOM 171 CB ALA A 23 6.085 43.191 -7.122 1.00 14.59 C
ANISOU 171 CB ALA A 23 1783 2137 1622 660 572 997 C
ATOM 172 N ALA A 24 3.552 41.632 -8.002 1.00 15.28 N
ANISOU 172 N ALA A 24 1978 2319 1508 700 407 898 N
ATOM 173 CA ALA A 24 2.887 40.654 -8.857 1.00 16.23 C
ANISOU 173 CA ALA A 24 2192 2484 1490 696 324 873 C
ATOM 174 C ALA A 24 1.622 41.252 -9.461 1.00 16.10 C
ANISOU 174 C ALA A 24 2178 2510 1429 691 245 924 C
ATOM 175 O ALA A 24 1.327 41.045 -10.638 1.00 17.11 O
ANISOU 175 O ALA A 24 2398 2669 1434 696 198 949 O
ATOM 176 CB ALA A 24 2.554 39.397 -8.068 1.00 17.43 C
ANISOU 176 CB ALA A 24 2365 2633 1623 636 243 802 C
ATOM 177 N ARG A 25 0.879 41.996 -8.648 1.00 15.53 N
ANISOU 177 N ARG A 25 2009 2446 1445 697 233 946 N
ATOM 178 CA ARG A 25 -0.355 42.627 -9.103 1.00 16.63 C
ANISOU 178 CA ARG A 25 2119 2646 1553 730 167 1009 C
ATOM 179 C ARG A 25 -0.073 43.557 -10.277 1.00 18.49 C
ANISOU 179 C ARG A 25 2425 2853 1746 784 202 1080 C
ATOM 180 O ARG A 25 -0.803 43.561 -11.268 1.00 19.18 O
ANISOU 180 O ARG A 25 2554 2996 1738 793 123 1128 O
ATOM 181 CB ARG A 25 -1.009 43.409 -7.963 1.00 17.35 C
ANISOU 181 CB ARG A 25 2102 2751 1739 778 192 1023 C
ATOM 182 CG ARG A 25 -1.676 42.533 -6.916 1.00 23.37 C
ANISOU 182 CG ARG A 25 2770 3594 2515 723 142 986 C
ATOM 183 CD ARG A 25 -2.478 43.362 -5.926 1.00 28.90 C
ANISOU 183 CD ARG A 25 3367 4345 3268 803 182 1014 C
ATOM 184 NE ARG A 25 -3.859 43.551 -6.360 1.00 33.70 N
ANISOU 184 NE ARG A 25 3885 5099 3822 849 118 1089 N
ATOM 185 CZ ARG A 25 -4.710 44.402 -5.796 1.00 40.23 C
ANISOU 185 CZ ARG A 25 4632 5993 4659 966 160 1132 C
ATOM 186 NH1 ARG A 25 -4.323 45.147 -4.769 1.00 45.00 N1+
ANISOU 186 NH1 ARG A 25 5279 6504 5316 1042 251 1096 N1+
ATOM 187 NH2 ARG A 25 -5.948 44.509 -6.257 1.00 42.66 N
ANISOU 187 NH2 ARG A 25 4833 6462 4913 1011 101 1213 N
ATOM 188 N GLN A 26 0.991 44.345 -10.158 1.00 19.98 N
ANISOU 188 N GLN A 26 2633 2957 2001 802 304 1100 N
ATOM 189 CA GLN A 26 1.373 45.279 -11.210 1.00 19.15 C
ANISOU 189 CA GLN A 26 2601 2819 1858 829 338 1187 C
ATOM 190 C GLN A 26 1.806 44.523 -12.460 1.00 19.95 C
ANISOU 190 C GLN A 26 2782 2976 1824 817 340 1191 C
ATOM 191 O GLN A 26 1.496 44.926 -13.581 1.00 23.75 O
ANISOU 191 O GLN A 26 3333 3480 2210 837 312 1260 O
ATOM 192 CB GLN A 26 2.506 46.188 -10.731 1.00 21.66 C
ANISOU 192 CB GLN A 26 2925 3034 2271 804 427 1223 C
ATOM 193 CG GLN A 26 2.998 47.170 -11.782 1.00 20.84 C
ANISOU 193 CG GLN A 26 2905 2891 2124 797 457 1335 C
ATOM 194 CD GLN A 26 1.928 48.158 -12.203 1.00 25.45 C
ANISOU 194 CD GLN A 26 3548 3437 2685 860 388 1404 C
ATOM 195 OE1 GLN A 26 1.014 48.464 -11.438 1.00 22.72 O
ANISOU 195 OE1 GLN A 26 3173 3069 2392 920 342 1378 O
ATOM 196 NE2 GLN A 26 2.037 48.662 -13.427 1.00 29.35 N
ANISOU 196 NE2 GLN A 26 4126 3934 3091 861 383 1501 N
ATOM 197 N ALA A 27 2.525 43.423 -12.259 1.00 19.20 N
ANISOU 197 N ALA A 27 2693 2898 1706 798 374 1119 N
ATOM 198 CA ALA A 27 3.002 42.604 -13.369 1.00 24.95 C
ANISOU 198 CA ALA A 27 3525 3673 2283 818 391 1107 C
ATOM 199 C ALA A 27 1.836 42.056 -14.195 1.00 23.76 C
ANISOU 199 C ALA A 27 3474 3568 1987 792 252 1101 C
ATOM 200 O ALA A 27 1.910 42.000 -15.425 1.00 28.09 O
ANISOU 200 O ALA A 27 4132 4151 2390 811 248 1136 O
ATOM 201 CB ALA A 27 3.872 41.462 -12.847 1.00 19.97 C
ANISOU 201 CB ALA A 27 2897 3040 1651 836 443 1023 C
ATOM 202 N LEU A 28 0.768 41.656 -13.513 1.00 22.52 N
ANISOU 202 N LEU A 28 3275 3421 1860 737 132 1070 N
ATOM 203 CA LEU A 28 -0.410 41.115 -14.181 1.00 26.50 C
ANISOU 203 CA LEU A 28 3856 3977 2234 673 -36 1084 C
ATOM 204 C LEU A 28 -1.044 42.160 -15.092 1.00 35.14 C
ANISOU 204 C LEU A 28 4954 5108 3289 712 -73 1187 C
ATOM 205 O LEU A 28 -1.278 41.908 -16.274 1.00 34.52 O
ANISOU 205 O LEU A 28 5004 5061 3050 686 -147 1218 O
ATOM 206 CB LEU A 28 -1.431 40.623 -13.153 1.00 33.12 C
ANISOU 206 CB LEU A 28 4607 4843 3133 602 -151 1059 C
ATOM 207 CG LEU A 28 -1.106 39.301 -12.454 1.00 34.94 C
ANISOU 207 CG LEU A 28 4894 5035 3344 522 -187 969 C
ATOM 208 CD1 LEU A 28 -2.311 38.796 -11.676 1.00 35.27 C
ANISOU 208 CD1 LEU A 28 4869 5125 3408 431 -329 970 C
ATOM 209 CD2 LEU A 28 -0.638 38.262 -13.461 1.00 38.68 C
ANISOU 209 CD2 LEU A 28 5575 5489 3632 482 -232 931 C
ATOM 210 N LYS A 29 -1.321 43.334 -14.534 1.00 30.18 N
ANISOU 210 N LYS A 29 4204 4469 2796 777 -26 1241 N
ATOM 211 CA LYS A 29 -1.926 44.419 -15.295 1.00 38.16 C
ANISOU 211 CA LYS A 29 5221 5498 3781 836 -60 1347 C
ATOM 212 C LYS A 29 -1.006 44.869 -16.423 1.00 38.43 C
ANISOU 212 C LYS A 29 5377 5498 3728 851 17 1400 C
ATOM 213 O LYS A 29 -1.453 45.461 -17.405 1.00 45.23 O
ANISOU 213 O LYS A 29 6300 6380 4503 874 -39 1491 O
ATOM 214 CB LYS A 29 -2.252 45.601 -14.379 1.00 40.51 C
ANISOU 214 CB LYS A 29 5403 5759 4231 921 -9 1386 C
ATOM 215 CG LYS A 29 -3.455 45.375 -13.478 1.00 46.69 C
ANISOU 215 CG LYS A 29 6042 6628 5068 940 -83 1373 C
ATOM 216 CD LYS A 29 -3.986 46.688 -12.927 1.00 51.46 C
ANISOU 216 CD LYS A 29 6576 7210 5766 1070 -43 1432 C
ATOM 217 CE LYS A 29 -5.194 46.462 -12.031 1.00 54.11 C
ANISOU 217 CE LYS A 29 6741 7677 6139 1111 -86 1431 C
ATOM 218 NZ LYS A 29 -4.886 45.538 -10.906 1.00 52.96 N1+
ANISOU 218 NZ LYS A 29 6529 7547 6046 1027 -50 1337 N1+
ATOM 219 N ALA A 30 0.284 44.583 -16.276 1.00 40.75 N
ANISOU 219 N ALA A 30 5691 5755 4037 842 146 1356 N
ATOM 220 CA ALA A 30 1.271 44.955 -17.281 1.00 42.04 C
ANISOU 220 CA ALA A 30 5939 5919 4114 858 245 1416 C
ATOM 221 C ALA A 30 1.141 44.072 -18.516 1.00 41.33 C
ANISOU 221 C ALA A 30 5991 5902 3810 846 191 1402 C
ATOM 222 O ALA A 30 0.451 44.424 -19.473 1.00 38.72 O
ANISOU 222 O ALA A 30 5738 5605 3367 839 100 1476 O
ATOM 223 CB ALA A 30 2.674 44.853 -16.703 1.00 44.66 C
ANISOU 223 CB ALA A 30 6216 6224 4527 862 397 1386 C
TER 224 ALA A 30
ATOM 225 N ALA B 1 -9.071 38.628 -14.640 1.00 28.44 N
ANISOU 225 N ALA B 1 4969 3693 2145 1222 -712 -363 N
ATOM 226 CA ALA B 1 -9.555 37.219 -14.644 1.00 33.00 C
ANISOU 226 CA ALA B 1 5303 4348 2886 1300 -792 -526 C
ATOM 227 C ALA B 1 -9.255 36.558 -13.299 1.00 24.38 C
ANISOU 227 C ALA B 1 3983 3295 1987 1221 -722 -594 C
ATOM 228 O ALA B 1 -9.015 37.247 -12.307 1.00 20.78 O
ANISOU 228 O ALA B 1 3515 2793 1586 1140 -649 -533 O
ATOM 229 CB ALA B 1 -8.918 36.441 -15.789 1.00 33.54 C
ANISOU 229 CB ALA B 1 5394 4532 2819 1292 -730 -556 C
ATOM 230 N GLU B 2 -9.262 35.226 -13.277 1.00 22.01 N
ANISOU 230 N GLU B 2 3511 3048 1806 1227 -739 -704 N
ATOM 231 CA GLU B 2 -9.142 34.470 -12.037 1.00 18.42 C
ANISOU 231 CA GLU B 2 2861 2588 1551 1153 -703 -764 C
ATOM 232 C GLU B 2 -7.857 34.799 -11.274 1.00 19.06 C
ANISOU 232 C GLU B 2 2921 2723 1598 1043 -512 -706 C
ATOM 233 O GLU B 2 -7.879 34.957 -10.054 1.00 17.95 O
ANISOU 233 O GLU B 2 2672 2533 1614 961 -467 -684 O
ATOM 234 CB GLU B 2 -9.202 32.968 -12.328 1.00 21.17 C
ANISOU 234 CB GLU B 2 3107 2948 1988 1172 -756 -858 C
ATOM 235 CG GLU B 2 -10.591 32.459 -12.707 1.00 27.30 C
ANISOU 235 CG GLU B 2 3839 3669 2865 1230 -930 -944 C
ATOM 236 CD GLU B 2 -10.988 32.796 -14.136 1.00 30.81 C
ANISOU 236 CD GLU B 2 4418 4131 3158 1349 -1011 -950 C
ATOM 237 OE1 GLU B 2 -10.094 33.073 -14.960 1.00 29.36 O
ANISOU 237 OE1 GLU B 2 4365 4008 2783 1370 -929 -895 O
ATOM 238 OE2 GLU B 2 -12.200 32.786 -14.436 1.00 28.26 O1-
ANISOU 238 OE2 GLU B 2 4062 3774 2902 1407 -1146 -1019 O1-
ATOM 239 N ALA B 3 -6.745 34.918 -11.991 1.00 21.26 N
ANISOU 239 N ALA B 3 3265 3111 1700 1011 -381 -666 N
ATOM 240 CA ALA B 3 -5.467 35.200 -11.347 1.00 19.85 C
ANISOU 240 CA ALA B 3 3019 3033 1491 894 -191 -629 C
ATOM 241 C ALA B 3 -5.525 36.536 -10.620 1.00 16.87 C
ANISOU 241 C ALA B 3 2699 2565 1148 765 -128 -495 C
ATOM 242 O ALA B 3 -5.124 36.638 -9.457 1.00 16.59 O
ANISOU 242 O ALA B 3 2536 2520 1250 669 -55 -478 O
ATOM 243 CB ALA B 3 -4.343 35.203 -12.363 1.00 21.22 C
ANISOU 243 CB ALA B 3 3222 3371 1470 844 -53 -616 C
ATOM 244 N GLU B 4 -6.021 37.556 -11.312 1.00 20.63 N
ANISOU 244 N GLU B 4 3392 2956 1490 773 -173 -402 N
ATOM 245 CA GLU B 4 -6.131 38.892 -10.739 1.00 20.23 C
ANISOU 245 CA GLU B 4 3460 2772 1456 672 -142 -278 C
ATOM 246 C GLU B 4 -7.058 38.888 -9.529 1.00 16.51 C
ANISOU 246 C GLU B 4 2852 2185 1235 721 -239 -320 C
ATOM 247 O GLU B 4 -6.750 39.487 -8.499 1.00 15.83 O
ANISOU 247 O GLU B 4 2725 2049 1241 609 -160 -274 O
ATOM 248 CB GLU B 4 -6.646 39.883 -11.785 1.00 24.89 C
ANISOU 248 CB GLU B 4 4365 3248 1843 727 -230 -180 C
ATOM 249 CG GLU B 4 -5.558 40.472 -12.667 1.00 50.05 C
ANISOU 249 CG GLU B 4 7757 6512 4746 563 -66 -69 C
ATOM 250 CD GLU B 4 -6.101 41.453 -13.687 1.00 70.83 C
ANISOU 250 CD GLU B 4 10770 8991 7152 615 -173 51 C
ATOM 251 OE1 GLU B 4 -5.331 42.323 -14.146 1.00 79.13 O
ANISOU 251 OE1 GLU B 4 12004 10023 8040 406 -36 185 O
ATOM 252 OE2 GLU B 4 -7.298 41.355 -14.029 1.00 78.31 O1-
ANISOU 252 OE2 GLU B 4 11756 9836 8164 837 -395 2 O1-
ATOM 253 N SER B 5 -8.194 38.210 -9.659 1.00 16.47 N
ANISOU 253 N SER B 5 2770 2159 1329 871 -406 -421 N
ATOM 254 CA SER B 5 -9.159 38.136 -8.571 1.00 15.53 C
ANISOU 254 CA SER B 5 2494 1980 1427 899 -482 -482 C
ATOM 255 C SER B 5 -8.544 37.425 -7.371 1.00 14.00 C
ANISOU 255 C SER B 5 2108 1835 1378 774 -367 -507 C
ATOM 256 O SER B 5 -8.792 37.789 -6.217 1.00 14.05 O
ANISOU 256 O SER B 5 2030 1797 1512 717 -337 -500 O
ATOM 257 CB SER B 5 -10.427 37.415 -9.025 1.00 18.41 C
ANISOU 257 CB SER B 5 2778 2362 1855 1040 -668 -608 C
ATOM 258 OG SER B 5 -11.099 38.166 -10.021 1.00 22.19 O
ANISOU 258 OG SER B 5 3434 2793 2204 1192 -812 -595 O
ATOM 259 N ALA B 6 -7.729 36.417 -7.657 1.00 13.44 N
ANISOU 259 N ALA B 6 1983 1855 1268 755 -315 -544 N
ATOM 260 CA ALA B 6 -7.092 35.634 -6.608 1.00 12.24 C
ANISOU 260 CA ALA B 6 1685 1738 1228 678 -244 -572 C
ATOM 261 C ALA B 6 -6.096 36.489 -5.834 1.00 13.46 C
ANISOU 261 C ALA B 6 1826 1918 1369 552 -99 -490 C
ATOM 262 O ALA B 6 -6.013 36.404 -4.607 1.00 10.89 O
ANISOU 262 O ALA B 6 1403 1571 1162 484 -68 -489 O
ATOM 263 CB ALA B 6 -6.401 34.416 -7.191 1.00 12.65 C
ANISOU 263 CB ALA B 6 1712 1873 1222 739 -249 -652 C
ATOM 264 N LEU B 7 -5.343 37.321 -6.548 1.00 12.87 N
ANISOU 264 N LEU B 7 1863 1893 1135 498 -9 -423 N
ATOM 265 CA LEU B 7 -4.333 38.143 -5.892 1.00 12.92 C
ANISOU 265 CA LEU B 7 1853 1938 1117 336 131 -358 C
ATOM 266 C LEU B 7 -4.990 39.254 -5.095 1.00 12.58 C
ANISOU 266 C LEU B 7 1888 1739 1154 285 107 -297 C
ATOM 267 O LEU B 7 -4.516 39.599 -4.014 1.00 12.02 O
ANISOU 267 O LEU B 7 1745 1667 1153 176 174 -285 O
ATOM 268 CB LEU B 7 -3.351 38.723 -6.911 1.00 14.62 C
ANISOU 268 CB LEU B 7 2172 2263 1119 237 253 -305 C
ATOM 269 CG LEU B 7 -2.435 37.703 -7.595 1.00 16.96 C
ANISOU 269 CG LEU B 7 2350 2776 1317 285 314 -397 C
ATOM 270 CD1 LEU B 7 -1.372 38.435 -8.382 1.00 19.05 C
ANISOU 270 CD1 LEU B 7 2678 3198 1363 120 484 -347 C
ATOM 271 CD2 LEU B 7 -1.792 36.732 -6.606 1.00 16.25 C
ANISOU 271 CD2 LEU B 7 2030 2785 1358 322 320 -495 C
ATOM 272 N GLU B 8 -6.089 39.798 -5.608 1.00 13.28 N
ANISOU 272 N GLU B 8 2120 1701 1226 388 -4 -278 N
ATOM 273 CA GLU B 8 -6.831 40.824 -4.871 1.00 14.07 C
ANISOU 273 CA GLU B 8 2291 1652 1402 400 -54 -257 C
ATOM 274 C GLU B 8 -7.398 40.254 -3.566 1.00 15.31 C
ANISOU 274 C GLU B 8 2242 1828 1749 415 -73 -339 C
ATOM 275 O GLU B 8 -7.307 40.873 -2.502 1.00 13.48 O
ANISOU 275 O GLU B 8 1992 1549 1581 344 -27 -332 O
ATOM 276 CB GLU B 8 -7.960 41.400 -5.730 1.00 16.73 C
ANISOU 276 CB GLU B 8 2804 1873 1681 571 -209 -254 C
ATOM 277 CG GLU B 8 -8.711 42.543 -5.060 1.00 25.33 C
ANISOU 277 CG GLU B 8 3989 2805 2831 637 -281 -257 C
ATOM 278 CD GLU B 8 -9.753 43.170 -5.965 1.00 41.37 C
ANISOU 278 CD GLU B 8 6214 4722 4784 852 -466 -265 C
ATOM 279 OE1 GLU B 8 -10.042 42.594 -7.034 1.00 48.13 O
ANISOU 279 OE1 GLU B 8 7091 5638 5559 947 -547 -281 O
ATOM 280 OE2 GLU B 8 -10.282 44.243 -5.606 1.00 45.98 O1-
ANISOU 280 OE2 GLU B 8 6939 5152 5380 946 -548 -269 O1-
ATOM 281 N TYR B 9 -7.975 39.061 -3.655 1.00 12.85 N
ANISOU 281 N TYR B 9 1791 1580 1509 489 -139 -418 N
ATOM 282 CA TYR B 9 -8.501 38.371 -2.485 1.00 12.43 C
ANISOU 282 CA TYR B 9 1567 1553 1604 459 -143 -484 C
ATOM 283 C TYR B 9 -7.382 38.086 -1.493 1.00 12.67 C
ANISOU 283 C TYR B 9 1533 1627 1654 331 -33 -453 C
ATOM 284 O TYR B 9 -7.532 38.314 -0.298 1.00 11.65 O
ANISOU 284 O TYR B 9 1344 1485 1597 269 3 -461 O
ATOM 285 CB TYR B 9 -9.189 37.078 -2.925 1.00 10.73 C
ANISOU 285 CB TYR B 9 1265 1380 1434 514 -232 -563 C
ATOM 286 CG TYR B 9 -9.652 36.162 -1.815 1.00 10.07 C
ANISOU 286 CG TYR B 9 1042 1314 1470 430 -226 -615 C
ATOM 287 CD1 TYR B 9 -10.964 36.198 -1.369 1.00 13.84 C
ANISOU 287 CD1 TYR B 9 1411 1811 2035 428 -272 -692 C
ATOM 288 CD2 TYR B 9 -8.791 35.232 -1.241 1.00 14.42 C
ANISOU 288 CD2 TYR B 9 1578 1873 2030 353 -179 -594 C
ATOM 289 CE1 TYR B 9 -11.404 35.348 -0.376 1.00 16.09 C
ANISOU 289 CE1 TYR B 9 1590 2125 2400 302 -244 -729 C
ATOM 290 CE2 TYR B 9 -9.223 34.379 -0.245 1.00 12.95 C
ANISOU 290 CE2 TYR B 9 1329 1672 1921 258 -181 -618 C
ATOM 291 CZ TYR B 9 -10.529 34.441 0.182 1.00 15.51 C
ANISOU 291 CZ TYR B 9 1560 2016 2318 207 -200 -677 C
ATOM 292 OH TYR B 9 -10.968 33.592 1.174 1.00 18.01 O
ANISOU 292 OH TYR B 9 1830 2328 2683 62 -178 -691 O
ATOM 293 N ALA B 10 -6.252 37.609 -1.998 1.00 9.48 N
ANISOU 293 N ALA B 10 1134 1298 1172 309 14 -434 N
ATOM 294 CA ALA B 10 -5.119 37.286 -1.144 1.00 9.87 C
ANISOU 294 CA ALA B 10 1100 1419 1229 225 89 -429 C
ATOM 295 C ALA B 10 -4.650 38.514 -0.380 1.00 11.10 C
ANISOU 295 C ALA B 10 1282 1558 1378 106 169 -383 C
ATOM 296 O ALA B 10 -4.384 38.444 0.820 1.00 10.54 O
ANISOU 296 O ALA B 10 1140 1500 1364 45 192 -393 O
ATOM 297 CB ALA B 10 -3.988 36.717 -1.964 1.00 9.68 C
ANISOU 297 CB ALA B 10 1052 1520 1107 253 124 -451 C
ATOM 298 N GLN B 11 -4.554 39.641 -1.086 1.00 10.25 N
ANISOU 298 N GLN B 11 1308 1402 1185 67 201 -330 N
ATOM 299 CA GLN B 11 -4.120 40.891 -0.459 1.00 10.94 C
ANISOU 299 CA GLN B 11 1471 1432 1255 -68 264 -289 C
ATOM 300 C GLN B 11 -5.120 41.324 0.614 1.00 11.04 C
ANISOU 300 C GLN B 11 1487 1334 1373 -27 215 -320 C
ATOM 301 O GLN B 11 -4.729 41.771 1.694 1.00 12.36 O
ANISOU 301 O GLN B 11 1628 1496 1571 -122 258 -330 O
ATOM 302 CB GLN B 11 -3.959 41.996 -1.502 1.00 15.53 C
ANISOU 302 CB GLN B 11 2268 1930 1705 -126 289 -212 C
ATOM 303 CG GLN B 11 -3.407 43.300 -0.946 1.00 26.14 C
ANISOU 303 CG GLN B 11 3737 3180 3013 -305 351 -167 C
ATOM 304 CD GLN B 11 -1.969 43.177 -0.474 1.00 42.13 C
ANISOU 304 CD GLN B 11 5616 5381 5011 -502 469 -183 C
ATOM 305 OE1 GLN B 11 -1.692 43.208 0.725 1.00 52.60 O
ANISOU 305 OE1 GLN B 11 6835 6733 6418 -557 477 -229 O
ATOM 306 NE2 GLN B 11 -1.043 43.044 -1.420 1.00 38.97 N
ANISOU 306 NE2 GLN B 11 5197 5128 4482 -606 560 -161 N
ATOM 307 N GLN B 12 -6.403 41.171 0.324 1.00 9.96 N
ANISOU 307 N GLN B 12 1362 1138 1284 117 125 -356 N
ATOM 308 CA GLN B 12 -7.440 41.503 1.295 1.00 11.17 C
ANISOU 308 CA GLN B 12 1471 1243 1529 172 89 -421 C
ATOM 309 C GLN B 12 -7.353 40.606 2.533 1.00 10.64 C
ANISOU 309 C GLN B 12 1239 1269 1533 102 134 -458 C
ATOM 310 O GLN B 12 -7.467 41.084 3.656 1.00 11.66 O
ANISOU 310 O GLN B 12 1350 1389 1692 58 168 -489 O
ATOM 311 CB GLN B 12 -8.821 41.399 0.648 1.00 12.77 C
ANISOU 311 CB GLN B 12 1663 1424 1764 343 -21 -482 C
ATOM 312 CG GLN B 12 -9.092 42.515 -0.348 1.00 17.18 C
ANISOU 312 CG GLN B 12 2436 1851 2239 451 -101 -449 C
ATOM 313 CD GLN B 12 -10.339 42.288 -1.177 1.00 30.50 C
ANISOU 313 CD GLN B 12 4100 3550 3940 646 -241 -520 C
ATOM 314 OE1 GLN B 12 -10.731 41.151 -1.436 1.00 31.54 O
ANISOU 314 OE1 GLN B 12 4075 3794 4116 659 -266 -569 O
ATOM 315 NE2 GLN B 12 -10.972 43.377 -1.599 1.00 39.02 N
ANISOU 315 NE2 GLN B 12 5347 4503 4975 807 -353 -536 N
ATOM 316 N ALA B 13 -7.124 39.311 2.320 1.00 10.77 N
ANISOU 316 N ALA B 13 1171 1361 1559 97 124 -456 N
ATOM 317 CA ALA B 13 -6.953 38.360 3.418 1.00 10.66 C
ANISOU 317 CA ALA B 13 1067 1402 1583 30 145 -469 C
ATOM 318 C ALA B 13 -5.746 38.708 4.288 1.00 9.88 C
ANISOU 318 C ALA B 13 969 1336 1447 -62 202 -442 C
ATOM 319 O ALA B 13 -5.821 38.652 5.515 1.00 9.63 O
ANISOU 319 O ALA B 13 908 1319 1430 -120 224 -456 O
ATOM 320 CB ALA B 13 -6.816 36.938 2.875 1.00 9.29 C
ANISOU 320 CB ALA B 13 867 1253 1409 62 94 -471 C
ATOM 321 N LEU B 14 -4.642 39.078 3.655 1.00 9.97 N
ANISOU 321 N LEU B 14 1006 1384 1399 -90 230 -413 N
ATOM 322 CA LEU B 14 -3.445 39.448 4.396 1.00 10.99 C
ANISOU 322 CA LEU B 14 1101 1581 1493 -192 276 -412 C
ATOM 323 C LEU B 14 -3.670 40.724 5.209 1.00 10.33 C
ANISOU 323 C LEU B 14 1085 1423 1417 -274 309 -420 C
ATOM 324 O LEU B 14 -3.169 40.836 6.322 1.00 11.65 O
ANISOU 324 O LEU B 14 1214 1631 1579 -346 322 -443 O
ATOM 325 CB LEU B 14 -2.254 39.619 3.449 1.00 13.58 C
ANISOU 325 CB LEU B 14 1408 2007 1744 -237 319 -401 C
ATOM 326 CG LEU B 14 -1.760 38.349 2.750 1.00 16.06 C
ANISOU 326 CG LEU B 14 1639 2431 2034 -133 287 -429 C
ATOM 327 CD1 LEU B 14 -0.505 38.669 1.951 1.00 15.24 C
ANISOU 327 CD1 LEU B 14 1473 2485 1834 -200 362 -446 C
ATOM 328 CD2 LEU B 14 -1.510 37.216 3.737 1.00 19.41 C
ANISOU 328 CD2 LEU B 14 1992 2891 2492 -66 218 -465 C
ATOM 329 N GLU B 15 -4.425 41.671 4.659 1.00 9.15 N
ANISOU 329 N GLU B 15 1052 1154 1270 -242 302 -412 N
ATOM 330 CA GLU B 15 -4.759 42.906 5.371 1.00 11.48 C
ANISOU 330 CA GLU B 15 1449 1343 1572 -277 309 -441 C
ATOM 331 C GLU B 15 -5.525 42.588 6.650 1.00 13.50 C
ANISOU 331 C GLU B 15 1622 1629 1877 -238 306 -508 C
ATOM 332 O GLU B 15 -5.277 43.183 7.707 1.00 13.37 O
ANISOU 332 O GLU B 15 1628 1603 1848 -306 329 -547 O
ATOM 333 CB GLU B 15 -5.579 43.846 4.477 1.00 15.24 C
ANISOU 333 CB GLU B 15 2093 1663 2035 -182 260 -432 C
ATOM 334 CG GLU B 15 -4.744 44.599 3.450 1.00 17.44 C
ANISOU 334 CG GLU B 15 2540 1867 2220 -286 282 -352 C
ATOM 335 CD GLU B 15 -5.577 45.309 2.400 1.00 28.76 C
ANISOU 335 CD GLU B 15 4182 3136 3612 -159 203 -321 C
ATOM 336 OE1 GLU B 15 -6.822 45.243 2.470 1.00 32.76 O
ANISOU 336 OE1 GLU B 15 4665 3605 4179 35 119 -387 O
ATOM 337 OE2 GLU B 15 -4.977 45.932 1.498 1.00 34.64 O1-
ANISOU 337 OE2 GLU B 15 5114 3800 4249 -259 222 -237 O1-
ATOM 338 N LYS B 16 -6.452 41.645 6.554 1.00 12.19 N
ANISOU 338 N LYS B 16 1367 1510 1753 -153 284 -527 N
ATOM 339 CA LYS B 16 -7.216 41.209 7.717 1.00 14.24 C
ANISOU 339 CA LYS B 16 1544 1833 2035 -159 307 -584 C
ATOM 340 C LYS B 16 -6.335 40.496 8.746 1.00 12.57 C
ANISOU 340 C LYS B 16 1300 1694 1780 -264 331 -554 C
ATOM 341 O LYS B 16 -6.499 40.683 9.948 1.00 10.58 O
ANISOU 341 O LYS B 16 1045 1477 1499 -312 365 -593 O
ATOM 342 CB LYS B 16 -8.366 40.309 7.278 1.00 13.13 C
ANISOU 342 CB LYS B 16 1314 1736 1940 -98 284 -610 C
ATOM 343 CG LYS B 16 -9.403 41.042 6.451 1.00 15.62 C
ANISOU 343 CG LYS B 16 1635 2008 2291 42 234 -674 C
ATOM 344 CD LYS B 16 -10.497 40.119 5.953 1.00 20.37 C
ANISOU 344 CD LYS B 16 2117 2685 2939 82 197 -717 C
ATOM 345 CE LYS B 16 -11.448 40.879 5.039 1.00 22.86 C
ANISOU 345 CE LYS B 16 2448 2971 3265 243 101 -763 C
ATOM 346 NZ LYS B 16 -12.523 40.010 4.489 1.00 26.66 N1+
ANISOU 346 NZ LYS B 16 2808 3543 3778 258 43 -810 N1+
ATOM 347 N ALA B 17 -5.388 39.688 8.282 1.00 11.18 N
ANISOU 347 N ALA B 17 1110 1552 1588 -277 301 -497 N
ATOM 348 CA ALA B 17 -4.460 39.038 9.197 1.00 12.24 C
ANISOU 348 CA ALA B 17 1228 1753 1671 -328 284 -479 C
ATOM 349 C ALA B 17 -3.635 40.080 9.938 1.00 11.84 C
ANISOU 349 C ALA B 17 1191 1726 1582 -406 304 -510 C
ATOM 350 O ALA B 17 -3.346 39.930 11.124 1.00 12.49 O
ANISOU 350 O ALA B 17 1278 1854 1613 -450 295 -526 O
ATOM 351 CB ALA B 17 -3.546 38.084 8.448 1.00 10.93 C
ANISOU 351 CB ALA B 17 1031 1630 1493 -276 228 -449 C
ATOM 352 N GLN B 18 -3.267 41.144 9.235 1.00 9.30 N
ANISOU 352 N GLN B 18 902 1363 1269 -440 327 -518 N
ATOM 353 CA GLN B 18 -2.385 42.148 9.808 1.00 12.54 C
ANISOU 353 CA GLN B 18 1337 1784 1643 -557 341 -553 C
ATOM 354 C GLN B 18 -3.071 42.933 10.904 1.00 10.28 C
ANISOU 354 C GLN B 18 1124 1432 1348 -571 356 -614 C
ATOM 355 O GLN B 18 -2.455 43.235 11.932 1.00 11.93 O
ANISOU 355 O GLN B 18 1333 1689 1510 -651 347 -658 O
ATOM 356 CB GLN B 18 -1.896 43.100 8.738 1.00 10.61 C
ANISOU 356 CB GLN B 18 1157 1483 1392 -633 370 -533 C
ATOM 357 CG GLN B 18 -0.887 42.493 7.832 1.00 14.01 C
ANISOU 357 CG GLN B 18 1493 2038 1793 -649 376 -500 C
ATOM 358 CD GLN B 18 -0.554 43.423 6.722 1.00 25.13 C
ANISOU 358 CD GLN B 18 2990 3392 3167 -763 431 -468 C
ATOM 359 OE1 GLN B 18 -1.366 43.645 5.824 1.00 25.27 O
ANISOU 359 OE1 GLN B 18 3125 3288 3190 -691 429 -422 O
ATOM 360 NE2 GLN B 18 0.635 44.006 6.776 1.00 25.91 N
ANISOU 360 NE2 GLN B 18 3079 3565 3199 -879 445 -470 N
ATOM 361 N LEU B 19 -4.337 43.275 10.697 1.00 10.21 N
ANISOU 361 N LEU B 19 1166 1336 1377 -480 371 -639 N
ATOM 362 CA LEU B 19 -5.037 44.076 11.697 1.00 11.74 C
ANISOU 362 CA LEU B 19 1416 1489 1555 -460 389 -731 C
ATOM 363 C LEU B 19 -5.340 43.236 12.940 1.00 13.59 C
ANISOU 363 C LEU B 19 1578 1849 1739 -475 417 -754 C
ATOM 364 O LEU B 19 -5.301 43.753 14.053 1.00 11.93 O
ANISOU 364 O LEU B 19 1404 1659 1468 -512 433 -826 O
ATOM 365 CB LEU B 19 -6.309 44.704 11.110 1.00 14.68 C
ANISOU 365 CB LEU B 19 1839 1763 1977 -318 381 -784 C
ATOM 366 CG LEU B 19 -7.479 43.853 10.613 1.00 14.91 C
ANISOU 366 CG LEU B 19 1756 1859 2052 -206 385 -789 C
ATOM 367 CD1 LEU B 19 -8.432 43.543 11.752 1.00 14.93 C
ANISOU 367 CD1 LEU B 19 1658 1982 2032 -191 431 -858 C
ATOM 368 CD2 LEU B 19 -8.222 44.554 9.481 1.00 19.60 C
ANISOU 368 CD2 LEU B 19 2417 2338 2690 -58 326 -814 C
ATOM 369 N ALA B 20 -5.614 41.945 12.756 1.00 12.47 N
ANISOU 369 N ALA B 20 1362 1776 1601 -461 418 -691 N
ATOM 370 CA ALA B 20 -5.807 41.042 13.888 1.00 12.03 C
ANISOU 370 CA ALA B 20 1292 1812 1466 -512 439 -680 C
ATOM 371 C ALA B 20 -4.487 40.835 14.632 1.00 13.41 C
ANISOU 371 C ALA B 20 1502 2032 1562 -573 382 -652 C
ATOM 372 O ALA B 20 -4.465 40.752 15.861 1.00 13.65 O
ANISOU 372 O ALA B 20 1577 2120 1491 -620 390 -675 O
ATOM 373 CB ALA B 20 -6.369 39.705 13.422 1.00 11.40 C
ANISOU 373 CB ALA B 20 1177 1750 1406 -506 436 -611 C
ATOM 374 N LEU B 21 -3.391 40.790 13.885 1.00 11.41 N
ANISOU 374 N LEU B 21 1219 1776 1342 -567 322 -619 N
ATOM 375 CA LEU B 21 -2.075 40.625 14.484 1.00 11.87 C
ANISOU 375 CA LEU B 21 1259 1917 1334 -603 248 -625 C
ATOM 376 C LEU B 21 -1.742 41.836 15.354 1.00 14.45 C
ANISOU 376 C LEU B 21 1623 2252 1617 -689 258 -713 C
ATOM 377 O LEU B 21 -1.159 41.694 16.429 1.00 14.81 O
ANISOU 377 O LEU B 21 1682 2376 1568 -718 203 -742 O
ATOM 378 CB LEU B 21 -1.011 40.450 13.400 1.00 13.95 C
ANISOU 378 CB LEU B 21 1432 2225 1642 -586 205 -609 C
ATOM 379 CG LEU B 21 0.354 39.960 13.888 1.00 24.40 C
ANISOU 379 CG LEU B 21 2680 3689 2904 -574 105 -637 C
ATOM 380 CD1 LEU B 21 0.187 38.899 14.966 1.00 32.43 C
ANISOU 380 CD1 LEU B 21 3779 4713 3828 -504 25 -601 C
ATOM 381 CD2 LEU B 21 1.177 39.424 12.727 1.00 30.88 C
ANISOU 381 CD2 LEU B 21 3380 4591 3761 -510 75 -635 C
ATOM 382 N GLN B 22 -2.112 43.026 14.885 1.00 13.33 N
ANISOU 382 N GLN B 22 1522 2010 1533 -709 309 -749 N
ATOM 383 CA GLN B 22 -1.842 44.258 15.629 1.00 14.23 C
ANISOU 383 CA GLN B 22 1706 2083 1617 -760 308 -807 C
ATOM 384 C GLN B 22 -2.640 44.304 16.925 1.00 14.11 C
ANISOU 384 C GLN B 22 1741 2092 1527 -734 332 -868 C
ATOM 385 O GLN B 22 -2.141 44.770 17.952 1.00 15.32 O
ANISOU 385 O GLN B 22 1931 2278 1613 -775 300 -912 O
ATOM 386 CB GLN B 22 -2.156 45.490 14.776 1.00 15.42 C
ANISOU 386 CB GLN B 22 1948 2077 1834 -763 331 -816 C
ATOM 387 CG GLN B 22 -1.038 45.867 13.808 1.00 22.49 C
ANISOU 387 CG GLN B 22 2833 2963 2748 -854 317 -761 C
ATOM 388 CD GLN B 22 0.205 46.347 14.538 1.00 28.62 C
ANISOU 388 CD GLN B 22 3587 3814 3474 -965 280 -789 C
ATOM 389 OE1 GLN B 22 0.236 47.456 15.071 1.00 37.10 O
ANISOU 389 OE1 GLN B 22 4769 4793 4533 -1025 265 -838 O
ATOM 390 NE2 GLN B 22 1.224 45.503 14.584 1.00 36.40 N
ANISOU 390 NE2 GLN B 22 4431 4968 4431 -976 250 -775 N
ATOM 391 N ALA B 23 -3.881 43.833 16.874 1.00 13.08 N
ANISOU 391 N ALA B 23 1602 1965 1404 -667 395 -874 N
ATOM 392 CA ALA B 23 -4.700 43.719 18.075 1.00 15.11 C
ANISOU 392 CA ALA B 23 1879 2290 1573 -653 445 -917 C
ATOM 393 C ALA B 23 -4.041 42.769 19.076 1.00 15.63 C
ANISOU 393 C ALA B 23 1972 2465 1503 -718 406 -875 C
ATOM 394 O ALA B 23 -3.982 43.054 20.268 1.00 16.75 O
ANISOU 394 O ALA B 23 2168 2654 1543 -739 403 -912 O
ATOM 395 CB ALA B 23 -6.094 43.232 17.723 1.00 16.34 C
ANISOU 395 CB ALA B 23 1972 2470 1766 -593 520 -914 C
ATOM 396 N ALA B 24 -3.541 41.640 18.578 1.00 16.92 N
ANISOU 396 N ALA B 24 2117 2657 1655 -730 357 -797 N
ATOM 397 CA ALA B 24 -2.900 40.646 19.435 1.00 19.53 C
ANISOU 397 CA ALA B 24 2512 3058 1851 -747 275 -733 C
ATOM 398 C ALA B 24 -1.620 41.188 20.059 1.00 16.45 C
ANISOU 398 C ALA B 24 2120 2722 1410 -761 167 -788 C
ATOM 399 O ALA B 24 -1.341 40.942 21.233 1.00 17.36 O
ANISOU 399 O ALA B 24 2318 2895 1383 -767 112 -786 O
ATOM 400 CB ALA B 24 -2.603 39.378 18.651 1.00 18.36 C
ANISOU 400 CB ALA B 24 2351 2880 1746 -691 207 -616 C
ATOM 401 N ARG B 25 -0.835 41.924 19.277 1.00 15.27 N
ANISOU 401 N ARG B 25 1875 2547 1378 -767 136 -819 N
ATOM 402 CA ARG B 25 0.402 42.490 19.805 1.00 16.18 C
ANISOU 402 CA ARG B 25 1953 2722 1472 -795 45 -865 C
ATOM 403 C ARG B 25 0.100 43.498 20.912 1.00 17.68 C
ANISOU 403 C ARG B 25 2231 2883 1602 -833 71 -937 C
ATOM 404 O ARG B 25 0.792 43.527 21.933 1.00 19.53 O
ANISOU 404 O ARG B 25 2491 3189 1739 -840 -17 -973 O
ATOM 405 CB ARG B 25 1.214 43.137 18.693 1.00 15.98 C
ANISOU 405 CB ARG B 25 1820 2682 1571 -834 49 -871 C
ATOM 406 CG ARG B 25 1.750 42.112 17.710 1.00 18.11 C
ANISOU 406 CG ARG B 25 1979 3021 1882 -774 6 -821 C
ATOM 407 CD ARG B 25 2.612 42.751 16.654 1.00 17.67 C
ANISOU 407 CD ARG B 25 1821 2983 1910 -825 38 -825 C
ATOM 408 NE ARG B 25 3.887 43.212 17.194 1.00 28.42 N
ANISOU 408 NE ARG B 25 3102 4457 3239 -882 -24 -887 N
ATOM 409 CZ ARG B 25 4.638 44.157 16.638 1.00 37.77 C
ANISOU 409 CZ ARG B 25 4242 5652 4458 -995 22 -910 C
ATOM 410 NH1 ARG B 25 4.238 44.761 15.526 1.00 38.98 N1+
ANISOU 410 NH1 ARG B 25 4454 5693 4665 -1052 118 -862 N1+
ATOM 411 NH2 ARG B 25 5.785 44.506 17.200 1.00 39.84 N
ANISOU 411 NH2 ARG B 25 4414 6036 4687 -1059 -36 -982 N
ATOM 412 N GLN B 26 -0.937 44.307 20.720 1.00 18.20 N
ANISOU 412 N GLN B 26 2346 2848 1722 -831 175 -970 N
ATOM 413 CA GLN B 26 -1.371 45.245 21.758 1.00 18.44 C
ANISOU 413 CA GLN B 26 2465 2849 1691 -831 196 -1056 C
ATOM 414 C GLN B 26 -1.828 44.503 23.017 1.00 19.23 C
ANISOU 414 C GLN B 26 2628 3052 1629 -810 209 -1050 C
ATOM 415 O GLN B 26 -1.496 44.899 24.139 1.00 22.60 O
ANISOU 415 O GLN B 26 3120 3517 1950 -820 162 -1109 O
ATOM 416 CB GLN B 26 -2.495 46.141 21.229 1.00 19.51 C
ANISOU 416 CB GLN B 26 2637 2864 1912 -777 282 -1104 C
ATOM 417 CG GLN B 26 -3.036 47.147 22.239 1.00 19.92 C
ANISOU 417 CG GLN B 26 2783 2883 1902 -735 294 -1217 C
ATOM 418 CD GLN B 26 -1.970 48.104 22.732 1.00 24.16 C
ANISOU 418 CD GLN B 26 3390 3370 2421 -804 198 -1280 C
ATOM 419 OE1 GLN B 26 -1.061 48.473 21.989 1.00 24.45 O
ANISOU 419 OE1 GLN B 26 3409 3345 2537 -886 146 -1251 O
ATOM 420 NE2 GLN B 26 -2.074 48.508 23.993 1.00 26.79 N
ANISOU 420 NE2 GLN B 26 3799 3740 2641 -784 178 -1369 N
ATOM 421 N ALA B 27 -2.585 43.426 22.824 1.00 18.26 N
ANISOU 421 N ALA B 27 2501 2965 1473 -795 271 -973 N
ATOM 422 CA ALA B 27 -3.087 42.620 23.930 1.00 22.99 C
ANISOU 422 CA ALA B 27 3189 3649 1899 -811 302 -933 C
ATOM 423 C ALA B 27 -1.937 42.057 24.766 1.00 25.42 C
ANISOU 423 C ALA B 27 3579 4016 2062 -812 156 -899 C
ATOM 424 O ALA B 27 -2.045 41.943 25.989 1.00 30.79 O
ANISOU 424 O ALA B 27 4370 4753 2577 -819 149 -903 O
ATOM 425 CB ALA B 27 -3.971 41.489 23.400 1.00 18.61 C
ANISOU 425 CB ALA B 27 2626 3099 1344 -833 384 -836 C
ATOM 426 N LEU B 28 -0.839 41.688 24.132 1.00 20.75 N
ANISOU 426 N LEU B 28 2931 3429 1526 -787 29 -872 N
ATOM 427 CA LEU B 28 0.304 41.126 24.851 1.00 26.43 C
ANISOU 427 CA LEU B 28 3704 4219 2121 -741 -149 -858 C
ATOM 428 C LEU B 28 1.097 42.175 25.642 1.00 34.20 C
ANISOU 428 C LEU B 28 4669 5240 3087 -753 -226 -970 C
ATOM 429 O LEU B 28 1.691 41.876 26.632 1.00 34.40 O
ANISOU 429 O LEU B 28 4779 5327 2966 -712 -350 -979 O
ATOM 430 CB LEU B 28 1.270 40.401 23.902 1.00 33.77 C
ANISOU 430 CB LEU B 28 4533 5173 3126 -676 -277 -823 C
ATOM 431 CG LEU B 28 1.030 38.942 23.517 1.00 32.69 C
ANISOU 431 CG LEU B 28 4486 5015 2920 -615 -326 -707 C
ATOM 432 CD1 LEU B 28 -0.293 38.772 22.848 1.00 39.48 C
ANISOU 432 CD1 LEU B 28 5367 5795 3837 -690 -147 -652 C
ATOM 433 CD2 LEU B 28 2.095 38.410 22.625 1.00 35.74 C
ANISOU 433 CD2 LEU B 28 4739 5448 3392 -507 -470 -715 C
ATOM 434 N LYS B 29 1.088 43.398 25.174 1.00 30.01 N
ANISOU 434 N LYS B 29 4053 4653 2696 -809 -161 -1050 N
ATOM 435 CA LYS B 29 1.800 44.459 25.836 1.00 36.29 C
ANISOU 435 CA LYS B 29 4848 5457 3482 -849 -229 -1157 C
ATOM 436 C LYS B 29 1.247 44.766 27.190 1.00 34.93 C
ANISOU 436 C LYS B 29 4821 5300 3149 -834 -211 -1211 C
ATOM 437 O LYS B 29 1.977 45.156 28.073 1.00 32.04 O
ANISOU 437 O LYS B 29 4495 4979 2701 -838 -322 -1284 O
ATOM 438 CB LYS B 29 1.767 45.722 25.018 1.00 40.40 C
ANISOU 438 CB LYS B 29 5311 5871 4167 -922 -160 -1214 C
ATOM 439 CG LYS B 29 2.704 45.699 23.845 1.00 45.68 C
ANISOU 439 CG LYS B 29 5833 6553 4971 -969 -192 -1184 C
ATOM 440 CD LYS B 29 2.842 47.046 23.182 1.00 50.78 C
ANISOU 440 CD LYS B 29 6480 7079 5736 -1070 -143 -1229 C
ATOM 441 CE LYS B 29 3.770 47.001 21.968 1.00 55.93 C
ANISOU 441 CE LYS B 29 6989 7767 6496 -1139 -142 -1187 C
ATOM 442 NZ LYS B 29 4.054 45.706 21.237 1.00 57.63 N1+
ANISOU 442 NZ LYS B 29 7074 8093 6731 -1062 -153 -1110 N1+
ATOM 443 N ALA B 30 -0.041 44.591 27.356 1.00 35.84 N
ANISOU 443 N ALA B 30 5004 5396 3217 -816 -70 -1183 N
ATOM 444 CA ALA B 30 -0.712 44.919 28.613 1.00 43.04 C
ANISOU 444 CA ALA B 30 6037 6346 3972 -800 -16 -1242 C
ATOM 445 C ALA B 30 -0.075 44.192 29.794 1.00 46.52 C
ANISOU 445 C ALA B 30 6597 6882 4197 -774 -140 -1212 C
ATOM 446 O ALA B 30 -0.766 43.563 30.595 1.00 49.98 O
ANISOU 446 O ALA B 30 7152 7377 4461 -766 -75 -1158 O
ATOM 447 CB ALA B 30 -2.193 44.580 28.524 1.00 43.81 C
ANISOU 447 CB ALA B 30 6141 6453 4051 -793 165 -1203 C
TER 448 ALA B 30
HETATM 449 C1 60C A 101 12.139 29.216 18.950 1.00 21.87 C
HETATM 450 C2 60C A 101 12.480 28.432 17.850 1.00 26.08 C
HETATM 451 C3 60C A 101 11.388 28.423 16.963 1.00 28.50 C
HETATM 452 C4 60C A 101 10.511 31.012 19.088 1.00 29.83 C
HETATM 453 C5 60C A 101 11.469 31.828 19.678 1.00 29.30 C
HETATM 454 C6 60C A 101 12.756 31.354 19.915 1.00 25.41 C
HETATM 455 C7 60C A 101 13.113 30.048 19.556 1.00 21.38 C
HETATM 456 C8 60C A 101 13.806 28.476 17.330 1.00 25.87 C
HETATM 457 C9 60C A 101 14.760 29.299 17.956 1.00 28.13 C
HETATM 458 C10 60C A 101 14.437 30.079 19.039 1.00 26.98 C
HETATM 459 C11 60C A 101 11.610 28.426 15.503 1.00 29.42 C
HETATM 460 C12 60C A 101 12.921 28.456 15.003 1.00 28.66 C
HETATM 461 C13 60C A 101 9.703 31.823 18.249 1.00 30.27 C
HETATM 462 C14 60C A 101 9.760 30.050 15.192 1.00 27.28 C
HETATM 463 C15 60C A 101 10.780 29.257 14.659 1.00 24.48 C
HETATM 464 C16 60C A 101 11.244 33.154 19.215 1.00 29.44 C
HETATM 465 C17 60C A 101 10.149 33.109 18.336 1.00 30.79 C
HETATM 466 C18 60C A 101 14.898 31.385 19.098 1.00 25.22 C
HETATM 467 C19 60C A 101 13.878 32.194 19.646 1.00 26.72 C
HETATM 468 C20 60C A 101 9.586 31.311 14.765 1.00 26.16 C
HETATM 469 C21 60C A 101 9.228 32.136 15.882 1.00 30.24 C
HETATM 470 C22 60C A 101 12.929 29.267 13.877 1.00 28.75 C
HETATM 471 C23 60C A 101 11.589 29.778 13.685 1.00 24.06 C
HETATM 472 C24 60C A 101 13.680 33.514 19.175 1.00 27.19 C
HETATM 473 C25 60C A 101 12.396 34.012 18.970 1.00 29.95 C
HETATM 474 C26 60C A 101 9.665 33.450 15.963 1.00 28.52 C
HETATM 475 C27 60C A 101 10.130 33.955 17.183 1.00 24.80 C
HETATM 476 C28 60C A 101 11.384 31.053 13.223 1.00 24.95 C
HETATM 477 C29 60C A 101 10.388 31.829 13.745 1.00 20.40 C
HETATM 478 C30 60C A 101 15.121 30.096 14.511 1.00 29.22 C
HETATM 479 C31 60C A 101 14.036 30.097 13.622 1.00 30.00 C
HETATM 480 C32 60C A 101 16.079 31.115 16.999 1.00 32.51 C
HETATM 481 C33 60C A 101 15.737 31.902 18.063 1.00 22.98 C
HETATM 482 C34 60C A 101 12.410 34.829 17.796 1.00 28.77 C
HETATM 483 C35 60C A 101 11.278 34.805 16.914 1.00 24.37 C
HETATM 484 C36 60C A 101 16.090 31.971 15.789 1.00 32.14 C
HETATM 485 C37 60C A 101 15.618 31.468 14.595 1.00 31.83 C
HETATM 486 C38 60C A 101 13.826 31.414 13.196 1.00 28.31 C
HETATM 487 C39 60C A 101 12.529 31.917 12.967 1.00 25.05 C
HETATM 488 C40 60C A 101 10.871 33.195 13.831 1.00 18.95 C
HETATM 489 C41 60C A 101 10.522 33.994 14.895 1.00 21.45 C
HETATM 490 C42 60C A 101 12.193 33.217 13.324 1.00 22.71 C
HETATM 491 C43 60C A 101 14.821 32.256 13.788 1.00 28.58 C
HETATM 492 C44 60C A 101 9.213 31.309 17.027 1.00 31.70 C
HETATM 493 C45 60C A 101 9.549 30.053 16.649 1.00 30.17 C
HETATM 494 C46 60C A 101 10.379 29.229 17.503 1.00 29.38 C
HETATM 495 C47 60C A 101 10.824 29.714 18.725 1.00 28.89 C
HETATM 496 C48 60C A 101 14.021 28.492 15.884 1.00 25.47 C
HETATM 497 C49 60C A 101 15.105 29.288 15.657 1.00 32.51 C
HETATM 498 C50 60C A 101 15.594 29.816 16.921 1.00 33.46 C
HETATM 499 C51 60C A 101 11.500 34.807 15.495 1.00 24.11 C
HETATM 500 C52 60C A 101 13.158 34.029 13.915 1.00 23.94 C
HETATM 501 C53 60C A 101 12.820 34.814 14.994 1.00 25.40 C
HETATM 502 C54 60C A 101 13.721 34.821 17.291 1.00 31.53 C
HETATM 503 C55 60C A 101 14.537 34.033 18.122 1.00 28.47 C
HETATM 504 C56 60C A 101 13.943 34.827 15.898 1.00 30.73 C
HETATM 505 C57 60C A 101 15.522 33.239 17.580 1.00 26.33 C
HETATM 506 C58 60C A 101 15.745 33.237 16.164 1.00 30.76 C
HETATM 507 C59 60C A 101 14.502 33.517 14.145 1.00 28.09 C
HETATM 508 C60 60C A 101 14.965 34.023 15.350 1.00 29.32 C
HETATM 509 O HOH A 201 1.335 42.666 9.248 1.00 40.08 O
HETATM 510 O HOH A 202 14.300 32.016 23.920 1.00 31.17 O
HETATM 511 O HOH A 203 11.955 39.517 13.514 1.00 32.58 O
HETATM 512 O HOH A 204 4.753 45.831 2.990 1.00 23.47 O
HETATM 513 O HOH A 205 0.219 50.692 -14.001 1.00 34.52 O
HETATM 514 O HOH A 206 -3.601 43.028 -11.117 1.00 32.40 O
HETATM 515 O HOH A 207 11.192 39.171 16.174 1.00 26.46 O
HETATM 516 O HOH A 208 8.989 43.550 7.033 1.00 30.67 O
HETATM 517 O HOH A 209 10.560 39.975 22.774 1.00 32.57 O
HETATM 518 O HOH A 210 4.463 43.235 -16.191 1.00 36.31 O
HETATM 519 O HOH A 211 -0.958 47.446 -9.499 1.00 34.07 O
HETATM 520 O HOH A 212 11.953 39.378 8.873 1.00 35.77 O
HETATM 521 O HOH A 213 6.013 34.585 25.513 1.00 27.63 O
HETATM 522 O HOH A 214 10.842 37.470 7.764 1.00 35.58 O
HETATM 523 O HOH B 101 -14.287 31.719 -13.254 1.00 28.26 O
HETATM 524 O HOH B 102 3.617 43.119 21.641 1.00 32.59 O
HETATM 525 O HOH B 103 -12.111 39.370 -2.848 1.00 31.54 O
HETATM 526 O HOH B 104 -1.783 49.149 14.708 1.00 30.00 O
HETATM 527 O HOH B 105 -0.229 46.717 18.154 1.00 26.22 O
HETATM 528 O HOH B 106 -4.901 45.940 7.438 1.00 26.71 O
HETATM 529 O HOH B 107 4.914 41.826 19.413 1.00 25.12 O
HETATM 530 O HOH B 108 -10.463 39.907 -12.161 1.00 33.49 O
HETATM 531 O HOH B 109 -11.185 39.227 -5.728 1.00 24.17 O
HETATM 532 O HOH B 110 -6.242 37.721 -14.166 1.00 31.37 O
HETATM 533 O HOH B 111 0.873 47.557 20.033 1.00 34.06 O
HETATM 534 O HOH B 112 -6.295 34.359 -14.864 1.00 26.35 O
HETATM 535 O HOH B 113 -4.864 41.741 -8.889 1.00 24.56 O
HETATM 536 O HOH B 114 -12.066 39.509 1.561 1.00 30.11 O
HETATM 537 O HOH B 115 -10.496 38.086 2.116 1.00 26.07 O
CONECT 449 450 455 495
CONECT 450 449 451 456
CONECT 451 450 459 494
CONECT 452 453 461 495
CONECT 453 452 454 464
CONECT 454 453 455 467
CONECT 455 449 454 458
CONECT 456 450 457 496
CONECT 457 456 458 498
CONECT 458 455 457 466
CONECT 459 451 460 463
CONECT 460 459 470 496
CONECT 461 452 465 492
CONECT 462 463 468 493
CONECT 463 459 462 471
CONECT 464 453 465 473
CONECT 465 461 464 475
CONECT 466 458 467 481
CONECT 467 454 466 472
CONECT 468 462 469 477
CONECT 469 468 474 492
CONECT 470 460 471 479
CONECT 471 463 470 476
CONECT 472 467 473 503
CONECT 473 464 472 482
CONECT 474 469 475 489
CONECT 475 465 474 483
CONECT 476 471 477 487
CONECT 477 468 476 488
CONECT 478 479 485 497
CONECT 479 470 478 486
CONECT 480 481 484 498
CONECT 481 466 480 505
CONECT 482 473 483 502
CONECT 483 475 482 499
CONECT 484 480 485 506
CONECT 485 478 484 491
CONECT 486 479 487 491
CONECT 487 476 486 490
CONECT 488 477 489 490
CONECT 489 474 488 499
CONECT 490 487 488 500
CONECT 491 485 486 507
CONECT 492 461 469 493
CONECT 493 462 492 494
CONECT 494 451 493 495
CONECT 495 449 452 494
CONECT 496 456 460 497
CONECT 497 478 496 498
CONECT 498 457 480 497
CONECT 499 483 489 501
CONECT 500 490 501 507
CONECT 501 499 500 504
CONECT 502 482 503 504
CONECT 503 472 502 505
CONECT 504 501 502 508
CONECT 505 481 503 506
CONECT 506 484 505 508
CONECT 507 491 500 508
CONECT 508 504 506 507
MASTER 255 0 1 2 0 0 2 6 535 2 60 6
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