Browse entries in the PDBbind-CN Database
HEADER STRUCTURAL PROTEIN/CONTRACTILE PROTEIN 01-OCT-08 2V52 TITLE STRUCTURE OF MAL-RPEL2 COMPLEXED TO G-ACTIN CAVEAT 2V52 THR B 194 HAS WRONG CHIRALITY AT ATOM CB COMPND MOL_ID: 1; COMPND 2 MOLECULE: ACTIN, ALPHA SKELETAL MUSCLE; COMPND 3 CHAIN: B; COMPND 4 SYNONYM: ACTIN, ALPHA SKELETAL MUSCLE, ALPHA-ACTIN-1; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MKL/MYOCARDIN-LIKE PROTEIN 1; COMPND 7 CHAIN: M; COMPND 8 FRAGMENT: RPEL2; COMPND 9 SYNONYM: MRTF-A, MAL, MEGAKARYOBLASTIC LEUKEMIA 1 PROTEIN HOMOLOG, COMPND 10 BASIC SAP COILED-COIL TRANSCRIPTION ACTIVATOR; COMPND 11 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 3 ORGANISM_COMMON: RABBIT; SOURCE 4 ORGANISM_TAXID: 9986; SOURCE 5 MOL_ID: 2; SOURCE 6 SYNTHETIC: YES; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_COMMON: MOUSE; SOURCE 9 ORGANISM_TAXID: 10090 KEYWDS STRUCTURAL PROTEIN/CONTRACTILE PROTEIN, STRUCTURAL PROTEIN, KEYWDS 2 CONTRACTILE PROTEIN, NUCLEOTIDE-BINDING, ALTERNATIVE SPLICING, KEYWDS 3 TRANSCRIPTION REGULATION, TRANSCRIPTION, PHOSPHOPROTEIN, MUSCLE KEYWDS 4 PROTEIN, METHYLATION, ATP-BINDING, COILED COIL, CYTOSKELETON, MAL, KEYWDS 5 RPEL, ACTIN, NUCLEUS, CYTOPLASM, ACETYLATION, STRUCTURAL PROTEIN- KEYWDS 6 CONTRACTILE PROTEIN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR S.MOUILLERON,S.GUETTLER,C.A.LANGER,R.TREISMAN,N.Q.MCDONALD REVDAT 4 28-FEB-18 2V52 1 JRNL ATOM REVDAT 3 12-JUL-17 2V52 1 REVDAT 2 24-FEB-09 2V52 1 VERSN REVDAT 1 25-NOV-08 2V52 0 JRNL AUTH S.MOUILLERON,S.GUETTLER,C.A.LANGER,R.TREISMAN,N.Q.MCDONALD JRNL TITL MOLECULAR BASIS FOR G-ACTIN BINDING TO RPEL MOTIFS FROM THE JRNL TITL 2 SERUM RESPONSE FACTOR COACTIVATOR MAL. JRNL REF EMBO J. V. 27 3198 2008 JRNL REFN ESSN 1460-2075 JRNL PMID 19008859 JRNL DOI 10.1038/EMBOJ.2008.235 REMARK 2 REMARK 2 RESOLUTION. 1.45 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) 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) : 1.45 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.35 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 74958 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.149 REMARK 3 R VALUE (WORKING SET) : 0.147 REMARK 3 FREE R VALUE : 0.188 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3769 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 29.3579 - 4.3455 0.99 2848 170 0.1858 0.2291 REMARK 3 2 4.3455 - 3.4509 1.00 2749 139 0.1331 0.1845 REMARK 3 3 3.4509 - 3.0152 0.99 2681 156 0.1409 0.1598 REMARK 3 4 3.0152 - 2.7397 1.00 2673 145 0.1445 0.1638 REMARK 3 5 2.7397 - 2.5435 1.00 2663 157 0.1358 0.1703 REMARK 3 6 2.5435 - 2.3936 1.00 2709 110 0.1329 0.1343 REMARK 3 7 2.3936 - 2.2737 1.00 2649 142 0.1233 0.1795 REMARK 3 8 2.2737 - 2.1748 1.00 2652 130 0.1194 0.1784 REMARK 3 9 2.1748 - 2.0911 1.00 2656 140 0.1158 0.1531 REMARK 3 10 2.0911 - 2.0190 1.00 2652 140 0.1108 0.1495 REMARK 3 11 2.0190 - 1.9558 1.00 2638 139 0.1104 0.1549 REMARK 3 12 1.9558 - 1.9000 1.00 2671 120 0.1063 0.1478 REMARK 3 13 1.9000 - 1.8499 1.00 2630 131 0.1093 0.1522 REMARK 3 14 1.8499 - 1.8048 1.00 2671 126 0.1102 0.1711 REMARK 3 15 1.8048 - 1.7638 1.00 2604 162 0.1142 0.1676 REMARK 3 16 1.7638 - 1.7263 1.00 2618 162 0.1184 0.1627 REMARK 3 17 1.7263 - 1.6917 1.00 2614 141 0.1199 0.1892 REMARK 3 18 1.6917 - 1.6598 1.00 2621 141 0.1309 0.1762 REMARK 3 19 1.6598 - 1.6302 1.00 2638 135 0.1422 0.2006 REMARK 3 20 1.6302 - 1.6025 1.00 2643 133 0.1483 0.2134 REMARK 3 21 1.6025 - 1.5767 1.00 2642 141 0.1530 0.2186 REMARK 3 22 1.5767 - 1.5524 1.00 2614 137 0.1684 0.2166 REMARK 3 23 1.5524 - 1.5296 1.00 2612 135 0.1799 0.2358 REMARK 3 24 1.5296 - 1.5081 1.00 2623 141 0.1922 0.2385 REMARK 3 25 1.5081 - 1.4877 0.97 2528 141 0.2059 0.2428 REMARK 3 26 1.4877 - 1.4684 0.95 2483 121 0.2244 0.2687 REMARK 3 27 1.4684 - 1.4500 0.92 2407 134 0.2259 0.2512 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 : 0.39 REMARK 3 B_SOL : 63.74 REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.830 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 17.81 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.78 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.75110 REMARK 3 B22 (A**2) : 2.64270 REMARK 3 B33 (A**2) : -6.39370 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 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 : 0.060 3483 REMARK 3 ANGLE : 2.840 4772 REMARK 3 CHIRALITY : 0.200 529 REMARK 3 PLANARITY : 0.020 609 REMARK 3 DIHEDRAL : 18.780 1362 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 2V52 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-OCT-08. REMARK 100 THE DEPOSITION ID IS D_1290037691. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-OCT-07 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I03 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.933 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74958 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.200 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 5.200 REMARK 200 R MERGE (I) : 0.07000 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53 REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0 REMARK 200 DATA REDUNDANCY IN SHELL : 2.90 REMARK 200 R MERGE FOR SHELL (I) : 0.55000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200 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: NULL REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 38.22 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z 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 -1.000000 0.000000 0.000000 27.37500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.19500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.72000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.19500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.37500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.72000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PQS REMARK 350 TOTAL BURIED SURFACE AREA: 2460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20010 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.8 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, M 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET B -1 REMARK 465 CYS B 0 REMARK 465 ASP B 1 REMARK 465 GLU B 2 REMARK 465 HIS B 40 REMARK 465 GLN B 41 REMARK 465 GLY B 42 REMARK 465 VAL B 43 REMARK 465 MET B 44 REMARK 465 VAL B 45 REMARK 465 GLY B 46 REMARK 465 MET B 47 REMARK 465 GLY B 48 REMARK 465 GLN B 49 REMARK 465 LYS B 61 REMARK 465 ARG B 62 REMARK 465 GLY B 63 REMARK 465 SER M 141 REMARK 465 ALA M 142 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG B 39 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 50 CG CD CE NZ REMARK 470 SER B 60 OG REMARK 470 ILE B 64 CG1 CG2 CD1 REMARK 470 SER B 235 OG REMARK 470 ARG M 113 CG CD NE CZ NH1 NH2 REMARK 470 GLU M 127 CG CD OE1 OE2 REMARK 470 GLU M 139 CG CD OE1 OE2 REMARK 470 THR M 140 OG1 CG2 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 NH2 ARG M 123 O HOH M 201 1.79 REMARK 500 O HOH B 539 O HOH B 614 1.97 REMARK 500 O HOH B 728 O HOH B 744 2.04 REMARK 500 OD2 ASP B 56 O HOH B 501 2.05 REMARK 500 O HOH B 796 O HOH B 831 2.08 REMARK 500 OE2 GLU B 276 O HOH B 502 2.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH B 765 O HOH B 766 3445 2.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU B 4 CD GLU B 4 OE1 -0.095 REMARK 500 GLU B 4 CD GLU B 4 OE2 -0.072 REMARK 500 GLU B 4 C GLU B 4 O -0.122 REMARK 500 TYR B 53 CE1 TYR B 53 CZ -0.088 REMARK 500 GLU B 57 CD GLU B 57 OE2 -0.068 REMARK 500 HIS B 87 C HIS B 87 O -0.116 REMARK 500 GLU B 99 CB GLU B 99 CG -0.208 REMARK 500 GLU B 99 CG GLU B 99 CD 0.122 REMARK 500 GLU B 99 CD GLU B 99 OE1 -0.114 REMARK 500 GLU B 99 CD GLU B 99 OE2 -0.109 REMARK 500 GLU B 100 CD GLU B 100 OE1 -0.068 REMARK 500 GLU B 100 CD GLU B 100 OE2 -0.102 REMARK 500 GLU B 100 C GLU B 100 O -0.131 REMARK 500 ARG B 147 C ARG B 147 O -0.119 REMARK 500 THR B 148 C THR B 148 O -0.164 REMARK 500 THR B 149 C THR B 149 O -0.188 REMARK 500 LEU B 178 CB LEU B 178 CG -0.223 REMARK 500 LEU B 178 CG LEU B 178 CD2 -0.317 REMARK 500 ILE B 192 C ILE B 192 O -0.146 REMARK 500 GLU B 195 CD GLU B 195 OE1 -0.145 REMARK 500 GLU B 195 CD GLU B 195 OE2 -0.068 REMARK 500 ARG B 196 CD ARG B 196 NE -0.110 REMARK 500 ARG B 196 NE ARG B 196 CZ -0.087 REMARK 500 ARG B 196 CZ ARG B 196 NH1 -0.087 REMARK 500 GLY B 197 N GLY B 197 CA -0.133 REMARK 500 GLY B 197 C GLY B 197 O -0.153 REMARK 500 TYR B 198 CB TYR B 198 CG -0.107 REMARK 500 TYR B 198 CD1 TYR B 198 CE1 -0.258 REMARK 500 TYR B 198 CE2 TYR B 198 CD2 -0.163 REMARK 500 ALA B 230 CA ALA B 230 CB -0.164 REMARK 500 SER B 234 CB SER B 234 OG -0.115 REMARK 500 GLU B 237 CB GLU B 237 CG -0.146 REMARK 500 GLU B 237 CG GLU B 237 CD -0.103 REMARK 500 GLU B 237 CD GLU B 237 OE1 -0.117 REMARK 500 GLU B 237 CD GLU B 237 OE2 -0.068 REMARK 500 ASN B 297 C ASN B 297 O -0.159 REMARK 500 VAL B 370 CB VAL B 370 CG1 -0.132 REMARK 500 HIS B 371 C HIS B 371 O -0.134 REMARK 500 ARG B 372 CB ARG B 372 CG -0.201 REMARK 500 LYS B 373 C LYS B 373 O -0.122 REMARK 500 ALA M 129 C GLU M 130 N -0.145 REMARK 500 GLU M 130 CB GLU M 130 CG -0.243 REMARK 500 GLU M 130 CB GLU M 130 CG -0.115 REMARK 500 GLU M 130 CD GLU M 130 OE1 -0.117 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 GLU B 57 CG - CD - OE1 ANGL. DEV. = 13.3 DEGREES REMARK 500 LEU B 178 CB - CA - C ANGL. DEV. = -14.1 DEGREES REMARK 500 LEU B 178 CB - CG - CD2 ANGL. DEV. = -20.3 DEGREES REMARK 500 ARG B 196 CD - NE - CZ ANGL. DEV. = 9.1 DEGREES REMARK 500 ARG B 196 NE - CZ - NH1 ANGL. DEV. = -8.3 DEGREES REMARK 500 ARG B 196 NE - CZ - NH2 ANGL. DEV. = 4.3 DEGREES REMARK 500 ARG B 372 NE - CZ - NH1 ANGL. DEV. = 7.3 DEGREES REMARK 500 ARG B 372 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 LYS B 373 CD - CE - NZ ANGL. DEV. = 15.0 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ALA B 181 -154.13 -152.99 REMARK 500 ALA B 181 -154.13 -149.31 REMARK 500 VAL B 201 -49.85 -133.95 REMARK 500 ALA B 231 -2.65 -48.60 REMARK 500 SER B 232 -87.15 -130.13 REMARK 500 SER B 233 -157.28 -53.73 REMARK 500 SER B 234 106.04 162.49 REMARK 500 ASN B 296 55.84 -142.09 REMARK 500 ASN B 296 54.06 -142.09 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER B 233 SER B 234 137.75 REMARK 500 SER B 234 SER B 235 126.23 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG B 403 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ATP B 402 O1G REMARK 620 2 ATP B 402 O1B 84.1 REMARK 620 3 HOH B 574 O 88.4 90.5 REMARK 620 4 HOH B 552 O 93.5 177.3 88.1 REMARK 620 5 HOH B 575 O 167.3 88.0 81.8 94.2 REMARK 620 6 HOH B 686 O 105.2 94.4 165.9 87.5 85.2 REMARK 620 N 1 2 3 4 5 REMARK 700 REMARK 700 SHEET REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, REMARK 700 TWO SHEETS ARE DEFINED. REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LAB B1376 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B1377 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B1378 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1379 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1380 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1LCU RELATED DB: PDB REMARK 900 POLYLYSINE INDUCES AN ANTIPARALLEL ACTIN DIMER THATNUCLEATES REMARK 900 FILAMENT ASSEMBLY: CRYSTAL STRUCTURE AT 3.5 ARESOLUTION REMARK 900 RELATED ID: 2A42 RELATED DB: PDB REMARK 900 ACTIN-DNASE I COMPLEX REMARK 900 RELATED ID: 2ASO RELATED DB: PDB REMARK 900 STRUCTURE OF RABBIT ACTIN IN COMPLEX WITH SPHINXOLIDE B REMARK 900 RELATED ID: 1IJJ RELATED DB: PDB REMARK 900 THE X-RAY CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RABBITSKELETAL REMARK 900 MUSCLE ACTIN AND LATRUNCULIN A AT 2.85 ARESOLUTION REMARK 900 RELATED ID: 1WUA RELATED DB: PDB REMARK 900 THE STRUCTURE OF APLYRONINE A-ACTIN COMPLEX REMARK 900 RELATED ID: 1O18 RELATED DB: PDB REMARK 900 MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROMTOMOGRAMS OF REMARK 900 INSECT FLIGHT MUSCLE REMARK 900 RELATED ID: 1M8Q RELATED DB: PDB REMARK 900 MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROMTOMOGRAMS OF REMARK 900 INSECT FLIGHT MUSCLE REMARK 900 RELATED ID: 1O1A RELATED DB: PDB REMARK 900 MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROMTOMOGRAMS OF REMARK 900 INSECT FLIGHT MUSCLE REMARK 900 RELATED ID: 1RFQ RELATED DB: PDB REMARK 900 ACTIN CRYSTAL DYNAMICS: STRUCTURAL IMPLICATIONS FOR F- REMARK 900 ACTINNUCLEATION, POLYMERIZATION AND BRANCHING MEDIATED BY THEANTI- REMARK 900 PARALLEL DIMER REMARK 900 RELATED ID: 1UY5 RELATED DB: PDB REMARK 900 A MODEL OF THYMOSIN_BETA4 BOUND TO MONOMERIC ACTIN USING NMR AND REMARK 900 BIOCHEMICAL DATA. REMARK 900 RELATED ID: 1MA9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN VITAMIN D BINDINGPROTEIN REMARK 900 AND RABBIT MUSCLE ACTIN REMARK 900 RELATED ID: 2D1K RELATED DB: PDB REMARK 900 TERNARY COMPLEX OF THE WH2 DOMAIN OF MIM WITH ACTIN-DNASE I REMARK 900 RELATED ID: 1RDW RELATED DB: PDB REMARK 900 ACTIN CRYSTAL DYNAMICS: STRUCTURAL IMPLICATIONS FOR F- REMARK 900 ACTINNUCLEATION, POLYMERIZATION AND BRANCHING MEDIATED BY THEANTI- REMARK 900 PARALLEL DIMER REMARK 900 RELATED ID: 1O1B RELATED DB: PDB REMARK 900 MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROMTOMOGRAMS OF REMARK 900 INSECT FLIGHT MUSCLE REMARK 900 RELATED ID: 1O1D RELATED DB: PDB REMARK 900 MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROMTOMOGRAMS OF REMARK 900 INSECT FLIGHT MUSCLE REMARK 900 RELATED ID: 2A40 RELATED DB: PDB REMARK 900 TERNARY COMPLEX OF THE WH2 DOMAIN OF WAVE WITH ACTIN-DNASE I REMARK 900 RELATED ID: 2A5X RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF A CROSS-LINKED ACTIN DIMER REMARK 900 RELATED ID: 1QZ5 RELATED DB: PDB REMARK 900 STRUCTURE OF RABBIT ACTIN IN COMPLEX WITH KABIRAMIDE C REMARK 900 RELATED ID: 1NWK RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF MONOMERIC ACTIN IN THE ATP STATE REMARK 900 RELATED ID: 1J6Z RELATED DB: PDB REMARK 900 UNCOMPLEXED ACTIN REMARK 900 RELATED ID: 1SQK RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN REMARK 900 RELATED ID: 1ATN RELATED DB: PDB REMARK 900 DEOXYRIBONUCLEASE I COMPLEX WITH ACTIN REMARK 900 RELATED ID: 1S22 RELATED DB: PDB REMARK 900 ABSOLUTE STEREOCHEMISTRY OF ULAPUALIDE A REMARK 900 RELATED ID: 1T44 RELATED DB: PDB REMARK 900 STRUCTURAL BASIS OF ACTIN SEQUESTRATION BY THYMOSIN-B4:IMPLICATIONS REMARK 900 FOR ARP2/3 ACTIVATION REMARK 900 RELATED ID: 2FF3 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF GELSOLIN DOMAIN 1:N- WASP V2 MOTIFHYBRID IN REMARK 900 COMPLEX WITH ACTIN REMARK 900 RELATED ID: 1EQY RELATED DB: PDB REMARK 900 COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLIN DOMAIN 1 REMARK 900 RELATED ID: 1MVW RELATED DB: PDB REMARK 900 MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROMTOMOGRAMS OF REMARK 900 INSECT FLIGHT MUSCLE REMARK 900 RELATED ID: 2FF6 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF GELSOLIN DOMAIN 1: CIBOULOT DOMAIN 2HYBRID IN REMARK 900 COMPLEX WITH ACTIN REMARK 900 RELATED ID: 2FXU RELATED DB: PDB REMARK 900 X-RAY STRUCTURE OF BISTRAMIDE A- ACTIN COMPLEX AT 1.35 ARESOLUTION. REMARK 900 RELATED ID: 1O1F RELATED DB: PDB REMARK 900 MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROMTOMOGRAMS OF REMARK 900 INSECT FLIGHT MUSCLE REMARK 900 RELATED ID: 1KXP RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN VITAMIN D-BINDING PROTEIN INCOMPLEX WITH REMARK 900 SKELETAL ACTIN REMARK 900 RELATED ID: 2ASP RELATED DB: PDB REMARK 900 STRUCTURE OF RABBIT ACTIN IN COMPLEX WITH REIDISPONGIOLIDE C REMARK 900 RELATED ID: 1RGI RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF GELSOLIN DOMAINS G1-G3 BOUND TO ACTIN REMARK 900 RELATED ID: 1O19 RELATED DB: PDB REMARK 900 MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROMTOMOGRAMS OF REMARK 900 INSECT FLIGHT MUSCLE REMARK 900 RELATED ID: 1Y64 RELATED DB: PDB REMARK 900 BNI1P FORMIN HOMOLOGY 2 DOMAIN COMPLEXED WITH ATP-ACTIN REMARK 900 RELATED ID: 1ALM RELATED DB: PDB REMARK 900 THE STRUCTURE OF THE ACTO-MYOSIN SUBFRAGMENT -ONE COMPLEX. RESULTS REMARK 900 OF SEARCHES USING DATA FROM ELECTRON MICROSCOPY AND X-RAY REMARK 900 CRYSTALLOGRAPHY. THEORETICAL MODEL, ALPHA CARBONS. REMARK 900 RELATED ID: 1O1E RELATED DB: PDB REMARK 900 MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROMTOMOGRAMS OF REMARK 900 INSECT FLIGHT MUSCLE REMARK 900 RELATED ID: 1ESV RELATED DB: PDB REMARK 900 COMPLEX BETWEEN LATRUNCULIN A:RABBIT MUSCLE ALPHA ACTIN:HUMAN REMARK 900 GELSOLIN DOMAIN 1 REMARK 900 RELATED ID: 1P8Z RELATED DB: PDB REMARK 900 COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLINRESIDUES REMARK 900 VAL26-GLU156 REMARK 900 RELATED ID: 1H1V RELATED DB: PDB REMARK 900 GELSOLIN G4-G6/ACTIN COMPLEX REMARK 900 RELATED ID: 1O1C RELATED DB: PDB REMARK 900 MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROMTOMOGRAMS OF REMARK 900 INSECT FLIGHT MUSCLE REMARK 900 RELATED ID: 2VCP RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF N-WASP VC DOMAIN IN COMPLEX WITH SKELETAL ACTIN REMARK 900 RELATED ID: 1O1G RELATED DB: PDB REMARK 900 MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROMTOMOGRAMS OF REMARK 900 INSECT FLIGHT MUSCLE REMARK 900 RELATED ID: 2A3Z RELATED DB: PDB REMARK 900 TERNARY COMPLEX OF THE WH2 DOMAIN OF WASP WITH ACTIN-DNASE I REMARK 900 RELATED ID: 1LOT RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX OF ACTIN WITH VITAMIN D-BINDING REMARK 900 PROTEIN REMARK 900 RELATED ID: 2ASM RELATED DB: PDB REMARK 900 STRUCTURE OF RABBIT ACTIN IN COMPLEX WITH REIDISPONGIOLIDE A REMARK 900 RELATED ID: 2A41 RELATED DB: PDB REMARK 900 TERNARY COMPLEX OF THE WH2 DOMAIN OF WIP WITH ACTIN-DNASE I REMARK 900 RELATED ID: 2VYP RELATED DB: PDB REMARK 900 RABBIT-MUSCLE G-ACTIN IN COMPLEX WITH MYXOBACTERIAL RHIZOPODIN REMARK 900 RELATED ID: 1QZ6 RELATED DB: PDB REMARK 900 STRUCTURE OF RABBIT ACTIN IN COMPLEX WITH JASPISAMIDE A REMARK 900 RELATED ID: 2V51 RELATED DB: PDB REMARK 900 STRUCTURE OF MAL-RPEL1 COMPLEXED TO ACTIN DBREF 2V52 B -1 375 UNP P68135 ACTS_RABIT 1 377 DBREF 2V52 M 111 142 UNP Q8K4J6 MKL1_MOUSE 54 85 SEQRES 1 B 377 MET CYS ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP SEQRES 2 B 377 ASN GLY SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP SEQRES 3 B 377 ASP ALA PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG SEQRES 4 B 377 PRO ARG HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS SEQRES 5 B 377 ASP SER TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY SEQRES 6 B 377 ILE LEU THR LEU LYS TYR PRO ILE GLU HIS GLY ILE ILE SEQRES 7 B 377 THR ASN TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR SEQRES 8 B 377 PHE TYR ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO SEQRES 9 B 377 THR LEU LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN SEQRES 10 B 377 ARG GLU LYS MET THR GLN ILE MET PHE GLU THR PHE ASN SEQRES 11 B 377 VAL PRO ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER SEQRES 12 B 377 LEU TYR ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP SEQRES 13 B 377 SER GLY ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU SEQRES 14 B 377 GLY TYR ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU SEQRES 15 B 377 ALA GLY ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU SEQRES 16 B 377 THR GLU ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG SEQRES 17 B 377 GLU ILE VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL SEQRES 18 B 377 ALA LEU ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER SEQRES 19 B 377 SER SER SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY SEQRES 20 B 377 GLN VAL ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO SEQRES 21 B 377 GLU THR LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER SEQRES 22 B 377 ALA GLY ILE HIS GLU THR THR TYR ASN SER ILE MET LYS SEQRES 23 B 377 CYS ASP ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN SEQRES 24 B 377 VAL MET SER GLY GLY THR THR MET TYR PRO GLY ILE ALA SEQRES 25 B 377 ASP ARG MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER SEQRES 26 B 377 THR MET LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS SEQRES 27 B 377 TYR SER VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU SEQRES 28 B 377 SER THR PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR SEQRES 29 B 377 ASP GLU ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE SEQRES 1 M 32 ARG ALA ARG THR GLU ASP TYR LEU LYS ARG LYS ILE ARG SEQRES 2 M 32 SER ARG PRO GLU ARG ALA GLU LEU VAL ARG MET HIS ILE SEQRES 3 M 32 LEU GLU GLU THR SER ALA HET LAB B 401 27 HET ATP B 402 31 HET MG B 403 1 HET GOL B 404 6 HET GOL B 405 6 HETNAM LAB LATRUNCULIN B HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE HETNAM MG MAGNESIUM ION HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 LAB C20 H29 N O5 S FORMUL 4 ATP C10 H16 N5 O13 P3 FORMUL 5 MG MG 2+ FORMUL 6 GOL 2(C3 H8 O3) FORMUL 8 HOH *359(H2 O) HELIX 1 1 GLY B 55 SER B 60 1 6 HELIX 2 2 ASN B 78 ASN B 92 1 15 HELIX 3 3 ALA B 97 HIS B 101 5 5 HELIX 4 4 PRO B 112 THR B 126 1 15 HELIX 5 5 GLN B 137 SER B 145 1 9 HELIX 6 6 PRO B 172 ILE B 175 5 4 HELIX 7 7 ALA B 181 THR B 194 1 14 HELIX 8 8 GLU B 195 GLY B 197 5 3 HELIX 9 9 THR B 202 CYS B 217 1 16 HELIX 10 10 ASP B 222 ALA B 231 1 10 HELIX 11 11 ASN B 252 GLN B 263 1 12 HELIX 12 12 PRO B 264 GLY B 268 5 5 HELIX 13 13 GLY B 273 LYS B 284 1 12 HELIX 14 14 ASP B 286 ASP B 288 5 3 HELIX 15 15 ILE B 289 ALA B 295 1 7 HELIX 16 16 GLY B 301 MET B 305 5 5 HELIX 17 17 GLY B 308 ALA B 321 1 14 HELIX 18 18 GLU B 334 LYS B 336 5 3 HELIX 19 19 TYR B 337 SER B 348 1 12 HELIX 20 20 LEU B 349 TRP B 356 5 8 HELIX 21 21 LYS B 359 GLY B 366 1 8 HELIX 22 22 SER B 368 CYS B 374 1 7 HELIX 23 23 GLU M 115 SER M 124 1 10 HELIX 24 24 GLU M 127 MET M 134 1 8 SHEET 1 BA 6 ALA B 29 PRO B 32 0 SHEET 2 BA 6 LEU B 16 PHE B 21 -1 O VAL B 17 N PHE B 31 SHEET 3 BA 6 LEU B 8 ASN B 12 -1 O VAL B 9 N GLY B 20 SHEET 4 BA 6 THR B 103 GLU B 107 1 O LEU B 104 N CYS B 10 SHEET 5 BA 6 ALA B 131 ILE B 136 1 O ALA B 131 N THR B 103 SHEET 6 BA 6 ILE B 357 THR B 358 -1 O ILE B 357 N MET B 132 SHEET 1 BB 3 TYR B 53 VAL B 54 0 SHEET 2 BB 3 VAL B 35 PRO B 38 -1 O GLY B 36 N TYR B 53 SHEET 3 BB 3 LEU B 65 LYS B 68 -1 O THR B 66 N ARG B 37 SHEET 1 BC 2 ILE B 71 GLU B 72 0 SHEET 2 BC 2 ILE B 75 ILE B 76 -1 O ILE B 75 N GLU B 72 SHEET 1 BD 5 TYR B 169 ALA B 170 0 SHEET 2 BD 5 THR B 160 TYR B 166 -1 O TYR B 166 N TYR B 169 SHEET 3 BD 5 GLY B 150 SER B 155 -1 O GLY B 150 N ILE B 165 SHEET 4 BD 5 ASN B 297 SER B 300 1 O VAL B 298 N LEU B 153 SHEET 5 BD 5 ILE B 329 ILE B 330 1 O ILE B 330 N MET B 299 SHEET 1 BE 3 TYR B 169 ALA B 170 0 SHEET 2 BE 3 THR B 160 TYR B 166 -1 O TYR B 166 N TYR B 169 SHEET 3 BE 3 MET B 176 LEU B 178 -1 O MET B 176 N ASN B 162 SHEET 1 BF 2 LYS B 238 GLU B 241 0 SHEET 2 BF 2 VAL B 247 ILE B 250 -1 O ILE B 248 N TYR B 240 LINK O1G ATP B 402 MG MG B 403 1555 1555 2.12 LINK O1B ATP B 402 MG MG B 403 1555 1555 2.11 LINK MG MG B 403 O HOH B 574 1555 1555 2.20 LINK MG MG B 403 O HOH B 552 1555 1555 2.08 LINK MG MG B 403 O HOH B 575 1555 1555 2.13 LINK MG MG B 403 O HOH B 686 1555 1555 2.08 SITE 1 AC1 13 GLY B 15 LEU B 16 ILE B 34 GLN B 59 SITE 2 AC1 13 TYR B 69 ASP B 157 ARG B 183 THR B 186 SITE 3 AC1 13 ARG B 206 GLU B 207 ARG B 210 LYS B 213 SITE 4 AC1 13 HOH B 619 SITE 1 AC2 32 GLY B 13 SER B 14 GLY B 15 LEU B 16 SITE 2 AC2 32 LYS B 18 GLY B 156 ASP B 157 GLY B 158 SITE 3 AC2 32 VAL B 159 GLY B 182 ARG B 210 LYS B 213 SITE 4 AC2 32 GLU B 214 GLY B 301 GLY B 302 THR B 303 SITE 5 AC2 32 MET B 305 TYR B 306 LYS B 336 MG B 403 SITE 6 AC2 32 HOH B 686 HOH B 575 HOH B 552 HOH B 644 SITE 7 AC2 32 HOH B 621 HOH B 553 HOH B 633 HOH B 616 SITE 8 AC2 32 HOH B 560 HOH B 574 HOH B 750 HOH B 680 SITE 1 AC3 5 ATP B 402 HOH B 686 HOH B 575 HOH B 552 SITE 2 AC3 5 HOH B 574 SITE 1 AC4 8 TYR B 133 TYR B 143 PHE B 375 HOH B 735 SITE 2 AC4 8 HOH B 519 HOH B 592 ILE M 122 ARG M 125 SITE 1 AC5 5 PRO B 102 ALA B 131 TRP B 356 THR B 358 SITE 2 AC5 5 HOH B 702 CRYST1 54.750 55.440 138.390 90.00 90.00 90.00 P 21 21 21 4 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 0.018265 0.000000 0.000000 0.00000 SCALE2 0.000000 0.018038 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007226 0.00000 ATOM 1 N ASP B 3 -27.294 7.409 21.055 1.00 29.18 N ANISOU 1 N ASP B 3 2116 4587 4383 496 -68 197 N ATOM 2 CA ASP B 3 -26.313 6.666 21.613 1.00 29.19 C ANISOU 2 CA ASP B 3 2861 4114 4114 90 156 303 C ATOM 3 C ASP B 3 -25.433 7.395 22.522 1.00 27.42 C ANISOU 3 C ASP B 3 2798 3686 3933 15 574 279 C ATOM 4 O ASP B 3 -24.378 6.974 22.735 1.00 27.76 O ANISOU 4 O ASP B 3 2839 3998 3708 364 609 -326 O ATOM 5 CB ASP B 3 -25.517 5.968 20.503 1.00 33.59 C ANISOU 5 CB ASP B 3 3860 4754 4149 -273 79 33 C ATOM 6 CG ASP B 3 -26.236 4.765 19.879 1.00 34.92 C ANISOU 6 CG ASP B 3 4205 5018 4046 -341 -159 16 C ATOM 7 OD1 ASP B 3 -26.735 3.871 20.532 1.00 36.55 O ANISOU 7 OD1 ASP B 3 4192 5633 4063 -391 -239 -236 O ATOM 8 OD2 ASP B 3 -26.214 4.693 18.723 1.00 33.71 O ANISOU 8 OD2 ASP B 3 4225 4616 3966 32 -102 118 O ATOM 9 N GLU B 4 -25.894 8.437 23.108 1.00 25.09 N ANISOU 9 N GLU B 4 2813 2758 3962 554 455 400 N ATOM 10 CA GLU B 4 -25.082 9.174 24.042 1.00 26.90 C ANISOU 10 CA GLU B 4 3614 2544 4063 312 352 375 C ATOM 11 C GLU B 4 -24.595 8.443 25.286 1.00 25.19 C ANISOU 11 C GLU B 4 3812 2067 3694 333 711 236 C ATOM 12 O GLU B 4 -23.621 8.709 25.739 1.00 25.45 O ANISOU 12 O GLU B 4 3565 2324 3782 238 1057 453 O ATOM 13 CB GLU B 4 -25.688 10.507 24.494 1.00 29.66 C ANISOU 13 CB GLU B 4 4079 2682 4510 -138 -108 475 C ATOM 14 CG GLU B 4 -24.672 11.379 25.186 1.00 34.05 C ANISOU 14 CG GLU B 4 4735 3271 4931 186 -225 492 C ATOM 15 CD GLU B 4 -25.166 12.792 25.445 1.00 36.67 C ANISOU 15 CD GLU B 4 4782 3872 5281 232 -238 445 C ATOM 16 OE1 GLU B 4 -26.194 13.075 24.997 1.00 36.22 O ANISOU 16 OE1 GLU B 4 4451 3822 5488 343 -560 590 O ATOM 17 OE2 GLU B 4 -24.502 13.521 26.093 1.00 36.60 O ANISOU 17 OE2 GLU B 4 4376 4173 5358 322 73 341 O ATOM 18 N THR B 5 -25.402 7.536 25.792 1.00 22.55 N ANISOU 18 N THR B 5 3620 1533 3414 600 875 14 N ATOM 19 CA THR B 5 -24.955 6.793 26.973 1.00 21.05 C ANISOU 19 CA THR B 5 3185 1652 3161 1088 734 -68 C ATOM 20 C THR B 5 -25.050 5.248 26.782 1.00 20.64 C ANISOU 20 C THR B 5 3195 1652 2994 910 706 135 C ATOM 21 O THR B 5 -24.846 4.491 27.733 1.00 23.68 O ANISOU 21 O THR B 5 4241 1790 2964 1368 913 329 O ATOM 22 CB THR B 5 -25.753 7.193 28.250 1.00 21.23 C ANISOU 22 CB THR B 5 3131 1640 3293 659 877 -157 C ATOM 23 OG1 THR B 5 -27.122 6.901 27.982 1.00 20.78 O ANISOU 23 OG1 THR B 5 2998 1715 3183 291 586 -121 O ATOM 24 CG2 THR B 5 -25.555 8.741 28.538 1.00 19.87 C ANISOU 24 CG2 THR B 5 2983 1207 3359 130 1101 -120 C ATOM 25 N THR B 6 -25.318 4.781 25.565 1.00 19.71 N ANISOU 25 N THR B 6 2696 1642 3153 916 639 29 N ATOM 26 CA THR B 6 -25.422 3.344 25.303 1.00 19.77 C ANISOU 26 CA THR B 6 2871 1498 3144 632 247 69 C ATOM 27 C THR B 6 -24.148 2.617 25.748 1.00 17.03 C ANISOU 27 C THR B 6 2094 1334 3044 684 650 159 C ATOM 28 O THR B 6 -23.012 3.104 25.522 1.00 16.85 O ANISOU 28 O THR B 6 1898 1394 3110 325 565 -16 O ATOM 29 CB THR B 6 -25.605 3.099 23.813 1.00 22.76 C ANISOU 29 CB THR B 6 3293 2017 3338 795 61 18 C ATOM 30 OG1 THR B 6 -26.744 3.845 23.376 1.00 25.12 O ANISOU 30 OG1 THR B 6 3260 2681 3604 1019 130 -22 O ATOM 31 CG2 THR B 6 -25.859 1.611 23.530 1.00 23.42 C ANISOU 31 CG2 THR B 6 3594 2067 3239 341 185 -243 C ATOM 32 N ALA B 7 -24.286 1.449 26.379 1.00 17.58 N ANISOU 32 N ALA B 7 2602 1054 3025 476 414 79 N ATOM 33 CA ALA B 7 -23.068 0.729 26.745 1.00 16.42 C ANISOU 33 CA ALA B 7 2054 1281 2902 699 260 497 C ATOM 34 C ALA B 7 -22.199 0.444 25.512 1.00 13.33 C ANISOU 34 C ALA B 7 1240 1116 2708 418 201 -19 C ATOM 35 O ALA B 7 -22.744 0.247 24.414 1.00 15.37 O ANISOU 35 O ALA B 7 1823 1395 2620 403 101 -144 O ATOM 36 CB ALA B 7 -23.421 -0.584 27.389 1.00 16.58 C ANISOU 36 CB ALA B 7 2262 1183 2854 338 279 537 C ATOM 37 N LEU B 8 -20.889 0.463 25.675 1.00 13.11 N ANISOU 37 N LEU B 8 1394 929 2659 435 693 44 N ATOM 38 CA LEU B 8 -19.986 0.161 24.573 1.00 16.19 C ANISOU 38 CA LEU B 8 2468 921 2764 102 811 308 C ATOM 39 C LEU B 8 -19.502 -1.258 24.680 1.00 14.43 C ANISOU 39 C LEU B 8 2075 962 2446 211 695 179 C ATOM 40 O LEU B 8 -19.383 -1.789 25.794 1.00 15.93 O ANISOU 40 O LEU B 8 2281 1269 2502 394 494 176 O ATOM 41 CB LEU B 8 -18.788 1.065 24.670 1.00 18.38 C ANISOU 41 CB LEU B 8 2747 1129 3108 -234 1103 239 C ATOM 42 CG LEU B 8 -19.102 2.565 24.627 1.00 21.41 C ANISOU 42 CG LEU B 8 3376 1248 3510 286 962 396 C ATOM 43 CD1 LEU B 8 -17.750 3.293 24.751 1.00 22.93 C ANISOU 43 CD1 LEU B 8 3084 1707 3923 -339 695 392 C ATOM 44 CD2 LEU B 8 -19.907 2.926 23.365 1.00 24.25 C ANISOU 44 CD2 LEU B 8 3918 1603 3694 775 808 705 C ATOM 45 N VAL B 9 -19.166 -1.850 23.533 1.00 14.06 N ANISOU 45 N VAL B 9 1685 904 2754 115 582 -42 N ATOM 46 CA VAL B 9 -18.616 -3.193 23.548 1.00 13.94 C ANISOU 46 CA VAL B 9 1592 831 2872 24 445 66 C ATOM 47 C VAL B 9 -17.345 -3.134 22.691 1.00 15.32 C ANISOU 47 C VAL B 9 2015 865 2941 253 340 47 C ATOM 48 O VAL B 9 -17.418 -2.685 21.533 1.00 14.71 O ANISOU 48 O VAL B 9 1792 934 2863 175 427 198 O ATOM 49 CB VAL B 9 -19.585 -4.220 22.936 1.00 12.93 C ANISOU 49 CB VAL B 9 1177 952 2783 -51 471 -69 C ATOM 50 CG1 VAL B 9 -18.940 -5.646 22.916 1.00 13.24 C ANISOU 50 CG1 VAL B 9 1160 1193 2677 157 123 -125 C ATOM 51 CG2 VAL B 9 -20.848 -4.236 23.734 1.00 14.84 C ANISOU 51 CG2 VAL B 9 1199 1375 3063 -46 404 76 C ATOM 52 N CYS B 10 -16.216 -3.564 23.257 1.00 14.92 N ANISOU 52 N CYS B 10 1652 1075 2942 143 409 151 N ATOM 53 CA ACYS B 10 -14.959 -3.552 22.532 0.70 14.05 C ANISOU 53 CA ACYS B 10 1100 1163 3077 86 718 166 C ATOM 54 CA BCYS B 10 -14.939 -3.580 22.543 0.30 16.33 C ANISOU 54 CA BCYS B 10 1825 1267 3114 125 462 227 C ATOM 55 C CYS B 10 -14.310 -4.939 22.657 1.00 13.75 C ANISOU 55 C CYS B 10 1306 1028 2892 503 616 336 C ATOM 56 O CYS B 10 -14.009 -5.367 23.759 1.00 16.96 O ANISOU 56 O CYS B 10 2640 1245 2558 246 362 284 O ATOM 57 CB ACYS B 10 -14.044 -2.483 23.125 0.70 16.75 C ANISOU 57 CB ACYS B 10 1636 1310 3417 -46 939 134 C ATOM 58 CB BCYS B 10 -13.954 -2.603 23.158 0.30 20.38 C ANISOU 58 CB BCYS B 10 2665 1559 3520 -201 298 270 C ATOM 59 SG ACYS B 10 -12.474 -2.277 22.320 0.70 17.60 S ANISOU 59 SG ACYS B 10 1575 1488 3623 -111 960 290 S ATOM 60 SG BCYS B 10 -14.446 -0.946 22.980 0.30 23.08 S ANISOU 60 SG BCYS B 10 3204 1687 3880 -559 110 327 S ATOM 61 N ASP B 11 -14.107 -5.570 21.508 1.00 13.66 N ANISOU 61 N ASP B 11 1595 831 2764 152 797 98 N ATOM 62 CA ASP B 11 -13.470 -6.864 21.436 1.00 12.29 C ANISOU 62 CA ASP B 11 840 1093 2738 30 326 38 C ATOM 63 C ASP B 11 -12.077 -6.610 20.834 1.00 13.75 C ANISOU 63 C ASP B 11 1347 1122 2757 73 232 150 C ATOM 64 O ASP B 11 -11.916 -6.373 19.619 1.00 16.44 O ANISOU 64 O ASP B 11 1996 1487 2762 385 383 169 O ATOM 65 CB ASP B 11 -14.284 -7.791 20.537 1.00 12.92 C ANISOU 65 CB ASP B 11 1579 677 2653 -338 382 -202 C ATOM 66 CG ASP B 11 -13.565 -9.149 20.259 1.00 13.38 C ANISOU 66 CG ASP B 11 1403 972 2710 -531 197 -164 C ATOM 67 OD1 ASP B 11 -13.971 -9.762 19.264 1.00 13.96 O ANISOU 67 OD1 ASP B 11 1374 1247 2685 -97 221 -169 O ATOM 68 OD2 ASP B 11 -12.666 -9.531 21.066 1.00 14.32 O ANISOU 68 OD2 ASP B 11 1469 1432 2539 -112 -114 192 O ATOM 69 N ASN B 12 -11.098 -6.621 21.713 1.00 13.55 N ANISOU 69 N ASN B 12 821 1272 3057 160 99 -49 N ATOM 70 CA ASN B 12 -9.749 -6.360 21.286 1.00 14.74 C ANISOU 70 CA ASN B 12 900 1625 3075 363 283 -596 C ATOM 71 C ASN B 12 -9.018 -7.611 20.805 1.00 15.17 C ANISOU 71 C ASN B 12 1102 1683 2977 294 140 -328 C ATOM 72 O ASN B 12 -8.547 -8.409 21.622 1.00 18.50 O ANISOU 72 O ASN B 12 2075 1930 3022 218 55 -172 O ATOM 73 CB ASN B 12 -8.966 -5.733 22.425 1.00 17.94 C ANISOU 73 CB ASN B 12 1656 1883 3277 128 142 -736 C ATOM 74 CG ASN B 12 -9.387 -4.316 22.691 1.00 19.37 C ANISOU 74 CG ASN B 12 1845 2101 3414 -110 312 -84 C ATOM 75 OD1 ASN B 12 -9.936 -4.050 23.739 1.00 19.50 O ANISOU 75 OD1 ASN B 12 2032 2108 3270 -764 522 -224 O ATOM 76 ND2 ASN B 12 -9.154 -3.393 21.705 1.00 21.35 N ANISOU 76 ND2 ASN B 12 2212 2377 3524 -503 313 75 N ATOM 77 N GLY B 13 -8.920 -7.744 19.502 1.00 14.40 N ANISOU 77 N GLY B 13 1371 1107 2994 40 302 -17 N ATOM 78 CA GLY B 13 -8.195 -8.873 18.925 1.00 13.71 C ANISOU 78 CA GLY B 13 992 1411 2806 358 300 48 C ATOM 79 C GLY B 13 -6.700 -8.665 18.674 1.00 15.01 C ANISOU 79 C GLY B 13 1359 1488 2856 -134 529 -185 C ATOM 80 O GLY B 13 -6.222 -7.530 18.654 1.00 16.49 O ANISOU 80 O GLY B 13 1579 1555 3133 -218 608 -370 O ATOM 81 N SER B 14 -5.996 -9.740 18.320 1.00 16.41 N ANISOU 81 N SER B 14 1626 1691 2916 -266 59 -329 N ATOM 82 CA SER B 14 -4.586 -9.598 17.942 1.00 18.12 C ANISOU 82 CA SER B 14 1634 1937 3313 -156 67 -217 C ATOM 83 C SER B 14 -4.454 -8.821 16.650 1.00 18.33 C ANISOU 83 C SER B 14 1783 2007 3174 -395 547 -277 C ATOM 84 O SER B 14 -3.500 -8.044 16.442 1.00 20.12 O ANISOU 84 O SER B 14 1856 2401 3388 -473 779 -40 O ATOM 85 CB SER B 14 -3.965 -10.947 17.706 1.00 17.72 C ANISOU 85 CB SER B 14 1852 1504 3376 -347 287 -233 C ATOM 86 OG SER B 14 -4.093 -11.747 18.846 1.00 18.27 O ANISOU 86 OG SER B 14 1539 2077 3328 -134 824 141 O ATOM 87 N GLY B 15 -5.425 -9.008 15.775 1.00 15.74 N ANISOU 87 N GLY B 15 1323 1676 2980 16 565 -74 N ATOM 88 CA GLY B 15 -5.407 -8.336 14.470 1.00 16.67 C ANISOU 88 CA GLY B 15 1579 1539 3218 -5 478 -273 C ATOM 89 C GLY B 15 -6.342 -7.146 14.339 1.00 14.89 C ANISOU 89 C GLY B 15 1270 1225 3163 117 619 -121 C ATOM 90 O GLY B 15 -5.928 -6.075 13.843 1.00 17.15 O ANISOU 90 O GLY B 15 1725 1532 3257 -99 725 66 O ATOM 91 N LEU B 16 -7.607 -7.323 14.763 1.00 14.67 N ANISOU 91 N LEU B 16 995 1595 2985 22 686 -5 N ATOM 92 CA LEU B 16 -8.646 -6.306 14.591 1.00 15.65 C ANISOU 92 CA LEU B 16 1958 1213 2776 32 845 -115 C ATOM 93 C LEU B 16 -9.296 -5.978 15.920 1.00 14.49 C ANISOU 93 C LEU B 16 1872 868 2768 -260 521 -148 C ATOM 94 O LEU B 16 -9.630 -6.881 16.708 1.00 14.21 O ANISOU 94 O LEU B 16 1568 1191 2640 -177 438 197 O ATOM 95 CB LEU B 16 -9.756 -6.776 13.644 1.00 15.34 C ANISOU 95 CB LEU B 16 2006 1304 2520 -213 783 68 C ATOM 96 CG LEU B 16 -9.289 -7.013 12.200 1.00 14.15 C ANISOU 96 CG LEU B 16 1699 1255 2424 -199 623 330 C ATOM 97 CD1 LEU B 16 -10.447 -7.592 11.379 1.00 15.31 C ANISOU 97 CD1 LEU B 16 1454 1823 2540 -61 117 -61 C ATOM 98 CD2 LEU B 16 -8.770 -5.663 11.593 1.00 15.85 C ANISOU 98 CD2 LEU B 16 2324 1202 2497 -63 623 367 C ATOM 99 N VAL B 17 -9.499 -4.678 16.118 1.00 16.01 N ANISOU 99 N VAL B 17 2193 952 2939 62 881 -193 N ATOM 100 CA VAL B 17 -10.420 -4.203 17.134 1.00 14.64 C ANISOU 100 CA VAL B 17 1580 976 3008 -81 953 -208 C ATOM 101 C VAL B 17 -11.808 -4.211 16.564 1.00 15.23 C ANISOU 101 C VAL B 17 1769 1345 2673 -13 500 -242 C ATOM 102 O VAL B 17 -11.998 -3.722 15.446 1.00 16.13 O ANISOU 102 O VAL B 17 2129 1361 2638 -110 434 125 O ATOM 103 CB VAL B 17 -10.068 -2.774 17.594 1.00 15.70 C ANISOU 103 CB VAL B 17 1449 1124 3394 -152 893 -497 C ATOM 104 CG1 VAL B 17 -11.011 -2.362 18.775 1.00 17.66 C ANISOU 104 CG1 VAL B 17 1403 1863 3443 -158 1302 -488 C ATOM 105 CG2 VAL B 17 -8.612 -2.725 18.014 1.00 19.29 C ANISOU 105 CG2 VAL B 17 1550 2150 3630 -333 -9 -222 C ATOM 106 N LYS B 18 -12.802 -4.766 17.300 1.00 13.22 N ANISOU 106 N LYS B 18 1141 1354 2530 140 499 -3 N ATOM 107 CA LYS B 18 -14.195 -4.669 16.905 1.00 12.82 C ANISOU 107 CA LYS B 18 1322 1138 2412 -108 274 255 C ATOM 108 C LYS B 18 -14.821 -3.870 18.017 1.00 13.88 C ANISOU 108 C LYS B 18 2223 752 2299 -35 515 311 C ATOM 109 O LYS B 18 -14.806 -4.308 19.171 1.00 13.97 O ANISOU 109 O LYS B 18 1625 1233 2450 231 659 436 O ATOM 110 CB LYS B 18 -14.847 -6.060 16.859 1.00 13.13 C ANISOU 110 CB LYS B 18 1441 1192 2356 -388 498 176 C ATOM 111 CG LYS B 18 -14.519 -6.888 15.603 1.00 14.87 C ANISOU 111 CG LYS B 18 1741 1471 2437 156 357 248 C ATOM 112 CD LYS B 18 -13.082 -7.353 15.422 1.00 15.08 C ANISOU 112 CD LYS B 18 1869 1252 2611 361 566 302 C ATOM 113 CE LYS B 18 -12.679 -8.351 16.527 1.00 12.38 C ANISOU 113 CE LYS B 18 797 1179 2728 -48 454 271 C ATOM 114 NZ LYS B 18 -11.421 -9.041 16.201 1.00 12.98 N ANISOU 114 NZ LYS B 18 1018 1390 2524 38 546 164 N ATOM 115 N ALA B 19 -15.448 -2.742 17.657 1.00 15.02 N ANISOU 115 N ALA B 19 2426 787 2493 6 726 138 N ATOM 116 CA ALA B 19 -15.981 -1.874 18.711 1.00 15.26 C ANISOU 116 CA ALA B 19 1852 1176 2772 362 620 -7 C ATOM 117 C ALA B 19 -17.314 -1.300 18.271 1.00 15.75 C ANISOU 117 C ALA B 19 2221 1016 2746 447 824 207 C ATOM 118 O ALA B 19 -17.584 -1.149 17.051 1.00 17.96 O ANISOU 118 O ALA B 19 2561 1538 2727 470 886 480 O ATOM 119 CB ALA B 19 -14.960 -0.746 19.050 1.00 17.14 C ANISOU 119 CB ALA B 19 2132 1308 3071 -165 535 214 C ATOM 120 N GLY B 20 -18.176 -0.991 19.246 1.00 15.19 N ANISOU 120 N GLY B 20 1979 989 2805 304 583 16 N ATOM 121 CA GLY B 20 -19.505 -0.511 18.899 1.00 15.75 C ANISOU 121 CA GLY B 20 1961 1351 2671 210 561 19 C ATOM 122 C GLY B 20 -20.356 -0.350 20.122 1.00 15.61 C ANISOU 122 C GLY B 20 1834 1316 2781 869 326 181 C ATOM 123 O GLY B 20 -19.846 -0.290 21.250 1.00 15.61 O ANISOU 123 O GLY B 20 2168 1021 2743 421 261 174 O ATOM 124 N PHE B 21 -21.652 -0.321 19.852 1.00 16.63 N ANISOU 124 N PHE B 21 1719 1671 2927 1063 600 221 N ATOM 125 CA PHE B 21 -22.667 -0.050 20.896 1.00 16.70 C ANISOU 125 CA PHE B 21 1680 1646 3021 979 511 247 C ATOM 126 C PHE B 21 -23.547 -1.248 21.170 1.00 18.10 C ANISOU 126 C PHE B 21 2209 1748 2922 823 374 -1 C ATOM 127 O PHE B 21 -24.057 -1.895 20.238 1.00 16.82 O ANISOU 127 O PHE B 21 2115 1623 2652 490 196 -112 O ATOM 128 CB PHE B 21 -23.528 1.180 20.511 1.00 16.68 C ANISOU 128 CB PHE B 21 1512 1612 3213 765 143 166 C ATOM 129 CG PHE B 21 -22.721 2.412 20.297 1.00 18.40 C ANISOU 129 CG PHE B 21 1680 1721 3591 346 678 511 C ATOM 130 CD1 PHE B 21 -22.464 3.274 21.339 1.00 24.74 C ANISOU 130 CD1 PHE B 21 2753 2755 3891 318 850 274 C ATOM 131 CD2 PHE B 21 -22.139 2.677 19.045 1.00 22.87 C ANISOU 131 CD2 PHE B 21 2725 1987 3978 576 569 824 C ATOM 132 CE1 PHE B 21 -21.670 4.422 21.138 1.00 27.02 C ANISOU 132 CE1 PHE B 21 3291 2896 4080 528 618 497 C ATOM 133 CE2 PHE B 21 -21.364 3.844 18.842 1.00 26.18 C ANISOU 133 CE2 PHE B 21 3429 2403 4114 500 312 863 C ATOM 134 CZ PHE B 21 -21.122 4.695 19.888 1.00 25.72 C ANISOU 134 CZ PHE B 21 3131 2622 4019 852 386 667 C ATOM 135 N ALA B 22 -23.737 -1.525 22.456 1.00 17.61 N ANISOU 135 N ALA B 22 2572 1436 2681 847 159 141 N ATOM 136 CA ALA B 22 -24.613 -2.606 22.860 1.00 17.09 C ANISOU 136 CA ALA B 22 2303 1401 2790 455 -167 -5 C ATOM 137 C ALA B 22 -25.998 -2.439 22.274 1.00 18.05 C ANISOU 137 C ALA B 22 2251 1510 3098 333 -68 -93 C ATOM 138 O ALA B 22 -26.587 -1.336 22.285 1.00 21.05 O ANISOU 138 O ALA B 22 2573 1918 3507 610 47 -232 O ATOM 139 CB ALA B 22 -24.693 -2.696 24.361 1.00 19.21 C ANISOU 139 CB ALA B 22 3049 1675 2576 364 -31 -193 C ATOM 140 N GLY B 23 -26.516 -3.531 21.754 1.00 17.87 N ANISOU 140 N GLY B 23 1667 2056 3065 173 -28 140 N ATOM 141 CA GLY B 23 -27.824 -3.550 21.146 1.00 19.95 C ANISOU 141 CA GLY B 23 1911 2593 3074 459 -62 -53 C ATOM 142 C GLY B 23 -27.777 -3.463 19.627 1.00 20.86 C ANISOU 142 C GLY B 23 1787 3038 3103 699 -337 -105 C ATOM 143 O GLY B 23 -28.772 -3.799 18.958 1.00 22.24 O ANISOU 143 O GLY B 23 1513 3760 3176 333 -400 -390 O ATOM 144 N ASP B 24 -26.644 -3.009 19.076 1.00 22.93 N ANISOU 144 N ASP B 24 2461 3087 3164 865 -204 -350 N ATOM 145 CA ASP B 24 -26.427 -3.039 17.624 1.00 24.28 C ANISOU 145 CA ASP B 24 2634 3436 3155 770 -276 -250 C ATOM 146 C ASP B 24 -26.133 -4.481 17.202 1.00 22.27 C ANISOU 146 C ASP B 24 2149 3467 2844 595 -326 -505 C ATOM 147 O ASP B 24 -25.580 -5.307 17.986 1.00 21.27 O ANISOU 147 O ASP B 24 1840 3360 2882 862 -258 -258 O ATOM 148 CB ASP B 24 -25.253 -2.164 17.196 1.00 22.45 C ANISOU 148 CB ASP B 24 2635 2545 3348 1115 -305 131 C ATOM 149 CG ASP B 24 -25.536 -0.696 17.273 1.00 27.88 C ANISOU 149 CG ASP B 24 3361 3480 3753 1167 -148 333 C ATOM 150 OD1 ASP B 24 -26.720 -0.326 17.522 1.00 29.04 O ANISOU 150 OD1 ASP B 24 3440 3570 4026 1066 -74 219 O ATOM 151 OD2 ASP B 24 -24.561 0.068 17.114 1.00 27.71 O ANISOU 151 OD2 ASP B 24 3630 3060 3838 1301 100 310 O ATOM 152 N ASP B 25 -26.480 -4.794 15.955 1.00 24.56 N ANISOU 152 N ASP B 25 2085 4265 2981 425 -69 -340 N ATOM 153 CA AASP B 25 -26.326 -6.114 15.386 0.60 24.98 C ANISOU 153 CA AASP B 25 1998 4567 2926 301 -121 -339 C ATOM 154 CA BASP B 25 -26.277 -6.173 15.531 0.40 24.37 C ANISOU 154 CA BASP B 25 2216 4226 2819 511 -81 -194 C ATOM 155 C ASP B 25 -24.885 -6.413 14.934 1.00 23.11 C ANISOU 155 C ASP B 25 1985 4062 2735 381 -4 -231 C ATOM 156 O ASP B 25 -24.554 -7.534 14.675 1.00 24.19 O ANISOU 156 O ASP B 25 2664 3735 2792 311 -44 -70 O ATOM 157 CB AASP B 25 -27.295 -6.254 14.198 0.60 29.42 C ANISOU 157 CB AASP B 25 2468 5507 3205 -208 -130 -233 C ATOM 158 CB BASP B 25 -27.389 -6.692 14.604 0.40 27.02 C ANISOU 158 CB BASP B 25 2997 4445 2824 597 -75 213 C ATOM 159 CG AASP B 25 -28.761 -6.230 14.634 0.60 34.85 C ANISOU 159 CG AASP B 25 3322 6420 3501 -525 -159 -160 C ATOM 160 CG BASP B 25 -27.251 -6.180 13.205 0.40 28.50 C ANISOU 160 CG BASP B 25 3540 4593 2697 624 -121 468 C ATOM 161 OD1AASP B 25 -29.049 -6.648 15.779 0.60 36.56 O ANISOU 161 OD1AASP B 25 3574 6690 3627 -778 -31 -327 O ATOM 162 OD1BASP B 25 -26.968 -4.966 13.086 0.40 29.20 O ANISOU 162 OD1BASP B 25 4111 4218 2766 829 -124 96 O ATOM 163 OD2AASP B 25 -29.625 -5.804 13.838 0.60 39.44 O ANISOU 163 OD2AASP B 25 4197 7009 3781 -473 22 -113 O ATOM 164 OD2BASP B 25 -27.402 -6.993 12.248 0.40 28.54 O ANISOU 164 OD2BASP B 25 3328 4923 2594 1164 -233 998 O ATOM 165 N ALA B 26 -24.085 -5.364 14.770 1.00 21.38 N ANISOU 165 N ALA B 26 2160 3328 2636 641 -115 -82 N ATOM 166 CA ALA B 26 -22.699 -5.470 14.274 1.00 20.87 C ANISOU 166 CA ALA B 26 2264 3034 2631 127 277 -310 C ATOM 167 C ALA B 26 -21.824 -4.379 14.848 1.00 17.79 C ANISOU 167 C ALA B 26 1954 2105 2702 572 395 -2 C ATOM 168 O ALA B 26 -22.339 -3.324 15.218 1.00 19.64 O ANISOU 168 O ALA B 26 2473 2094 2895 658 -135 -231 O ATOM 169 CB ALA B 26 -22.668 -5.391 12.734 1.00 25.41 C ANISOU 169 CB ALA B 26 3398 3529 2727 295 140 -18 C ATOM 170 N PRO B 27 -20.485 -4.587 14.899 1.00 16.74 N ANISOU 170 N PRO B 27 1842 1600 2918 241 619 -1 N ATOM 171 CA PRO B 27 -19.630 -3.497 15.407 1.00 18.20 C ANISOU 171 CA PRO B 27 2528 1497 2891 226 478 256 C ATOM 172 C PRO B 27 -19.597 -2.320 14.433 1.00 20.38 C ANISOU 172 C PRO B 27 3786 1312 2645 256 732 562 C ATOM 173 O PRO B 27 -19.375 -2.526 13.239 1.00 26.25 O ANISOU 173 O PRO B 27 5130 2133 2712 -289 673 341 O ATOM 174 CB PRO B 27 -18.237 -4.129 15.508 1.00 18.43 C ANISOU 174 CB PRO B 27 2353 1529 3121 541 926 -236 C ATOM 175 CG PRO B 27 -18.304 -5.374 14.629 1.00 17.51 C ANISOU 175 CG PRO B 27 1911 1698 3044 -373 741 -319 C ATOM 176 CD PRO B 27 -19.727 -5.827 14.593 1.00 16.90 C ANISOU 176 CD PRO B 27 2044 1378 3000 196 728 -266 C ATOM 177 N ARG B 28 -19.789 -1.132 14.965 1.00 21.03 N ANISOU 177 N ARG B 28 3652 1449 2892 469 575 756 N ATOM 178 CA ARG B 28 -19.769 0.138 14.223 1.00 23.02 C ANISOU 178 CA ARG B 28 3651 1930 3164 407 988 726 C ATOM 179 C ARG B 28 -18.373 0.394 13.630 1.00 21.32 C ANISOU 179 C ARG B 28 3345 1626 3130 570 799 814 C ATOM 180 O ARG B 28 -18.266 1.035 12.581 1.00 24.56 O ANISOU 180 O ARG B 28 3978 2127 3226 317 481 1172 O ATOM 181 CB ARG B 28 -20.137 1.278 15.227 1.00 25.32 C ANISOU 181 CB ARG B 28 4309 1605 3709 1350 979 521 C ATOM 182 CG ARG B 28 -20.639 2.604 14.645 1.00 33.58 C ANISOU 182 CG ARG B 28 5176 3304 4280 850 474 445 C ATOM 183 CD ARG B 28 -22.030 2.439 14.029 1.00 36.28 C ANISOU 183 CD ARG B 28 5446 3882 4458 1079 249 538 C ATOM 184 NE ARG B 28 -23.116 2.173 14.989 1.00 35.84 N ANISOU 184 NE ARG B 28 5575 3606 4437 760 404 739 N ATOM 185 CZ ARG B 28 -23.685 3.104 15.771 1.00 35.58 C ANISOU 185 CZ ARG B 28 5665 3374 4478 737 217 736 C ATOM 186 NH1 ARG B 28 -24.685 2.772 16.584 1.00 32.30 N ANISOU 186 NH1 ARG B 28 5102 2735 4437 776 154 768 N ATOM 187 NH2 ARG B 28 -23.258 4.372 15.759 1.00 36.20 N ANISOU 187 NH2 ARG B 28 6035 3161 4560 895 172 743 N ATOM 188 N ALA B 29 -17.322 -0.042 14.322 1.00 20.46 N ANISOU 188 N ALA B 29 3336 1262 3175 238 708 407 N ATOM 189 CA ALA B 29 -15.941 0.237 13.986 1.00 18.40 C ANISOU 189 CA ALA B 29 3058 822 3111 485 909 160 C ATOM 190 C ALA B 29 -15.132 -1.041 14.050 1.00 17.87 C ANISOU 190 C ALA B 29 2804 1125 2862 263 899 109 C ATOM 191 O ALA B 29 -15.148 -1.719 15.065 1.00 19.94 O ANISOU 191 O ALA B 29 2973 1928 2675 249 714 350 O ATOM 192 CB ALA B 29 -15.343 1.273 14.948 1.00 21.46 C ANISOU 192 CB ALA B 29 2703 2015 3435 342 1102 -171 C ATOM 193 N VAL B 30 -14.413 -1.351 12.964 1.00 17.85 N ANISOU 193 N VAL B 30 2283 1657 2842 241 891 65 N ATOM 194 CA VAL B 30 -13.531 -2.507 12.910 1.00 18.89 C ANISOU 194 CA VAL B 30 2458 1836 2882 434 960 67 C ATOM 195 C VAL B 30 -12.271 -1.962 12.270 1.00 18.79 C ANISOU 195 C VAL B 30 2367 1885 2887 -103 994 138 C ATOM 196 O VAL B 30 -12.323 -1.400 11.139 1.00 21.45 O ANISOU 196 O VAL B 30 2873 2263 3013 -159 1018 557 O ATOM 197 CB VAL B 30 -14.101 -3.642 12.053 1.00 16.42 C ANISOU 197 CB VAL B 30 1701 1692 2846 258 694 381 C ATOM 198 CG1 VAL B 30 -13.165 -4.861 12.047 1.00 18.58 C ANISOU 198 CG1 VAL B 30 2221 1732 3107 607 512 359 C ATOM 199 CG2 VAL B 30 -15.514 -4.034 12.495 1.00 17.00 C ANISOU 199 CG2 VAL B 30 1862 1682 2914 409 115 114 C ATOM 200 N PHE B 31 -11.185 -2.016 13.015 1.00 17.38 N ANISOU 200 N PHE B 31 2174 1357 3072 162 1064 94 N ATOM 201 CA PHE B 31 -9.933 -1.407 12.545 1.00 19.57 C ANISOU 201 CA PHE B 31 2981 1240 3213 -49 1414 -104 C ATOM 202 C PHE B 31 -8.733 -2.150 13.052 1.00 18.30 C ANISOU 202 C PHE B 31 2543 1159 3252 -224 1166 -44 C ATOM 203 O PHE B 31 -8.842 -2.928 14.012 1.00 18.38 O ANISOU 203 O PHE B 31 2232 1362 3390 -397 1176 257 O ATOM 204 CB PHE B 31 -9.862 0.082 12.935 1.00 22.20 C ANISOU 204 CB PHE B 31 3898 1080 3458 53 1413 10 C ATOM 205 CG PHE B 31 -9.889 0.320 14.402 1.00 23.97 C ANISOU 205 CG PHE B 31 4431 1087 3590 -447 1401 -172 C ATOM 206 CD1 PHE B 31 -8.708 0.455 15.119 1.00 25.79 C ANISOU 206 CD1 PHE B 31 4718 1419 3663 -708 1362 -62 C ATOM 207 CD2 PHE B 31 -11.109 0.400 15.076 1.00 23.97 C ANISOU 207 CD2 PHE B 31 4616 961 3529 -320 1745 -401 C ATOM 208 CE1 PHE B 31 -8.722 0.684 16.487 1.00 26.36 C ANISOU 208 CE1 PHE B 31 4951 1376 3688 -188 1230 1 C ATOM 209 CE2 PHE B 31 -11.123 0.617 16.453 1.00 25.73 C ANISOU 209 CE2 PHE B 31 4980 1162 3633 -41 1505 -114 C ATOM 210 CZ PHE B 31 -9.927 0.766 17.143 1.00 24.92 C ANISOU 210 CZ PHE B 31 4607 1187 3675 -147 1363 43 C ATOM 211 N PRO B 32 -7.600 -2.035 12.343 1.00 19.04 N ANISOU 211 N PRO B 32 2476 1456 3303 -380 1056 16 N ATOM 212 CA PRO B 32 -6.468 -2.820 12.781 1.00 19.65 C ANISOU 212 CA PRO B 32 2329 1790 3346 -301 909 314 C ATOM 213 C PRO B 32 -5.903 -2.443 14.131 1.00 19.97 C ANISOU 213 C PRO B 32 2428 1672 3488 -873 960 175 C ATOM 214 O PRO B 32 -5.803 -1.252 14.493 1.00 20.14 O ANISOU 214 O PRO B 32 2265 1563 3823 -838 919 -46 O ATOM 215 CB PRO B 32 -5.399 -2.592 11.673 1.00 19.61 C ANISOU 215 CB PRO B 32 2543 1452 3455 -349 1099 613 C ATOM 216 CG PRO B 32 -5.750 -1.281 11.084 1.00 19.82 C ANISOU 216 CG PRO B 32 2245 1624 3660 -639 1254 240 C ATOM 217 CD PRO B 32 -7.287 -1.212 11.145 1.00 19.60 C ANISOU 217 CD PRO B 32 2217 1713 3519 -641 1238 385 C ATOM 218 N SER B 33 -5.545 -3.464 14.886 1.00 18.66 N ANISOU 218 N SER B 33 1751 2022 3314 -449 838 -54 N ATOM 219 CA ASER B 33 -4.927 -3.326 16.182 0.80 19.88 C ANISOU 219 CA ASER B 33 2335 1938 3280 -640 632 -81 C ATOM 220 CA BSER B 33 -4.827 -3.326 16.182 0.20 21.08 C ANISOU 220 CA BSER B 33 2171 2439 3398 -447 717 -197 C ATOM 221 C SER B 33 -3.410 -3.121 16.083 1.00 21.63 C ANISOU 221 C SER B 33 2274 2415 3528 -704 824 -298 C ATOM 222 O SER B 33 -2.621 -3.964 16.415 1.00 20.65 O ANISOU 222 O SER B 33 1464 2739 3644 -792 813 -546 O ATOM 223 CB ASER B 33 -5.319 -4.524 17.077 0.80 18.95 C ANISOU 223 CB ASER B 33 2233 1871 3096 0 601 -298 C ATOM 224 CB BSER B 33 -5.219 -4.524 17.077 0.20 22.24 C ANISOU 224 CB BSER B 33 2209 2872 3371 -53 570 -325 C ATOM 225 OG ASER B 33 -4.839 -4.329 18.395 0.80 18.53 O ANISOU 225 OG ASER B 33 1720 2189 3131 -799 562 -350 O ATOM 226 OG BSER B 33 -4.772 -5.736 16.497 0.20 23.09 O ANISOU 226 OG BSER B 33 2033 3359 3383 128 470 -411 O ATOM 227 N ILE B 34 -3.053 -1.938 15.605 1.00 20.68 N ANISOU 227 N ILE B 34 2240 1882 3734 -1089 837 -483 N ATOM 228 CA ILE B 34 -1.638 -1.628 15.316 1.00 23.04 C ANISOU 228 CA ILE B 34 2386 2417 3950 -1204 1268 -444 C ATOM 229 C ILE B 34 -1.321 -0.209 15.763 1.00 24.89 C ANISOU 229 C ILE B 34 2630 2402 4427 -905 1117 -774 C ATOM 230 O ILE B 34 -2.190 0.663 15.730 1.00 23.91 O ANISOU 230 O ILE B 34 2375 2330 4381 -1029 1720 -768 O ATOM 231 CB ILE B 34 -1.343 -1.746 13.792 1.00 21.34 C ANISOU 231 CB ILE B 34 2155 2148 3807 -645 903 -252 C ATOM 232 CG1 ILE B 34 -2.309 -0.859 12.975 1.00 24.50 C ANISOU 232 CG1 ILE B 34 2650 2730 3928 -452 990 -96 C ATOM 233 CG2 ILE B 34 -1.437 -3.221 13.366 1.00 22.17 C ANISOU 233 CG2 ILE B 34 2592 2070 3760 -679 710 -466 C ATOM 234 CD1 ILE B 34 -2.136 -0.905 11.449 1.00 25.00 C ANISOU 234 CD1 ILE B 34 2444 2965 4091 -886 949 106 C ATOM 235 N VAL B 35 -0.069 0.018 16.143 1.00 25.99 N ANISOU 235 N VAL B 35 2633 2438 4804 -866 1515 -626 N ATOM 236 CA VAL B 35 0.459 1.384 16.195 1.00 28.59 C ANISOU 236 CA VAL B 35 3132 2669 5061 -1112 1625 -745 C ATOM 237 C VAL B 35 1.622 1.432 15.195 1.00 32.12 C ANISOU 237 C VAL B 35 3406 3300 5497 -1484 1856 -542 C ATOM 238 O VAL B 35 2.469 0.536 15.205 1.00 31.67 O ANISOU 238 O VAL B 35 2862 3542 5629 -1836 1842 -633 O ATOM 239 CB VAL B 35 0.902 1.727 17.609 1.00 29.44 C ANISOU 239 CB VAL B 35 3372 2781 5033 -1032 1317 -985 C ATOM 240 CG1 VAL B 35 1.583 3.134 17.665 1.00 29.52 C ANISOU 240 CG1 VAL B 35 3664 2511 5043 -1357 1135 -1010 C ATOM 241 CG2 VAL B 35 -0.298 1.632 18.569 1.00 28.91 C ANISOU 241 CG2 VAL B 35 3275 2733 4979 -949 1138 -914 C ATOM 242 N GLY B 36 1.610 2.437 14.314 1.00 32.71 N ANISOU 242 N GLY B 36 3613 3055 5761 -1774 2045 -234 N ATOM 243 CA GLY B 36 2.681 2.607 13.312 1.00 34.97 C ANISOU 243 CA GLY B 36 3945 3289 6053 -1666 2147 -226 C ATOM 244 C GLY B 36 3.577 3.784 13.650 1.00 35.84 C ANISOU 244 C GLY B 36 3594 3716 6309 -1671 2192 -563 C ATOM 245 O GLY B 36 3.091 4.812 14.116 1.00 36.17 O ANISOU 245 O GLY B 36 3602 3757 6385 -1496 2054 -678 O ATOM 246 N ARG B 37 4.882 3.623 13.424 1.00 36.77 N ANISOU 246 N ARG B 37 3609 3913 6448 -2154 2250 -882 N ATOM 247 CA ARG B 37 5.853 4.700 13.642 1.00 38.53 C ANISOU 247 CA ARG B 37 3794 4236 6610 -1829 2337 -822 C ATOM 248 C ARG B 37 6.765 4.818 12.425 1.00 39.24 C ANISOU 248 C ARG B 37 3861 4241 6808 -1708 2230 -619 C ATOM 249 O ARG B 37 7.070 3.798 11.789 1.00 41.10 O ANISOU 249 O ARG B 37 3843 4772 7003 -1161 1812 -676 O ATOM 250 CB ARG B 37 6.674 4.422 14.892 1.00 39.71 C ANISOU 250 CB ARG B 37 4009 4517 6561 -2186 2290 -797 C ATOM 251 CG ARG B 37 5.858 4.549 16.169 1.00 40.67 C ANISOU 251 CG ARG B 37 3956 4934 6563 -1984 2128 -829 C ATOM 252 CD ARG B 37 6.625 4.007 17.345 1.00 42.01 C ANISOU 252 CD ARG B 37 4001 5388 6571 -2083 1892 -841 C ATOM 253 NE ARG B 37 5.931 4.279 18.597 1.00 43.27 N ANISOU 253 NE ARG B 37 4056 5823 6562 -2163 1785 -877 N ATOM 254 CZ ARG B 37 5.050 3.455 19.171 1.00 42.37 C ANISOU 254 CZ ARG B 37 3806 5807 6484 -2682 1804 -877 C ATOM 255 NH1 ARG B 37 4.472 3.808 20.314 1.00 43.93 N ANISOU 255 NH1 ARG B 37 4345 5794 6553 -2582 1515 -1078 N ATOM 256 NH2 ARG B 37 4.753 2.284 18.616 1.00 42.62 N ANISOU 256 NH2 ARG B 37 3562 6234 6399 -2258 1663 -976 N ATOM 257 N PRO B 38 7.188 6.059 12.085 1.00 41.25 N ANISOU 257 N PRO B 38 4303 4456 6915 -1436 2262 -503 N ATOM 258 CA PRO B 38 8.174 6.273 11.013 1.00 42.19 C ANISOU 258 CA PRO B 38 4586 4493 6953 -1717 2154 -336 C ATOM 259 C PRO B 38 9.342 5.284 11.105 1.00 44.57 C ANISOU 259 C PRO B 38 5020 4918 6996 -1762 2064 -327 C ATOM 260 O PRO B 38 9.948 5.134 12.181 1.00 44.78 O ANISOU 260 O PRO B 38 4838 5127 7048 -1701 2127 -433 O ATOM 261 CB PRO B 38 8.649 7.707 11.276 1.00 40.93 C ANISOU 261 CB PRO B 38 4465 4101 6984 -1661 2179 -359 C ATOM 262 CG PRO B 38 7.415 8.392 11.816 1.00 41.88 C ANISOU 262 CG PRO B 38 4356 4608 6947 -1521 2470 -206 C ATOM 263 CD PRO B 38 6.793 7.336 12.722 1.00 42.04 C ANISOU 263 CD PRO B 38 4360 4678 6937 -1316 2370 -323 C ATOM 264 N ARG B 39 9.631 4.612 9.986 1.00 46.50 N ANISOU 264 N ARG B 39 5182 5528 6959 -1503 2046 -344 N ATOM 265 CA ARG B 39 10.648 3.544 9.923 1.00 50.89 C ANISOU 265 CA ARG B 39 5673 6601 7061 -993 1597 -388 C ATOM 266 C ARG B 39 12.081 4.042 10.161 1.00 53.44 C ANISOU 266 C ARG B 39 5685 7490 7129 -538 1467 -351 C ATOM 267 O ARG B 39 12.854 3.412 10.898 1.00 54.20 O ANISOU 267 O ARG B 39 5541 7926 7127 -419 1459 -324 O ATOM 268 CB ARG B 39 10.575 2.808 8.581 1.00 51.47 C ANISOU 268 CB ARG B 39 5888 6647 7021 -818 1466 -552 C ATOM 269 N LYS B 50 2.529 12.586 14.950 1.00 57.56 N ANISOU 269 N LYS B 50 7205 6478 8187 -585 1194 -560 N ATOM 270 CA LYS B 50 3.383 12.297 13.869 1.00 57.04 C ANISOU 270 CA LYS B 50 7231 6281 8161 -671 1186 -566 C ATOM 271 C LYS B 50 4.321 11.421 14.550 1.00 55.96 C ANISOU 271 C LYS B 50 7104 6021 8138 -1351 1235 -657 C ATOM 272 O LYS B 50 5.053 10.737 13.945 1.00 56.97 O ANISOU 272 O LYS B 50 7132 6316 8197 -1338 1366 -658 O ATOM 273 CB LYS B 50 4.057 13.448 13.386 1.00 57.88 C ANISOU 273 CB LYS B 50 7390 6437 8164 -356 1092 -485 C ATOM 274 N ASP B 51 4.259 11.354 15.833 1.00 52.63 N ANISOU 274 N ASP B 51 6725 5228 8043 -2060 1181 -787 N ATOM 275 CA ASP B 51 5.207 10.499 16.408 1.00 49.23 C ANISOU 275 CA ASP B 51 6098 4657 7950 -2821 1225 -856 C ATOM 276 C ASP B 51 4.686 9.008 16.213 1.00 47.47 C ANISOU 276 C ASP B 51 5532 4634 7872 -2866 1554 -1022 C ATOM 277 O ASP B 51 5.433 8.112 16.135 1.00 47.84 O ANISOU 277 O ASP B 51 5392 4828 7958 -3195 1624 -949 O ATOM 278 CB ASP B 51 5.383 10.843 17.843 0.50 49.56 C ANISOU 278 CB ASP B 51 6115 4833 7883 -2618 1020 -885 C ATOM 279 CG ASP B 51 6.646 11.711 18.131 0.50 50.88 C ANISOU 279 CG ASP B 51 6203 5268 7863 -2297 909 -896 C ATOM 280 OD1 ASP B 51 7.222 12.312 17.236 0.50 50.97 O ANISOU 280 OD1 ASP B 51 6118 5365 7881 -2092 925 -894 O ATOM 281 OD2 ASP B 51 7.002 11.751 19.284 0.50 51.77 O ANISOU 281 OD2 ASP B 51 6347 5477 7844 -2185 792 -970 O ATOM 282 N SER B 52 3.382 8.879 16.150 1.00 44.31 N ANISOU 282 N SER B 52 4665 4585 7586 -2560 2010 -1228 N ATOM 283 CA SER B 52 2.752 7.554 16.028 1.00 42.22 C ANISOU 283 CA SER B 52 4565 4169 7307 -2039 2250 -1284 C ATOM 284 C SER B 52 1.412 7.620 15.392 1.00 41.58 C ANISOU 284 C SER B 52 4836 3799 7162 -1883 2355 -1027 C ATOM 285 O SER B 52 0.785 8.611 15.374 1.00 41.63 O ANISOU 285 O SER B 52 5062 3512 7244 -1858 2305 -887 O ATOM 286 CB SER B 52 2.759 6.861 17.328 1.00 43.24 C ANISOU 286 CB SER B 52 4544 4593 7292 -1703 2159 -1549 C ATOM 287 OG SER B 52 1.915 7.433 18.256 1.00 44.41 O ANISOU 287 OG SER B 52 4577 5047 7250 -1532 2221 -1841 O ATOM 288 N TYR B 53 1.006 6.530 14.789 1.00 38.44 N ANISOU 288 N TYR B 53 4487 3224 6893 -2016 2448 -875 N ATOM 289 CA TYR B 53 -0.177 6.520 14.063 1.00 37.84 C ANISOU 289 CA TYR B 53 4501 3143 6734 -1653 2513 -490 C ATOM 290 C TYR B 53 -0.932 5.221 14.494 1.00 35.15 C ANISOU 290 C TYR B 53 4047 3048 6259 -1332 2423 -522 C ATOM 291 O TYR B 53 -0.353 4.259 14.587 1.00 36.14 O ANISOU 291 O TYR B 53 3797 3711 6226 -1311 2330 -363 O ATOM 292 CB TYR B 53 0.021 6.511 12.590 1.00 41.54 C ANISOU 292 CB TYR B 53 4845 3854 7084 -2072 2501 78 C ATOM 293 CG TYR B 53 0.674 7.717 11.992 1.00 44.97 C ANISOU 293 CG TYR B 53 5107 4609 7371 -2311 2579 493 C ATOM 294 CD1 TYR B 53 1.989 7.731 11.718 1.00 44.66 C ANISOU 294 CD1 TYR B 53 4614 4874 7482 -2521 2722 614 C ATOM 295 CD2 TYR B 53 -0.073 8.803 11.686 1.00 47.56 C ANISOU 295 CD2 TYR B 53 5432 5105 7533 -2429 2546 593 C ATOM 296 CE1 TYR B 53 2.590 8.813 11.148 1.00 47.26 C ANISOU 296 CE1 TYR B 53 5147 5225 7586 -2128 2784 652 C ATOM 297 CE2 TYR B 53 0.518 9.899 11.119 1.00 45.88 C ANISOU 297 CE2 TYR B 53 4857 4952 7622 -3301 2843 777 C ATOM 298 CZ TYR B 53 1.894 9.861 10.850 1.00 46.86 C ANISOU 298 CZ TYR B 53 5103 5044 7657 -2760 2881 859 C ATOM 299 OH TYR B 53 2.557 10.983 10.296 1.00 50.35 O ANISOU 299 OH TYR B 53 6075 5233 7821 -2036 2447 713 O ATOM 300 N VAL B 54 -2.199 5.347 14.787 1.00 31.07 N ANISOU 300 N VAL B 54 3701 2299 5806 -1120 2553 -568 N ATOM 301 CA VAL B 54 -2.933 4.245 15.407 1.00 31.54 C ANISOU 301 CA VAL B 54 3771 2653 5560 -910 2379 -507 C ATOM 302 C VAL B 54 -4.029 3.744 14.489 1.00 29.96 C ANISOU 302 C VAL B 54 3572 2222 5588 -1021 2352 -644 C ATOM 303 O VAL B 54 -4.713 4.530 13.827 1.00 31.18 O ANISOU 303 O VAL B 54 3860 2326 5660 -1144 2281 -775 O ATOM 304 CB VAL B 54 -3.538 4.690 16.751 1.00 34.12 C ANISOU 304 CB VAL B 54 4445 3148 5369 -578 1939 -455 C ATOM 305 CG1 VAL B 54 -4.136 3.511 17.432 1.00 32.74 C ANISOU 305 CG1 VAL B 54 4114 3098 5226 -247 2148 19 C ATOM 306 CG2 VAL B 54 -2.473 5.305 17.629 1.00 34.53 C ANISOU 306 CG2 VAL B 54 4499 3218 5401 -719 1562 -491 C ATOM 307 N GLY B 55 -4.203 2.423 14.433 1.00 29.52 N ANISOU 307 N GLY B 55 3555 2129 5532 -828 2397 -564 N ATOM 308 CA GLY B 55 -5.329 1.883 13.677 1.00 31.75 C ANISOU 308 CA GLY B 55 4160 2357 5545 -1077 2221 -375 C ATOM 309 C GLY B 55 -5.269 2.167 12.185 1.00 33.84 C ANISOU 309 C GLY B 55 4768 2420 5672 -980 1731 -243 C ATOM 310 O GLY B 55 -4.208 2.025 11.560 1.00 32.35 O ANISOU 310 O GLY B 55 4364 2307 5621 -851 1566 -183 O ATOM 311 N ASP B 56 -6.331 2.567 11.593 1.00 37.07 N ANISOU 311 N ASP B 56 5450 2765 5870 -1265 1696 -215 N ATOM 312 CA ASP B 56 -6.297 2.823 10.217 1.00 40.46 C ANISOU 312 CA ASP B 56 5922 3322 6127 -1055 1774 58 C ATOM 313 C ASP B 56 -5.371 4.014 9.814 1.00 40.72 C ANISOU 313 C ASP B 56 5753 3457 6261 -1108 1923 312 C ATOM 314 O ASP B 56 -5.062 4.111 8.727 1.00 40.46 O ANISOU 314 O ASP B 56 5682 3568 6124 -1110 1854 721 O ATOM 315 CB ASP B 56 -7.639 2.918 9.566 1.00 43.66 C ANISOU 315 CB ASP B 56 6396 3962 6230 -958 1630 -71 C ATOM 316 CG ASP B 56 -8.208 1.551 9.173 1.00 47.08 C ANISOU 316 CG ASP B 56 6745 4902 6242 -697 1783 -50 C ATOM 317 OD1 ASP B 56 -7.526 0.713 8.543 1.00 47.40 O ANISOU 317 OD1 ASP B 56 6913 4944 6155 -1205 1975 229 O ATOM 318 OD2 ASP B 56 -9.329 1.324 9.531 1.00 48.24 O ANISOU 318 OD2 ASP B 56 6564 5493 6273 -208 1826 -149 O ATOM 319 N GLU B 57 -4.971 4.815 10.750 1.00 40.41 N ANISOU 319 N GLU B 57 5785 3050 6520 -1314 2136 295 N ATOM 320 CA GLU B 57 -4.047 5.915 10.477 1.00 41.51 C ANISOU 320 CA GLU B 57 5765 3170 6839 -1197 2241 215 C ATOM 321 C GLU B 57 -2.770 5.327 10.098 1.00 41.05 C ANISOU 321 C GLU B 57 5463 3205 6928 -934 2310 250 C ATOM 322 O GLU B 57 -2.075 5.880 9.393 1.00 41.10 O ANISOU 322 O GLU B 57 5356 3308 6952 -864 2334 371 O ATOM 323 CB GLU B 57 -3.691 6.696 11.723 1.00 43.25 C ANISOU 323 CB GLU B 57 6327 3062 7045 -974 2223 96 C ATOM 324 CG GLU B 57 -4.674 7.500 12.338 1.00 46.52 C ANISOU 324 CG GLU B 57 6872 3485 7319 -822 2017 66 C ATOM 325 CD GLU B 57 -4.275 8.144 13.720 1.00 48.12 C ANISOU 325 CD GLU B 57 7016 3698 7568 -393 1926 19 C ATOM 326 OE1 GLU B 57 -3.375 7.868 14.527 1.00 44.22 O ANISOU 326 OE1 GLU B 57 6455 2777 7571 -632 1962 265 O ATOM 327 OE2 GLU B 57 -5.026 9.014 14.006 1.00 51.67 O ANISOU 327 OE2 GLU B 57 7559 4325 7747 -257 1637 -17 O ATOM 328 N ALA B 58 -2.453 4.210 10.635 1.00 40.49 N ANISOU 328 N ALA B 58 5289 3095 6999 -751 2198 251 N ATOM 329 CA ALA B 58 -1.242 3.593 10.338 1.00 43.32 C ANISOU 329 CA ALA B 58 5451 3912 7094 -692 1882 143 C ATOM 330 C ALA B 58 -1.303 2.770 9.105 1.00 47.40 C ANISOU 330 C ALA B 58 6029 4756 7223 -259 1692 122 C ATOM 331 O ALA B 58 -0.311 2.422 8.603 1.00 47.61 O ANISOU 331 O ALA B 58 5999 4889 7202 -152 2045 -44 O ATOM 332 CB ALA B 58 -0.850 2.782 11.428 1.00 43.70 C ANISOU 332 CB ALA B 58 5331 4158 7113 -815 1674 -60 C ATOM 333 N GLN B 59 -2.466 2.431 8.644 1.00 51.60 N ANISOU 333 N GLN B 59 6659 5592 7354 84 1198 260 N ATOM 334 CA GLN B 59 -2.663 1.458 7.581 1.00 55.78 C ANISOU 334 CA GLN B 59 7250 6437 7506 451 964 589 C ATOM 335 C GLN B 59 -2.500 2.252 6.370 1.00 58.91 C ANISOU 335 C GLN B 59 7652 7151 7581 559 1011 744 C ATOM 336 O GLN B 59 -1.678 1.963 5.631 1.00 61.31 O ANISOU 336 O GLN B 59 8159 7490 7646 595 692 783 O ATOM 337 CB GLN B 59 -4.015 0.772 7.541 1.00 56.21 C ANISOU 337 CB GLN B 59 7459 6349 7551 483 760 801 C ATOM 338 CG GLN B 59 -4.083 -0.004 6.375 1.00 57.13 C ANISOU 338 CG GLN B 59 7622 6466 7617 782 593 931 C ATOM 339 CD GLN B 59 -5.405 -0.349 6.071 1.00 58.53 C ANISOU 339 CD GLN B 59 7916 6652 7670 1210 534 1083 C ATOM 340 OE1 GLN B 59 -6.248 0.006 6.781 1.00 56.44 O ANISOU 340 OE1 GLN B 59 7575 6175 7693 1797 636 1184 O ATOM 341 NE2 GLN B 59 -5.608 -1.109 4.995 1.00 60.50 N ANISOU 341 NE2 GLN B 59 8245 7058 7685 1294 407 1144 N ATOM 342 N SER B 60 -3.216 3.318 6.229 1.00 59.83 N ANISOU 342 N SER B 60 7682 7389 7663 775 1091 786 N ATOM 343 CA SER B 60 -2.927 4.307 5.225 1.00 61.09 C ANISOU 343 CA SER B 60 7805 7576 7829 788 993 741 C ATOM 344 C SER B 60 -1.449 4.542 4.986 1.00 62.27 C ANISOU 344 C SER B 60 7984 7742 7933 765 835 688 C ATOM 345 O SER B 60 -0.631 4.309 5.844 1.00 63.27 O ANISOU 345 O SER B 60 8133 7926 7981 675 693 584 O ATOM 346 CB SER B 60 -3.580 5.581 5.540 1.00 61.06 C ANISOU 346 CB SER B 60 7758 7601 7841 777 1069 728 C ATOM 347 N ILE B 64 6.334 3.265 4.794 1.00 51.31 N ANISOU 347 N ILE B 64 6698 6290 6507 -1659 845 -322 N ATOM 348 CA ILE B 64 6.747 4.477 5.509 1.00 51.37 C ANISOU 348 CA ILE B 64 6525 6422 6570 -1460 950 -313 C ATOM 349 C ILE B 64 6.802 4.216 7.014 1.00 48.43 C ANISOU 349 C ILE B 64 5587 6200 6614 -1794 1265 -316 C ATOM 350 O ILE B 64 7.666 4.752 7.718 1.00 47.92 O ANISOU 350 O ILE B 64 5323 6169 6717 -2036 1195 -312 O ATOM 351 CB ILE B 64 5.822 5.694 5.211 1.00 51.88 C ANISOU 351 CB ILE B 64 6806 6349 6557 -953 860 -268 C ATOM 352 N LEU B 65 5.890 3.371 7.496 1.00 44.79 N ANISOU 352 N LEU B 65 4561 5882 6574 -1791 1603 -386 N ATOM 353 CA LEU B 65 5.811 3.062 8.921 1.00 44.05 C ANISOU 353 CA LEU B 65 4352 5872 6513 -1153 1598 -552 C ATOM 354 C LEU B 65 6.149 1.613 9.242 1.00 44.09 C ANISOU 354 C LEU B 65 4238 6010 6503 -1183 1591 -427 C ATOM 355 O LEU B 65 5.844 0.699 8.465 1.00 47.42 O ANISOU 355 O LEU B 65 5098 6281 6639 -609 1605 -536 O ATOM 356 CB LEU B 65 4.404 3.374 9.460 1.00 43.24 C ANISOU 356 CB LEU B 65 4226 5689 6515 -829 1661 -695 C ATOM 357 CG LEU B 65 3.827 4.774 9.247 1.00 43.37 C ANISOU 357 CG LEU B 65 4306 5627 6547 -198 1665 -1083 C ATOM 358 CD1 LEU B 65 2.323 4.768 9.482 1.00 44.36 C ANISOU 358 CD1 LEU B 65 4449 5816 6590 -59 1586 -1245 C ATOM 359 CD2 LEU B 65 4.524 5.771 10.152 1.00 42.11 C ANISOU 359 CD2 LEU B 65 4120 5314 6566 -59 1615 -1101 C ATOM 360 N THR B 66 6.765 1.408 10.397 1.00 40.90 N ANISOU 360 N THR B 66 3428 5808 6305 -1339 1930 -179 N ATOM 361 CA THR B 66 6.875 0.069 10.978 1.00 39.75 C ANISOU 361 CA THR B 66 3160 5728 6214 -1178 1819 -299 C ATOM 362 C THR B 66 5.711 -0.138 11.960 1.00 35.76 C ANISOU 362 C THR B 66 3186 4525 5874 -996 1758 -576 C ATOM 363 O THR B 66 5.334 0.756 12.714 1.00 32.66 O ANISOU 363 O THR B 66 2552 4032 5827 -992 1763 -611 O ATOM 364 CB THR B 66 8.218 -0.156 11.690 1.00 42.00 C ANISOU 364 CB THR B 66 2707 6818 6433 -1079 1634 -252 C ATOM 365 OG1 THR B 66 8.447 0.907 12.617 1.00 46.48 O ANISOU 365 OG1 THR B 66 3678 7434 6549 -756 1215 -178 O ATOM 366 CG2 THR B 66 9.375 -0.186 10.665 1.00 41.89 C ANISOU 366 CG2 THR B 66 2399 6976 6541 -1952 1865 -78 C ATOM 367 N LEU B 67 5.119 -1.319 11.899 1.00 32.50 N ANISOU 367 N LEU B 67 2736 4006 5607 -913 1892 -540 N ATOM 368 CA LEU B 67 3.915 -1.604 12.646 1.00 31.15 C ANISOU 368 CA LEU B 67 2733 3732 5372 -830 1414 -668 C ATOM 369 C LEU B 67 4.219 -2.440 13.865 1.00 31.22 C ANISOU 369 C LEU B 67 2557 4066 5240 -813 1227 -519 C ATOM 370 O LEU B 67 5.076 -3.344 13.834 1.00 31.24 O ANISOU 370 O LEU B 67 2517 4003 5351 -750 1195 -395 O ATOM 371 CB LEU B 67 2.923 -2.341 11.736 1.00 30.82 C ANISOU 371 CB LEU B 67 2828 3503 5378 -1152 1070 -596 C ATOM 372 CG LEU B 67 2.417 -1.612 10.486 1.00 32.08 C ANISOU 372 CG LEU B 67 3266 3608 5314 -647 1117 -575 C ATOM 373 CD1 LEU B 67 1.438 -2.501 9.684 1.00 31.81 C ANISOU 373 CD1 LEU B 67 3100 3671 5317 -1162 779 -578 C ATOM 374 CD2 LEU B 67 1.780 -0.226 10.800 1.00 32.97 C ANISOU 374 CD2 LEU B 67 3635 3529 5361 -519 1235 -498 C ATOM 375 N LYS B 68 3.521 -2.128 14.955 1.00 29.21 N ANISOU 375 N LYS B 68 1967 4214 4917 -1295 1042 -474 N ATOM 376 CA ALYS B 68 3.569 -2.928 16.164 0.50 28.54 C ANISOU 376 CA ALYS B 68 2010 4022 4811 -1522 814 -391 C ATOM 377 CA BLYS B 68 3.569 -2.995 16.107 0.50 28.72 C ANISOU 377 CA BLYS B 68 1981 4023 4910 -1351 938 -413 C ATOM 378 C LYS B 68 2.135 -3.355 16.466 1.00 27.24 C ANISOU 378 C LYS B 68 2021 3612 4716 -1268 790 -438 C ATOM 379 O LYS B 68 1.240 -2.534 16.359 1.00 26.17 O ANISOU 379 O LYS B 68 1889 3285 4767 -1071 813 -245 O ATOM 380 CB ALYS B 68 4.081 -2.100 17.352 0.50 28.39 C ANISOU 380 CB ALYS B 68 2216 3842 4728 -1750 572 -625 C ATOM 381 CB BLYS B 68 4.297 -2.348 17.297 0.50 29.25 C ANISOU 381 CB BLYS B 68 2132 3937 5047 -1148 966 -647 C ATOM 382 CG ALYS B 68 5.563 -1.726 17.308 0.50 30.67 C ANISOU 382 CG ALYS B 68 2738 4114 4800 -2244 243 -687 C ATOM 383 CG BLYS B 68 5.840 -2.228 17.100 0.50 31.99 C ANISOU 383 CG BLYS B 68 2628 4230 5296 -1297 922 -739 C ATOM 384 CD ALYS B 68 6.031 -1.198 18.668 0.50 33.79 C ANISOU 384 CD ALYS B 68 3239 4802 4797 -1896 207 -766 C ATOM 385 CD BLYS B 68 6.219 -0.790 16.784 0.50 35.11 C ANISOU 385 CD BLYS B 68 3000 4891 5451 -905 1097 -603 C ATOM 386 CE ALYS B 68 7.542 -1.067 18.704 0.50 35.29 C ANISOU 386 CE ALYS B 68 3329 5286 4792 -1871 79 -865 C ATOM 387 CE BLYS B 68 7.542 -0.631 16.027 0.50 35.27 C ANISOU 387 CE BLYS B 68 2844 4986 5571 -554 931 -658 C ATOM 388 NZ ALYS B 68 8.033 -0.986 20.107 0.50 36.07 N ANISOU 388 NZ ALYS B 68 3316 5638 4750 -1763 -90 -906 N ATOM 389 NZ BLYS B 68 7.567 0.672 15.296 0.50 33.00 N ANISOU 389 NZ BLYS B 68 2268 4703 5570 -397 890 -729 N ATOM 390 N TYR B 69 1.951 -4.611 16.844 1.00 23.12 N ANISOU 390 N TYR B 69 1759 2787 4240 -1270 837 -278 N ATOM 391 CA TYR B 69 0.642 -5.103 17.308 1.00 20.90 C ANISOU 391 CA TYR B 69 1418 2471 4053 -905 576 -369 C ATOM 392 C TYR B 69 0.720 -5.266 18.827 1.00 21.94 C ANISOU 392 C TYR B 69 1808 2402 4128 -313 440 -469 C ATOM 393 O TYR B 69 1.483 -6.113 19.321 1.00 24.44 O ANISOU 393 O TYR B 69 1828 2991 4467 -65 334 -307 O ATOM 394 CB TYR B 69 0.395 -6.471 16.725 1.00 21.87 C ANISOU 394 CB TYR B 69 1776 2606 3928 -583 530 -463 C ATOM 395 CG TYR B 69 0.260 -6.569 15.222 1.00 20.03 C ANISOU 395 CG TYR B 69 1461 2330 3821 -872 656 -423 C ATOM 396 CD1 TYR B 69 1.385 -6.504 14.379 1.00 22.74 C ANISOU 396 CD1 TYR B 69 2003 2711 3928 -184 710 -240 C ATOM 397 CD2 TYR B 69 -0.978 -6.811 14.631 1.00 19.05 C ANISOU 397 CD2 TYR B 69 1053 2436 3750 -1031 267 -415 C ATOM 398 CE1 TYR B 69 1.260 -6.637 12.992 1.00 22.59 C ANISOU 398 CE1 TYR B 69 2009 2664 3910 63 584 -88 C ATOM 399 CE2 TYR B 69 -1.131 -6.950 13.227 1.00 19.26 C ANISOU 399 CE2 TYR B 69 1215 2474 3630 -95 656 -293 C ATOM 400 CZ TYR B 69 0.011 -6.864 12.409 1.00 21.17 C ANISOU 400 CZ TYR B 69 1378 2867 3800 82 748 -53 C ATOM 401 OH TYR B 69 -0.153 -7.019 11.050 1.00 21.44 O ANISOU 401 OH TYR B 69 1362 2922 3860 -140 742 -80 O ATOM 402 N PRO B 70 -0.048 -4.464 19.589 1.00 20.52 N ANISOU 402 N PRO B 70 1739 2075 3982 -491 659 -306 N ATOM 403 CA PRO B 70 0.098 -4.500 21.050 1.00 22.37 C ANISOU 403 CA PRO B 70 2112 2535 3853 -221 515 -325 C ATOM 404 C PRO B 70 -0.505 -5.764 21.684 1.00 21.21 C ANISOU 404 C PRO B 70 2166 2292 3601 -547 341 -572 C ATOM 405 O PRO B 70 -0.257 -6.048 22.853 1.00 20.26 O ANISOU 405 O PRO B 70 1289 2888 3520 -183 160 -601 O ATOM 406 CB PRO B 70 -0.688 -3.267 21.523 1.00 21.63 C ANISOU 406 CB PRO B 70 1829 2516 3873 -289 236 -254 C ATOM 407 CG PRO B 70 -1.393 -2.753 20.393 1.00 26.30 C ANISOU 407 CG PRO B 70 2693 3306 3993 39 230 -263 C ATOM 408 CD PRO B 70 -0.839 -3.311 19.125 1.00 21.30 C ANISOU 408 CD PRO B 70 1633 2551 3910 -276 615 -312 C ATOM 409 N ILE B 71 -1.306 -6.502 20.911 1.00 19.16 N ANISOU 409 N ILE B 71 1752 2051 3476 -590 377 -296 N ATOM 410 CA ILE B 71 -1.825 -7.770 21.384 1.00 17.46 C ANISOU 410 CA ILE B 71 1044 2041 3551 -430 -78 -433 C ATOM 411 C ILE B 71 -1.212 -8.854 20.512 1.00 20.25 C ANISOU 411 C ILE B 71 1499 2473 3723 135 -14 -281 C ATOM 412 O ILE B 71 -1.305 -8.807 19.269 1.00 20.85 O ANISOU 412 O ILE B 71 1845 2220 3857 -281 56 -202 O ATOM 413 CB ILE B 71 -3.402 -7.808 21.289 1.00 16.44 C ANISOU 413 CB ILE B 71 997 1644 3605 -506 294 -388 C ATOM 414 CG1 ILE B 71 -3.948 -6.811 22.294 1.00 18.99 C ANISOU 414 CG1 ILE B 71 1318 2143 3755 107 264 -921 C ATOM 415 CG2 ILE B 71 -3.969 -9.243 21.521 1.00 19.94 C ANISOU 415 CG2 ILE B 71 1661 2453 3463 -980 416 -391 C ATOM 416 CD1 ILE B 71 -5.460 -6.761 22.322 1.00 21.15 C ANISOU 416 CD1 ILE B 71 1501 2649 3885 578 227 -845 C ATOM 417 N GLU B 72 -0.596 -9.811 21.191 1.00 19.61 N ANISOU 417 N GLU B 72 1293 2269 3890 312 223 -173 N ATOM 418 CA AGLU B 72 0.006 -10.973 20.554 0.70 18.04 C ANISOU 418 CA AGLU B 72 518 2256 4079 -569 287 -333 C ATOM 419 CA BGLU B 72 -0.001 -10.972 20.560 0.30 21.52 C ANISOU 419 CA BGLU B 72 1324 2833 4020 -20 285 -75 C ATOM 420 C GLU B 72 -0.691 -12.216 21.075 1.00 19.22 C ANISOU 420 C GLU B 72 925 2415 3961 -165 372 -93 C ATOM 421 O GLU B 72 -0.770 -12.433 22.311 1.00 20.30 O ANISOU 421 O GLU B 72 1615 2101 3996 388 417 -274 O ATOM 422 CB AGLU B 72 1.496 -11.099 20.903 0.70 20.31 C ANISOU 422 CB AGLU B 72 881 2592 4244 -860 164 -282 C ATOM 423 CB BGLU B 72 1.481 -11.071 20.904 0.30 26.12 C ANISOU 423 CB BGLU B 72 2015 3761 4147 -225 196 162 C ATOM 424 CG AGLU B 72 2.342 -9.938 20.469 0.70 20.44 C ANISOU 424 CG AGLU B 72 671 2816 4279 167 625 -418 C ATOM 425 CG BGLU B 72 2.395 -10.393 19.934 0.30 29.88 C ANISOU 425 CG BGLU B 72 2543 4569 4241 -41 268 401 C ATOM 426 CD AGLU B 72 3.748 -10.059 20.997 0.70 25.86 C ANISOU 426 CD AGLU B 72 1251 4203 4373 -135 431 -418 C ATOM 427 CD BGLU B 72 3.804 -10.932 20.063 0.30 31.38 C ANISOU 427 CD BGLU B 72 2527 5117 4280 65 295 589 C ATOM 428 OE1AGLU B 72 3.976 -9.640 22.137 0.70 25.59 O ANISOU 428 OE1AGLU B 72 1090 4401 4230 -432 -135 -419 O ATOM 429 OE1BGLU B 72 4.071 -11.641 21.060 0.30 31.39 O ANISOU 429 OE1BGLU B 72 2449 5125 4353 161 260 739 O ATOM 430 OE2AGLU B 72 4.613 -10.599 20.274 0.70 29.76 O ANISOU 430 OE2AGLU B 72 1544 5249 4512 -296 476 -272 O ATOM 431 OE2BGLU B 72 4.633 -10.645 19.179 0.30 33.16 O ANISOU 431 OE2BGLU B 72 2871 5466 4261 58 294 629 O ATOM 432 N HIS B 73 -1.184 -13.020 20.151 1.00 19.02 N ANISOU 432 N HIS B 73 1227 2257 3745 -47 136 -343 N ATOM 433 CA HIS B 73 -1.854 -14.280 20.475 1.00 17.62 C ANISOU 433 CA HIS B 73 1140 1906 3649 154 83 134 C ATOM 434 C HIS B 73 -2.942 -14.030 21.497 1.00 16.43 C ANISOU 434 C HIS B 73 1354 1563 3327 -61 98 224 C ATOM 435 O HIS B 73 -3.137 -14.833 22.409 1.00 17.16 O ANISOU 435 O HIS B 73 1618 1602 3300 -124 24 363 O ATOM 436 CB HIS B 73 -0.871 -15.335 21.006 1.00 18.36 C ANISOU 436 CB HIS B 73 749 2325 3901 733 206 -97 C ATOM 437 CG HIS B 73 0.318 -15.532 20.123 1.00 19.42 C ANISOU 437 CG HIS B 73 607 2799 3973 517 -165 -167 C ATOM 438 ND1 HIS B 73 0.197 -15.982 18.823 1.00 20.70 N ANISOU 438 ND1 HIS B 73 1102 2875 3888 222 28 -431 N ATOM 439 CD2 HIS B 73 1.640 -15.337 20.341 1.00 24.95 C ANISOU 439 CD2 HIS B 73 2006 3351 4123 623 -248 -145 C ATOM 440 CE1 HIS B 73 1.401 -16.065 18.281 1.00 25.25 C ANISOU 440 CE1 HIS B 73 2127 3509 3958 125 -77 -490 C ATOM 441 NE2 HIS B 73 2.290 -15.686 19.184 1.00 27.16 N ANISOU 441 NE2 HIS B 73 2540 3696 4085 457 -123 -455 N ATOM 442 N GLY B 74 -3.615 -12.895 21.367 1.00 16.09 N ANISOU 442 N GLY B 74 1369 1582 3160 -128 341 -111 N ATOM 443 CA GLY B 74 -4.785 -12.595 22.201 1.00 15.37 C ANISOU 443 CA GLY B 74 1314 1593 2933 -223 189 -132 C ATOM 444 C GLY B 74 -4.475 -11.961 23.553 1.00 15.63 C ANISOU 444 C GLY B 74 1500 1510 2929 -114 -23 -294 C ATOM 445 O GLY B 74 -5.368 -11.513 24.256 1.00 16.63 O ANISOU 445 O GLY B 74 1540 1727 3053 -149 306 -12 O ATOM 446 N ILE B 75 -3.196 -11.883 23.905 1.00 17.58 N ANISOU 446 N ILE B 75 1496 2162 3022 -149 -366 -156 N ATOM 447 CA ILE B 75 -2.794 -11.357 25.231 1.00 18.76 C ANISOU 447 CA ILE B 75 1608 2220 3299 322 -342 -260 C ATOM 448 C ILE B 75 -2.192 -9.984 25.017 1.00 19.67 C ANISOU 448 C ILE B 75 1726 2234 3514 -249 -382 -262 C ATOM 449 O ILE B 75 -1.409 -9.799 24.070 1.00 19.64 O ANISOU 449 O ILE B 75 1549 2444 3468 -241 -177 -204 O ATOM 450 CB ILE B 75 -1.775 -12.267 25.950 1.00 19.98 C ANISOU 450 CB ILE B 75 1428 2746 3416 -307 -618 -324 C ATOM 451 CG1 ILE B 75 -2.273 -13.711 26.017 1.00 21.23 C ANISOU 451 CG1 ILE B 75 1933 2609 3525 -52 -101 -406 C ATOM 452 CG2 ILE B 75 -1.322 -11.674 27.328 1.00 21.32 C ANISOU 452 CG2 ILE B 75 1637 3156 3306 -256 -696 -169 C ATOM 453 CD1 ILE B 75 -3.620 -13.921 26.742 1.00 23.29 C ANISOU 453 CD1 ILE B 75 2166 3154 3531 253 230 -129 C ATOM 454 N ILE B 76 -2.590 -9.006 25.845 1.00 19.15 N ANISOU 454 N ILE B 76 1634 1812 3831 -617 -289 -449 N ATOM 455 CA ILE B 76 -1.984 -7.662 25.725 1.00 19.26 C ANISOU 455 CA ILE B 76 1012 2140 4168 -173 -296 -425 C ATOM 456 C ILE B 76 -0.543 -7.743 26.223 1.00 22.80 C ANISOU 456 C ILE B 76 1626 2577 4460 -251 -380 -615 C ATOM 457 O ILE B 76 -0.309 -8.173 27.351 1.00 24.85 O ANISOU 457 O ILE B 76 1925 3044 4472 -618 -502 -318 O ATOM 458 CB ILE B 76 -2.770 -6.632 26.551 1.00 20.36 C ANISOU 458 CB ILE B 76 1514 2230 3990 -1 279 -523 C ATOM 459 CG1 ILE B 76 -4.239 -6.556 26.060 1.00 21.14 C ANISOU 459 CG1 ILE B 76 1584 2385 4064 274 795 -386 C ATOM 460 CG2 ILE B 76 -2.069 -5.242 26.499 1.00 20.57 C ANISOU 460 CG2 ILE B 76 1418 2411 3987 -225 583 -201 C ATOM 461 CD1 ILE B 76 -5.209 -5.858 27.032 1.00 20.78 C ANISOU 461 CD1 ILE B 76 1298 2551 4049 135 780 -335 C ATOM 462 N ATHR B 77 0.397 -7.351 25.371 0.40 25.18 N ANISOU 462 N ATHR B 77 2113 2818 4636 -539 -436 -822 N ATOM 463 N BTHR B 77 0.402 -7.347 25.364 0.60 23.73 N ANISOU 463 N BTHR B 77 1763 2631 4622 -416 -220 -771 N ATOM 464 CA ATHR B 77 1.816 -7.360 25.752 0.40 28.22 C ANISOU 464 CA ATHR B 77 2716 3181 4824 -720 -543 -791 C ATOM 465 CA BTHR B 77 1.854 -7.381 25.696 0.60 25.51 C ANISOU 465 CA BTHR B 77 2054 2833 4807 -553 -179 -640 C ATOM 466 C ATHR B 77 2.390 -5.949 25.880 0.40 28.42 C ANISOU 466 C ATHR B 77 2754 3141 4903 -889 -361 -672 C ATOM 467 C BTHR B 77 2.581 -6.043 25.566 0.60 25.83 C ANISOU 467 C BTHR B 77 1797 3115 4903 -525 -194 -612 C ATOM 468 O ATHR B 77 3.247 -5.701 26.746 0.40 29.15 O ANISOU 468 O ATHR B 77 2998 3151 4926 -848 -310 -678 O ATOM 469 O BTHR B 77 3.750 -5.940 25.932 0.60 26.81 O ANISOU 469 O BTHR B 77 1672 3512 5003 -442 -234 -536 O ATOM 470 CB ATHR B 77 2.672 -8.210 24.799 0.40 29.56 C ANISOU 470 CB ATHR B 77 2679 3634 4916 -675 -699 -744 C ATOM 471 CB BTHR B 77 2.628 -8.399 24.858 0.60 23.41 C ANISOU 471 CB BTHR B 77 1146 2874 4873 -729 139 -318 C ATOM 472 OG1ATHR B 77 2.125 -9.537 24.729 0.40 32.20 O ANISOU 472 OG1ATHR B 77 3328 3897 5008 -446 -689 -729 O ATOM 473 OG1BTHR B 77 2.584 -8.005 23.481 0.60 22.64 O ANISOU 473 OG1BTHR B 77 1110 2602 4892 -140 711 160 O ATOM 474 CG2ATHR B 77 4.108 -8.285 25.319 0.40 30.15 C ANISOU 474 CG2ATHR B 77 2691 3831 4934 -425 -560 -583 C ATOM 475 CG2BTHR B 77 2.043 -9.829 25.052 0.60 24.80 C ANISOU 475 CG2BTHR B 77 1739 2779 4906 -1105 343 -261 C ATOM 476 N ASN B 78 1.895 -5.033 25.047 1.00 26.73 N ANISOU 476 N ASN B 78 2336 2897 4924 -668 -104 -747 N ATOM 477 CA ASN B 78 2.416 -3.672 25.006 1.00 26.01 C ANISOU 477 CA ASN B 78 2054 2786 5043 -589 308 -525 C ATOM 478 C ASN B 78 1.328 -2.734 25.536 1.00 26.13 C ANISOU 478 C ASN B 78 2159 2789 4978 -290 4 -589 C ATOM 479 O ASN B 78 0.435 -2.313 24.785 1.00 25.52 O ANISOU 479 O ASN B 78 1886 2959 4851 14 -390 -731 O ATOM 480 CB ASN B 78 2.848 -3.264 23.589 1.00 25.94 C ANISOU 480 CB ASN B 78 1519 3041 5295 -1079 90 -350 C ATOM 481 CG ASN B 78 3.609 -1.918 23.571 1.00 27.92 C ANISOU 481 CG ASN B 78 1644 3392 5572 -647 595 -389 C ATOM 482 OD1 ASN B 78 3.208 -0.949 24.241 1.00 28.24 O ANISOU 482 OD1 ASN B 78 1882 3103 5743 -722 633 -811 O ATOM 483 ND2 ASN B 78 4.710 -1.867 22.815 1.00 32.30 N ANISOU 483 ND2 ASN B 78 2831 3802 5641 -687 520 -453 N ATOM 484 N TRP B 79 1.424 -2.399 26.823 1.00 26.64 N ANISOU 484 N TRP B 79 2334 2879 4910 -696 -7 -775 N ATOM 485 CA TRP B 79 0.400 -1.593 27.486 1.00 27.02 C ANISOU 485 CA TRP B 79 2443 2983 4840 -1004 -120 -682 C ATOM 486 C TRP B 79 0.337 -0.129 27.041 1.00 26.57 C ANISOU 486 C TRP B 79 2482 2606 5008 -1053 -22 -628 C ATOM 487 O TRP B 79 -0.741 0.456 27.019 1.00 27.85 O ANISOU 487 O TRP B 79 2849 2626 5107 -346 -156 -410 O ATOM 488 CB TRP B 79 0.504 -1.708 29.011 1.00 25.27 C ANISOU 488 CB TRP B 79 1869 3251 4481 -1151 -719 -543 C ATOM 489 CG TRP B 79 0.157 -3.059 29.465 1.00 26.16 C ANISOU 489 CG TRP B 79 2169 3427 4344 -514 -488 -466 C ATOM 490 CD1 TRP B 79 1.014 -4.109 29.667 1.00 27.06 C ANISOU 490 CD1 TRP B 79 2313 3603 4367 -131 -251 -150 C ATOM 491 CD2 TRP B 79 -1.167 -3.568 29.690 1.00 23.39 C ANISOU 491 CD2 TRP B 79 1522 3196 4170 -380 -58 -353 C ATOM 492 NE1 TRP B 79 0.307 -5.236 30.036 1.00 26.35 N ANISOU 492 NE1 TRP B 79 2095 3518 4401 -529 -107 -176 N ATOM 493 CE2 TRP B 79 -1.034 -4.928 30.064 1.00 23.19 C ANISOU 493 CE2 TRP B 79 1221 3345 4243 -707 -184 -151 C ATOM 494 CE3 TRP B 79 -2.458 -3.002 29.620 1.00 25.18 C ANISOU 494 CE3 TRP B 79 2184 3384 4002 -87 439 -410 C ATOM 495 CZ2 TRP B 79 -2.146 -5.741 30.362 1.00 23.70 C ANISOU 495 CZ2 TRP B 79 1385 3542 4078 -423 -27 -275 C ATOM 496 CZ3 TRP B 79 -3.566 -3.821 29.914 1.00 25.99 C ANISOU 496 CZ3 TRP B 79 2406 3443 4025 270 501 -199 C ATOM 497 CH2 TRP B 79 -3.393 -5.179 30.288 1.00 24.96 C ANISOU 497 CH2 TRP B 79 1849 3655 3978 -85 238 -146 C ATOM 498 N ASP B 80 1.484 0.474 26.705 1.00 26.46 N ANISOU 498 N ASP B 80 2283 2645 5126 -1294 318 -721 N ATOM 499 CA ASP B 80 1.415 1.855 26.262 1.00 28.68 C ANISOU 499 CA ASP B 80 2777 2754 5366 -1647 573 -725 C ATOM 500 C ASP B 80 0.708 1.953 24.937 1.00 26.68 C ANISOU 500 C ASP B 80 2434 2408 5296 -1131 615 -864 C ATOM 501 O ASP B 80 -0.133 2.823 24.736 1.00 28.45 O ANISOU 501 O ASP B 80 3016 2480 5315 -823 982 -814 O ATOM 502 CB ASP B 80 2.813 2.485 26.154 1.00 32.83 C ANISOU 502 CB ASP B 80 3131 3639 5705 -2220 441 -542 C ATOM 503 CG ASP B 80 3.411 2.815 27.502 1.00 39.08 C ANISOU 503 CG ASP B 80 3931 4825 6094 -1968 431 -399 C ATOM 504 OD1 ASP B 80 2.714 2.714 28.540 1.00 41.97 O ANISOU 504 OD1 ASP B 80 4388 5325 6234 -1520 206 -281 O ATOM 505 OD2 ASP B 80 4.615 3.174 27.521 1.00 43.48 O ANISOU 505 OD2 ASP B 80 4810 5370 6340 -1599 395 -297 O ATOM 506 N ASP B 81 1.024 1.033 24.023 1.00 25.55 N ANISOU 506 N ASP B 81 1925 2552 5232 -879 499 -1111 N ATOM 507 CA ASP B 81 0.377 1.049 22.735 1.00 27.20 C ANISOU 507 CA ASP B 81 2593 2614 5126 -565 668 -1069 C ATOM 508 C ASP B 81 -1.078 0.559 22.888 1.00 23.82 C ANISOU 508 C ASP B 81 1941 2266 4844 -588 739 -881 C ATOM 509 O ASP B 81 -1.960 1.002 22.163 1.00 23.41 O ANISOU 509 O ASP B 81 1759 2325 4811 -660 904 -350 O ATOM 510 CB ASP B 81 1.162 0.233 21.684 1.00 27.38 C ANISOU 510 CB ASP B 81 2065 2999 5339 -373 740 -1199 C ATOM 511 CG ASP B 81 2.361 0.984 21.146 1.00 30.51 C ANISOU 511 CG ASP B 81 2657 3419 5519 -482 1052 -1120 C ATOM 512 OD1 ASP B 81 2.544 2.171 21.497 1.00 30.32 O ANISOU 512 OD1 ASP B 81 2479 3471 5571 -672 845 -1095 O ATOM 513 OD2 ASP B 81 3.134 0.380 20.376 1.00 32.83 O ANISOU 513 OD2 ASP B 81 3300 3461 5715 -733 836 -812 O ATOM 514 N MET B 82 -1.332 -0.314 23.847 1.00 23.05 N ANISOU 514 N MET B 82 1982 2138 4638 -743 703 -667 N ATOM 515 CA MET B 82 -2.750 -0.720 24.073 1.00 22.05 C ANISOU 515 CA MET B 82 1749 2007 4623 -399 255 -668 C ATOM 516 C MET B 82 -3.588 0.465 24.521 1.00 21.89 C ANISOU 516 C MET B 82 1775 1993 4550 -647 359 -653 C ATOM 517 O MET B 82 -4.714 0.660 24.062 1.00 21.84 O ANISOU 517 O MET B 82 1749 2045 4505 -450 510 -427 O ATOM 518 CB MET B 82 -2.885 -1.838 25.107 1.00 22.71 C ANISOU 518 CB MET B 82 1807 2157 4665 -947 159 -586 C ATOM 519 CG MET B 82 -4.306 -2.488 25.136 1.00 21.99 C ANISOU 519 CG MET B 82 1719 1943 4693 -322 265 -737 C ATOM 520 SD MET B 82 -4.538 -3.371 23.587 1.00 24.21 S ANISOU 520 SD MET B 82 2146 2065 4988 -397 -55 -919 S ATOM 521 CE MET B 82 -6.289 -3.063 23.281 1.00 22.50 C ANISOU 521 CE MET B 82 1612 2178 4761 -228 -222 -427 C ATOM 522 N GLU B 83 -3.022 1.277 25.411 1.00 21.87 N ANISOU 522 N GLU B 83 1754 2043 4513 -627 400 -772 N ATOM 523 CA GLU B 83 -3.678 2.508 25.818 1.00 23.48 C ANISOU 523 CA GLU B 83 2353 2027 4540 -899 392 -843 C ATOM 524 C GLU B 83 -3.931 3.427 24.626 1.00 23.49 C ANISOU 524 C GLU B 83 2585 1972 4369 -1354 781 -570 C ATOM 525 O GLU B 83 -4.981 4.024 24.528 1.00 23.26 O ANISOU 525 O GLU B 83 2658 2041 4139 -802 757 -490 O ATOM 526 CB GLU B 83 -2.865 3.207 26.908 1.00 26.56 C ANISOU 526 CB GLU B 83 2661 2577 4852 -1048 397 -1367 C ATOM 527 CG GLU B 83 -3.517 4.449 27.381 1.00 34.57 C ANISOU 527 CG GLU B 83 4184 3751 5199 -874 261 -1718 C ATOM 528 CD GLU B 83 -2.864 4.998 28.637 1.00 40.92 C ANISOU 528 CD GLU B 83 5353 4660 5536 -830 91 -2054 C ATOM 529 OE1 GLU B 83 -2.443 4.190 29.501 1.00 43.33 O ANISOU 529 OE1 GLU B 83 5672 5169 5622 -227 135 -2258 O ATOM 530 OE2 GLU B 83 -2.807 6.247 28.735 1.00 45.20 O ANISOU 530 OE2 GLU B 83 5920 5533 5721 -1028 147 -2044 O ATOM 531 N LYS B 84 -2.965 3.512 23.698 1.00 22.31 N ANISOU 531 N LYS B 84 2046 2039 4393 -1238 1115 -246 N ATOM 532 CA LYS B 84 -3.176 4.263 22.447 1.00 22.44 C ANISOU 532 CA LYS B 84 1948 2167 4409 -875 1311 -360 C ATOM 533 C LYS B 84 -4.338 3.657 21.656 1.00 21.87 C ANISOU 533 C LYS B 84 2159 1861 4291 -666 1132 -312 C ATOM 534 O LYS B 84 -5.174 4.348 21.048 1.00 21.15 O ANISOU 534 O LYS B 84 2094 1797 4146 -638 970 -249 O ATOM 535 CB LYS B 84 -1.903 4.319 21.569 1.00 24.18 C ANISOU 535 CB LYS B 84 2200 2273 4713 -1335 1381 -168 C ATOM 536 CG LYS B 84 -0.803 5.173 22.194 1.00 28.27 C ANISOU 536 CG LYS B 84 2687 3096 4960 -1941 1122 -219 C ATOM 537 CD LYS B 84 0.439 5.273 21.278 1.00 32.71 C ANISOU 537 CD LYS B 84 2775 4521 5132 -1853 1074 -354 C ATOM 538 CE LYS B 84 1.702 5.820 22.047 1.00 37.63 C ANISOU 538 CE LYS B 84 3026 5935 5336 -2136 881 -255 C ATOM 539 NZ LYS B 84 2.395 4.810 22.955 1.00 41.04 N ANISOU 539 NZ LYS B 84 3446 6791 5357 -2398 950 -362 N ATOM 540 N ILE B 85 -4.399 2.322 21.631 1.00 21.18 N ANISOU 540 N ILE B 85 2404 1360 4285 -857 1214 -322 N ATOM 541 CA ILE B 85 -5.476 1.691 20.899 1.00 20.02 C ANISOU 541 CA ILE B 85 2088 1339 4180 -592 1002 -475 C ATOM 542 C ILE B 85 -6.848 1.994 21.529 1.00 17.76 C ANISOU 542 C ILE B 85 1452 1459 3835 -308 701 -325 C ATOM 543 O ILE B 85 -7.823 2.270 20.819 1.00 18.50 O ANISOU 543 O ILE B 85 1761 1552 3715 2 1034 -264 O ATOM 544 CB ILE B 85 -5.252 0.137 20.821 1.00 18.76 C ANISOU 544 CB ILE B 85 1287 1406 4436 -881 922 -483 C ATOM 545 CG1 ILE B 85 -4.184 -0.209 19.778 1.00 25.64 C ANISOU 545 CG1 ILE B 85 2188 3059 4494 -875 1201 -354 C ATOM 546 CG2 ILE B 85 -6.561 -0.611 20.460 1.00 19.57 C ANISOU 546 CG2 ILE B 85 1378 1572 4488 -455 662 -420 C ATOM 547 CD1 ILE B 85 -4.612 0.141 18.397 1.00 28.06 C ANISOU 547 CD1 ILE B 85 2631 3513 4519 -268 1737 -283 C ATOM 548 N TRP B 86 -6.913 1.931 22.852 1.00 17.18 N ANISOU 548 N TRP B 86 1559 1478 3492 -322 541 -328 N ATOM 549 CA TRP B 86 -8.185 2.262 23.523 1.00 16.90 C ANISOU 549 CA TRP B 86 1884 1093 3446 -262 867 -168 C ATOM 550 C TRP B 86 -8.578 3.738 23.342 1.00 17.73 C ANISOU 550 C TRP B 86 2237 891 3610 -723 612 -388 C ATOM 551 O TRP B 86 -9.731 4.075 23.008 1.00 18.72 O ANISOU 551 O TRP B 86 2138 1345 3630 -431 787 -10 O ATOM 552 CB TRP B 86 -8.144 1.915 24.986 1.00 16.98 C ANISOU 552 CB TRP B 86 1803 1256 3394 -337 523 -95 C ATOM 553 CG TRP B 86 -8.304 0.424 25.218 1.00 16.61 C ANISOU 553 CG TRP B 86 1326 1639 3345 -281 604 -285 C ATOM 554 CD1 TRP B 86 -9.100 -0.437 24.488 1.00 18.01 C ANISOU 554 CD1 TRP B 86 1813 1568 3463 -824 755 -201 C ATOM 555 CD2 TRP B 86 -7.627 -0.368 26.194 1.00 19.47 C ANISOU 555 CD2 TRP B 86 2360 1676 3361 -135 651 -204 C ATOM 556 NE1 TRP B 86 -8.984 -1.717 24.994 1.00 16.91 N ANISOU 556 NE1 TRP B 86 1508 1422 3493 -417 428 3 N ATOM 557 CE2 TRP B 86 -8.085 -1.718 26.033 1.00 18.85 C ANISOU 557 CE2 TRP B 86 2374 1378 3411 -33 484 -140 C ATOM 558 CE3 TRP B 86 -6.714 -0.075 27.208 1.00 20.72 C ANISOU 558 CE3 TRP B 86 2594 1855 3422 52 399 -68 C ATOM 559 CZ2 TRP B 86 -7.663 -2.765 26.886 1.00 19.79 C ANISOU 559 CZ2 TRP B 86 2322 1757 3439 297 631 -341 C ATOM 560 CZ3 TRP B 86 -6.261 -1.130 28.034 1.00 22.15 C ANISOU 560 CZ3 TRP B 86 2819 1979 3619 86 187 -176 C ATOM 561 CH2 TRP B 86 -6.739 -2.465 27.851 1.00 21.00 C ANISOU 561 CH2 TRP B 86 2739 1708 3533 -39 501 -384 C ATOM 562 N HIS B 87 -7.614 4.619 23.448 1.00 19.98 N ANISOU 562 N HIS B 87 2899 985 3706 -1055 989 -255 N ATOM 563 CA HIS B 87 -7.847 6.017 23.155 1.00 19.84 C ANISOU 563 CA HIS B 87 2549 928 4062 -941 973 41 C ATOM 564 C HIS B 87 -8.368 6.271 21.816 1.00 23.43 C ANISOU 564 C HIS B 87 3059 1848 3996 -381 1180 62 C ATOM 565 O HIS B 87 -9.268 6.900 21.637 1.00 23.45 O ANISOU 565 O HIS B 87 3478 1471 3963 -763 1168 -78 O ATOM 566 CB HIS B 87 -6.551 6.839 23.462 1.00 21.06 C ANISOU 566 CB HIS B 87 2644 935 4423 -818 1021 -212 C ATOM 567 CG HIS B 87 -6.772 8.322 23.416 1.00 24.18 C ANISOU 567 CG HIS B 87 2922 1418 4847 -1001 641 -261 C ATOM 568 ND1 HIS B 87 -6.911 8.998 22.257 1.00 28.82 N ANISOU 568 ND1 HIS B 87 3917 1883 5149 -994 780 -323 N ATOM 569 CD2 HIS B 87 -6.864 9.229 24.385 1.00 25.12 C ANISOU 569 CD2 HIS B 87 3139 1270 5135 -323 743 -411 C ATOM 570 CE1 HIS B 87 -7.138 10.257 22.511 1.00 28.70 C ANISOU 570 CE1 HIS B 87 3807 1885 5215 -656 651 -541 C ATOM 571 NE2 HIS B 87 -7.058 10.422 23.783 1.00 28.13 N ANISOU 571 NE2 HIS B 87 3729 1668 5290 -428 697 -511 N ATOM 572 N HIS B 88 -7.712 5.647 20.829 1.00 21.18 N ANISOU 572 N HIS B 88 2560 1602 3887 -452 1456 -108 N ATOM 573 CA HIS B 88 -8.185 5.729 19.471 1.00 21.68 C ANISOU 573 CA HIS B 88 2803 1711 3722 -165 1362 -67 C ATOM 574 C HIS B 88 -9.623 5.188 19.300 1.00 20.41 C ANISOU 574 C HIS B 88 2757 1441 3555 -324 1095 77 C ATOM 575 O HIS B 88 -10.461 5.738 18.570 1.00 20.76 O ANISOU 575 O HIS B 88 2810 1597 3481 86 1453 116 O ATOM 576 CB HIS B 88 -7.191 4.993 18.557 1.00 22.12 C ANISOU 576 CB HIS B 88 3064 1570 3773 -184 1725 132 C ATOM 577 CG HIS B 88 -7.454 5.145 17.092 1.00 25.11 C ANISOU 577 CG HIS B 88 3388 2167 3986 -70 1774 43 C ATOM 578 ND1 HIS B 88 -6.995 6.229 16.358 1.00 27.93 N ANISOU 578 ND1 HIS B 88 4011 2537 4064 -423 1595 208 N ATOM 579 CD2 HIS B 88 -8.111 4.346 16.215 1.00 27.03 C ANISOU 579 CD2 HIS B 88 3597 2681 3990 -27 1841 -89 C ATOM 580 CE1 HIS B 88 -7.371 6.088 15.099 1.00 28.38 C ANISOU 580 CE1 HIS B 88 3859 2831 4095 -281 1585 -11 C ATOM 581 NE2 HIS B 88 -8.045 4.952 14.984 1.00 28.50 N ANISOU 581 NE2 HIS B 88 3960 2778 4093 -259 1723 -233 N ATOM 582 N THR B 89 -9.904 4.051 19.948 1.00 17.56 N ANISOU 582 N THR B 89 2292 898 3480 -716 973 -319 N ATOM 583 CA THR B 89 -11.231 3.477 19.840 1.00 17.55 C ANISOU 583 CA THR B 89 2118 993 3556 -466 655 -25 C ATOM 584 C THR B 89 -12.267 4.490 20.341 1.00 18.37 C ANISOU 584 C THR B 89 2499 1108 3372 16 737 -153 C ATOM 585 O THR B 89 -13.306 4.653 19.707 1.00 17.44 O ANISOU 585 O THR B 89 2088 1283 3255 14 880 -67 O ATOM 586 CB THR B 89 -11.312 2.195 20.721 1.00 17.30 C ANISOU 586 CB THR B 89 1661 1302 3610 -95 961 258 C ATOM 587 OG1 THR B 89 -10.320 1.234 20.313 1.00 18.51 O ANISOU 587 OG1 THR B 89 2425 1064 3545 114 894 -189 O ATOM 588 CG2 THR B 89 -12.678 1.569 20.660 1.00 18.58 C ANISOU 588 CG2 THR B 89 1309 1907 3842 -251 582 53 C ATOM 589 N PHE B 90 -12.011 5.119 21.499 1.00 17.71 N ANISOU 589 N PHE B 90 2409 988 3330 -163 771 -164 N ATOM 590 CA PHE B 90 -13.028 6.002 22.054 1.00 19.57 C ANISOU 590 CA PHE B 90 2833 1273 3328 -220 605 -7 C ATOM 591 C PHE B 90 -13.110 7.307 21.258 1.00 19.84 C ANISOU 591 C PHE B 90 2853 1308 3378 9 902 298 C ATOM 592 O PHE B 90 -14.197 7.708 20.862 1.00 19.91 O ANISOU 592 O PHE B 90 2752 1422 3391 268 1008 116 O ATOM 593 CB PHE B 90 -12.680 6.345 23.503 1.00 19.71 C ANISOU 593 CB PHE B 90 2857 1437 3194 -506 615 43 C ATOM 594 CG PHE B 90 -12.824 5.198 24.465 1.00 19.65 C ANISOU 594 CG PHE B 90 2635 1595 3236 162 375 -81 C ATOM 595 CD1 PHE B 90 -11.809 4.887 25.340 1.00 16.68 C ANISOU 595 CD1 PHE B 90 1940 1290 3106 20 -67 -80 C ATOM 596 CD2 PHE B 90 -14.041 4.531 24.597 1.00 21.91 C ANISOU 596 CD2 PHE B 90 2971 1880 3475 -21 -18 364 C ATOM 597 CE1 PHE B 90 -11.945 3.874 26.268 1.00 18.60 C ANISOU 597 CE1 PHE B 90 2441 1437 3187 -218 -177 -257 C ATOM 598 CE2 PHE B 90 -14.199 3.507 25.573 1.00 22.41 C ANISOU 598 CE2 PHE B 90 2737 2389 3389 -286 -400 393 C ATOM 599 CZ PHE B 90 -13.157 3.203 26.408 1.00 19.27 C ANISOU 599 CZ PHE B 90 2041 1974 3305 -909 -479 85 C ATOM 600 N TYR B 91 -11.955 7.934 20.999 1.00 21.19 N ANISOU 600 N TYR B 91 3111 1264 3675 -96 803 403 N ATOM 601 CA TYR B 91 -11.951 9.330 20.477 1.00 22.75 C ANISOU 601 CA TYR B 91 3523 1402 3717 -19 817 347 C ATOM 602 C TYR B 91 -11.941 9.458 18.972 1.00 23.93 C ANISOU 602 C TYR B 91 3855 1416 3820 129 1127 533 C ATOM 603 O TYR B 91 -12.323 10.508 18.431 1.00 28.36 O ANISOU 603 O TYR B 91 5094 1798 3883 672 668 462 O ATOM 604 CB TYR B 91 -10.776 10.088 21.068 1.00 25.20 C ANISOU 604 CB TYR B 91 4008 1845 3722 -45 1127 -89 C ATOM 605 CG TYR B 91 -11.021 10.363 22.532 1.00 22.91 C ANISOU 605 CG TYR B 91 3669 1317 3719 -417 1499 -51 C ATOM 606 CD1 TYR B 91 -10.473 9.549 23.506 1.00 23.66 C ANISOU 606 CD1 TYR B 91 3860 1390 3741 -717 1273 -208 C ATOM 607 CD2 TYR B 91 -11.845 11.418 22.921 1.00 25.07 C ANISOU 607 CD2 TYR B 91 3923 1826 3777 -245 1372 22 C ATOM 608 CE1 TYR B 91 -10.715 9.764 24.849 1.00 23.18 C ANISOU 608 CE1 TYR B 91 3496 1474 3835 -1075 1219 -392 C ATOM 609 CE2 TYR B 91 -12.101 11.641 24.267 1.00 25.37 C ANISOU 609 CE2 TYR B 91 3757 2123 3759 -346 1328 -172 C ATOM 610 CZ TYR B 91 -11.527 10.824 25.214 1.00 24.43 C ANISOU 610 CZ TYR B 91 3544 1903 3837 -595 1295 -237 C ATOM 611 OH TYR B 91 -11.781 11.055 26.542 1.00 26.54 O ANISOU 611 OH TYR B 91 3526 2644 3915 -533 1327 -493 O ATOM 612 N ASN B 92 -11.479 8.428 18.277 1.00 22.91 N ANISOU 612 N ASN B 92 3512 1356 3839 -16 1236 365 N ATOM 613 CA ASN B 92 -11.335 8.542 16.846 1.00 24.07 C ANISOU 613 CA ASN B 92 3363 1734 4050 229 1105 660 C ATOM 614 C ASN B 92 -12.338 7.683 16.111 1.00 26.16 C ANISOU 614 C ASN B 92 3852 2133 3954 461 1073 291 C ATOM 615 O ASN B 92 -12.933 8.084 15.110 1.00 29.02 O ANISOU 615 O ASN B 92 4599 2306 4119 118 1164 179 O ATOM 616 CB ASN B 92 -9.899 8.220 16.438 1.00 26.78 C ANISOU 616 CB ASN B 92 3526 2271 4378 358 1249 521 C ATOM 617 CG ASN B 92 -8.906 9.235 16.979 1.00 33.05 C ANISOU 617 CG ASN B 92 4470 3319 4768 18 1063 683 C ATOM 618 OD1 ASN B 92 -8.366 9.103 18.078 1.00 34.50 O ANISOU 618 OD1 ASN B 92 4615 3556 4937 -305 1238 731 O ATOM 619 ND2 ASN B 92 -8.659 10.269 16.189 1.00 38.52 N ANISOU 619 ND2 ASN B 92 5484 4138 5015 -518 922 597 N ATOM 620 N GLU B 93 -12.539 6.470 16.618 1.00 23.38 N ANISOU 620 N GLU B 93 3497 1582 3805 230 1093 232 N ATOM 621 CA GLU B 93 -13.385 5.535 15.927 1.00 22.73 C ANISOU 621 CA GLU B 93 3324 1692 3623 296 1022 363 C ATOM 622 C GLU B 93 -14.850 5.654 16.361 1.00 24.56 C ANISOU 622 C GLU B 93 3359 2543 3427 671 717 299 C ATOM 623 O GLU B 93 -15.741 5.900 15.537 1.00 28.40 O ANISOU 623 O GLU B 93 4056 3366 3369 1306 813 422 O ATOM 624 CB GLU B 93 -12.836 4.116 16.132 1.00 24.15 C ANISOU 624 CB GLU B 93 3690 1792 3692 104 1153 402 C ATOM 625 CG GLU B 93 -11.565 3.894 15.320 1.00 25.69 C ANISOU 625 CG GLU B 93 4114 1751 3898 -176 1167 346 C ATOM 626 CD GLU B 93 -11.879 3.616 13.849 1.00 31.26 C ANISOU 626 CD GLU B 93 4963 2863 4051 -54 1729 489 C ATOM 627 OE1 GLU B 93 -13.060 3.484 13.444 1.00 35.13 O ANISOU 627 OE1 GLU B 93 5774 3602 3970 -640 1788 389 O ATOM 628 OE2 GLU B 93 -10.920 3.521 13.067 1.00 34.01 O ANISOU 628 OE2 GLU B 93 5443 3125 4355 13 1876 526 O ATOM 629 N LEU B 94 -15.122 5.440 17.649 1.00 21.27 N ANISOU 629 N LEU B 94 3007 1768 3308 228 840 367 N ATOM 630 CA LEU B 94 -16.513 5.551 18.108 1.00 21.16 C ANISOU 630 CA LEU B 94 2870 1801 3369 264 932 287 C ATOM 631 C LEU B 94 -16.927 7.005 18.336 1.00 23.53 C ANISOU 631 C LEU B 94 3784 1815 3343 437 946 289 C ATOM 632 O LEU B 94 -18.127 7.297 18.228 1.00 25.83 O ANISOU 632 O LEU B 94 4470 1976 3368 656 671 -329 O ATOM 633 CB LEU B 94 -16.730 4.752 19.395 1.00 19.24 C ANISOU 633 CB LEU B 94 2461 1333 3514 430 846 225 C ATOM 634 CG LEU B 94 -16.491 3.226 19.269 1.00 20.38 C ANISOU 634 CG LEU B 94 2628 1403 3712 322 650 -357 C ATOM 635 CD1 LEU B 94 -16.721 2.624 20.647 1.00 21.40 C ANISOU 635 CD1 LEU B 94 2865 1532 3736 240 1180 8 C ATOM 636 CD2 LEU B 94 -17.418 2.644 18.216 1.00 23.74 C ANISOU 636 CD2 LEU B 94 2909 2025 4088 795 486 -491 C ATOM 637 N ARG B 95 -15.938 7.838 18.672 1.00 22.47 N ANISOU 637 N ARG B 95 3859 1430 3249 477 1417 229 N ATOM 638 CA ARG B 95 -16.124 9.286 18.999 1.00 23.06 C ANISOU 638 CA ARG B 95 4033 1492 3237 989 1819 332 C ATOM 639 C ARG B 95 -17.170 9.425 20.113 1.00 23.29 C ANISOU 639 C ARG B 95 4025 1454 3368 109 1374 440 C ATOM 640 O ARG B 95 -18.309 9.870 19.900 1.00 21.71 O ANISOU 640 O ARG B 95 3794 1093 3363 76 1405 284 O ATOM 641 CB ARG B 95 -16.474 10.092 17.751 1.00 27.63 C ANISOU 641 CB ARG B 95 4612 2464 3422 401 2167 633 C ATOM 642 CG ARG B 95 -15.272 10.338 16.819 1.00 31.60 C ANISOU 642 CG ARG B 95 5310 3201 3494 89 2437 770 C ATOM 643 CD ARG B 95 -15.537 11.552 15.919 1.00 34.76 C ANISOU 643 CD ARG B 95 6153 3659 3397 -759 2775 1243 C ATOM 644 NE ARG B 95 -16.250 11.106 14.729 1.00 42.21 N ANISOU 644 NE ARG B 95 6972 4945 4122 -640 1743 772 N ATOM 645 CZ ARG B 95 -17.362 11.640 14.252 1.00 43.17 C ANISOU 645 CZ ARG B 95 6999 5142 4261 -558 1608 257 C ATOM 646 NH1 ARG B 95 -17.931 12.681 14.830 1.00 42.02 N ANISOU 646 NH1 ARG B 95 6670 4944 4353 -78 1988 -97 N ATOM 647 NH2 ARG B 95 -17.889 11.134 13.156 1.00 45.10 N ANISOU 647 NH2 ARG B 95 7373 5445 4316 -617 1493 -47 N ATOM 648 N VAL B 96 -16.737 8.975 21.289 1.00 20.44 N ANISOU 648 N VAL B 96 3407 1062 3296 -63 1584 343 N ATOM 649 CA VAL B 96 -17.600 9.047 22.478 1.00 18.73 C ANISOU 649 CA VAL B 96 2748 1010 3356 50 1437 361 C ATOM 650 C VAL B 96 -16.801 9.719 23.588 1.00 19.52 C ANISOU 650 C VAL B 96 2702 1035 3678 170 1217 285 C ATOM 651 O VAL B 96 -15.572 9.747 23.568 1.00 21.57 O ANISOU 651 O VAL B 96 2635 1724 3835 -211 1357 135 O ATOM 652 CB VAL B 96 -18.010 7.605 22.974 1.00 18.11 C ANISOU 652 CB VAL B 96 2433 1104 3343 344 1329 274 C ATOM 653 CG1 VAL B 96 -18.978 6.971 22.023 1.00 20.69 C ANISOU 653 CG1 VAL B 96 3227 1374 3261 -27 1038 88 C ATOM 654 CG2 VAL B 96 -16.751 6.752 23.261 1.00 20.59 C ANISOU 654 CG2 VAL B 96 3040 1248 3536 524 1305 602 C ATOM 655 N ALA B 97 -17.516 10.246 24.583 1.00 20.25 N ANISOU 655 N ALA B 97 3069 920 3706 223 1311 129 N ATOM 656 CA ALA B 97 -16.857 10.567 25.836 1.00 19.72 C ANISOU 656 CA ALA B 97 2814 865 3814 -220 1048 116 C ATOM 657 C ALA B 97 -16.923 9.303 26.722 1.00 19.24 C ANISOU 657 C ALA B 97 2495 996 3818 -48 1360 90 C ATOM 658 O ALA B 97 -18.024 8.868 27.061 1.00 20.83 O ANISOU 658 O ALA B 97 2920 1281 3714 -102 1391 -101 O ATOM 659 CB ALA B 97 -17.588 11.739 26.539 1.00 21.71 C ANISOU 659 CB ALA B 97 3354 966 3929 212 1047 23 C ATOM 660 N PRO B 98 -15.830 8.724 27.050 1.00 19.38 N ANISOU 660 N PRO B 98 2458 1262 3645 19 1109 54 N ATOM 661 CA PRO B 98 -15.916 7.450 27.772 1.00 18.91 C ANISOU 661 CA PRO B 98 2375 1201 3610 85 1267 -72 C ATOM 662 C PRO B 98 -16.665 7.515 29.095 1.00 18.05 C ANISOU 662 C PRO B 98 3080 389 3391 -454 1334 -284 C ATOM 663 O PRO B 98 -17.219 6.548 29.484 1.00 19.31 O ANISOU 663 O PRO B 98 3238 699 3399 -312 1039 123 O ATOM 664 CB PRO B 98 -14.452 7.032 27.945 1.00 19.08 C ANISOU 664 CB PRO B 98 2250 1365 3633 -314 1342 -82 C ATOM 665 CG PRO B 98 -13.680 7.874 26.976 1.00 22.16 C ANISOU 665 CG PRO B 98 3039 1719 3662 161 1106 -35 C ATOM 666 CD PRO B 98 -14.440 9.077 26.779 1.00 20.35 C ANISOU 666 CD PRO B 98 3064 1010 3658 382 1012 -320 C ATOM 667 N GLU B 99 -16.672 8.672 29.735 1.00 19.88 N ANISOU 667 N GLU B 99 3374 742 3435 -148 1477 -227 N ATOM 668 CA GLU B 99 -17.420 8.886 30.981 1.00 20.74 C ANISOU 668 CA GLU B 99 3235 1081 3565 286 1691 -599 C ATOM 669 C GLU B 99 -18.921 8.706 30.832 1.00 22.34 C ANISOU 669 C GLU B 99 3349 1467 3670 -112 1758 -266 C ATOM 670 O GLU B 99 -19.545 8.559 31.760 1.00 22.95 O ANISOU 670 O GLU B 99 3672 1182 3864 -254 1976 -268 O ATOM 671 CB GLU B 99 -17.185 10.425 31.391 1.00 25.27 C ANISOU 671 CB GLU B 99 3810 2038 3754 -506 1244 -676 C ATOM 672 CG GLU B 99 -15.945 10.737 31.670 1.00 26.21 C ANISOU 672 CG GLU B 99 3491 2701 3765 -1016 621 -653 C ATOM 673 CD GLU B 99 -15.018 11.371 30.479 1.00 27.08 C ANISOU 673 CD GLU B 99 3966 2328 3995 -302 375 -339 C ATOM 674 OE1 GLU B 99 -14.141 11.997 30.844 1.00 29.75 O ANISOU 674 OE1 GLU B 99 4239 2867 4196 -692 -86 255 O ATOM 675 OE2 GLU B 99 -15.160 11.139 29.369 1.00 24.28 O ANISOU 675 OE2 GLU B 99 4092 1304 3830 -318 668 -127 O ATOM 676 N GLU B 100 -19.442 8.719 29.698 1.00 19.74 N ANISOU 676 N GLU B 100 2700 1061 3740 -228 1070 -291 N ATOM 677 CA GLU B 100 -20.805 8.554 29.488 1.00 21.25 C ANISOU 677 CA GLU B 100 2785 1575 3716 -135 1058 190 C ATOM 678 C GLU B 100 -21.269 7.095 29.267 1.00 21.89 C ANISOU 678 C GLU B 100 3235 1521 3561 326 704 -77 C ATOM 679 O GLU B 100 -22.331 6.925 29.045 1.00 21.24 O ANISOU 679 O GLU B 100 3548 1075 3448 205 783 -115 O ATOM 680 CB GLU B 100 -21.329 9.364 28.313 1.00 21.57 C ANISOU 680 CB GLU B 100 2902 1245 4049 498 1097 341 C ATOM 681 CG GLU B 100 -21.213 10.851 28.513 1.00 23.97 C ANISOU 681 CG GLU B 100 3409 1500 4196 700 1166 309 C ATOM 682 CD GLU B 100 -21.757 11.664 27.333 1.00 28.32 C ANISOU 682 CD GLU B 100 4550 2050 4160 848 1490 224 C ATOM 683 OE1 GLU B 100 -22.595 12.460 27.589 1.00 32.49 O ANISOU 683 OE1 GLU B 100 5644 2543 4157 588 1486 338 O ATOM 684 OE2 GLU B 100 -21.419 11.529 26.242 1.00 26.74 O ANISOU 684 OE2 GLU B 100 4554 1506 4102 59 1601 231 O ATOM 685 N HIS B 101 -20.320 6.179 29.172 1.00 18.03 N ANISOU 685 N HIS B 101 2759 827 3266 361 818 74 N ATOM 686 CA HIS B 101 -20.693 4.815 28.721 1.00 16.65 C ANISOU 686 CA HIS B 101 2566 1027 2733 340 759 83 C ATOM 687 C HIS B 101 -20.121 3.687 29.588 1.00 16.25 C ANISOU 687 C HIS B 101 2429 1072 2675 -147 355 -94 C ATOM 688 O HIS B 101 -18.899 3.528 29.647 1.00 17.54 O ANISOU 688 O HIS B 101 2751 1187 2728 -30 5 -308 O ATOM 689 CB HIS B 101 -20.168 4.562 27.291 1.00 17.45 C ANISOU 689 CB HIS B 101 2577 1374 2680 470 875 115 C ATOM 690 CG HIS B 101 -20.625 5.590 26.309 1.00 16.07 C ANISOU 690 CG HIS B 101 2089 1345 2672 711 600 550 C ATOM 691 ND1 HIS B 101 -21.740 5.409 25.521 1.00 16.55 N ANISOU 691 ND1 HIS B 101 1818 1764 2706 438 474 751 N ATOM 692 CD2 HIS B 101 -20.139 6.827 26.019 1.00 17.00 C ANISOU 692 CD2 HIS B 101 2280 1392 2787 443 851 309 C ATOM 693 CE1 HIS B 101 -21.919 6.493 24.775 1.00 17.56 C ANISOU 693 CE1 HIS B 101 1909 1727 3036 142 771 428 C ATOM 694 NE2 HIS B 101 -20.958 7.355 25.052 1.00 18.76 N ANISOU 694 NE2 HIS B 101 2495 1661 2972 108 819 271 N ATOM 695 N PRO B 102 -21.008 2.839 30.143 1.00 14.91 N ANISOU 695 N PRO B 102 2021 947 2697 155 632 -93 N ATOM 696 CA PRO B 102 -20.510 1.553 30.654 1.00 15.51 C ANISOU 696 CA PRO B 102 2184 878 2830 -151 482 -106 C ATOM 697 C PRO B 102 -19.806 0.852 29.499 1.00 15.37 C ANISOU 697 C PRO B 102 1948 1102 2790 57 123 -271 C ATOM 698 O PRO B 102 -20.350 0.838 28.395 1.00 15.73 O ANISOU 698 O PRO B 102 1929 1296 2752 259 167 -188 O ATOM 699 CB PRO B 102 -21.790 0.821 31.023 1.00 16.13 C ANISOU 699 CB PRO B 102 1870 1083 3175 12 781 -252 C ATOM 700 CG PRO B 102 -22.788 1.929 31.339 1.00 18.91 C ANISOU 700 CG PRO B 102 2787 1405 2995 350 754 236 C ATOM 701 CD PRO B 102 -22.471 2.925 30.222 1.00 16.46 C ANISOU 701 CD PRO B 102 2141 1234 2877 382 936 205 C ATOM 702 N THR B 103 -18.671 0.247 29.784 1.00 13.67 N ANISOU 702 N THR B 103 1765 827 2603 236 418 -180 N ATOM 703 CA THR B 103 -17.863 -0.369 28.730 1.00 14.10 C ANISOU 703 CA THR B 103 1751 780 2827 347 373 -9 C ATOM 704 C THR B 103 -17.555 -1.844 29.024 1.00 14.01 C ANISOU 704 C THR B 103 1625 1079 2618 -123 419 -254 C ATOM 705 O THR B 103 -16.930 -2.185 30.050 1.00 14.19 O ANISOU 705 O THR B 103 1568 1367 2456 -105 237 -165 O ATOM 706 CB THR B 103 -16.557 0.398 28.599 1.00 16.87 C ANISOU 706 CB THR B 103 2366 848 3197 10 379 -122 C ATOM 707 OG1 THR B 103 -16.857 1.750 28.228 1.00 17.69 O ANISOU 707 OG1 THR B 103 2165 1138 3420 -121 127 80 O ATOM 708 CG2 THR B 103 -15.615 -0.183 27.557 1.00 16.41 C ANISOU 708 CG2 THR B 103 1786 1276 3171 -308 600 -254 C ATOM 709 N LEU B 104 -18.011 -2.702 28.100 1.00 12.55 N ANISOU 709 N LEU B 104 1401 843 2523 65 195 -144 N ATOM 710 CA ALEU B 104 -17.695 -4.149 28.133 0.50 11.84 C ANISOU 710 CA ALEU B 104 1275 795 2430 -23 172 -135 C ATOM 711 CA BLEU B 104 -17.681 -4.136 28.164 0.50 13.77 C ANISOU 711 CA BLEU B 104 1751 860 2623 267 241 -67 C ATOM 712 C LEU B 104 -16.480 -4.432 27.249 1.00 12.56 C ANISOU 712 C LEU B 104 1466 865 2442 79 231 -152 C ATOM 713 O LEU B 104 -16.503 -4.112 26.064 1.00 14.30 O ANISOU 713 O LEU B 104 1459 1438 2536 15 390 215 O ATOM 714 CB ALEU B 104 -18.873 -4.949 27.593 0.50 9.53 C ANISOU 714 CB ALEU B 104 828 598 2196 -328 120 -249 C ATOM 715 CB BLEU B 104 -18.897 -4.976 27.774 0.50 15.52 C ANISOU 715 CB BLEU B 104 2248 885 2764 240 284 -35 C ATOM 716 CG ALEU B 104 -18.680 -6.462 27.390 0.50 7.28 C ANISOU 716 CG ALEU B 104 410 490 1867 -440 65 -79 C ATOM 717 CG BLEU B 104 -18.779 -6.504 27.852 0.50 16.85 C ANISOU 717 CG BLEU B 104 2570 989 2844 1021 436 -143 C ATOM 718 CD1ALEU B 104 -18.201 -7.156 28.716 0.50 7.88 C ANISOU 718 CD1ALEU B 104 240 816 1938 -157 108 87 C ATOM 719 CD1BLEU B 104 -20.128 -7.169 28.006 0.50 19.96 C ANISOU 719 CD1BLEU B 104 3020 1567 2998 603 399 2 C ATOM 720 CD2ALEU B 104 -19.921 -7.083 26.829 0.50 8.32 C ANISOU 720 CD2ALEU B 104 515 739 1909 -435 74 -167 C ATOM 721 CD2BLEU B 104 -18.062 -7.041 26.645 0.50 18.06 C ANISOU 721 CD2BLEU B 104 2566 1524 2771 595 237 -45 C ATOM 722 N LEU B 105 -15.454 -5.006 27.849 1.00 12.46 N ANISOU 722 N LEU B 105 964 1105 2665 -67 281 103 N ATOM 723 CA ALEU B 105 -14.243 -5.410 27.118 0.70 12.58 C ANISOU 723 CA ALEU B 105 1119 971 2691 -179 262 -102 C ATOM 724 CA BLEU B 105 -14.256 -5.415 27.112 0.30 11.91 C ANISOU 724 CA BLEU B 105 751 1076 2698 -105 367 -50 C ATOM 725 C LEU B 105 -14.205 -6.939 27.054 1.00 13.21 C ANISOU 725 C LEU B 105 1312 1005 2701 -158 318 -41 C ATOM 726 O LEU B 105 -14.879 -7.622 27.846 1.00 14.69 O ANISOU 726 O LEU B 105 1430 1258 2892 -181 455 -120 O ATOM 727 CB ALEU B 105 -12.974 -4.941 27.825 0.70 16.10 C ANISOU 727 CB ALEU B 105 2204 1035 2880 -661 66 -143 C ATOM 728 CB BLEU B 105 -12.983 -4.890 27.774 0.30 12.38 C ANISOU 728 CB BLEU B 105 691 1210 2803 -205 443 -86 C ATOM 729 CG ALEU B 105 -12.919 -3.427 27.939 0.70 17.92 C ANISOU 729 CG ALEU B 105 2738 1250 2821 -564 273 -282 C ATOM 730 CG BLEU B 105 -12.860 -3.373 27.759 0.30 11.31 C ANISOU 730 CG BLEU B 105 385 1119 2793 456 635 -204 C ATOM 731 CD1ALEU B 105 -11.781 -3.144 28.862 0.70 21.45 C ANISOU 731 CD1ALEU B 105 3519 1987 2644 -651 261 -536 C ATOM 732 CD1BLEU B 105 -13.380 -2.787 29.052 0.30 10.93 C ANISOU 732 CD1BLEU B 105 217 1264 2671 61 239 -11 C ATOM 733 CD2ALEU B 105 -12.635 -2.815 26.610 0.70 19.40 C ANISOU 733 CD2ALEU B 105 3203 1386 2783 19 120 220 C ATOM 734 CD2BLEU B 105 -11.404 -3.062 27.627 0.30 13.08 C ANISOU 734 CD2BLEU B 105 715 1307 2947 -165 903 -347 C ATOM 735 N THR B 106 -13.425 -7.464 26.121 1.00 11.47 N ANISOU 735 N THR B 106 851 768 2739 -139 302 49 N ATOM 736 CA THR B 106 -13.259 -8.911 26.059 1.00 10.17 C ANISOU 736 CA THR B 106 563 753 2549 15 184 33 C ATOM 737 C THR B 106 -11.784 -9.287 26.332 1.00 11.12 C ANISOU 737 C THR B 106 232 1410 2583 -66 149 6 C ATOM 738 O THR B 106 -10.817 -8.458 26.247 1.00 14.00 O ANISOU 738 O THR B 106 1278 1290 2753 -105 153 -1 O ATOM 739 CB THR B 106 -13.575 -9.476 24.670 1.00 12.52 C ANISOU 739 CB THR B 106 812 1368 2578 -116 241 -76 C ATOM 740 OG1 THR B 106 -12.500 -9.115 23.776 1.00 12.40 O ANISOU 740 OG1 THR B 106 1155 973 2584 17 212 109 O ATOM 741 CG2 THR B 106 -14.942 -8.916 24.195 1.00 13.35 C ANISOU 741 CG2 THR B 106 1547 911 2612 -49 23 -6 C ATOM 742 N GLU B 107 -11.599 -10.570 26.648 1.00 13.39 N ANISOU 742 N GLU B 107 1166 1260 2661 236 219 64 N ATOM 743 CA GLU B 107 -10.233 -11.082 26.920 1.00 12.83 C ANISOU 743 CA GLU B 107 977 1238 2661 123 -21 -66 C ATOM 744 C GLU B 107 -10.124 -12.510 26.437 1.00 10.97 C ANISOU 744 C GLU B 107 307 1120 2739 -210 -43 132 C ATOM 745 O GLU B 107 -11.134 -13.208 26.255 1.00 12.21 O ANISOU 745 O GLU B 107 688 1181 2770 -74 79 131 O ATOM 746 CB GLU B 107 -9.890 -11.002 28.425 1.00 15.46 C ANISOU 746 CB GLU B 107 1773 1571 2530 -204 -3 344 C ATOM 747 CG GLU B 107 -10.812 -11.870 29.259 1.00 17.61 C ANISOU 747 CG GLU B 107 1745 2217 2728 -125 -15 305 C ATOM 748 CD GLU B 107 -10.568 -11.772 30.749 1.00 22.60 C ANISOU 748 CD GLU B 107 2658 2963 2966 37 -7 139 C ATOM 749 OE1 GLU B 107 -9.598 -11.096 31.185 1.00 24.03 O ANISOU 749 OE1 GLU B 107 2671 3402 3059 409 -451 -210 O ATOM 750 OE2 GLU B 107 -11.375 -12.373 31.478 1.00 28.22 O ANISOU 750 OE2 GLU B 107 4077 3811 2834 -367 87 471 O ATOM 751 N ALA B 108 -8.883 -12.932 26.247 1.00 13.93 N ANISOU 751 N ALA B 108 708 1527 3059 152 408 -234 N ATOM 752 CA ALA B 108 -8.605 -14.297 25.874 1.00 15.75 C ANISOU 752 CA ALA B 108 1043 1439 3503 290 251 -33 C ATOM 753 C ALA B 108 -8.897 -15.226 27.038 1.00 17.12 C ANISOU 753 C ALA B 108 1326 1347 3831 156 2 -167 C ATOM 754 O ALA B 108 -8.761 -14.847 28.193 1.00 17.91 O ANISOU 754 O ALA B 108 1587 1595 3624 160 -158 96 O ATOM 755 CB ALA B 108 -7.095 -14.398 25.495 1.00 15.55 C ANISOU 755 CB ALA B 108 685 1569 3653 125 392 -240 C ATOM 756 N PRO B 109 -9.202 -16.491 26.724 1.00 18.70 N ANISOU 756 N PRO B 109 1451 1432 4220 356 -285 -142 N ATOM 757 CA PRO B 109 -9.203 -17.518 27.738 1.00 21.65 C ANISOU 757 CA PRO B 109 2258 1438 4530 188 -637 395 C ATOM 758 C PRO B 109 -7.789 -17.573 28.371 1.00 22.57 C ANISOU 758 C PRO B 109 2375 1655 4545 138 -732 394 C ATOM 759 O PRO B 109 -6.785 -17.283 27.683 1.00 22.35 O ANISOU 759 O PRO B 109 2338 1612 4542 261 -938 236 O ATOM 760 CB PRO B 109 -9.449 -18.782 26.888 1.00 20.57 C ANISOU 760 CB PRO B 109 2133 1028 4655 132 -757 301 C ATOM 761 CG PRO B 109 -10.168 -18.259 25.649 1.00 24.22 C ANISOU 761 CG PRO B 109 2519 2066 4617 -275 -286 149 C ATOM 762 CD PRO B 109 -9.392 -17.047 25.376 1.00 20.59 C ANISOU 762 CD PRO B 109 1716 1669 4438 86 -574 -253 C ATOM 763 N LEU B 110 -7.718 -17.844 29.671 1.00 21.82 N ANISOU 763 N LEU B 110 2273 1527 4492 82 -805 570 N ATOM 764 CA LEU B 110 -6.420 -17.984 30.371 1.00 22.44 C ANISOU 764 CA LEU B 110 2331 1755 4442 152 -623 119 C ATOM 765 C LEU B 110 -5.626 -16.654 30.444 1.00 23.05 C ANISOU 765 C LEU B 110 2645 1889 4225 19 -348 194 C ATOM 766 O LEU B 110 -4.402 -16.619 30.639 1.00 25.29 O ANISOU 766 O LEU B 110 3130 2000 4478 -157 -527 340 O ATOM 767 CB LEU B 110 -5.580 -19.121 29.767 1.00 21.13 C ANISOU 767 CB LEU B 110 1985 1513 4531 13 -859 133 C ATOM 768 CG LEU B 110 -6.217 -20.524 29.536 1.00 23.38 C ANISOU 768 CG LEU B 110 1938 2337 4610 -79 -881 330 C ATOM 769 CD1 LEU B 110 -5.295 -21.468 28.774 1.00 26.49 C ANISOU 769 CD1 LEU B 110 2771 2555 4738 255 -902 258 C ATOM 770 CD2 LEU B 110 -6.676 -21.134 30.852 1.00 25.41 C ANISOU 770 CD2 LEU B 110 2325 2758 4572 -659 -921 747 C ATOM 771 N ASN B 111 -6.336 -15.541 30.300 1.00 21.44 N ANISOU 771 N ASN B 111 2110 2081 3954 314 -132 -144 N ATOM 772 CA ASN B 111 -5.676 -14.240 30.473 1.00 21.23 C ANISOU 772 CA ASN B 111 2422 1948 3698 -111 -395 -229 C ATOM 773 C ASN B 111 -5.143 -14.110 31.917 1.00 22.96 C ANISOU 773 C ASN B 111 2653 2382 3688 442 -804 -339 C ATOM 774 O ASN B 111 -5.900 -14.386 32.864 1.00 26.50 O ANISOU 774 O ASN B 111 3530 2756 3782 707 -870 -312 O ATOM 775 CB ASN B 111 -6.664 -13.105 30.198 1.00 20.15 C ANISOU 775 CB ASN B 111 2416 1801 3441 557 -133 -285 C ATOM 776 CG ASN B 111 -5.993 -11.754 30.095 1.00 20.70 C ANISOU 776 CG ASN B 111 2295 2291 3280 70 -303 -336 C ATOM 777 OD1 ASN B 111 -4.851 -11.662 29.661 1.00 19.37 O ANISOU 777 OD1 ASN B 111 1865 2225 3269 325 -150 -274 O ATOM 778 ND2 ASN B 111 -6.732 -10.682 30.426 1.00 20.67 N ANISOU 778 ND2 ASN B 111 2249 2437 3169 260 -141 -473 N ATOM 779 N PRO B 112 -3.842 -13.754 32.080 1.00 23.70 N ANISOU 779 N PRO B 112 2349 2989 3666 560 -703 -587 N ATOM 780 CA PRO B 112 -3.320 -13.650 33.469 1.00 25.35 C ANISOU 780 CA PRO B 112 2750 3216 3665 556 -730 -412 C ATOM 781 C PRO B 112 -4.113 -12.656 34.315 1.00 25.54 C ANISOU 781 C PRO B 112 3295 2759 3649 528 -689 -209 C ATOM 782 O PRO B 112 -4.551 -11.608 33.816 1.00 24.64 O ANISOU 782 O PRO B 112 2968 2654 3739 98 -776 -348 O ATOM 783 CB PRO B 112 -1.878 -13.172 33.276 1.00 26.93 C ANISOU 783 CB PRO B 112 3011 3447 3772 377 -949 -604 C ATOM 784 CG PRO B 112 -1.469 -13.765 31.938 1.00 26.55 C ANISOU 784 CG PRO B 112 2867 3458 3764 505 -918 -402 C ATOM 785 CD PRO B 112 -2.767 -13.676 31.080 1.00 24.62 C ANISOU 785 CD PRO B 112 2441 3236 3676 631 -979 -414 C ATOM 786 N LYS B 113 -4.266 -12.975 35.600 1.00 26.58 N ANISOU 786 N LYS B 113 3635 2915 3550 833 -884 -292 N ATOM 787 CA LYS B 113 -4.955 -12.095 36.546 1.00 29.61 C ANISOU 787 CA LYS B 113 4016 3601 3633 855 -1059 -55 C ATOM 788 C LYS B 113 -4.424 -10.654 36.534 1.00 26.47 C ANISOU 788 C LYS B 113 3025 3564 3468 814 -1170 -88 C ATOM 789 O LYS B 113 -5.212 -9.707 36.530 1.00 26.18 O ANISOU 789 O LYS B 113 2804 3624 3519 954 -1005 -215 O ATOM 790 CB LYS B 113 -4.944 -12.719 37.952 1.00 35.67 C ANISOU 790 CB LYS B 113 4934 4632 3989 519 -767 296 C ATOM 791 CG LYS B 113 -6.007 -13.840 38.113 1.00 40.40 C ANISOU 791 CG LYS B 113 5735 5247 4367 433 -851 389 C ATOM 792 CD LYS B 113 -5.959 -14.599 39.464 1.00 44.86 C ANISOU 792 CD LYS B 113 6136 6189 4720 -186 -712 264 C ATOM 793 CE LYS B 113 -6.036 -13.658 40.669 1.00 49.13 C ANISOU 793 CE LYS B 113 6643 6846 5178 -387 -634 163 C ATOM 794 NZ LYS B 113 -4.679 -13.138 41.059 1.00 51.95 N ANISOU 794 NZ LYS B 113 7093 7189 5458 -507 -551 192 N ATOM 795 N ALA B 114 -3.101 -10.477 36.491 1.00 27.17 N ANISOU 795 N ALA B 114 3243 3444 3636 203 -657 -312 N ATOM 796 CA ALA B 114 -2.512 -9.131 36.472 1.00 27.26 C ANISOU 796 CA ALA B 114 2931 3616 3810 491 -484 -322 C ATOM 797 C ALA B 114 -2.998 -8.328 35.266 1.00 25.09 C ANISOU 797 C ALA B 114 2372 3331 3830 418 -585 -534 C ATOM 798 O ALA B 114 -3.165 -7.116 35.346 1.00 25.29 O ANISOU 798 O ALA B 114 2730 2881 3996 417 -623 -224 O ATOM 799 CB ALA B 114 -0.998 -9.211 36.457 1.00 27.59 C ANISOU 799 CB ALA B 114 2953 3654 3877 900 -576 -399 C ATOM 800 N ASN B 115 -3.207 -9.023 34.143 1.00 23.50 N ANISOU 800 N ASN B 115 2192 3158 3581 113 -662 -755 N ATOM 801 CA ASN B 115 -3.652 -8.345 32.930 1.00 21.59 C ANISOU 801 CA ASN B 115 1960 2713 3530 680 -719 -776 C ATOM 802 C ASN B 115 -5.077 -7.832 33.083 1.00 20.88 C ANISOU 802 C ASN B 115 1729 2702 3503 685 -443 -460 C ATOM 803 O ASN B 115 -5.395 -6.721 32.638 1.00 21.05 O ANISOU 803 O ASN B 115 1616 2685 3699 416 46 -787 O ATOM 804 CB ASN B 115 -3.526 -9.282 31.714 1.00 22.18 C ANISOU 804 CB ASN B 115 1565 2970 3893 458 -289 -1046 C ATOM 805 CG ASN B 115 -2.101 -9.525 31.355 1.00 28.25 C ANISOU 805 CG ASN B 115 2431 4115 4189 608 -412 -962 C ATOM 806 OD1 ASN B 115 -1.275 -9.762 32.238 1.00 32.97 O ANISOU 806 OD1 ASN B 115 2952 5317 4257 437 -412 -919 O ATOM 807 ND2 ASN B 115 -1.782 -9.439 30.063 1.00 28.11 N ANISOU 807 ND2 ASN B 115 2235 4143 4304 137 -502 -1012 N ATOM 808 N ARG B 116 -5.923 -8.657 33.693 1.00 21.61 N ANISOU 808 N ARG B 116 1893 2905 3414 -156 -373 -306 N ATOM 809 CA ARG B 116 -7.312 -8.345 33.916 1.00 22.18 C ANISOU 809 CA ARG B 116 2040 2762 3625 -161 -28 -285 C ATOM 810 C ARG B 116 -7.364 -7.116 34.817 1.00 23.08 C ANISOU 810 C ARG B 116 2528 2837 3404 1 -226 -508 C ATOM 811 O ARG B 116 -8.150 -6.196 34.591 1.00 20.74 O ANISOU 811 O ARG B 116 1922 2642 3317 -30 -319 -479 O ATOM 812 CB ARG B 116 -8.037 -9.508 34.579 1.00 23.24 C ANISOU 812 CB ARG B 116 2155 2653 4022 185 549 -546 C ATOM 813 CG ARG B 116 -7.783 -10.878 33.993 1.00 28.13 C ANISOU 813 CG ARG B 116 2380 3998 4308 381 656 -91 C ATOM 814 CD ARG B 116 -8.696 -11.847 34.717 1.00 28.30 C ANISOU 814 CD ARG B 116 2963 3606 4183 293 279 143 C ATOM 815 NE ARG B 116 -10.064 -11.740 34.219 1.00 25.47 N ANISOU 815 NE ARG B 116 2669 3080 3931 401 226 134 N ATOM 816 CZ ARG B 116 -11.162 -11.914 34.947 1.00 26.31 C ANISOU 816 CZ ARG B 116 2783 3224 3990 352 28 216 C ATOM 817 NH1 ARG B 116 -11.066 -12.173 36.253 1.00 29.61 N ANISOU 817 NH1 ARG B 116 3755 3522 3974 -205 353 -154 N ATOM 818 NH2 ARG B 116 -12.365 -11.864 34.354 1.00 25.50 N ANISOU 818 NH2 ARG B 116 2661 2938 4090 -14 33 63 N ATOM 819 N GLU B 117 -6.524 -7.114 35.848 1.00 22.00 N ANISOU 819 N GLU B 117 2422 2764 3171 -149 -387 -390 N ATOM 820 CA GLU B 117 -6.492 -5.962 36.775 1.00 21.01 C ANISOU 820 CA GLU B 117 2515 2275 3191 -119 -791 -574 C ATOM 821 C GLU B 117 -6.044 -4.686 36.098 1.00 22.71 C ANISOU 821 C GLU B 117 2420 2902 3309 45 -412 -400 C ATOM 822 O GLU B 117 -6.614 -3.598 36.328 1.00 23.04 O ANISOU 822 O GLU B 117 2404 3045 3305 299 -250 -660 O ATOM 823 CB GLU B 117 -5.579 -6.280 37.968 1.00 22.27 C ANISOU 823 CB GLU B 117 2447 2589 3426 -19 -991 -73 C ATOM 824 CG GLU B 117 -6.149 -7.367 38.855 1.00 25.85 C ANISOU 824 CG GLU B 117 3146 2838 3837 -123 -869 36 C ATOM 825 CD GLU B 117 -5.319 -7.631 40.097 1.00 33.53 C ANISOU 825 CD GLU B 117 4089 4256 4396 -96 -1238 393 C ATOM 826 OE1 GLU B 117 -4.443 -6.792 40.444 1.00 37.62 O ANISOU 826 OE1 GLU B 117 4633 5081 4579 -331 -1437 437 O ATOM 827 OE2 GLU B 117 -5.583 -8.667 40.731 1.00 34.62 O ANISOU 827 OE2 GLU B 117 4332 4262 4560 466 -1409 649 O ATOM 828 N LYS B 118 -5.002 -4.806 35.283 1.00 20.70 N ANISOU 828 N LYS B 118 1773 2859 3232 -323 -499 -314 N ATOM 829 CA ALYS B 118 -4.470 -3.633 34.579 0.50 22.18 C ANISOU 829 CA ALYS B 118 2389 2708 3330 -343 -325 -343 C ATOM 830 CA BLYS B 118 -4.462 -3.639 34.576 0.50 23.63 C ANISOU 830 CA BLYS B 118 2533 3065 3379 -194 -235 -261 C ATOM 831 C LYS B 118 -5.485 -3.042 33.598 1.00 21.56 C ANISOU 831 C LYS B 118 2281 2625 3285 -251 -377 -366 C ATOM 832 O LYS B 118 -5.663 -1.822 33.540 1.00 21.01 O ANISOU 832 O LYS B 118 2063 2631 3288 -613 -215 -164 O ATOM 833 CB ALYS B 118 -3.134 -3.941 33.888 0.50 20.68 C ANISOU 833 CB ALYS B 118 2261 2146 3451 -300 -270 -370 C ATOM 834 CB BLYS B 118 -3.140 -3.990 33.883 0.50 25.26 C ANISOU 834 CB BLYS B 118 2788 3213 3599 170 33 -120 C ATOM 835 CG ALYS B 118 -2.338 -2.695 33.441 0.50 24.90 C ANISOU 835 CG ALYS B 118 2627 3223 3611 -316 -113 -524 C ATOM 836 CG BLYS B 118 -2.244 -2.792 33.547 0.50 30.15 C ANISOU 836 CG BLYS B 118 3406 4218 3830 176 305 -176 C ATOM 837 CD ALYS B 118 -1.888 -1.868 34.641 0.50 25.85 C ANISOU 837 CD ALYS B 118 2778 3400 3644 -147 -83 -698 C ATOM 838 CD BLYS B 118 -0.797 -3.213 33.319 0.50 32.46 C ANISOU 838 CD BLYS B 118 3830 4551 3951 221 531 -171 C ATOM 839 CE ALYS B 118 -1.549 -0.439 34.237 0.50 29.96 C ANISOU 839 CE ALYS B 118 3471 4136 3778 427 17 -231 C ATOM 840 CE BLYS B 118 0.032 -2.055 32.789 0.50 35.98 C ANISOU 840 CE BLYS B 118 4798 4767 4104 587 501 -340 C ATOM 841 NZ ALYS B 118 -0.200 -0.344 33.598 0.50 32.70 N ANISOU 841 NZ ALYS B 118 4069 4411 3943 684 -7 -231 N ATOM 842 NZ BLYS B 118 0.240 -0.989 33.811 0.50 37.43 N ANISOU 842 NZ BLYS B 118 5093 4919 4212 799 504 -319 N ATOM 843 N AMET B 119 -6.192 -3.896 32.861 0.60 21.12 N ANISOU 843 N AMET B 119 2196 2607 3223 -251 -322 -680 N ATOM 844 N BMET B 119 -6.177 -3.918 32.858 0.40 21.46 N ANISOU 844 N BMET B 119 2137 2816 3201 -332 -347 -602 N ATOM 845 CA AMET B 119 -7.262 -3.399 31.999 0.60 19.00 C ANISOU 845 CA AMET B 119 2128 1956 3135 -130 -237 -953 C ATOM 846 CA BMET B 119 -7.313 -3.507 32.022 0.40 20.34 C ANISOU 846 CA BMET B 119 2001 2622 3106 -253 -284 -780 C ATOM 847 C AMET B 119 -8.352 -2.670 32.790 0.60 19.87 C ANISOU 847 C AMET B 119 2378 2155 3018 379 -14 -546 C ATOM 848 C BMET B 119 -8.277 -2.652 32.821 0.40 19.56 C ANISOU 848 C BMET B 119 1861 2594 2978 -82 -260 -508 C ATOM 849 O AMET B 119 -8.885 -1.660 32.336 0.60 21.16 O ANISOU 849 O AMET B 119 2859 2102 3079 492 -1 -260 O ATOM 850 O BMET B 119 -8.633 -1.545 32.415 0.40 18.64 O ANISOU 850 O BMET B 119 1545 2579 2957 -259 -596 -314 O ATOM 851 CB AMET B 119 -7.871 -4.541 31.188 0.60 18.25 C ANISOU 851 CB AMET B 119 2126 1535 3273 -219 -423 -801 C ATOM 852 CB BMET B 119 -8.075 -4.735 31.484 0.40 21.24 C ANISOU 852 CB BMET B 119 2123 2751 3195 -208 -246 -785 C ATOM 853 CG AMET B 119 -9.129 -4.150 30.485 0.60 18.73 C ANISOU 853 CG AMET B 119 2023 1613 3482 149 -377 -779 C ATOM 854 CG BMET B 119 -7.344 -5.519 30.404 0.40 21.33 C ANISOU 854 CG BMET B 119 2069 2768 3268 -354 -154 -781 C ATOM 855 SD AMET B 119 -10.023 -5.616 29.944 0.60 21.47 S ANISOU 855 SD AMET B 119 2420 2124 3614 156 -353 -381 S ATOM 856 SD BMET B 119 -8.042 -7.165 29.998 0.40 21.45 S ANISOU 856 SD BMET B 119 2002 2817 3332 -292 78 -542 S ATOM 857 CE AMET B 119 -9.173 -6.029 28.438 0.60 19.78 C ANISOU 857 CE AMET B 119 1540 2507 3467 972 -559 -910 C ATOM 858 CE BMET B 119 -6.507 -8.022 30.174 0.40 23.21 C ANISOU 858 CE BMET B 119 2474 2992 3351 63 205 -443 C ATOM 859 N THR B 120 -8.671 -3.193 33.968 1.00 19.97 N ANISOU 859 N THR B 120 2187 2525 2874 217 22 -547 N ATOM 860 CA THR B 120 -9.676 -2.573 34.839 1.00 17.66 C ANISOU 860 CA THR B 120 1754 2156 2800 -88 302 -616 C ATOM 861 C THR B 120 -9.188 -1.220 35.349 1.00 18.79 C ANISOU 861 C THR B 120 1781 2321 3036 -191 254 -570 C ATOM 862 O THR B 120 -9.861 -0.204 35.231 1.00 19.51 O ANISOU 862 O THR B 120 2180 2262 2970 103 40 -580 O ATOM 863 CB THR B 120 -10.003 -3.527 36.002 1.00 19.06 C ANISOU 863 CB THR B 120 2491 1895 2857 -78 -139 -655 C ATOM 864 OG1 THR B 120 -10.446 -4.769 35.451 1.00 19.70 O ANISOU 864 OG1 THR B 120 2626 1921 2939 -433 -204 -514 O ATOM 865 CG2 THR B 120 -11.092 -2.953 36.933 1.00 19.35 C ANISOU 865 CG2 THR B 120 2183 2286 2884 398 -110 -575 C ATOM 866 N GLN B 121 -7.957 -1.216 35.848 1.00 19.64 N ANISOU 866 N GLN B 121 1472 2860 3131 -380 -118 -648 N ATOM 867 CA GLN B 121 -7.371 0.033 36.328 1.00 21.69 C ANISOU 867 CA GLN B 121 2044 2745 3454 -682 -97 -982 C ATOM 868 C GLN B 121 -7.303 1.112 35.245 1.00 20.58 C ANISOU 868 C GLN B 121 2035 2240 3545 -318 -198 -844 C ATOM 869 O GLN B 121 -7.616 2.275 35.463 1.00 22.69 O ANISOU 869 O GLN B 121 2511 2304 3808 -492 -223 -894 O ATOM 870 CB GLN B 121 -5.965 -0.223 36.822 1.00 23.79 C ANISOU 870 CB GLN B 121 2366 2939 3733 -356 -391 -1261 C ATOM 871 CG GLN B 121 -5.278 1.067 37.302 1.00 26.21 C ANISOU 871 CG GLN B 121 2184 3715 4059 -657 -870 -1430 C ATOM 872 CD GLN B 121 -3.947 0.773 37.901 1.00 35.31 C ANISOU 872 CD GLN B 121 3350 5405 4660 -322 -570 -1215 C ATOM 873 OE1 GLN B 121 -3.188 -0.055 37.396 1.00 39.25 O ANISOU 873 OE1 GLN B 121 3674 6282 4958 -332 -498 -1005 O ATOM 874 NE2 GLN B 121 -3.660 1.427 39.008 1.00 39.60 N ANISOU 874 NE2 GLN B 121 4169 5974 4905 -525 -619 -1030 N ATOM 875 N ILE B 122 -6.904 0.726 34.037 1.00 21.23 N ANISOU 875 N ILE B 122 2047 2524 3494 -468 -146 -522 N ATOM 876 CA ILE B 122 -6.807 1.713 32.955 1.00 20.34 C ANISOU 876 CA ILE B 122 2099 2296 3334 -423 135 -306 C ATOM 877 C ILE B 122 -8.192 2.256 32.582 1.00 20.43 C ANISOU 877 C ILE B 122 2322 2161 3279 -415 -52 -522 C ATOM 878 O ILE B 122 -8.409 3.454 32.383 1.00 20.47 O ANISOU 878 O ILE B 122 2448 1965 3364 -382 -174 -527 O ATOM 879 CB ILE B 122 -6.061 1.139 31.738 1.00 17.52 C ANISOU 879 CB ILE B 122 1273 1993 3389 -169 497 -202 C ATOM 880 CG1 ILE B 122 -4.587 0.937 32.116 1.00 20.11 C ANISOU 880 CG1 ILE B 122 1193 2738 3710 324 202 -803 C ATOM 881 CG2 ILE B 122 -6.242 2.053 30.517 1.00 20.03 C ANISOU 881 CG2 ILE B 122 2204 2224 3185 -221 522 -32 C ATOM 882 CD1 ILE B 122 -3.761 0.073 31.134 1.00 24.44 C ANISOU 882 CD1 ILE B 122 1794 3453 4037 997 562 -656 C ATOM 883 N MET B 123 -9.157 1.370 32.482 1.00 19.62 N ANISOU 883 N MET B 123 1851 2306 3297 -508 -62 -466 N ATOM 884 CA MET B 123 -10.467 1.825 32.105 1.00 19.18 C ANISOU 884 CA MET B 123 2208 1946 3133 -472 145 -580 C ATOM 885 C MET B 123 -11.031 2.828 33.121 1.00 18.05 C ANISOU 885 C MET B 123 2230 1605 3022 -73 322 -519 C ATOM 886 O MET B 123 -11.622 3.850 32.733 1.00 18.20 O ANISOU 886 O MET B 123 2116 1701 3098 -206 352 -388 O ATOM 887 CB MET B 123 -11.407 0.627 31.939 1.00 19.63 C ANISOU 887 CB MET B 123 2674 1705 3079 -340 105 -624 C ATOM 888 CG MET B 123 -11.136 -0.142 30.633 1.00 19.30 C ANISOU 888 CG MET B 123 2622 1686 3027 -402 326 -393 C ATOM 889 SD MET B 123 -11.562 0.877 29.213 1.00 19.57 S ANISOU 889 SD MET B 123 2576 1885 2977 -215 275 -390 S ATOM 890 CE MET B 123 -10.129 0.560 28.238 1.00 20.26 C ANISOU 890 CE MET B 123 2365 2029 3303 -272 683 -272 C ATOM 891 N PHE B 124 -10.932 2.490 34.403 1.00 19.13 N ANISOU 891 N PHE B 124 2490 1768 3012 -278 97 -683 N ATOM 892 CA PHE B 124 -11.498 3.407 35.429 1.00 19.47 C ANISOU 892 CA PHE B 124 2824 1487 3085 -566 67 -543 C ATOM 893 C PHE B 124 -10.624 4.627 35.689 1.00 21.49 C ANISOU 893 C PHE B 124 3015 1759 3389 -501 249 -639 C ATOM 894 O PHE B 124 -11.170 5.725 35.873 1.00 21.89 O ANISOU 894 O PHE B 124 3003 1697 3617 -557 235 -799 O ATOM 895 CB PHE B 124 -11.715 2.676 36.740 1.00 18.81 C ANISOU 895 CB PHE B 124 2344 1759 3043 -259 388 -180 C ATOM 896 CG PHE B 124 -12.960 1.823 36.761 1.00 18.18 C ANISOU 896 CG PHE B 124 2310 1543 3054 -561 264 -65 C ATOM 897 CD1 PHE B 124 -14.221 2.391 36.635 1.00 18.38 C ANISOU 897 CD1 PHE B 124 2174 1830 2979 -68 380 -267 C ATOM 898 CD2 PHE B 124 -12.855 0.436 36.924 1.00 18.54 C ANISOU 898 CD2 PHE B 124 2133 2087 2824 -888 403 192 C ATOM 899 CE1 PHE B 124 -15.340 1.598 36.633 1.00 17.81 C ANISOU 899 CE1 PHE B 124 2180 1781 2805 -225 203 -329 C ATOM 900 CE2 PHE B 124 -13.978 -0.334 36.977 1.00 14.78 C ANISOU 900 CE2 PHE B 124 885 1878 2852 -29 107 -337 C ATOM 901 CZ PHE B 124 -15.224 0.221 36.818 1.00 15.67 C ANISOU 901 CZ PHE B 124 1374 1844 2736 83 449 -289 C ATOM 902 N GLU B 125 -9.311 4.454 35.730 1.00 22.53 N ANISOU 902 N GLU B 125 2760 2375 3425 -1042 28 -918 N ATOM 903 CA GLU B 125 -8.461 5.594 36.150 1.00 24.73 C ANISOU 903 CA GLU B 125 3257 2325 3815 -844 16 -793 C ATOM 904 C GLU B 125 -8.039 6.476 35.003 1.00 24.64 C ANISOU 904 C GLU B 125 3036 2366 3961 -1202 239 -851 C ATOM 905 O GLU B 125 -7.965 7.716 35.163 1.00 27.12 O ANISOU 905 O GLU B 125 3772 2363 4168 -1146 361 -892 O ATOM 906 CB GLU B 125 -7.257 5.122 36.946 1.00 25.99 C ANISOU 906 CB GLU B 125 2978 2830 4067 -977 -387 -916 C ATOM 907 CG GLU B 125 -7.628 4.433 38.224 1.00 28.95 C ANISOU 907 CG GLU B 125 3323 3454 4222 -1102 -686 -826 C ATOM 908 CD GLU B 125 -6.426 4.100 39.102 1.00 33.77 C ANISOU 908 CD GLU B 125 3726 4457 4647 -1245 -824 -595 C ATOM 909 OE1 GLU B 125 -5.316 4.611 38.827 1.00 37.38 O ANISOU 909 OE1 GLU B 125 3885 5329 4991 -1641 -1180 -229 O ATOM 910 OE2 GLU B 125 -6.591 3.313 40.054 1.00 33.50 O ANISOU 910 OE2 GLU B 125 3780 4433 4514 -1384 -857 -760 O ATOM 911 N THR B 126 -7.756 5.876 33.849 1.00 23.62 N ANISOU 911 N THR B 126 2645 2390 3939 -1022 269 -494 N ATOM 912 CA THR B 126 -7.293 6.643 32.688 1.00 24.57 C ANISOU 912 CA THR B 126 2696 2554 4085 -1147 190 -532 C ATOM 913 C THR B 126 -8.448 7.164 31.861 1.00 24.24 C ANISOU 913 C THR B 126 2993 2152 4067 -962 325 -546 C ATOM 914 O THR B 126 -8.452 8.317 31.465 1.00 26.67 O ANISOU 914 O THR B 126 3714 2180 4239 -1021 110 -645 O ATOM 915 CB THR B 126 -6.321 5.830 31.804 1.00 24.83 C ANISOU 915 CB THR B 126 1896 3185 4352 -338 -5 -47 C ATOM 916 OG1 THR B 126 -5.133 5.575 32.564 1.00 28.22 O ANISOU 916 OG1 THR B 126 2331 3856 4534 298 -57 228 O ATOM 917 CG2 THR B 126 -5.965 6.598 30.515 1.00 24.76 C ANISOU 917 CG2 THR B 126 1931 2957 4518 -177 269 -150 C ATOM 918 N PHE B 127 -9.431 6.300 31.552 1.00 22.29 N ANISOU 918 N PHE B 127 2554 2062 3853 -874 348 -656 N ATOM 919 CA PHE B 127 -10.547 6.690 30.707 1.00 20.36 C ANISOU 919 CA PHE B 127 2588 1598 3549 -770 462 -662 C ATOM 920 C PHE B 127 -11.794 7.104 31.476 1.00 21.62 C ANISOU 920 C PHE B 127 3074 1611 3528 -1005 535 -742 C ATOM 921 O PHE B 127 -12.734 7.583 30.878 1.00 23.92 O ANISOU 921 O PHE B 127 3310 2201 3579 -818 830 -698 O ATOM 922 CB PHE B 127 -10.845 5.563 29.703 1.00 19.02 C ANISOU 922 CB PHE B 127 2066 1737 3423 -487 285 -400 C ATOM 923 CG PHE B 127 -9.743 5.348 28.764 1.00 20.66 C ANISOU 923 CG PHE B 127 2424 1938 3489 -864 404 -395 C ATOM 924 CD1 PHE B 127 -8.974 4.217 28.849 1.00 22.16 C ANISOU 924 CD1 PHE B 127 2885 2038 3496 -603 562 -544 C ATOM 925 CD2 PHE B 127 -9.412 6.339 27.846 1.00 20.72 C ANISOU 925 CD2 PHE B 127 2659 1673 3540 -895 616 -223 C ATOM 926 CE1 PHE B 127 -7.897 4.041 28.003 1.00 21.80 C ANISOU 926 CE1 PHE B 127 2762 2001 3520 -1041 740 -505 C ATOM 927 CE2 PHE B 127 -8.342 6.180 26.982 1.00 22.08 C ANISOU 927 CE2 PHE B 127 3041 1627 3720 -496 670 -199 C ATOM 928 CZ PHE B 127 -7.574 5.041 27.053 1.00 21.87 C ANISOU 928 CZ PHE B 127 2972 1716 3623 -507 673 -529 C ATOM 929 N AASN B 128 -11.806 6.933 32.791 0.50 21.55 N ANISOU 929 N AASN B 128 3036 1725 3429 -987 645 -827 N ATOM 930 N BASN B 128 -11.772 6.882 32.794 0.50 22.81 N ANISOU 930 N BASN B 128 3380 1787 3501 -1081 671 -905 N ATOM 931 CA AASN B 128 -12.904 7.463 33.587 0.50 21.78 C ANISOU 931 CA AASN B 128 3232 1626 3419 -638 563 -685 C ATOM 932 CA BASN B 128 -12.818 7.322 33.726 0.50 24.32 C ANISOU 932 CA BASN B 128 3807 1866 3569 -778 636 -771 C ATOM 933 C AASN B 128 -14.266 6.870 33.174 0.50 19.59 C ANISOU 933 C AASN B 128 2684 1460 3300 -198 554 -579 C ATOM 934 C BASN B 128 -14.225 6.806 33.356 0.50 22.14 C ANISOU 934 C BASN B 128 3201 1847 3363 -558 642 -705 C ATOM 935 O AASN B 128 -15.293 7.562 33.142 0.50 17.90 O ANISOU 935 O AASN B 128 2469 1134 3198 53 304 -504 O ATOM 936 O BASN B 128 -15.237 7.483 33.546 0.50 22.78 O ANISOU 936 O BASN B 128 3369 2017 3269 -721 580 -709 O ATOM 937 CB AASN B 128 -12.927 9.006 33.492 0.50 23.01 C ANISOU 937 CB AASN B 128 3328 1923 3492 -677 534 -667 C ATOM 938 CB BASN B 128 -12.775 8.858 33.884 0.50 26.71 C ANISOU 938 CB BASN B 128 4334 2032 3784 -569 540 -824 C ATOM 939 CG AASN B 128 -11.614 9.650 33.946 0.50 24.24 C ANISOU 939 CG AASN B 128 3331 2288 3591 -770 556 -742 C ATOM 940 CG BASN B 128 -13.286 9.355 35.249 0.50 28.14 C ANISOU 940 CG BASN B 128 4664 2067 3963 -276 441 -781 C ATOM 941 OD1AASN B 128 -10.869 10.226 33.146 0.50 28.03 O ANISOU 941 OD1AASN B 128 4104 2624 3921 -821 476 -761 O ATOM 942 OD1BASN B 128 -13.261 8.648 36.268 0.50 28.86 O ANISOU 942 OD1BASN B 128 4678 2258 4029 209 379 -992 O ATOM 943 ND2AASN B 128 -11.331 9.547 35.222 0.50 22.13 N ANISOU 943 ND2AASN B 128 2828 2247 3333 -977 131 -973 N ATOM 944 ND2BASN B 128 -13.744 10.610 35.264 0.50 31.19 N ANISOU 944 ND2BASN B 128 4855 2888 4109 -521 369 -656 N ATOM 945 N VAL B 129 -14.293 5.577 32.821 1.00 19.72 N ANISOU 945 N VAL B 129 2729 1446 3316 -499 628 -545 N ATOM 946 CA VAL B 129 -15.576 4.980 32.497 1.00 18.86 C ANISOU 946 CA VAL B 129 2546 1415 3205 -98 504 -471 C ATOM 947 C VAL B 129 -16.411 4.858 33.792 1.00 17.23 C ANISOU 947 C VAL B 129 2292 1247 3008 -209 434 -395 C ATOM 948 O VAL B 129 -15.826 4.737 34.887 1.00 19.49 O ANISOU 948 O VAL B 129 2672 1585 3149 -556 179 -360 O ATOM 949 CB VAL B 129 -15.436 3.588 31.815 1.00 18.16 C ANISOU 949 CB VAL B 129 2699 1117 3086 -85 950 -247 C ATOM 950 CG1 VAL B 129 -14.564 3.677 30.522 1.00 19.16 C ANISOU 950 CG1 VAL B 129 2574 1716 2990 -666 1036 -444 C ATOM 951 CG2 VAL B 129 -14.871 2.572 32.749 1.00 17.68 C ANISOU 951 CG2 VAL B 129 2243 1330 3145 -274 643 -229 C ATOM 952 N PRO B 130 -17.746 4.946 33.661 1.00 16.29 N ANISOU 952 N PRO B 130 2301 961 2926 -232 422 -268 N ATOM 953 CA PRO B 130 -18.626 4.897 34.851 1.00 16.70 C ANISOU 953 CA PRO B 130 2028 1497 2821 218 559 -144 C ATOM 954 C PRO B 130 -18.804 3.466 35.359 1.00 16.18 C ANISOU 954 C PRO B 130 2284 1220 2646 -136 487 -298 C ATOM 955 O PRO B 130 -19.084 3.249 36.532 1.00 15.81 O ANISOU 955 O PRO B 130 2059 1379 2568 5 165 -247 O ATOM 956 CB PRO B 130 -19.966 5.453 34.340 1.00 17.26 C ANISOU 956 CB PRO B 130 2131 1542 2885 148 442 -350 C ATOM 957 CG PRO B 130 -19.956 5.097 32.877 1.00 16.30 C ANISOU 957 CG PRO B 130 1713 1537 2943 -150 716 -297 C ATOM 958 CD PRO B 130 -18.521 5.295 32.457 1.00 16.87 C ANISOU 958 CD PRO B 130 1918 1667 2824 -397 436 -249 C ATOM 959 N ALA B 131 -18.578 2.482 34.473 1.00 16.21 N ANISOU 959 N ALA B 131 2479 1048 2633 -134 377 -216 N ATOM 960 CA ALA B 131 -18.797 1.070 34.811 1.00 13.40 C ANISOU 960 CA ALA B 131 1588 871 2634 -224 400 -361 C ATOM 961 C ALA B 131 -18.085 0.271 33.733 1.00 13.34 C ANISOU 961 C ALA B 131 1668 841 2561 104 65 -30 C ATOM 962 O ALA B 131 -17.924 0.770 32.595 1.00 15.25 O ANISOU 962 O ALA B 131 2371 1011 2414 -13 254 -18 O ATOM 963 CB ALA B 131 -20.279 0.782 34.762 1.00 15.61 C ANISOU 963 CB ALA B 131 1484 1568 2877 -193 628 -111 C ATOM 964 N MET B 132 -17.653 -0.933 34.081 1.00 14.51 N ANISOU 964 N MET B 132 1902 998 2613 93 274 -238 N ATOM 965 CA AMET B 132 -17.067 -1.787 33.055 0.50 14.95 C ANISOU 965 CA AMET B 132 1871 1077 2733 -34 190 58 C ATOM 966 CA BMET B 132 -16.869 -1.775 33.169 0.50 15.80 C ANISOU 966 CA BMET B 132 1897 1352 2753 338 285 -183 C ATOM 967 C MET B 132 -17.205 -3.251 33.428 1.00 14.42 C ANISOU 967 C MET B 132 1732 1132 2614 -113 309 -170 C ATOM 968 O MET B 132 -17.696 -3.600 34.520 1.00 16.21 O ANISOU 968 O MET B 132 1997 1510 2652 -315 304 -403 O ATOM 969 CB AMET B 132 -15.606 -1.415 32.782 0.50 19.70 C ANISOU 969 CB AMET B 132 2767 1726 2993 -177 -26 519 C ATOM 970 CB BMET B 132 -15.357 -1.510 33.384 0.50 19.02 C ANISOU 970 CB BMET B 132 2094 2111 3024 797 150 -326 C ATOM 971 CG AMET B 132 -14.755 -1.457 34.014 0.50 22.32 C ANISOU 971 CG AMET B 132 2913 2539 3027 -322 -427 874 C ATOM 972 CG BMET B 132 -14.351 -2.228 32.444 0.50 24.48 C ANISOU 972 CG BMET B 132 2632 3371 3300 890 121 -368 C ATOM 973 SD AMET B 132 -14.059 -3.073 34.242 0.50 25.13 S ANISOU 973 SD AMET B 132 2668 3587 3292 -969 -317 1233 S ATOM 974 SD BMET B 132 -13.395 -3.558 33.281 0.50 32.50 S ANISOU 974 SD BMET B 132 3763 4989 3597 1116 -81 -843 S ATOM 975 CE AMET B 132 -12.736 -2.815 33.018 0.50 20.25 C ANISOU 975 CE AMET B 132 498 3941 3255 -585 -327 1520 C ATOM 976 CE BMET B 132 -11.886 -3.519 32.332 0.50 35.03 C ANISOU 976 CE BMET B 132 4240 5550 3519 1052 -234 -784 C ATOM 977 N TYR B 133 -16.877 -4.091 32.451 1.00 14.41 N ANISOU 977 N TYR B 133 1733 1065 2675 -10 69 -142 N ATOM 978 CA TYR B 133 -16.894 -5.532 32.644 1.00 12.91 C ANISOU 978 CA TYR B 133 1340 923 2643 73 88 -255 C ATOM 979 C TYR B 133 -15.902 -6.114 31.674 1.00 14.80 C ANISOU 979 C TYR B 133 1722 1237 2664 -51 35 -158 C ATOM 980 O TYR B 133 -15.675 -5.505 30.631 1.00 13.27 O ANISOU 980 O TYR B 133 1474 1018 2549 20 164 -107 O ATOM 981 CB TYR B 133 -18.303 -6.063 32.381 1.00 14.08 C ANISOU 981 CB TYR B 133 1505 951 2892 -49 263 135 C ATOM 982 CG TYR B 133 -18.529 -7.469 32.903 1.00 14.32 C ANISOU 982 CG TYR B 133 1442 1084 2916 355 380 159 C ATOM 983 CD1 TYR B 133 -18.269 -8.562 32.101 1.00 15.03 C ANISOU 983 CD1 TYR B 133 1515 985 3213 -100 211 340 C ATOM 984 CD2 TYR B 133 -19.102 -7.687 34.173 1.00 17.47 C ANISOU 984 CD2 TYR B 133 1964 1766 2908 -389 82 760 C ATOM 985 CE1 TYR B 133 -18.465 -9.853 32.574 1.00 16.92 C ANISOU 985 CE1 TYR B 133 1836 1146 3449 -79 107 348 C ATOM 986 CE2 TYR B 133 -19.331 -9.011 34.643 1.00 16.99 C ANISOU 986 CE2 TYR B 133 1871 1432 3151 -222 -353 344 C ATOM 987 CZ TYR B 133 -19.007 -10.061 33.824 1.00 18.77 C ANISOU 987 CZ TYR B 133 2241 1483 3407 -560 -148 249 C ATOM 988 OH TYR B 133 -19.228 -11.370 34.249 1.00 20.79 O ANISOU 988 OH TYR B 133 3093 1217 3590 -416 87 606 O ATOM 989 N VAL B 134 -15.355 -7.285 32.002 1.00 13.40 N ANISOU 989 N VAL B 134 1392 1152 2549 -24 157 -266 N ATOM 990 CA AVAL B 134 -14.473 -8.025 31.112 0.70 14.03 C ANISOU 990 CA AVAL B 134 1549 1048 2733 307 -280 -234 C ATOM 991 CA BVAL B 134 -14.560 -8.005 31.021 0.30 11.05 C ANISOU 991 CA BVAL B 134 943 830 2426 91 -246 -168 C ATOM 992 C VAL B 134 -15.003 -9.445 30.977 1.00 12.89 C ANISOU 992 C VAL B 134 1183 1228 2486 111 -5 -94 C ATOM 993 O VAL B 134 -15.139 -10.127 31.997 1.00 16.30 O ANISOU 993 O VAL B 134 2105 1693 2396 -119 45 260 O ATOM 994 CB AVAL B 134 -13.030 -8.139 31.707 0.70 18.21 C ANISOU 994 CB AVAL B 134 1769 2024 3127 -82 -406 -422 C ATOM 995 CB BVAL B 134 -13.011 -7.836 31.187 0.30 8.25 C ANISOU 995 CB BVAL B 134 173 679 2282 111 -429 14 C ATOM 996 CG1AVAL B 134 -12.069 -8.676 30.665 0.70 19.22 C ANISOU 996 CG1AVAL B 134 2167 1976 3162 564 -346 -208 C ATOM 997 CG1BVAL B 134 -12.529 -8.450 32.520 0.30 8.78 C ANISOU 997 CG1BVAL B 134 609 631 2096 304 -800 270 C ATOM 998 CG2AVAL B 134 -12.531 -6.837 32.280 0.70 19.28 C ANISOU 998 CG2AVAL B 134 1412 2687 3224 -235 -151 -553 C ATOM 999 CG2BVAL B 134 -12.278 -8.448 29.970 0.30 7.16 C ANISOU 999 CG2BVAL B 134 58 279 2382 56 -338 -287 C ATOM 1000 N ALA B 135 -15.325 -9.859 29.756 1.00 12.21 N ANISOU 1000 N ALA B 135 920 1246 2473 -119 216 -201 N ATOM 1001 CA ALA B 135 -15.789 -11.196 29.483 1.00 11.37 C ANISOU 1001 CA ALA B 135 533 1258 2530 -128 -141 -111 C ATOM 1002 C ALA B 135 -14.847 -11.970 28.573 1.00 13.36 C ANISOU 1002 C ALA B 135 1586 1114 2377 77 12 163 C ATOM 1003 O ALA B 135 -14.138 -11.395 27.729 1.00 13.36 O ANISOU 1003 O ALA B 135 1613 1029 2436 -9 64 81 O ATOM 1004 CB ALA B 135 -17.104 -11.127 28.823 1.00 13.62 C ANISOU 1004 CB ALA B 135 554 1829 2792 -21 106 67 C ATOM 1005 N ILE B 136 -14.818 -13.297 28.762 1.00 14.55 N ANISOU 1005 N ILE B 136 1868 1209 2450 111 -58 -10 N ATOM 1006 CA ILE B 136 -14.013 -14.144 27.894 1.00 12.85 C ANISOU 1006 CA ILE B 136 1424 1068 2389 183 -84 295 C ATOM 1007 C ILE B 136 -14.617 -14.204 26.497 1.00 10.81 C ANISOU 1007 C ILE B 136 711 902 2496 158 139 222 C ATOM 1008 O ILE B 136 -15.819 -14.441 26.320 1.00 11.43 O ANISOU 1008 O ILE B 136 891 916 2535 -78 26 58 O ATOM 1009 CB ILE B 136 -13.877 -15.570 28.482 1.00 13.33 C ANISOU 1009 CB ILE B 136 1349 1289 2427 30 -302 395 C ATOM 1010 CG1 ILE B 136 -13.075 -15.499 29.778 1.00 16.53 C ANISOU 1010 CG1 ILE B 136 2323 1413 2543 123 -326 521 C ATOM 1011 CG2 ILE B 136 -13.156 -16.493 27.495 1.00 15.97 C ANISOU 1011 CG2 ILE B 136 2213 1142 2712 571 197 288 C ATOM 1012 CD1 ILE B 136 -13.118 -16.883 30.532 1.00 18.83 C ANISOU 1012 CD1 ILE B 136 2751 1584 2818 -91 -385 480 C ATOM 1013 N GLN B 137 -13.756 -14.031 25.482 1.00 13.13 N ANISOU 1013 N GLN B 137 1501 1112 2375 80 147 134 N ATOM 1014 CA GLN B 137 -14.221 -13.969 24.102 1.00 11.62 C ANISOU 1014 CA GLN B 137 624 1211 2579 -327 106 151 C ATOM 1015 C GLN B 137 -15.076 -15.187 23.695 1.00 10.60 C ANISOU 1015 C GLN B 137 543 919 2566 -229 106 221 C ATOM 1016 O GLN B 137 -16.218 -15.040 23.224 1.00 10.33 O ANISOU 1016 O GLN B 137 549 1017 2360 -189 127 142 O ATOM 1017 CB GLN B 137 -12.986 -13.881 23.190 1.00 11.33 C ANISOU 1017 CB GLN B 137 655 669 2981 -284 387 184 C ATOM 1018 CG GLN B 137 -12.382 -12.466 23.313 1.00 12.12 C ANISOU 1018 CG GLN B 137 704 893 3008 -238 -60 186 C ATOM 1019 CD GLN B 137 -10.886 -12.365 23.018 1.00 13.02 C ANISOU 1019 CD GLN B 137 920 1037 2990 -63 40 112 C ATOM 1020 OE1 GLN B 137 -10.268 -13.313 22.493 1.00 13.95 O ANISOU 1020 OE1 GLN B 137 955 1315 3030 -212 194 52 O ATOM 1021 NE2 GLN B 137 -10.296 -11.188 23.365 1.00 13.67 N ANISOU 1021 NE2 GLN B 137 1178 1281 2735 -160 260 290 N ATOM 1022 N ALA B 138 -14.569 -16.395 23.933 1.00 12.67 N ANISOU 1022 N ALA B 138 1588 664 2564 -315 110 245 N ATOM 1023 CA ALA B 138 -15.304 -17.594 23.560 1.00 10.88 C ANISOU 1023 CA ALA B 138 778 831 2525 267 271 30 C ATOM 1024 C ALA B 138 -16.679 -17.698 24.275 1.00 12.13 C ANISOU 1024 C ALA B 138 1223 1091 2296 171 466 63 C ATOM 1025 O ALA B 138 -17.635 -18.186 23.676 1.00 12.86 O ANISOU 1025 O ALA B 138 1393 929 2565 293 206 -12 O ATOM 1026 CB ALA B 138 -14.481 -18.788 23.847 1.00 12.31 C ANISOU 1026 CB ALA B 138 1393 680 2604 638 202 110 C ATOM 1027 N VAL B 139 -16.766 -17.226 25.530 1.00 11.22 N ANISOU 1027 N VAL B 139 1174 824 2263 133 297 -11 N ATOM 1028 CA VAL B 139 -18.032 -17.287 26.246 1.00 13.02 C ANISOU 1028 CA VAL B 139 1377 1181 2388 335 449 12 C ATOM 1029 C VAL B 139 -19.035 -16.384 25.513 1.00 11.46 C ANISOU 1029 C VAL B 139 934 932 2488 -10 296 -119 C ATOM 1030 O VAL B 139 -20.211 -16.740 25.290 1.00 11.37 O ANISOU 1030 O VAL B 139 980 876 2466 5 225 -104 O ATOM 1031 CB VAL B 139 -17.892 -16.911 27.710 1.00 13.20 C ANISOU 1031 CB VAL B 139 1258 1245 2510 280 413 133 C ATOM 1032 CG1 VAL B 139 -19.307 -16.778 28.336 1.00 14.60 C ANISOU 1032 CG1 VAL B 139 738 1974 2835 182 337 356 C ATOM 1033 CG2 VAL B 139 -16.997 -17.967 28.413 1.00 14.58 C ANISOU 1033 CG2 VAL B 139 1620 1085 2836 255 -95 467 C ATOM 1034 N LEU B 140 -18.584 -15.187 25.106 1.00 10.77 N ANISOU 1034 N LEU B 140 695 885 2512 33 279 100 N ATOM 1035 CA LEU B 140 -19.496 -14.320 24.378 1.00 12.15 C ANISOU 1035 CA LEU B 140 1167 935 2513 -407 206 -81 C ATOM 1036 C LEU B 140 -19.971 -14.923 23.059 1.00 10.40 C ANISOU 1036 C LEU B 140 912 694 2344 41 194 26 C ATOM 1037 O LEU B 140 -21.135 -14.735 22.696 1.00 12.17 O ANISOU 1037 O LEU B 140 1104 1035 2485 -37 195 16 O ATOM 1038 CB LEU B 140 -18.876 -12.952 24.108 1.00 11.62 C ANISOU 1038 CB LEU B 140 696 1063 2657 -350 297 -219 C ATOM 1039 CG LEU B 140 -18.539 -12.171 25.368 1.00 11.16 C ANISOU 1039 CG LEU B 140 539 1023 2679 -203 318 -95 C ATOM 1040 CD1 LEU B 140 -17.878 -10.837 24.909 1.00 11.79 C ANISOU 1040 CD1 LEU B 140 888 823 2770 -543 236 54 C ATOM 1041 CD2 LEU B 140 -19.796 -11.874 26.196 1.00 13.89 C ANISOU 1041 CD2 LEU B 140 1155 1355 2768 287 550 -213 C ATOM 1042 N ASER B 141 -19.083 -15.604 22.326 0.50 12.38 N ANISOU 1042 N ASER B 141 1395 997 2313 -137 213 -183 N ATOM 1043 N BSER B 141 -19.111 -15.605 22.297 0.50 10.07 N ANISOU 1043 N BSER B 141 950 666 2210 257 265 110 N ATOM 1044 CA ASER B 141 -19.530 -16.234 21.092 0.50 13.74 C ANISOU 1044 CA ASER B 141 1292 1410 2518 -399 498 -232 C ATOM 1045 CA BSER B 141 -19.641 -16.168 21.053 0.50 10.67 C ANISOU 1045 CA BSER B 141 642 1120 2292 -45 691 286 C ATOM 1046 C ASER B 141 -20.586 -17.286 21.378 0.50 12.18 C ANISOU 1046 C ASER B 141 1346 813 2468 85 467 -49 C ATOM 1047 C BSER B 141 -20.566 -17.354 21.316 0.50 11.24 C ANISOU 1047 C BSER B 141 980 955 2336 10 523 57 C ATOM 1048 O ASER B 141 -21.592 -17.372 20.679 0.50 11.89 O ANISOU 1048 O ASER B 141 1361 551 2607 343 288 30 O ATOM 1049 O BSER B 141 -21.446 -17.623 20.503 0.50 11.77 O ANISOU 1049 O BSER B 141 895 1183 2394 -378 353 -143 O ATOM 1050 CB ASER B 141 -18.359 -16.845 20.322 0.50 14.64 C ANISOU 1050 CB ASER B 141 1040 1730 2791 -496 361 -339 C ATOM 1051 CB BSER B 141 -18.531 -16.554 20.070 0.50 10.42 C ANISOU 1051 CB BSER B 141 378 1199 2384 530 511 683 C ATOM 1052 OG ASER B 141 -17.586 -15.825 19.742 0.50 14.75 O ANISOU 1052 OG ASER B 141 712 1923 2970 -565 497 -451 O ATOM 1053 OG BSER B 141 -17.656 -17.492 20.674 0.50 10.20 O ANISOU 1053 OG BSER B 141 439 1038 2397 126 236 281 O ATOM 1054 N LEU B 142 -20.358 -18.057 22.426 1.00 10.90 N ANISOU 1054 N LEU B 142 874 910 2356 75 644 -9 N ATOM 1055 CA LEU B 142 -21.363 -19.061 22.837 1.00 11.33 C ANISOU 1055 CA LEU B 142 642 1289 2373 53 561 292 C ATOM 1056 C LEU B 142 -22.706 -18.401 23.131 1.00 12.36 C ANISOU 1056 C LEU B 142 1150 1042 2502 -26 23 -80 C ATOM 1057 O LEU B 142 -23.720 -18.827 22.587 1.00 13.13 O ANISOU 1057 O LEU B 142 1189 997 2802 17 384 116 O ATOM 1058 CB LEU B 142 -20.864 -19.879 24.027 1.00 10.56 C ANISOU 1058 CB LEU B 142 536 1036 2441 -210 175 216 C ATOM 1059 CG LEU B 142 -21.721 -21.093 24.417 1.00 13.69 C ANISOU 1059 CG LEU B 142 1420 1170 2613 -334 203 6 C ATOM 1060 CD1 LEU B 142 -21.571 -22.177 23.365 1.00 14.26 C ANISOU 1060 CD1 LEU B 142 1441 1024 2954 -221 47 -68 C ATOM 1061 CD2 LEU B 142 -21.235 -21.590 25.766 1.00 15.59 C ANISOU 1061 CD2 LEU B 142 1613 1675 2637 -209 -117 150 C ATOM 1062 N TYR B 143 -22.676 -17.293 23.882 1.00 11.44 N ANISOU 1062 N TYR B 143 993 981 2370 112 246 -257 N ATOM 1063 CA TYR B 143 -23.919 -16.604 24.214 1.00 13.24 C ANISOU 1063 CA TYR B 143 953 1509 2571 -24 333 -87 C ATOM 1064 C TYR B 143 -24.593 -16.076 22.966 1.00 12.65 C ANISOU 1064 C TYR B 143 763 1308 2735 64 356 -186 C ATOM 1065 O TYR B 143 -25.838 -16.060 22.914 1.00 14.70 O ANISOU 1065 O TYR B 143 1135 1530 2921 202 352 93 O ATOM 1066 CB TYR B 143 -23.624 -15.428 25.130 1.00 13.42 C ANISOU 1066 CB TYR B 143 1280 1311 2506 6 502 -284 C ATOM 1067 CG TYR B 143 -23.298 -15.802 26.541 1.00 12.73 C ANISOU 1067 CG TYR B 143 1338 931 2566 -107 633 -15 C ATOM 1068 CD1 TYR B 143 -23.040 -14.804 27.468 1.00 16.40 C ANISOU 1068 CD1 TYR B 143 2193 1408 2629 173 540 -295 C ATOM 1069 CD2 TYR B 143 -23.251 -17.146 26.989 1.00 15.28 C ANISOU 1069 CD2 TYR B 143 1943 1203 2660 -55 707 387 C ATOM 1070 CE1 TYR B 143 -22.744 -15.115 28.792 1.00 18.56 C ANISOU 1070 CE1 TYR B 143 2617 1656 2778 295 21 -63 C ATOM 1071 CE2 TYR B 143 -22.975 -17.458 28.303 1.00 14.95 C ANISOU 1071 CE2 TYR B 143 1754 1282 2644 -28 491 175 C ATOM 1072 CZ TYR B 143 -22.738 -16.453 29.210 1.00 17.06 C ANISOU 1072 CZ TYR B 143 2382 1408 2693 334 65 230 C ATOM 1073 OH TYR B 143 -22.452 -16.717 30.548 1.00 20.31 O ANISOU 1073 OH TYR B 143 3102 1945 2669 432 -206 274 O ATOM 1074 N ALA B 144 -23.819 -15.637 21.954 1.00 12.20 N ANISOU 1074 N ALA B 144 1082 996 2559 144 417 -138 N ATOM 1075 CA ALA B 144 -24.386 -15.108 20.721 1.00 13.11 C ANISOU 1075 CA ALA B 144 833 1279 2870 94 255 48 C ATOM 1076 C ALA B 144 -25.267 -16.160 20.046 1.00 15.89 C ANISOU 1076 C ALA B 144 1919 1234 2884 -118 -85 -174 C ATOM 1077 O ALA B 144 -26.221 -15.818 19.336 1.00 17.21 O ANISOU 1077 O ALA B 144 1827 1682 3031 160 -225 -32 O ATOM 1078 CB ALA B 144 -23.320 -14.596 19.760 1.00 13.05 C ANISOU 1078 CB ALA B 144 1134 1178 2648 -179 190 3 C ATOM 1079 N SER B 145 -24.964 -17.442 20.216 1.00 14.61 N ANISOU 1079 N SER B 145 1521 1137 2892 -174 88 32 N ATOM 1080 CA ASER B 145 -25.719 -18.552 19.693 0.50 14.41 C ANISOU 1080 CA ASER B 145 1307 1016 3154 -128 -180 -264 C ATOM 1081 CA BSER B 145 -25.715 -18.553 19.712 0.50 17.96 C ANISOU 1081 CA BSER B 145 1842 1549 3434 -235 -132 -204 C ATOM 1082 C SER B 145 -26.886 -18.878 20.571 1.00 18.87 C ANISOU 1082 C SER B 145 1682 1802 3686 -255 -373 -244 C ATOM 1083 O SER B 145 -27.531 -19.764 20.191 1.00 22.55 O ANISOU 1083 O SER B 145 2071 2246 4252 -328 -475 -112 O ATOM 1084 CB ASER B 145 -24.826 -19.796 19.469 0.50 13.77 C ANISOU 1084 CB ASER B 145 1480 838 2912 360 -115 -154 C ATOM 1085 CB BSER B 145 -24.792 -19.766 19.545 0.50 23.25 C ANISOU 1085 CB BSER B 145 2769 2314 3752 11 -33 -95 C ATOM 1086 OG ASER B 145 -24.590 -20.494 20.672 0.50 9.07 O ANISOU 1086 OG ASER B 145 490 366 2591 91 -167 -11 O ATOM 1087 OG BSER B 145 -23.971 -19.520 18.426 0.50 27.34 O ANISOU 1087 OG BSER B 145 3424 2897 4069 -98 -35 107 O ATOM 1088 N GLY B 146 -27.045 -18.295 21.692 1.00 17.26 N ANISOU 1088 N GLY B 146 818 1835 3906 291 383 277 N ATOM 1089 CA GLY B 146 -28.164 -18.587 22.572 1.00 19.41 C ANISOU 1089 CA GLY B 146 981 2256 4136 94 510 420 C ATOM 1090 C GLY B 146 -27.908 -19.666 23.633 1.00 18.49 C ANISOU 1090 C GLY B 146 638 2171 4215 -515 888 773 C ATOM 1091 O GLY B 146 -28.798 -20.019 24.322 1.00 24.15 O ANISOU 1091 O GLY B 146 1681 2985 4508 -669 679 881 O ATOM 1092 N ARG B 147 -26.677 -20.045 23.790 1.00 18.04 N ANISOU 1092 N ARG B 147 1256 1597 4003 180 271 154 N ATOM 1093 CA ARG B 147 -26.307 -21.122 24.622 1.00 19.62 C ANISOU 1093 CA ARG B 147 2163 1406 3887 483 92 266 C ATOM 1094 C ARG B 147 -25.457 -20.650 25.764 1.00 16.14 C ANISOU 1094 C ARG B 147 1343 1249 3539 -406 362 464 C ATOM 1095 O ARG B 147 -24.771 -19.788 25.630 1.00 15.49 O ANISOU 1095 O ARG B 147 1149 1166 3568 -183 466 -188 O ATOM 1096 CB ARG B 147 -25.443 -22.139 23.766 1.00 21.33 C ANISOU 1096 CB ARG B 147 2934 1096 4074 314 -195 -211 C ATOM 1097 CG ARG B 147 -26.114 -22.809 22.700 1.00 25.21 C ANISOU 1097 CG ARG B 147 3546 1605 4427 -639 17 -550 C ATOM 1098 CD ARG B 147 -25.285 -23.454 21.767 1.00 27.04 C ANISOU 1098 CD ARG B 147 3809 1954 4511 -1153 176 -1380 C ATOM 1099 NE ARG B 147 -26.042 -24.328 20.852 1.00 32.10 N ANISOU 1099 NE ARG B 147 4610 2662 4923 -276 -110 -871 N ATOM 1100 CZ ARG B 147 -26.718 -23.948 19.850 1.00 31.11 C ANISOU 1100 CZ ARG B 147 4388 2317 5114 -101 -705 -706 C ATOM 1101 NH1 ARG B 147 -27.352 -24.794 19.159 1.00 31.36 N ANISOU 1101 NH1 ARG B 147 4285 2293 5336 -73 -758 -373 N ATOM 1102 NH2 ARG B 147 -26.757 -22.734 19.515 1.00 32.23 N ANISOU 1102 NH2 ARG B 147 4798 2219 5229 -476 -979 -536 N ATOM 1103 N THR B 148 -25.484 -21.352 26.865 1.00 14.35 N ANISOU 1103 N THR B 148 1046 1143 3264 131 506 426 N ATOM 1104 CA THR B 148 -24.570 -21.195 27.911 1.00 16.08 C ANISOU 1104 CA THR B 148 1395 1390 3324 157 970 359 C ATOM 1105 C THR B 148 -23.561 -22.367 28.191 1.00 17.53 C ANISOU 1105 C THR B 148 2120 1265 3277 -183 879 167 C ATOM 1106 O THR B 148 -22.765 -22.248 28.888 1.00 16.20 O ANISOU 1106 O THR B 148 2089 954 3114 -32 946 108 O ATOM 1107 CB THR B 148 -25.173 -20.777 29.270 1.00 16.82 C ANISOU 1107 CB THR B 148 1995 1071 3324 128 1314 210 C ATOM 1108 OG1 THR B 148 -25.991 -21.786 29.705 1.00 19.28 O ANISOU 1108 OG1 THR B 148 2023 1818 3486 90 1041 354 O ATOM 1109 CG2 THR B 148 -25.982 -19.545 29.121 1.00 19.41 C ANISOU 1109 CG2 THR B 148 2051 1930 3394 602 1074 294 C ATOM 1110 N THR B 149 -23.783 -23.448 27.458 1.00 15.06 N ANISOU 1110 N THR B 149 1753 937 3031 209 637 185 N ATOM 1111 CA THR B 149 -22.962 -24.607 27.496 1.00 13.35 C ANISOU 1111 CA THR B 149 1263 978 2830 -98 609 64 C ATOM 1112 C THR B 149 -22.639 -25.067 26.101 1.00 16.71 C ANISOU 1112 C THR B 149 1964 1313 3070 192 654 217 C ATOM 1113 O THR B 149 -23.371 -25.072 25.361 1.00 15.26 O ANISOU 1113 O THR B 149 1195 1376 3229 41 811 -6 O ATOM 1114 CB THR B 149 -23.682 -25.783 28.350 1.00 13.85 C ANISOU 1114 CB THR B 149 1563 804 2894 -30 563 204 C ATOM 1115 OG1 THR B 149 -23.739 -25.405 29.691 1.00 15.75 O ANISOU 1115 OG1 THR B 149 1922 1099 2961 -194 673 -29 O ATOM 1116 CG2 THR B 149 -22.894 -27.060 28.216 1.00 14.54 C ANISOU 1116 CG2 THR B 149 1383 1154 2990 -74 620 249 C ATOM 1117 N GLY B 150 -21.352 -25.381 25.905 1.00 13.71 N ANISOU 1117 N GLY B 150 1420 897 2892 -75 560 124 N ATOM 1118 CA GLY B 150 -20.936 -25.872 24.604 1.00 13.12 C ANISOU 1118 CA GLY B 150 1146 1151 2688 -681 572 -59 C ATOM 1119 C GLY B 150 -19.412 -25.777 24.538 1.00 12.24 C ANISOU 1119 C GLY B 150 1094 890 2667 -765 355 124 C ATOM 1120 O GLY B 150 -18.745 -25.428 25.521 1.00 12.80 O ANISOU 1120 O GLY B 150 690 1245 2928 7 416 -189 O ATOM 1121 N ILE B 151 -18.863 -26.106 23.368 1.00 11.69 N ANISOU 1121 N ILE B 151 830 1045 2567 302 798 271 N ATOM 1122 CA ILE B 151 -17.419 -25.977 23.215 1.00 11.34 C ANISOU 1122 CA ILE B 151 697 1159 2453 127 563 280 C ATOM 1123 C ILE B 151 -17.179 -25.072 22.011 1.00 12.20 C ANISOU 1123 C ILE B 151 1108 1007 2521 -15 556 238 C ATOM 1124 O ILE B 151 -17.719 -25.303 20.928 1.00 12.92 O ANISOU 1124 O ILE B 151 1475 967 2467 -162 416 243 O ATOM 1125 CB ILE B 151 -16.701 -27.351 23.092 1.00 12.06 C ANISOU 1125 CB ILE B 151 830 1159 2595 330 369 19 C ATOM 1126 CG1 ILE B 151 -15.199 -27.087 22.956 1.00 11.62 C ANISOU 1126 CG1 ILE B 151 876 808 2729 375 376 169 C ATOM 1127 CG2 ILE B 151 -17.262 -28.198 21.973 1.00 12.30 C ANISOU 1127 CG2 ILE B 151 1142 941 2591 -207 362 135 C ATOM 1128 CD1 ILE B 151 -14.329 -28.357 23.069 1.00 13.38 C ANISOU 1128 CD1 ILE B 151 1205 948 2929 457 307 195 C ATOM 1129 N VAL B 152 -16.414 -24.009 22.243 1.00 12.20 N ANISOU 1129 N VAL B 152 1522 627 2487 22 405 184 N ATOM 1130 CA VAL B 152 -16.173 -23.050 21.167 1.00 11.36 C ANISOU 1130 CA VAL B 152 1248 555 2512 -95 294 208 C ATOM 1131 C VAL B 152 -14.830 -23.327 20.509 1.00 10.77 C ANISOU 1131 C VAL B 152 495 1003 2593 244 36 327 C ATOM 1132 O VAL B 152 -13.843 -23.578 21.211 1.00 12.90 O ANISOU 1132 O VAL B 152 730 1557 2613 437 124 335 O ATOM 1133 CB VAL B 152 -16.207 -21.666 21.760 1.00 9.73 C ANISOU 1133 CB VAL B 152 732 563 2401 -214 339 140 C ATOM 1134 CG1 VAL B 152 -15.853 -20.605 20.649 1.00 11.36 C ANISOU 1134 CG1 VAL B 152 1219 805 2290 254 622 178 C ATOM 1135 CG2 VAL B 152 -17.624 -21.381 22.270 1.00 12.05 C ANISOU 1135 CG2 VAL B 152 1071 1083 2425 -175 463 370 C ATOM 1136 N LEU B 153 -14.765 -23.242 19.183 1.00 10.60 N ANISOU 1136 N LEU B 153 651 872 2504 134 378 112 N ATOM 1137 CA LEU B 153 -13.476 -23.150 18.484 1.00 10.95 C ANISOU 1137 CA LEU B 153 942 686 2533 175 634 99 C ATOM 1138 C LEU B 153 -13.426 -21.703 18.081 1.00 10.50 C ANISOU 1138 C LEU B 153 592 1029 2368 83 109 119 C ATOM 1139 O LEU B 153 -14.243 -21.285 17.224 1.00 13.08 O ANISOU 1139 O LEU B 153 867 1406 2697 -28 -260 271 O ATOM 1140 CB LEU B 153 -13.473 -24.043 17.230 1.00 12.38 C ANISOU 1140 CB LEU B 153 978 1153 2574 108 633 -62 C ATOM 1141 CG LEU B 153 -12.250 -23.806 16.314 1.00 16.64 C ANISOU 1141 CG LEU B 153 1560 1888 2877 164 678 -373 C ATOM 1142 CD1 LEU B 153 -10.994 -24.369 16.965 1.00 18.45 C ANISOU 1142 CD1 LEU B 153 1859 1820 3331 112 551 -88 C ATOM 1143 CD2 LEU B 153 -12.504 -24.323 14.901 1.00 18.63 C ANISOU 1143 CD2 LEU B 153 2147 1965 2967 -306 627 -584 C ATOM 1144 N ASP B 154 -12.520 -20.942 18.713 1.00 10.98 N ANISOU 1144 N ASP B 154 768 948 2458 -376 128 223 N ATOM 1145 CA ASP B 154 -12.395 -19.511 18.421 1.00 11.60 C ANISOU 1145 CA ASP B 154 1056 1041 2312 -197 212 221 C ATOM 1146 C ASP B 154 -11.046 -19.346 17.729 1.00 10.76 C ANISOU 1146 C ASP B 154 538 1036 2515 -102 -92 438 C ATOM 1147 O ASP B 154 -10.018 -19.633 18.336 1.00 12.56 O ANISOU 1147 O ASP B 154 572 1396 2806 260 -89 629 O ATOM 1148 CB ASP B 154 -12.489 -18.665 19.731 1.00 13.55 C ANISOU 1148 CB ASP B 154 2120 639 2390 52 254 193 C ATOM 1149 CG ASP B 154 -12.740 -17.192 19.483 1.00 16.18 C ANISOU 1149 CG ASP B 154 1808 1772 2566 -296 39 124 C ATOM 1150 OD1 ASP B 154 -12.211 -16.389 20.240 1.00 19.07 O ANISOU 1150 OD1 ASP B 154 2652 1802 2791 -195 307 49 O ATOM 1151 OD2 ASP B 154 -13.533 -16.874 18.581 1.00 20.68 O ANISOU 1151 OD2 ASP B 154 2094 2673 3092 19 -82 -17 O ATOM 1152 N SER B 155 -11.031 -18.811 16.510 1.00 11.59 N ANISOU 1152 N SER B 155 721 1319 2364 -79 367 712 N ATOM 1153 CA SER B 155 -9.779 -18.757 15.738 1.00 12.51 C ANISOU 1153 CA SER B 155 931 1478 2346 -26 411 454 C ATOM 1154 C SER B 155 -9.758 -17.435 15.045 1.00 11.24 C ANISOU 1154 C SER B 155 379 1537 2354 -164 161 463 C ATOM 1155 O SER B 155 -10.602 -17.192 14.181 1.00 11.85 O ANISOU 1155 O SER B 155 815 1331 2358 254 110 363 O ATOM 1156 CB SER B 155 -9.697 -19.879 14.707 1.00 12.47 C ANISOU 1156 CB SER B 155 680 1458 2600 242 190 464 C ATOM 1157 OG SER B 155 -8.423 -19.889 14.096 1.00 15.36 O ANISOU 1157 OG SER B 155 1267 1717 2855 160 287 439 O ATOM 1158 N GLY B 156 -8.809 -16.592 15.407 1.00 10.65 N ANISOU 1158 N GLY B 156 120 1483 2444 -355 177 291 N ATOM 1159 CA GLY B 156 -8.758 -15.273 14.838 1.00 10.93 C ANISOU 1159 CA GLY B 156 338 1126 2688 -237 383 379 C ATOM 1160 C GLY B 156 -7.465 -15.065 14.054 1.00 11.86 C ANISOU 1160 C GLY B 156 332 1518 2655 -376 242 248 C ATOM 1161 O GLY B 156 -7.117 -15.904 13.218 1.00 14.17 O ANISOU 1161 O GLY B 156 1286 1370 2729 87 718 172 O ATOM 1162 N ASP B 157 -6.794 -13.936 14.290 1.00 11.91 N ANISOU 1162 N ASP B 157 553 1399 2573 -344 347 123 N ATOM 1163 CA ASP B 157 -5.580 -13.646 13.543 1.00 13.07 C ANISOU 1163 CA ASP B 157 1305 979 2681 -190 349 154 C ATOM 1164 C ASP B 157 -4.342 -14.191 14.219 1.00 13.22 C ANISOU 1164 C ASP B 157 1279 1158 2584 -256 46 107 C ATOM 1165 O ASP B 157 -3.350 -14.477 13.544 1.00 16.05 O ANISOU 1165 O ASP B 157 1406 2002 2690 327 436 264 O ATOM 1166 CB ASP B 157 -5.420 -12.111 13.435 1.00 12.95 C ANISOU 1166 CB ASP B 157 1114 1103 2703 -576 329 193 C ATOM 1167 CG ASP B 157 -4.361 -11.726 12.429 1.00 15.33 C ANISOU 1167 CG ASP B 157 1349 1635 2840 -477 469 150 C ATOM 1168 OD1 ASP B 157 -4.483 -12.191 11.278 1.00 15.83 O ANISOU 1168 OD1 ASP B 157 1538 1465 3013 33 411 279 O ATOM 1169 OD2 ASP B 157 -3.489 -10.960 12.810 1.00 14.82 O ANISOU 1169 OD2 ASP B 157 965 1777 2889 -48 213 111 O ATOM 1170 N GLY B 158 -4.351 -14.214 15.558 1.00 14.96 N ANISOU 1170 N GLY B 158 1561 1581 2543 -309 -95 183 N ATOM 1171 CA GLY B 158 -3.151 -14.478 16.319 1.00 16.02 C ANISOU 1171 CA GLY B 158 1865 1671 2553 -473 -157 279 C ATOM 1172 C GLY B 158 -3.207 -15.741 17.147 1.00 13.39 C ANISOU 1172 C GLY B 158 1037 1419 2631 -1 -103 212 C ATOM 1173 O GLY B 158 -2.161 -16.246 17.572 1.00 15.81 O ANISOU 1173 O GLY B 158 1246 1766 2994 125 211 425 O ATOM 1174 N VAL B 159 -4.401 -16.241 17.432 1.00 13.46 N ANISOU 1174 N VAL B 159 1152 1419 2542 -140 100 217 N ATOM 1175 CA VAL B 159 -4.489 -17.435 18.286 1.00 13.21 C ANISOU 1175 CA VAL B 159 840 1699 2478 -125 123 490 C ATOM 1176 C VAL B 159 -5.759 -18.196 18.000 1.00 12.43 C ANISOU 1176 C VAL B 159 917 1409 2397 -285 105 431 C ATOM 1177 O VAL B 159 -6.754 -17.602 17.540 1.00 13.94 O ANISOU 1177 O VAL B 159 1738 1312 2248 135 56 270 O ATOM 1178 CB VAL B 159 -4.460 -17.042 19.801 1.00 12.86 C ANISOU 1178 CB VAL B 159 826 1410 2650 268 22 583 C ATOM 1179 CG1 VAL B 159 -5.698 -16.286 20.223 1.00 14.34 C ANISOU 1179 CG1 VAL B 159 955 1623 2869 423 -65 576 C ATOM 1180 CG2 VAL B 159 -4.113 -18.201 20.729 1.00 15.20 C ANISOU 1180 CG2 VAL B 159 1326 1781 2667 344 308 81 C ATOM 1181 N THR B 160 -5.703 -19.502 18.263 1.00 12.26 N ANISOU 1181 N THR B 160 907 1326 2426 -276 382 462 N ATOM 1182 CA THR B 160 -6.861 -20.370 18.191 1.00 11.54 C ANISOU 1182 CA THR B 160 667 1257 2461 -110 481 318 C ATOM 1183 C THR B 160 -7.055 -21.049 19.540 1.00 11.59 C ANISOU 1183 C THR B 160 866 1213 2326 175 353 520 C ATOM 1184 O THR B 160 -6.082 -21.441 20.159 1.00 14.73 O ANISOU 1184 O THR B 160 1013 1946 2637 386 39 833 O ATOM 1185 CB THR B 160 -6.636 -21.439 17.104 1.00 11.99 C ANISOU 1185 CB THR B 160 1130 902 2523 -177 446 294 C ATOM 1186 OG1 THR B 160 -6.557 -20.757 15.851 1.00 12.61 O ANISOU 1186 OG1 THR B 160 1054 1089 2650 45 171 349 O ATOM 1187 CG2 THR B 160 -7.770 -22.445 17.026 1.00 13.42 C ANISOU 1187 CG2 THR B 160 1145 1202 2752 -68 181 197 C ATOM 1188 N HIS B 161 -8.287 -21.137 20.002 1.00 11.47 N ANISOU 1188 N HIS B 161 895 1049 2415 -44 308 387 N ATOM 1189 CA HIS B 161 -8.547 -21.890 21.247 1.00 12.29 C ANISOU 1189 CA HIS B 161 1322 1085 2263 -347 314 286 C ATOM 1190 C HIS B 161 -9.723 -22.836 21.046 1.00 13.06 C ANISOU 1190 C HIS B 161 1114 1390 2459 -46 459 379 C ATOM 1191 O HIS B 161 -10.672 -22.562 20.278 1.00 14.39 O ANISOU 1191 O HIS B 161 1702 1145 2620 66 363 517 O ATOM 1192 CB HIS B 161 -8.958 -20.965 22.374 1.00 13.38 C ANISOU 1192 CB HIS B 161 1369 1345 2371 -79 166 -155 C ATOM 1193 CG HIS B 161 -7.854 -20.121 22.910 1.00 14.01 C ANISOU 1193 CG HIS B 161 1423 1366 2533 -166 66 123 C ATOM 1194 ND1 HIS B 161 -7.654 -18.816 22.499 1.00 13.32 N ANISOU 1194 ND1 HIS B 161 933 1500 2627 -255 60 350 N ATOM 1195 CD2 HIS B 161 -6.982 -20.345 23.923 1.00 14.75 C ANISOU 1195 CD2 HIS B 161 1102 1774 2729 -355 268 164 C ATOM 1196 CE1 HIS B 161 -6.641 -18.305 23.187 1.00 14.09 C ANISOU 1196 CE1 HIS B 161 534 2215 2604 -59 -309 336 C ATOM 1197 NE2 HIS B 161 -6.251 -19.192 24.089 1.00 16.38 N ANISOU 1197 NE2 HIS B 161 1455 1878 2889 -92 45 240 N ATOM 1198 N ASN B 162 -9.650 -23.954 21.767 1.00 12.67 N ANISOU 1198 N ASN B 162 1042 1420 2350 1 464 678 N ATOM 1199 CA ASN B 162 -10.844 -24.762 21.998 1.00 12.93 C ANISOU 1199 CA ASN B 162 826 1488 2600 261 489 463 C ATOM 1200 C ASN B 162 -11.217 -24.480 23.453 1.00 14.41 C ANISOU 1200 C ASN B 162 1345 1593 2539 103 467 135 C ATOM 1201 O ASN B 162 -10.390 -24.654 24.347 1.00 14.38 O ANISOU 1201 O ASN B 162 1000 1883 2582 441 164 325 O ATOM 1202 CB ASN B 162 -10.561 -26.281 21.862 1.00 12.68 C ANISOU 1202 CB ASN B 162 912 986 2921 339 678 396 C ATOM 1203 CG ASN B 162 -9.898 -26.663 20.520 1.00 17.33 C ANISOU 1203 CG ASN B 162 1955 1619 3011 30 746 425 C ATOM 1204 OD1 ASN B 162 -8.698 -26.737 20.460 1.00 21.74 O ANISOU 1204 OD1 ASN B 162 2798 2314 3147 518 732 457 O ATOM 1205 ND2 ASN B 162 -10.663 -26.784 19.482 1.00 23.28 N ANISOU 1205 ND2 ASN B 162 3430 1844 3571 -212 153 -10 N ATOM 1206 N VAL B 163 -12.437 -24.003 23.665 1.00 12.64 N ANISOU 1206 N VAL B 163 969 1257 2576 197 790 279 N ATOM 1207 CA VAL B 163 -12.878 -23.557 25.008 1.00 11.36 C ANISOU 1207 CA VAL B 163 639 897 2779 502 972 -15 C ATOM 1208 C VAL B 163 -14.209 -24.235 25.377 1.00 11.52 C ANISOU 1208 C VAL B 163 444 1182 2750 156 571 173 C ATOM 1209 O VAL B 163 -15.272 -23.856 24.894 1.00 11.90 O ANISOU 1209 O VAL B 163 808 1029 2684 234 312 146 O ATOM 1210 CB VAL B 163 -13.078 -22.007 25.077 1.00 12.50 C ANISOU 1210 CB VAL B 163 707 986 3057 362 701 105 C ATOM 1211 CG1 VAL B 163 -13.346 -21.589 26.513 1.00 14.80 C ANISOU 1211 CG1 VAL B 163 1576 1069 2978 161 701 -127 C ATOM 1212 CG2 VAL B 163 -11.863 -21.280 24.496 1.00 15.73 C ANISOU 1212 CG2 VAL B 163 891 1832 3254 -449 495 566 C ATOM 1213 N PRO B 164 -14.146 -25.313 26.182 1.00 12.09 N ANISOU 1213 N PRO B 164 673 941 2981 186 323 281 N ATOM 1214 CA PRO B 164 -15.363 -25.877 26.717 1.00 11.61 C ANISOU 1214 CA PRO B 164 750 808 2853 230 618 241 C ATOM 1215 C PRO B 164 -15.886 -25.002 27.855 1.00 12.17 C ANISOU 1215 C PRO B 164 941 1058 2623 153 690 292 C ATOM 1216 O PRO B 164 -15.122 -24.498 28.680 1.00 14.46 O ANISOU 1216 O PRO B 164 1389 1300 2806 161 541 253 O ATOM 1217 CB PRO B 164 -14.942 -27.249 27.246 1.00 13.13 C ANISOU 1217 CB PRO B 164 781 1021 3188 362 -60 637 C ATOM 1218 CG PRO B 164 -13.469 -27.197 27.360 1.00 16.70 C ANISOU 1218 CG PRO B 164 1589 1481 3277 26 304 1041 C ATOM 1219 CD PRO B 164 -12.927 -25.947 26.716 1.00 14.30 C ANISOU 1219 CD PRO B 164 1148 1234 3050 92 473 634 C ATOM 1220 N ILE B 165 -17.193 -24.859 27.848 1.00 12.03 N ANISOU 1220 N ILE B 165 1250 696 2625 217 522 303 N ATOM 1221 CA ILE B 165 -17.867 -23.893 28.720 1.00 12.81 C ANISOU 1221 CA ILE B 165 1260 937 2670 457 668 362 C ATOM 1222 C ILE B 165 -19.106 -24.582 29.285 1.00 14.80 C ANISOU 1222 C ILE B 165 1612 1427 2583 191 645 125 C ATOM 1223 O ILE B 165 -19.878 -25.147 28.507 1.00 14.00 O ANISOU 1223 O ILE B 165 1578 1067 2673 84 768 428 O ATOM 1224 CB ILE B 165 -18.263 -22.653 27.920 1.00 10.95 C ANISOU 1224 CB ILE B 165 383 1120 2659 298 726 141 C ATOM 1225 CG1 ILE B 165 -17.023 -21.920 27.441 1.00 12.13 C ANISOU 1225 CG1 ILE B 165 779 1190 2640 137 904 469 C ATOM 1226 CG2 ILE B 165 -19.218 -21.737 28.741 1.00 14.00 C ANISOU 1226 CG2 ILE B 165 1047 1430 2842 446 1097 -44 C ATOM 1227 CD1 ILE B 165 -17.314 -21.081 26.206 1.00 14.08 C ANISOU 1227 CD1 ILE B 165 1574 1165 2611 -17 569 707 C ATOM 1228 N TYR B 166 -19.223 -24.563 30.619 1.00 13.21 N ANISOU 1228 N TYR B 166 1271 1307 2441 54 987 275 N ATOM 1229 CA TYR B 166 -20.413 -25.149 31.226 1.00 13.66 C ANISOU 1229 CA TYR B 166 1109 1410 2673 210 1140 248 C ATOM 1230 C TYR B 166 -21.113 -24.042 32.004 1.00 13.27 C ANISOU 1230 C TYR B 166 1183 1118 2742 8 827 144 C ATOM 1231 O TYR B 166 -20.559 -23.481 32.944 1.00 14.88 O ANISOU 1231 O TYR B 166 1539 1490 2623 -228 507 50 O ATOM 1232 CB TYR B 166 -20.010 -26.293 32.166 1.00 15.98 C ANISOU 1232 CB TYR B 166 1532 1430 3107 373 1273 454 C ATOM 1233 CG TYR B 166 -21.201 -27.077 32.654 1.00 19.32 C ANISOU 1233 CG TYR B 166 2223 1605 3513 115 1093 523 C ATOM 1234 CD1 TYR B 166 -21.823 -26.751 33.851 1.00 20.67 C ANISOU 1234 CD1 TYR B 166 2662 1493 3698 184 990 1014 C ATOM 1235 CD2 TYR B 166 -21.757 -28.054 31.847 1.00 21.26 C ANISOU 1235 CD2 TYR B 166 2448 1764 3864 -186 1002 266 C ATOM 1236 CE1 TYR B 166 -22.938 -27.468 34.287 1.00 23.78 C ANISOU 1236 CE1 TYR B 166 3135 1993 3909 -385 1046 1160 C ATOM 1237 CE2 TYR B 166 -22.895 -28.769 32.256 1.00 23.88 C ANISOU 1237 CE2 TYR B 166 2959 1965 4150 -434 917 706 C ATOM 1238 CZ TYR B 166 -23.475 -28.448 33.456 1.00 24.46 C ANISOU 1238 CZ TYR B 166 3268 1770 4256 -856 906 1210 C ATOM 1239 OH TYR B 166 -24.608 -29.147 33.870 1.00 28.43 O ANISOU 1239 OH TYR B 166 3032 2890 4881 -1311 357 1315 O ATOM 1240 N GLU B 167 -22.337 -23.779 31.613 1.00 15.43 N ANISOU 1240 N GLU B 167 1958 951 2954 499 995 155 N ATOM 1241 CA GLU B 167 -23.180 -22.731 32.256 1.00 17.57 C ANISOU 1241 CA GLU B 167 2344 1123 3211 58 1058 187 C ATOM 1242 C GLU B 167 -22.372 -21.444 32.413 1.00 16.25 C ANISOU 1242 C GLU B 167 1730 1364 3081 -14 827 99 C ATOM 1243 O GLU B 167 -22.356 -20.826 33.495 1.00 16.95 O ANISOU 1243 O GLU B 167 2034 1432 2975 189 803 -40 O ATOM 1244 CB GLU B 167 -23.784 -23.225 33.577 1.00 18.30 C ANISOU 1244 CB GLU B 167 1661 1567 3726 -107 1226 -41 C ATOM 1245 CG GLU B 167 -24.839 -24.329 33.355 1.00 22.68 C ANISOU 1245 CG GLU B 167 2360 1910 4346 -521 987 -82 C ATOM 1246 CD GLU B 167 -26.097 -23.841 32.625 1.00 28.94 C ANISOU 1246 CD GLU B 167 3005 2864 5126 -271 565 -51 C ATOM 1247 OE1 GLU B 167 -26.912 -24.705 32.212 1.00 33.39 O ANISOU 1247 OE1 GLU B 167 3778 3522 5386 -248 369 2 O ATOM 1248 OE2 GLU B 167 -26.291 -22.607 32.439 1.00 29.71 O ANISOU 1248 OE2 GLU B 167 3003 2861 5423 -330 659 -155 O ATOM 1249 N GLY B 168 -21.677 -21.058 31.336 1.00 15.08 N ANISOU 1249 N GLY B 168 1359 1190 3182 -223 521 170 N ATOM 1250 CA GLY B 168 -20.942 -19.788 31.320 1.00 14.61 C ANISOU 1250 CA GLY B 168 1018 1413 3119 -129 210 -95 C ATOM 1251 C GLY B 168 -19.543 -19.866 31.878 1.00 15.98 C ANISOU 1251 C GLY B 168 1332 1738 3002 -38 421 289 C ATOM 1252 O GLY B 168 -18.775 -18.925 31.653 1.00 17.64 O ANISOU 1252 O GLY B 168 1940 1512 3252 22 570 310 O ATOM 1253 N TYR B 169 -19.195 -20.944 32.591 1.00 16.56 N ANISOU 1253 N TYR B 169 2158 1429 2706 143 795 49 N ATOM 1254 CA TYR B 169 -17.853 -21.089 33.096 1.00 16.12 C ANISOU 1254 CA TYR B 169 2226 1217 2682 -193 687 84 C ATOM 1255 C TYR B 169 -16.956 -21.785 32.063 1.00 15.01 C ANISOU 1255 C TYR B 169 1834 1267 2601 -59 644 242 C ATOM 1256 O TYR B 169 -17.169 -22.932 31.741 1.00 15.41 O ANISOU 1256 O TYR B 169 1940 1215 2699 -79 602 90 O ATOM 1257 CB TYR B 169 -17.836 -21.927 34.397 1.00 15.28 C ANISOU 1257 CB TYR B 169 2145 1236 2426 -181 723 287 C ATOM 1258 CG TYR B 169 -18.614 -21.288 35.508 1.00 16.97 C ANISOU 1258 CG TYR B 169 2487 1221 2741 -58 791 -20 C ATOM 1259 CD1 TYR B 169 -18.000 -20.439 36.428 1.00 19.66 C ANISOU 1259 CD1 TYR B 169 3344 1431 2693 -174 679 73 C ATOM 1260 CD2 TYR B 169 -19.969 -21.545 35.622 1.00 14.79 C ANISOU 1260 CD2 TYR B 169 1709 1009 2901 258 603 258 C ATOM 1261 CE1 TYR B 169 -18.740 -19.885 37.458 1.00 19.96 C ANISOU 1261 CE1 TYR B 169 3484 1449 2652 -49 934 -276 C ATOM 1262 CE2 TYR B 169 -20.721 -21.016 36.661 1.00 18.19 C ANISOU 1262 CE2 TYR B 169 2726 1327 2859 147 756 201 C ATOM 1263 CZ TYR B 169 -20.104 -20.155 37.542 1.00 21.07 C ANISOU 1263 CZ TYR B 169 3276 1917 2812 -45 605 -61 C ATOM 1264 OH TYR B 169 -20.828 -19.566 38.588 1.00 23.19 O ANISOU 1264 OH TYR B 169 3572 2284 2954 -69 568 -211 O ATOM 1265 N ALA B 170 -15.960 -21.088 31.538 1.00 15.52 N ANISOU 1265 N ALA B 170 1455 1608 2832 -69 502 368 N ATOM 1266 CA ALA B 170 -14.904 -21.803 30.783 1.00 14.76 C ANISOU 1266 CA ALA B 170 1338 1314 2957 -17 565 378 C ATOM 1267 C ALA B 170 -14.228 -22.784 31.732 1.00 15.92 C ANISOU 1267 C ALA B 170 1800 1246 3002 -239 -147 159 C ATOM 1268 O ALA B 170 -14.055 -22.495 32.925 1.00 22.39 O ANISOU 1268 O ALA B 170 2839 2495 3172 151 -379 -118 O ATOM 1269 CB ALA B 170 -13.878 -20.800 30.207 1.00 16.91 C ANISOU 1269 CB ALA B 170 1687 1764 2974 -94 644 366 C ATOM 1270 N LEU B 171 -13.863 -23.946 31.227 1.00 14.15 N ANISOU 1270 N LEU B 171 1291 1120 2967 147 286 63 N ATOM 1271 CA LEU B 171 -13.272 -24.958 32.089 1.00 14.99 C ANISOU 1271 CA LEU B 171 1381 1423 2893 -434 464 301 C ATOM 1272 C LEU B 171 -11.771 -24.904 31.798 1.00 14.84 C ANISOU 1272 C LEU B 171 1391 1349 2899 -617 191 235 C ATOM 1273 O LEU B 171 -11.289 -25.514 30.850 1.00 16.07 O ANISOU 1273 O LEU B 171 1707 1540 2858 198 292 364 O ATOM 1274 CB LEU B 171 -13.855 -26.321 31.733 1.00 16.38 C ANISOU 1274 CB LEU B 171 1120 2147 2958 -287 598 248 C ATOM 1275 CG LEU B 171 -15.391 -26.327 31.783 1.00 16.55 C ANISOU 1275 CG LEU B 171 1747 1788 2754 -567 724 -293 C ATOM 1276 CD1 LEU B 171 -15.845 -27.753 31.516 1.00 19.19 C ANISOU 1276 CD1 LEU B 171 2509 1881 2903 -697 873 -418 C ATOM 1277 CD2 LEU B 171 -15.982 -25.825 33.121 1.00 18.86 C ANISOU 1277 CD2 LEU B 171 2050 2030 3086 314 510 -21 C ATOM 1278 N PRO B 172 -11.007 -24.199 32.649 1.00 16.28 N ANISOU 1278 N PRO B 172 1668 1500 3018 -103 -78 9 N ATOM 1279 CA PRO B 172 -9.621 -23.894 32.266 1.00 20.07 C ANISOU 1279 CA PRO B 172 2097 2382 3146 135 54 -141 C ATOM 1280 C PRO B 172 -8.729 -25.093 32.045 1.00 19.52 C ANISOU 1280 C PRO B 172 2092 2265 3061 -202 -148 386 C ATOM 1281 O PRO B 172 -7.812 -25.008 31.220 1.00 20.46 O ANISOU 1281 O PRO B 172 2207 2500 3066 -167 -6 414 O ATOM 1282 CB PRO B 172 -9.117 -23.052 33.431 1.00 24.29 C ANISOU 1282 CB PRO B 172 2727 3069 3432 328 -71 -490 C ATOM 1283 CG PRO B 172 -10.368 -22.561 34.148 1.00 26.16 C ANISOU 1283 CG PRO B 172 2865 3705 3371 -298 -171 -570 C ATOM 1284 CD PRO B 172 -11.393 -23.579 33.929 1.00 20.87 C ANISOU 1284 CD PRO B 172 2498 2249 3180 -388 -17 -600 C ATOM 1285 N HIS B 173 -8.956 -26.196 32.772 1.00 20.13 N ANISOU 1285 N HIS B 173 2469 2437 2743 255 -400 388 N ATOM 1286 CA HIS B 173 -8.062 -27.354 32.651 1.00 21.06 C ANISOU 1286 CA HIS B 173 2725 2656 2623 632 -358 760 C ATOM 1287 C HIS B 173 -8.193 -28.023 31.303 1.00 19.80 C ANISOU 1287 C HIS B 173 2377 2429 2717 344 -341 534 C ATOM 1288 O HIS B 173 -7.343 -28.820 30.916 1.00 22.36 O ANISOU 1288 O HIS B 173 2412 3087 2998 541 -279 589 O ATOM 1289 CB HIS B 173 -8.397 -28.412 33.716 1.00 24.68 C ANISOU 1289 CB HIS B 173 3755 2786 2836 318 -167 861 C ATOM 1290 CG HIS B 173 -9.818 -28.878 33.662 1.00 30.71 C ANISOU 1290 CG HIS B 173 4686 3761 3222 -179 231 907 C ATOM 1291 ND1 HIS B 173 -10.865 -28.138 34.183 1.00 32.59 N ANISOU 1291 ND1 HIS B 173 4941 4084 3358 -497 399 1162 N ATOM 1292 CD2 HIS B 173 -10.369 -30.006 33.148 1.00 32.43 C ANISOU 1292 CD2 HIS B 173 5314 3648 3360 -145 225 1043 C ATOM 1293 CE1 HIS B 173 -11.998 -28.790 33.983 1.00 33.37 C ANISOU 1293 CE1 HIS B 173 5027 4266 3384 -369 315 1021 C ATOM 1294 NE2 HIS B 173 -11.728 -29.910 33.330 1.00 32.36 N ANISOU 1294 NE2 HIS B 173 5063 3799 3433 -486 243 1012 N ATOM 1295 N ALA B 174 -9.297 -27.703 30.605 1.00 15.43 N ANISOU 1295 N ALA B 174 1535 1747 2581 -262 -48 686 N ATOM 1296 CA ALA B 174 -9.627 -28.386 29.337 1.00 15.17 C ANISOU 1296 CA ALA B 174 1394 1818 2552 2 -59 450 C ATOM 1297 C ALA B 174 -9.408 -27.448 28.153 1.00 16.01 C ANISOU 1297 C ALA B 174 1719 1693 2672 159 319 479 C ATOM 1298 O ALA B 174 -9.582 -27.862 27.012 1.00 17.68 O ANISOU 1298 O ALA B 174 2397 1734 2586 -98 223 392 O ATOM 1299 CB ALA B 174 -11.101 -28.920 29.335 1.00 15.03 C ANISOU 1299 CB ALA B 174 1287 1580 2846 -126 19 523 C ATOM 1300 N ILE B 175 -9.074 -26.193 28.432 1.00 15.36 N ANISOU 1300 N ILE B 175 1592 1643 2599 339 224 663 N ATOM 1301 CA ILE B 175 -8.871 -25.216 27.342 1.00 14.04 C ANISOU 1301 CA ILE B 175 1034 1677 2625 466 273 532 C ATOM 1302 C ILE B 175 -7.619 -25.601 26.567 1.00 15.96 C ANISOU 1302 C ILE B 175 888 2463 2713 81 262 702 C ATOM 1303 O ILE B 175 -6.570 -25.902 27.192 1.00 18.72 O ANISOU 1303 O ILE B 175 1767 2494 2850 -109 120 575 O ATOM 1304 CB ILE B 175 -8.774 -23.794 27.872 1.00 14.33 C ANISOU 1304 CB ILE B 175 1326 1459 2660 -78 268 560 C ATOM 1305 CG1 ILE B 175 -10.179 -23.373 28.328 1.00 16.30 C ANISOU 1305 CG1 ILE B 175 1465 1871 2857 -9 158 -12 C ATOM 1306 CG2 ILE B 175 -8.301 -22.798 26.765 1.00 16.95 C ANISOU 1306 CG2 ILE B 175 2072 1635 2732 -371 -14 446 C ATOM 1307 CD1 ILE B 175 -10.251 -22.028 29.073 1.00 18.50 C ANISOU 1307 CD1 ILE B 175 2485 1564 2978 714 -60 -25 C ATOM 1308 N MET B 176 -7.707 -25.567 25.223 1.00 15.24 N ANISOU 1308 N MET B 176 829 2107 2854 365 213 1055 N ATOM 1309 CA MET B 176 -6.520 -25.777 24.383 1.00 18.38 C ANISOU 1309 CA MET B 176 1271 2515 3199 287 190 791 C ATOM 1310 C MET B 176 -6.214 -24.480 23.674 1.00 18.82 C ANISOU 1310 C MET B 176 1359 2579 3213 9 468 785 C ATOM 1311 O MET B 176 -7.089 -23.862 23.114 1.00 17.37 O ANISOU 1311 O MET B 176 1291 2243 3065 152 539 352 O ATOM 1312 CB MET B 176 -6.736 -26.888 23.361 1.00 19.52 C ANISOU 1312 CB MET B 176 1185 2546 3686 -107 571 627 C ATOM 1313 CG MET B 176 -7.219 -28.193 23.958 1.00 24.64 C ANISOU 1313 CG MET B 176 2164 3092 4105 -74 386 785 C ATOM 1314 SD MET B 176 -5.880 -29.111 24.756 1.00 27.65 S ANISOU 1314 SD MET B 176 3028 2980 4496 562 221 788 S ATOM 1315 CE MET B 176 -6.832 -30.411 25.582 1.00 27.95 C ANISOU 1315 CE MET B 176 3154 3092 4372 -51 311 1280 C ATOM 1316 N ARG B 177 -4.942 -24.080 23.711 1.00 18.38 N ANISOU 1316 N ARG B 177 1153 2510 3319 -98 453 1307 N ATOM 1317 CA ARG B 177 -4.455 -22.891 22.991 1.00 20.48 C ANISOU 1317 CA ARG B 177 1435 2922 3422 211 427 1019 C ATOM 1318 C ARG B 177 -3.530 -23.384 21.880 1.00 19.65 C ANISOU 1318 C ARG B 177 1298 2790 3379 578 477 859 C ATOM 1319 O ARG B 177 -2.601 -24.185 22.124 1.00 20.79 O ANISOU 1319 O ARG B 177 1117 3244 3540 826 536 1014 O ATOM 1320 CB ARG B 177 -3.678 -21.947 23.919 1.00 19.61 C ANISOU 1320 CB ARG B 177 1068 2959 3423 316 597 686 C ATOM 1321 CG ARG B 177 -2.878 -20.860 23.167 1.00 21.37 C ANISOU 1321 CG ARG B 177 1868 2586 3666 -22 205 751 C ATOM 1322 CD ARG B 177 -2.363 -19.747 24.081 1.00 23.59 C ANISOU 1322 CD ARG B 177 2081 3021 3862 -867 183 256 C ATOM 1323 NE ARG B 177 -1.302 -18.994 23.386 1.00 23.71 N ANISOU 1323 NE ARG B 177 2095 2901 4013 -594 -238 120 N ATOM 1324 CZ ARG B 177 -0.492 -18.099 23.954 1.00 26.75 C ANISOU 1324 CZ ARG B 177 2650 3432 4081 -320 -199 392 C ATOM 1325 NH1 ARG B 177 0.444 -17.511 23.215 1.00 26.51 N ANISOU 1325 NH1 ARG B 177 2490 3536 4045 69 208 789 N ATOM 1326 NH2 ARG B 177 -0.639 -17.765 25.240 1.00 28.32 N ANISOU 1326 NH2 ARG B 177 2956 3678 4129 -378 -209 197 N ATOM 1327 N LEU B 178 -3.721 -22.938 20.676 1.00 16.73 N ANISOU 1327 N LEU B 178 645 2482 3230 469 445 550 N ATOM 1328 CA ALEU B 178 -2.790 -23.165 19.579 0.50 16.70 C ANISOU 1328 CA ALEU B 178 1040 2047 3257 40 360 355 C ATOM 1329 CA BLEU B 178 -2.752 -23.114 19.586 0.50 20.02 C ANISOU 1329 CA BLEU B 178 1636 2631 3341 320 340 322 C ATOM 1330 C LEU B 178 -2.378 -21.793 18.994 1.00 18.48 C ANISOU 1330 C LEU B 178 1434 2311 3275 274 236 644 C ATOM 1331 O LEU B 178 -3.177 -21.070 18.636 1.00 17.43 O ANISOU 1331 O LEU B 178 1031 2388 3205 306 5 684 O ATOM 1332 CB ALEU B 178 -3.531 -24.001 18.569 0.50 17.32 C ANISOU 1332 CB ALEU B 178 1108 2005 3467 -274 -3 146 C ATOM 1333 CB BLEU B 178 -3.265 -23.683 18.376 0.50 26.67 C ANISOU 1333 CB BLEU B 178 2942 3530 3663 208 5 47 C ATOM 1334 CG ALEU B 178 -2.970 -24.430 17.249 0.50 18.91 C ANISOU 1334 CG ALEU B 178 1036 2605 3545 -196 50 289 C ATOM 1335 CG BLEU B 178 -3.943 -24.783 18.248 0.50 32.25 C ANISOU 1335 CG BLEU B 178 3872 4499 3883 287 -164 -132 C ATOM 1336 CD1ALEU B 178 -1.706 -25.191 17.553 0.50 19.88 C ANISOU 1336 CD1ALEU B 178 1082 2879 3592 293 80 510 C ATOM 1337 CD1BLEU B 178 -4.019 -25.359 16.821 0.50 34.51 C ANISOU 1337 CD1BLEU B 178 4301 4833 3978 172 -242 -290 C ATOM 1338 CD2ALEU B 178 -3.993 -25.355 16.567 0.50 24.07 C ANISOU 1338 CD2ALEU B 178 2131 3269 3744 -308 -144 -79 C ATOM 1339 CD2BLEU B 178 -3.125 -25.378 18.888 0.50 34.22 C ANISOU 1339 CD2BLEU B 178 4439 4653 3909 87 -255 -84 C ATOM 1340 N AASP B 179 -1.083 -21.563 18.873 0.50 19.72 N ANISOU 1340 N AASP B 179 1936 2328 3230 252 354 549 N ATOM 1341 N BASP B 179 -1.080 -21.585 18.930 0.50 18.31 N ANISOU 1341 N BASP B 179 1118 2705 3134 -33 330 352 N ATOM 1342 CA AASP B 179 -0.701 -20.311 18.300 0.50 21.77 C ANISOU 1342 CA AASP B 179 2232 2688 3350 -283 147 500 C ATOM 1343 CA BASP B 179 -0.583 -20.386 18.313 0.50 17.30 C ANISOU 1343 CA BASP B 179 126 3277 3172 -540 226 133 C ATOM 1344 C AASP B 179 -0.990 -20.096 16.802 0.50 21.03 C ANISOU 1344 C AASP B 179 2720 2073 3197 -314 322 554 C ATOM 1345 C BASP B 179 -0.430 -20.681 16.833 0.50 15.25 C ANISOU 1345 C BASP B 179 52 2763 2980 -340 -69 -30 C ATOM 1346 O AASP B 179 -1.152 -18.966 16.372 0.50 23.11 O ANISOU 1346 O AASP B 179 3551 2040 3191 -19 383 490 O ATOM 1347 O BASP B 179 0.670 -20.764 16.287 0.50 16.59 O ANISOU 1347 O BASP B 179 27 3046 3229 33 246 357 O ATOM 1348 CB AASP B 179 0.668 -19.867 18.821 0.50 23.09 C ANISOU 1348 CB AASP B 179 1947 3116 3710 -618 -167 532 C ATOM 1349 CB BASP B 179 0.723 -19.942 18.980 0.50 19.47 C ANISOU 1349 CB BASP B 179 395 3561 3443 -631 -161 85 C ATOM 1350 CG AASP B 179 0.555 -19.313 20.207 0.50 27.96 C ANISOU 1350 CG AASP B 179 2764 3878 3981 -307 -296 609 C ATOM 1351 CG BASP B 179 0.478 -19.346 20.365 0.50 23.19 C ANISOU 1351 CG BASP B 179 1341 3908 3563 -302 -344 44 C ATOM 1352 OD1AASP B 179 1.535 -19.073 20.855 0.50 32.89 O ANISOU 1352 OD1AASP B 179 3534 4739 4223 -229 -359 533 O ATOM 1353 OD1BASP B 179 -0.696 -19.033 20.673 0.50 23.32 O ANISOU 1353 OD1BASP B 179 1793 3569 3497 -455 -70 29 O ATOM 1354 OD2AASP B 179 -0.535 -19.094 20.680 0.50 27.83 O ANISOU 1354 OD2AASP B 179 2963 3598 4011 -311 -23 764 O ATOM 1355 OD2BASP B 179 1.437 -19.170 21.151 0.50 29.63 O ANISOU 1355 OD2BASP B 179 2667 4749 3840 -264 -382 2 O ATOM 1356 N ALEU B 180 -1.237 -21.147 16.073 0.50 18.79 N ANISOU 1356 N ALEU B 180 2290 1682 3168 -89 343 362 N ATOM 1357 N BLEU B 180 -1.589 -20.838 16.196 0.50 16.01 N ANISOU 1357 N BLEU B 180 721 2518 2844 -696 -431 -140 N ATOM 1358 CA ALEU B 180 -1.599 -21.147 14.653 0.50 16.82 C ANISOU 1358 CA ALEU B 180 2037 1150 3203 312 -132 326 C ATOM 1359 CA BLEU B 180 -1.681 -21.117 14.789 0.50 15.12 C ANISOU 1359 CA BLEU B 180 830 2030 2886 173 -150 -42 C ATOM 1360 C ALEU B 180 -2.955 -20.504 14.449 0.50 16.25 C ANISOU 1360 C ALEU B 180 1900 1213 3063 188 20 463 C ATOM 1361 C BLEU B 180 -3.009 -20.540 14.388 0.50 15.75 C ANISOU 1361 C BLEU B 180 1102 1859 3024 78 -74 271 C ATOM 1362 O ALEU B 180 -3.957 -20.989 14.978 0.50 16.24 O ANISOU 1362 O ALEU B 180 2049 1050 3072 307 174 544 O ATOM 1363 O BLEU B 180 -4.057 -21.094 14.729 0.50 16.77 O ANISOU 1363 O BLEU B 180 1028 2145 3198 -25 5 329 O ATOM 1364 CB ALEU B 180 -1.631 -22.592 14.127 0.50 17.84 C ANISOU 1364 CB ALEU B 180 2254 1071 3453 362 -367 39 C ATOM 1365 CB BLEU B 180 -1.721 -22.631 14.577 0.50 17.57 C ANISOU 1365 CB BLEU B 180 1600 2099 2975 169 26 -254 C ATOM 1366 CG ALEU B 180 -2.516 -23.027 12.942 0.50 20.11 C ANISOU 1366 CG ALEU B 180 2256 1733 3650 -20 -506 -112 C ATOM 1367 CG BLEU B 180 -2.033 -23.105 13.160 0.50 18.72 C ANISOU 1367 CG BLEU B 180 1711 2272 3128 316 102 -435 C ATOM 1368 CD1ALEU B 180 -2.064 -22.460 11.612 0.50 20.93 C ANISOU 1368 CD1ALEU B 180 2048 2245 3660 258 -926 -262 C ATOM 1369 CD1BLEU B 180 -1.159 -22.370 12.189 0.50 16.86 C ANISOU 1369 CD1BLEU B 180 676 2550 3180 158 95 -570 C ATOM 1370 CD2ALEU B 180 -2.553 -24.557 12.867 0.50 21.84 C ANISOU 1370 CD2ALEU B 180 2337 2223 3738 463 -516 -142 C ATOM 1371 CD2BLEU B 180 -1.849 -24.619 13.031 0.50 20.75 C ANISOU 1371 CD2BLEU B 180 2208 2535 3143 661 164 -561 C ATOM 1372 N ALA B 181 -2.976 -19.417 13.684 1.00 13.50 N ANISOU 1372 N ALA B 181 1107 1251 2772 457 292 218 N ATOM 1373 CA ALA B 181 -4.228 -18.761 13.328 1.00 12.17 C ANISOU 1373 CA ALA B 181 1033 1122 2467 309 423 189 C ATOM 1374 C ALA B 181 -4.087 -18.022 11.997 1.00 12.59 C ANISOU 1374 C ALA B 181 1242 1137 2406 270 663 352 C ATOM 1375 O ALA B 181 -3.272 -18.432 11.163 1.00 12.70 O ANISOU 1375 O ALA B 181 658 1581 2588 376 523 205 O ATOM 1376 CB ALA B 181 -4.687 -17.816 14.422 1.00 14.53 C ANISOU 1376 CB ALA B 181 1542 1351 2627 174 368 -1 C ATOM 1377 N GLY B 182 -4.883 -16.984 11.771 1.00 12.91 N ANISOU 1377 N GLY B 182 1240 1290 2374 258 217 311 N ATOM 1378 CA GLY B 182 -5.038 -16.450 10.413 1.00 14.00 C ANISOU 1378 CA GLY B 182 1218 1744 2356 -223 326 614 C ATOM 1379 C GLY B 182 -3.718 -15.892 9.875 1.00 12.18 C ANISOU 1379 C GLY B 182 994 1207 2428 14 102 269 C ATOM 1380 O GLY B 182 -3.454 -16.061 8.680 1.00 12.80 O ANISOU 1380 O GLY B 182 814 1726 2325 -6 404 254 O ATOM 1381 N ARG B 183 -2.943 -15.206 10.731 1.00 13.01 N ANISOU 1381 N ARG B 183 574 1736 2632 -115 417 113 N ATOM 1382 CA ARG B 183 -1.679 -14.597 10.247 1.00 14.25 C ANISOU 1382 CA ARG B 183 923 1563 2929 -241 454 9 C ATOM 1383 C ARG B 183 -0.744 -15.677 9.773 1.00 14.28 C ANISOU 1383 C ARG B 183 1276 1325 2824 -137 443 252 C ATOM 1384 O ARG B 183 -0.071 -15.515 8.757 1.00 14.34 O ANISOU 1384 O ARG B 183 849 1805 2794 -126 338 349 O ATOM 1385 CB ARG B 183 -1.038 -13.672 11.309 1.00 16.27 C ANISOU 1385 CB ARG B 183 1320 1739 3121 -571 645 -282 C ATOM 1386 CG ARG B 183 -0.103 -12.632 10.682 1.00 19.85 C ANISOU 1386 CG ARG B 183 2133 1946 3462 -553 848 -236 C ATOM 1387 CD ARG B 183 0.482 -11.676 11.710 1.00 19.06 C ANISOU 1387 CD ARG B 183 1784 1765 3693 232 647 -117 C ATOM 1388 NE ARG B 183 -0.574 -11.055 12.511 1.00 18.48 N ANISOU 1388 NE ARG B 183 1201 1899 3922 -45 637 -318 N ATOM 1389 CZ ARG B 183 -0.347 -10.448 13.683 1.00 19.77 C ANISOU 1389 CZ ARG B 183 1155 2239 4117 119 202 -401 C ATOM 1390 NH1 ARG B 183 0.915 -10.302 14.110 1.00 23.68 N ANISOU 1390 NH1 ARG B 183 1684 3094 4221 -265 -62 31 N ATOM 1391 NH2 ARG B 183 -1.359 -9.968 14.409 1.00 19.80 N ANISOU 1391 NH2 ARG B 183 1595 1801 4129 -233 373 -349 N ATOM 1392 N ASP B 184 -0.698 -16.798 10.484 1.00 12.71 N ANISOU 1392 N ASP B 184 817 1257 2756 98 363 271 N ATOM 1393 CA ASP B 184 0.154 -17.899 10.080 1.00 15.45 C ANISOU 1393 CA ASP B 184 1842 1443 2584 682 176 366 C ATOM 1394 C ASP B 184 -0.320 -18.483 8.775 1.00 14.74 C ANISOU 1394 C ASP B 184 1545 1540 2514 18 262 465 C ATOM 1395 O ASP B 184 0.516 -18.933 7.953 1.00 15.55 O ANISOU 1395 O ASP B 184 1353 1869 2687 195 579 567 O ATOM 1396 CB ASP B 184 0.194 -18.985 11.181 1.00 17.69 C ANISOU 1396 CB ASP B 184 2291 1879 2552 474 416 344 C ATOM 1397 CG ASP B 184 0.670 -18.417 12.509 1.00 24.28 C ANISOU 1397 CG ASP B 184 3328 2868 3030 -283 261 20 C ATOM 1398 OD1 ASP B 184 -0.047 -18.565 13.511 1.00 28.95 O ANISOU 1398 OD1 ASP B 184 4408 3293 3298 -1370 455 71 O ATOM 1399 OD2 ASP B 184 1.720 -17.758 12.523 1.00 24.10 O ANISOU 1399 OD2 ASP B 184 2636 3341 3179 291 -271 -174 O ATOM 1400 N LEU B 185 -1.652 -18.536 8.582 1.00 13.33 N ANISOU 1400 N LEU B 185 1159 1432 2474 -186 259 343 N ATOM 1401 CA LEU B 185 -2.159 -19.105 7.339 1.00 12.50 C ANISOU 1401 CA LEU B 185 940 1211 2598 -53 248 286 C ATOM 1402 C LEU B 185 -1.796 -18.177 6.161 1.00 12.32 C ANISOU 1402 C LEU B 185 971 1240 2469 76 323 335 C ATOM 1403 O LEU B 185 -1.475 -18.685 5.078 1.00 13.22 O ANISOU 1403 O LEU B 185 971 1629 2425 20 458 231 O ATOM 1404 CB LEU B 185 -3.682 -19.323 7.409 1.00 12.84 C ANISOU 1404 CB LEU B 185 533 1496 2849 -53 213 532 C ATOM 1405 CG LEU B 185 -4.060 -20.425 8.417 1.00 14.66 C ANISOU 1405 CG LEU B 185 755 1443 3370 204 611 298 C ATOM 1406 CD1 LEU B 185 -5.562 -20.506 8.414 1.00 17.16 C ANISOU 1406 CD1 LEU B 185 1388 1585 3545 462 355 247 C ATOM 1407 CD2 LEU B 185 -3.360 -21.761 8.189 1.00 15.59 C ANISOU 1407 CD2 LEU B 185 779 1720 3423 501 699 399 C ATOM 1408 N THR B 186 -1.850 -16.862 6.370 1.00 13.00 N ANISOU 1408 N THR B 186 1103 1231 2605 -41 100 593 N ATOM 1409 CA THR B 186 -1.449 -15.925 5.314 1.00 12.41 C ANISOU 1409 CA THR B 186 1044 1063 2607 499 403 380 C ATOM 1410 C THR B 186 0.012 -16.195 4.997 1.00 13.94 C ANISOU 1410 C THR B 186 1101 1551 2643 387 429 147 C ATOM 1411 O THR B 186 0.415 -16.281 3.804 1.00 15.15 O ANISOU 1411 O THR B 186 1381 1671 2703 223 710 431 O ATOM 1412 CB THR B 186 -1.670 -14.479 5.747 1.00 13.44 C ANISOU 1412 CB THR B 186 989 1381 2738 182 911 407 C ATOM 1413 OG1 THR B 186 -3.093 -14.306 5.943 1.00 13.87 O ANISOU 1413 OG1 THR B 186 984 1469 2818 -34 834 256 O ATOM 1414 CG2 THR B 186 -1.119 -13.525 4.645 1.00 14.93 C ANISOU 1414 CG2 THR B 186 1401 1756 2518 112 463 681 C ATOM 1415 N ASP B 187 0.840 -16.258 6.050 1.00 14.98 N ANISOU 1415 N ASP B 187 976 1952 2763 246 305 294 N ATOM 1416 CA ASP B 187 2.296 -16.437 5.802 1.00 15.39 C ANISOU 1416 CA ASP B 187 1023 2003 2820 427 329 169 C ATOM 1417 C ASP B 187 2.529 -17.733 5.054 1.00 15.01 C ANISOU 1417 C ASP B 187 919 2030 2753 138 622 356 C ATOM 1418 O ASP B 187 3.364 -17.783 4.147 1.00 15.61 O ANISOU 1418 O ASP B 187 1168 1956 2806 228 757 532 O ATOM 1419 CB ASP B 187 3.022 -16.492 7.136 1.00 15.25 C ANISOU 1419 CB ASP B 187 768 2173 2852 -199 286 38 C ATOM 1420 CG ASP B 187 3.119 -15.150 7.809 1.00 19.47 C ANISOU 1420 CG ASP B 187 1580 2627 3189 -377 605 265 C ATOM 1421 OD1 ASP B 187 2.926 -14.143 7.114 1.00 21.64 O ANISOU 1421 OD1 ASP B 187 2010 2801 3412 -253 849 11 O ATOM 1422 OD2 ASP B 187 3.437 -15.088 9.033 1.00 22.05 O ANISOU 1422 OD2 ASP B 187 1761 3305 3311 22 274 -42 O ATOM 1423 N TYR B 188 1.779 -18.782 5.396 1.00 14.37 N ANISOU 1423 N TYR B 188 1212 1620 2627 121 295 156 N ATOM 1424 CA TYR B 188 1.951 -20.048 4.703 1.00 15.06 C ANISOU 1424 CA TYR B 188 1336 1802 2586 378 549 344 C ATOM 1425 C TYR B 188 1.504 -19.913 3.229 1.00 16.90 C ANISOU 1425 C TYR B 188 1782 2035 2603 330 695 626 C ATOM 1426 O TYR B 188 2.158 -20.477 2.316 1.00 15.77 O ANISOU 1426 O TYR B 188 1023 2330 2641 566 709 747 O ATOM 1427 CB TYR B 188 1.151 -21.162 5.401 1.00 14.48 C ANISOU 1427 CB TYR B 188 1219 1542 2739 -83 770 496 C ATOM 1428 CG TYR B 188 1.264 -22.515 4.747 1.00 14.57 C ANISOU 1428 CG TYR B 188 1267 1644 2623 103 830 538 C ATOM 1429 CD1 TYR B 188 2.535 -23.110 4.573 1.00 16.96 C ANISOU 1429 CD1 TYR B 188 2233 1537 2672 355 646 550 C ATOM 1430 CD2 TYR B 188 0.133 -23.196 4.289 1.00 16.65 C ANISOU 1430 CD2 TYR B 188 1897 1751 2679 102 552 394 C ATOM 1431 CE1 TYR B 188 2.653 -24.374 3.991 1.00 18.41 C ANISOU 1431 CE1 TYR B 188 2503 1648 2843 362 982 239 C ATOM 1432 CE2 TYR B 188 0.234 -24.455 3.682 1.00 18.67 C ANISOU 1432 CE2 TYR B 188 2480 1839 2775 421 1071 190 C ATOM 1433 CZ TYR B 188 1.512 -25.005 3.522 1.00 19.90 C ANISOU 1433 CZ TYR B 188 2851 1801 2908 344 663 49 C ATOM 1434 OH TYR B 188 1.625 -26.276 2.956 1.00 22.47 O ANISOU 1434 OH TYR B 188 3636 1938 2964 326 960 289 O ATOM 1435 N LEU B 189 0.401 -19.201 2.971 1.00 14.66 N ANISOU 1435 N LEU B 189 1356 1797 2418 72 380 453 N ATOM 1436 CA LEU B 189 -0.065 -19.020 1.593 1.00 14.54 C ANISOU 1436 CA LEU B 189 1163 1920 2444 253 381 566 C ATOM 1437 C LEU B 189 1.036 -18.256 0.806 1.00 14.36 C ANISOU 1437 C LEU B 189 1170 1834 2451 150 584 310 C ATOM 1438 O LEU B 189 1.284 -18.583 -0.376 1.00 16.05 O ANISOU 1438 O LEU B 189 1634 1994 2470 378 764 353 O ATOM 1439 CB LEU B 189 -1.422 -18.305 1.541 1.00 14.27 C ANISOU 1439 CB LEU B 189 1031 1654 2740 303 -79 398 C ATOM 1440 CG LEU B 189 -2.026 -18.165 0.136 1.00 14.88 C ANISOU 1440 CG LEU B 189 1431 1564 2660 153 199 -125 C ATOM 1441 CD1 LEU B 189 -2.084 -19.514 -0.606 1.00 16.73 C ANISOU 1441 CD1 LEU B 189 1947 1738 2672 -135 300 186 C ATOM 1442 CD2 LEU B 189 -3.384 -17.487 0.223 1.00 15.22 C ANISOU 1442 CD2 LEU B 189 1382 1614 2786 217 624 3 C ATOM 1443 N MET B 190 1.648 -17.268 1.422 1.00 15.00 N ANISOU 1443 N MET B 190 1194 1753 2752 189 787 408 N ATOM 1444 CA MET B 190 2.800 -16.561 0.768 1.00 17.06 C ANISOU 1444 CA MET B 190 1397 2145 2938 235 790 291 C ATOM 1445 C MET B 190 3.893 -17.550 0.355 1.00 18.84 C ANISOU 1445 C MET B 190 2067 2121 2972 387 838 336 C ATOM 1446 O MET B 190 4.467 -17.465 -0.767 1.00 20.61 O ANISOU 1446 O MET B 190 2199 2550 3080 361 1031 269 O ATOM 1447 CB MET B 190 3.392 -15.533 1.692 1.00 16.43 C ANISOU 1447 CB MET B 190 1243 1829 3173 333 682 146 C ATOM 1448 CG MET B 190 2.425 -14.408 2.008 1.00 18.14 C ANISOU 1448 CG MET B 190 1632 2063 3200 -113 584 67 C ATOM 1449 SD MET B 190 3.076 -13.304 3.262 1.00 19.89 S ANISOU 1449 SD MET B 190 1847 2345 3366 -92 474 274 S ATOM 1450 CE MET B 190 4.282 -12.440 2.279 1.00 21.30 C ANISOU 1450 CE MET B 190 2230 2520 3343 -713 789 152 C ATOM 1451 N LYS B 191 4.185 -18.497 1.247 1.00 14.92 N ANISOU 1451 N LYS B 191 1155 1648 2865 120 513 519 N ATOM 1452 CA LYS B 191 5.245 -19.480 0.965 1.00 17.73 C ANISOU 1452 CA LYS B 191 1821 2034 2880 855 520 574 C ATOM 1453 C LYS B 191 4.842 -20.389 -0.204 1.00 17.22 C ANISOU 1453 C LYS B 191 1748 2019 2774 -81 285 512 C ATOM 1454 O LYS B 191 5.609 -20.569 -1.177 1.00 18.10 O ANISOU 1454 O LYS B 191 1565 2544 2769 214 855 619 O ATOM 1455 CB LYS B 191 5.519 -20.325 2.200 1.00 20.60 C ANISOU 1455 CB LYS B 191 1740 2828 3259 898 340 1071 C ATOM 1456 CG LYS B 191 6.521 -21.403 1.979 1.00 24.65 C ANISOU 1456 CG LYS B 191 2123 3628 3617 1167 309 953 C ATOM 1457 CD LYS B 191 6.866 -22.039 3.345 1.00 28.80 C ANISOU 1457 CD LYS B 191 2398 4487 4058 1569 278 903 C ATOM 1458 CE LYS B 191 7.860 -23.205 3.173 1.00 35.29 C ANISOU 1458 CE LYS B 191 3567 5233 4608 769 69 384 C ATOM 1459 NZ LYS B 191 7.159 -24.444 2.721 1.00 40.88 N ANISOU 1459 NZ LYS B 191 4508 6058 4968 708 70 209 N ATOM 1460 N ILE B 192 3.676 -20.933 -0.211 1.00 16.48 N ANISOU 1460 N ILE B 192 1776 1958 2527 238 75 43 N ATOM 1461 CA ILE B 192 3.302 -21.853 -1.209 1.00 17.15 C ANISOU 1461 CA ILE B 192 1957 1898 2663 228 505 178 C ATOM 1462 C ILE B 192 3.009 -21.212 -2.602 1.00 19.33 C ANISOU 1462 C ILE B 192 2517 2016 2813 128 444 257 C ATOM 1463 O ILE B 192 3.134 -21.795 -3.506 1.00 18.74 O ANISOU 1463 O ILE B 192 2150 2168 2803 235 581 354 O ATOM 1464 CB ILE B 192 2.196 -22.873 -0.772 1.00 16.42 C ANISOU 1464 CB ILE B 192 1473 2189 2578 248 570 789 C ATOM 1465 CG1 ILE B 192 0.810 -22.250 -0.483 1.00 14.58 C ANISOU 1465 CG1 ILE B 192 1153 1743 2646 -194 777 239 C ATOM 1466 CG2 ILE B 192 2.650 -23.623 0.426 1.00 18.16 C ANISOU 1466 CG2 ILE B 192 2132 2251 2516 -49 262 781 C ATOM 1467 CD1 ILE B 192 -0.217 -23.262 -0.111 1.00 16.45 C ANISOU 1467 CD1 ILE B 192 1812 1832 2605 -20 815 216 C ATOM 1468 N LEU B 193 2.601 -19.967 -2.575 1.00 16.48 N ANISOU 1468 N LEU B 193 1822 1678 2762 73 946 444 N ATOM 1469 CA LEU B 193 2.395 -19.246 -3.808 1.00 19.17 C ANISOU 1469 CA LEU B 193 2355 2053 2875 365 656 629 C ATOM 1470 C LEU B 193 3.757 -19.076 -4.558 1.00 21.52 C ANISOU 1470 C LEU B 193 2398 2724 3056 251 549 723 C ATOM 1471 O LEU B 193 3.760 -18.990 -5.678 1.00 20.03 O ANISOU 1471 O LEU B 193 1941 2859 2808 -22 688 355 O ATOM 1472 CB LEU B 193 1.752 -17.904 -3.570 1.00 19.65 C ANISOU 1472 CB LEU B 193 2186 2468 2811 1008 1040 861 C ATOM 1473 CG LEU B 193 0.235 -17.902 -3.410 1.00 21.67 C ANISOU 1473 CG LEU B 193 2271 3175 2787 1679 1269 603 C ATOM 1474 CD1 LEU B 193 -0.168 -16.637 -2.912 1.00 27.22 C ANISOU 1474 CD1 LEU B 193 2483 4751 3108 1037 740 758 C ATOM 1475 CD2 LEU B 193 -0.446 -18.343 -4.642 1.00 24.99 C ANISOU 1475 CD2 LEU B 193 3306 3327 2863 1348 1346 1044 C ATOM 1476 N THR B 194 4.824 -19.085 -3.842 1.00 23.02 N ANISOU 1476 N THR B 194 1837 3482 3427 135 863 1156 N ATOM 1477 CA THR B 194 6.211 -19.206 -4.468 1.00 25.90 C ANISOU 1477 CA THR B 194 2059 3958 3823 -73 1292 1384 C ATOM 1478 C THR B 194 6.411 -20.353 -5.348 1.00 30.34 C ANISOU 1478 C THR B 194 2909 4276 4344 516 1880 1846 C ATOM 1479 O THR B 194 7.133 -20.217 -6.203 1.00 31.79 O ANISOU 1479 O THR B 194 2684 4784 4612 805 2016 1696 O ATOM 1480 CB THR B 194 7.224 -19.159 -3.482 1.00 30.21 C ANISOU 1480 CB THR B 194 3144 4085 4249 554 596 564 C ATOM 1481 OG1 THR B 194 7.315 -17.950 -2.804 1.00 32.65 O ANISOU 1481 OG1 THR B 194 3737 4189 4479 -482 178 137 O ATOM 1482 CG2 THR B 194 7.655 -20.314 -2.962 1.00 27.64 C ANISOU 1482 CG2 THR B 194 2524 3877 4100 1473 1337 152 C ATOM 1483 N GLU B 195 5.768 -21.493 -5.190 1.00 34.48 N ANISOU 1483 N GLU B 195 4296 4028 4778 -115 2273 1273 N ATOM 1484 CA GLU B 195 5.715 -22.555 -6.131 1.00 37.37 C ANISOU 1484 CA GLU B 195 5302 4194 4704 -370 1668 1059 C ATOM 1485 C GLU B 195 5.224 -22.291 -7.507 1.00 40.04 C ANISOU 1485 C GLU B 195 5817 4551 4846 624 1446 229 C ATOM 1486 O GLU B 195 5.858 -22.716 -8.416 1.00 43.71 O ANISOU 1486 O GLU B 195 6208 5270 5130 1030 1436 198 O ATOM 1487 CB GLU B 195 4.932 -23.791 -5.589 1.00 39.45 C ANISOU 1487 CB GLU B 195 5276 4994 4719 176 1932 820 C ATOM 1488 CG GLU B 195 5.280 -24.334 -4.229 1.00 40.03 C ANISOU 1488 CG GLU B 195 5186 5273 4752 208 1850 917 C ATOM 1489 CD GLU B 195 4.210 -25.355 -3.665 1.00 41.56 C ANISOU 1489 CD GLU B 195 5121 5878 4793 -513 1773 735 C ATOM 1490 OE1 GLU B 195 4.432 -25.836 -2.693 1.00 35.95 O ANISOU 1490 OE1 GLU B 195 3893 5139 4626 -185 2157 1303 O ATOM 1491 OE2 GLU B 195 3.245 -25.534 -4.328 1.00 46.81 O ANISOU 1491 OE2 GLU B 195 5959 6958 4869 -1696 1597 345 O ATOM 1492 N ARG B 196 4.107 -21.690 -7.735 1.00 33.86 N ANISOU 1492 N ARG B 196 4834 3434 4596 1875 855 -114 N ATOM 1493 CA ARG B 196 3.843 -21.287 -9.096 1.00 35.68 C ANISOU 1493 CA ARG B 196 4934 3924 4697 1203 749 182 C ATOM 1494 C ARG B 196 4.589 -20.130 -9.468 1.00 39.57 C ANISOU 1494 C ARG B 196 5475 4958 4600 1449 696 -57 C ATOM 1495 O ARG B 196 4.381 -19.476 -10.479 1.00 43.88 O ANISOU 1495 O ARG B 196 6368 5507 4797 1180 728 -138 O ATOM 1496 CB ARG B 196 2.371 -20.860 -9.242 1.00 36.23 C ANISOU 1496 CB ARG B 196 4800 4206 4760 1014 1051 460 C ATOM 1497 CG ARG B 196 1.351 -21.713 -8.703 1.00 36.81 C ANISOU 1497 CG ARG B 196 4717 4327 4943 196 1347 657 C ATOM 1498 CD ARG B 196 -0.043 -21.182 -8.815 1.00 38.64 C ANISOU 1498 CD ARG B 196 4741 4830 5113 157 1321 668 C ATOM 1499 NE ARG B 196 -0.827 -22.281 -8.829 1.00 40.73 N ANISOU 1499 NE ARG B 196 4486 5788 5202 218 1359 606 N ATOM 1500 CZ ARG B 196 -1.517 -22.810 -9.712 1.00 42.44 C ANISOU 1500 CZ ARG B 196 4565 6198 5362 188 1492 592 C ATOM 1501 NH1 ARG B 196 -1.909 -23.938 -9.380 1.00 41.66 N ANISOU 1501 NH1 ARG B 196 4224 6101 5502 118 1952 556 N ATOM 1502 NH2 ARG B 196 -1.897 -22.233 -10.763 1.00 43.04 N ANISOU 1502 NH2 ARG B 196 4532 6558 5262 161 1428 442 N ATOM 1503 N GLY B 197 5.436 -19.724 -8.627 1.00 34.39 N ANISOU 1503 N GLY B 197 4687 3911 4470 1766 636 -622 N ATOM 1504 CA GLY B 197 6.189 -18.747 -9.104 1.00 31.72 C ANISOU 1504 CA GLY B 197 4310 3525 4217 1853 848 -29 C ATOM 1505 C GLY B 197 5.805 -17.370 -8.772 1.00 29.85 C ANISOU 1505 C GLY B 197 3867 3314 4160 1127 978 679 C ATOM 1506 O GLY B 197 6.480 -16.617 -9.148 1.00 32.22 O ANISOU 1506 O GLY B 197 3726 4118 4398 1431 1494 1451 O ATOM 1507 N TYR B 198 4.810 -17.154 -7.924 1.00 23.31 N ANISOU 1507 N TYR B 198 2685 2383 3788 460 1232 743 N ATOM 1508 CA TYR B 198 4.426 -15.850 -7.466 1.00 23.09 C ANISOU 1508 CA TYR B 198 2632 2319 3823 309 839 721 C ATOM 1509 C TYR B 198 5.040 -15.459 -6.210 1.00 25.11 C ANISOU 1509 C TYR B 198 3666 2362 3511 -138 1080 590 C ATOM 1510 O TYR B 198 4.738 -16.019 -5.260 1.00 30.95 O ANISOU 1510 O TYR B 198 5766 2389 3604 -766 1148 89 O ATOM 1511 CB TYR B 198 2.921 -15.778 -7.212 1.00 22.98 C ANISOU 1511 CB TYR B 198 2287 2398 4047 272 1348 950 C ATOM 1512 CG TYR B 198 2.091 -16.125 -8.291 1.00 25.24 C ANISOU 1512 CG TYR B 198 2056 3053 4482 163 780 1171 C ATOM 1513 CD1 TYR B 198 1.942 -15.345 -9.377 1.00 25.55 C ANISOU 1513 CD1 TYR B 198 1991 3197 4520 526 754 1035 C ATOM 1514 CD2 TYR B 198 1.376 -17.239 -8.268 1.00 29.54 C ANISOU 1514 CD2 TYR B 198 2504 4026 4694 -507 388 1526 C ATOM 1515 CE1 TYR B 198 1.269 -15.628 -10.241 1.00 30.40 C ANISOU 1515 CE1 TYR B 198 2963 3840 4746 -161 381 1213 C ATOM 1516 CE2 TYR B 198 0.676 -17.573 -9.217 1.00 31.43 C ANISOU 1516 CE2 TYR B 198 2923 4247 4773 -1514 -23 1755 C ATOM 1517 CZ TYR B 198 0.517 -16.718 -10.225 1.00 33.18 C ANISOU 1517 CZ TYR B 198 3254 4473 4879 -1139 -359 1536 C ATOM 1518 OH TYR B 198 -0.247 -17.088 -11.225 1.00 38.02 O ANISOU 1518 OH TYR B 198 4388 4853 5206 -1896 -472 1651 O ATOM 1519 N ASER B 199 5.881 -14.446 -6.232 0.50 23.72 N ANISOU 1519 N ASER B 199 2623 2865 3525 12 978 686 N ATOM 1520 N BSER B 199 5.869 -14.423 -6.204 0.50 20.85 N ANISOU 1520 N BSER B 199 1824 2739 3359 -529 942 617 N ATOM 1521 CA ASER B 199 6.532 -13.945 -5.046 0.50 25.70 C ANISOU 1521 CA ASER B 199 2768 3568 3429 37 1050 585 C ATOM 1522 CA BSER B 199 6.609 -13.976 -5.016 0.50 22.16 C ANISOU 1522 CA BSER B 199 2127 3213 3081 -508 936 375 C ATOM 1523 C ASER B 199 5.723 -12.829 -4.408 0.50 24.59 C ANISOU 1523 C ASER B 199 2543 3648 3152 128 931 698 C ATOM 1524 C BSER B 199 6.002 -12.765 -4.279 0.50 22.26 C ANISOU 1524 C BSER B 199 1944 3538 2974 -206 998 551 C ATOM 1525 O ASER B 199 5.421 -11.817 -5.052 0.50 25.58 O ANISOU 1525 O ASER B 199 2862 3797 3060 772 768 1025 O ATOM 1526 O BSER B 199 6.114 -11.610 -4.716 0.50 23.35 O ANISOU 1526 O BSER B 199 2015 3988 2869 -228 940 588 O ATOM 1527 CB ASER B 199 7.920 -13.428 -5.390 0.50 29.16 C ANISOU 1527 CB ASER B 199 3039 4372 3670 368 1265 302 C ATOM 1528 CB BSER B 199 8.076 -13.694 -5.367 0.50 23.86 C ANISOU 1528 CB BSER B 199 2412 3651 3002 -274 812 -112 C ATOM 1529 OG ASER B 199 8.816 -14.505 -5.558 0.50 31.22 O ANISOU 1529 OG ASER B 199 3138 4891 3835 436 1268 258 O ATOM 1530 OG BSER B 199 8.680 -12.790 -4.441 0.50 22.50 O ANISOU 1530 OG BSER B 199 2016 3708 2824 -324 386 -306 O ATOM 1531 N PHE B 200 5.356 -13.022 -3.137 1.00 22.35 N ANISOU 1531 N PHE B 200 1856 3652 2983 165 1028 480 N ATOM 1532 CA PHE B 200 4.813 -11.954 -2.320 1.00 21.86 C ANISOU 1532 CA PHE B 200 1440 3714 3150 270 614 621 C ATOM 1533 C PHE B 200 5.674 -11.920 -1.062 1.00 24.89 C ANISOU 1533 C PHE B 200 2307 3795 3353 419 564 498 C ATOM 1534 O PHE B 200 5.867 -12.970 -0.440 1.00 24.30 O ANISOU 1534 O PHE B 200 2113 3677 3444 446 78 471 O ATOM 1535 CB PHE B 200 3.348 -12.262 -2.005 1.00 21.15 C ANISOU 1535 CB PHE B 200 860 3981 3196 6 333 674 C ATOM 1536 CG PHE B 200 2.426 -12.177 -3.213 1.00 20.55 C ANISOU 1536 CG PHE B 200 973 3699 3137 329 397 774 C ATOM 1537 CD1 PHE B 200 2.082 -13.313 -3.906 1.00 20.87 C ANISOU 1537 CD1 PHE B 200 1160 3770 2999 216 535 772 C ATOM 1538 CD2 PHE B 200 1.859 -10.971 -3.587 1.00 23.98 C ANISOU 1538 CD2 PHE B 200 2272 3555 3285 94 89 398 C ATOM 1539 CE1 PHE B 200 1.187 -13.283 -5.012 1.00 21.54 C ANISOU 1539 CE1 PHE B 200 1229 3966 2989 739 486 590 C ATOM 1540 CE2 PHE B 200 0.982 -10.907 -4.669 1.00 24.31 C ANISOU 1540 CE2 PHE B 200 2448 3624 3164 209 262 206 C ATOM 1541 CZ PHE B 200 0.633 -12.070 -5.373 1.00 22.86 C ANISOU 1541 CZ PHE B 200 1863 3781 3042 919 717 123 C ATOM 1542 N VAL B 201 6.196 -10.739 -0.709 1.00 24.80 N ANISOU 1542 N VAL B 201 1604 4369 3449 247 613 214 N ATOM 1543 CA VAL B 201 7.242 -10.592 0.301 1.00 26.92 C ANISOU 1543 CA VAL B 201 1648 4867 3713 448 875 7 C ATOM 1544 C VAL B 201 7.014 -9.487 1.320 1.00 25.28 C ANISOU 1544 C VAL B 201 1354 4718 3534 -300 1036 321 C ATOM 1545 O VAL B 201 7.130 -9.731 2.536 1.00 27.66 O ANISOU 1545 O VAL B 201 2144 4832 3532 -318 492 329 O ATOM 1546 CB VAL B 201 8.615 -10.390 -0.410 1.00 30.06 C ANISOU 1546 CB VAL B 201 1634 5718 4069 841 532 -120 C ATOM 1547 CG1 VAL B 201 9.707 -9.898 0.563 1.00 31.77 C ANISOU 1547 CG1 VAL B 201 1672 6080 4319 816 503 -194 C ATOM 1548 CG2 VAL B 201 9.010 -11.690 -1.145 1.00 32.56 C ANISOU 1548 CG2 VAL B 201 2198 6121 4051 417 1063 43 C ATOM 1549 N THR B 202 6.701 -8.288 0.859 1.00 24.88 N ANISOU 1549 N THR B 202 1628 4273 3552 -146 822 341 N ATOM 1550 CA THR B 202 6.622 -7.127 1.743 1.00 25.04 C ANISOU 1550 CA THR B 202 2021 3866 3628 -761 853 390 C ATOM 1551 C THR B 202 5.342 -7.142 2.585 1.00 24.41 C ANISOU 1551 C THR B 202 1979 3647 3647 8 828 62 C ATOM 1552 O THR B 202 4.416 -7.930 2.336 1.00 22.65 O ANISOU 1552 O THR B 202 1593 3377 3637 -150 686 89 O ATOM 1553 CB THR B 202 6.562 -5.826 0.957 1.00 26.74 C ANISOU 1553 CB THR B 202 2279 4062 3819 -1157 1099 625 C ATOM 1554 OG1 THR B 202 5.401 -5.847 0.114 1.00 29.22 O ANISOU 1554 OG1 THR B 202 2869 4321 3914 -730 1024 208 O ATOM 1555 CG2 THR B 202 7.847 -5.662 0.053 1.00 29.50 C ANISOU 1555 CG2 THR B 202 2456 4703 4048 -1149 1130 722 C ATOM 1556 N THR B 203 5.288 -6.212 3.528 1.00 23.09 N ANISOU 1556 N THR B 203 1931 3267 3575 -378 999 -120 N ATOM 1557 CA THR B 203 4.126 -6.055 4.421 1.00 22.79 C ANISOU 1557 CA THR B 203 1893 3049 3717 -377 1250 71 C ATOM 1558 C THR B 203 2.890 -5.800 3.574 1.00 22.75 C ANISOU 1558 C THR B 203 2459 2385 3800 -245 1321 210 C ATOM 1559 O THR B 203 1.804 -6.336 3.821 1.00 21.48 O ANISOU 1559 O THR B 203 2091 2283 3787 -462 1692 208 O ATOM 1560 CB THR B 203 4.352 -4.872 5.411 1.00 27.03 C ANISOU 1560 CB THR B 203 2819 3453 3999 -803 846 -42 C ATOM 1561 OG1 THR B 203 5.511 -5.127 6.202 1.00 30.40 O ANISOU 1561 OG1 THR B 203 2823 4506 4221 -1127 678 -54 O ATOM 1562 CG2 THR B 203 3.137 -4.701 6.353 1.00 26.76 C ANISOU 1562 CG2 THR B 203 2853 3385 3929 -733 1204 -36 C ATOM 1563 N ALA B 204 3.017 -4.941 2.575 1.00 24.44 N ANISOU 1563 N ALA B 204 2726 2582 3978 -429 1090 761 N ATOM 1564 CA ALA B 204 1.878 -4.678 1.717 1.00 24.07 C ANISOU 1564 CA ALA B 204 2569 2411 4164 -611 1070 935 C ATOM 1565 C ALA B 204 1.492 -5.903 0.901 1.00 22.03 C ANISOU 1565 C ALA B 204 1874 2427 4069 222 1105 803 C ATOM 1566 O ALA B 204 0.299 -6.140 0.652 1.00 21.98 O ANISOU 1566 O ALA B 204 1792 2209 4352 373 877 691 O ATOM 1567 CB ALA B 204 2.144 -3.471 0.773 1.00 25.85 C ANISOU 1567 CB ALA B 204 3134 2301 4386 -752 1246 1167 C ATOM 1568 N GLU B 205 2.497 -6.676 0.452 1.00 23.68 N ANISOU 1568 N GLU B 205 2796 2480 3721 145 956 704 N ATOM 1569 CA GLU B 205 2.201 -7.833 -0.351 1.00 21.75 C ANISOU 1569 CA GLU B 205 2047 2641 3576 220 882 910 C ATOM 1570 C GLU B 205 1.558 -8.894 0.538 1.00 20.74 C ANISOU 1570 C GLU B 205 1682 2741 3458 387 1042 638 C ATOM 1571 O GLU B 205 0.694 -9.627 0.084 1.00 22.17 O ANISOU 1571 O GLU B 205 2153 2649 3624 114 843 531 O ATOM 1572 CB GLU B 205 3.448 -8.362 -1.038 1.00 23.35 C ANISOU 1572 CB GLU B 205 1862 3593 3418 303 1285 1163 C ATOM 1573 CG GLU B 205 3.789 -7.488 -2.237 1.00 26.40 C ANISOU 1573 CG GLU B 205 1889 4540 3604 299 1633 1375 C ATOM 1574 CD GLU B 205 5.247 -7.629 -2.705 1.00 30.62 C ANISOU 1574 CD GLU B 205 2451 5129 4054 14 1111 1460 C ATOM 1575 OE1 GLU B 205 6.037 -8.410 -2.094 1.00 28.41 O ANISOU 1575 OE1 GLU B 205 1699 5035 4061 224 1015 1368 O ATOM 1576 OE2 GLU B 205 5.598 -6.917 -3.692 1.00 34.28 O ANISOU 1576 OE2 GLU B 205 2960 5734 4330 -34 828 1727 O ATOM 1577 N ARG B 206 1.989 -8.955 1.794 1.00 20.07 N ANISOU 1577 N ARG B 206 2088 2167 3372 41 1005 788 N ATOM 1578 CA ARG B 206 1.338 -9.855 2.761 1.00 18.94 C ANISOU 1578 CA ARG B 206 1946 1891 3361 535 953 523 C ATOM 1579 C ARG B 206 -0.175 -9.552 2.867 1.00 16.16 C ANISOU 1579 C ARG B 206 1311 1365 3466 499 1068 547 C ATOM 1580 O ARG B 206 -0.983 -10.460 2.967 1.00 17.91 O ANISOU 1580 O ARG B 206 1718 1707 3381 14 811 694 O ATOM 1581 CB ARG B 206 1.995 -9.741 4.114 1.00 20.23 C ANISOU 1581 CB ARG B 206 2489 1895 3302 -189 880 830 C ATOM 1582 CG ARG B 206 1.295 -10.702 5.091 1.00 22.71 C ANISOU 1582 CG ARG B 206 2645 2308 3677 -301 999 425 C ATOM 1583 CD ARG B 206 2.104 -11.188 6.186 1.00 26.53 C ANISOU 1583 CD ARG B 206 2843 3180 4057 -176 1032 -172 C ATOM 1584 NE ARG B 206 2.230 -10.230 7.259 1.00 27.13 N ANISOU 1584 NE ARG B 206 2697 3281 4331 59 1273 -865 N ATOM 1585 CZ ARG B 206 2.647 -10.539 8.493 1.00 25.96 C ANISOU 1585 CZ ARG B 206 2084 3153 4626 -269 1726 -362 C ATOM 1586 NH1 ARG B 206 2.982 -11.771 8.827 1.00 26.08 N ANISOU 1586 NH1 ARG B 206 2248 2524 5136 -425 1386 -730 N ATOM 1587 NH2 ARG B 206 2.762 -9.586 9.401 1.00 25.82 N ANISOU 1587 NH2 ARG B 206 2661 2770 4380 -527 1677 -445 N ATOM 1588 N GLU B 207 -0.540 -8.268 2.845 1.00 16.89 N ANISOU 1588 N GLU B 207 1140 1650 3627 369 993 426 N ATOM 1589 CA GLU B 207 -1.958 -7.888 2.852 1.00 16.97 C ANISOU 1589 CA GLU B 207 1435 1637 3378 65 941 292 C ATOM 1590 C GLU B 207 -2.673 -8.353 1.620 1.00 16.71 C ANISOU 1590 C GLU B 207 1497 1509 3344 -259 1000 649 C ATOM 1591 O GLU B 207 -3.853 -8.722 1.680 1.00 16.89 O ANISOU 1591 O GLU B 207 1437 1546 3433 -182 515 467 O ATOM 1592 CB GLU B 207 -2.136 -6.373 3.040 1.00 16.98 C ANISOU 1592 CB GLU B 207 1735 1413 3305 -139 840 175 C ATOM 1593 CG GLU B 207 -1.668 -5.870 4.398 1.00 16.57 C ANISOU 1593 CG GLU B 207 939 1879 3477 -123 1018 248 C ATOM 1594 CD GLU B 207 -2.470 -6.552 5.532 1.00 16.51 C ANISOU 1594 CD GLU B 207 999 1777 3499 349 1267 142 C ATOM 1595 OE1 GLU B 207 -3.729 -6.485 5.471 1.00 18.42 O ANISOU 1595 OE1 GLU B 207 1619 1750 3629 90 728 114 O ATOM 1596 OE2 GLU B 207 -1.833 -7.160 6.409 1.00 19.90 O ANISOU 1596 OE2 GLU B 207 1907 2068 3585 33 983 579 O ATOM 1597 N ILE B 208 -2.001 -8.313 0.455 1.00 17.71 N ANISOU 1597 N ILE B 208 2096 1647 2987 125 1004 778 N ATOM 1598 CA ILE B 208 -2.608 -8.845 -0.738 1.00 18.27 C ANISOU 1598 CA ILE B 208 2307 1593 3040 322 977 680 C ATOM 1599 C ILE B 208 -2.891 -10.347 -0.560 1.00 17.68 C ANISOU 1599 C ILE B 208 1954 1831 2933 500 648 905 C ATOM 1600 O ILE B 208 -3.962 -10.819 -0.901 1.00 18.35 O ANISOU 1600 O ILE B 208 2206 1847 2917 337 689 705 O ATOM 1601 CB ILE B 208 -1.721 -8.610 -2.026 1.00 19.42 C ANISOU 1601 CB ILE B 208 2371 1823 3184 44 1226 631 C ATOM 1602 CG1 ILE B 208 -1.646 -7.121 -2.336 1.00 22.23 C ANISOU 1602 CG1 ILE B 208 3093 1935 3417 53 1276 925 C ATOM 1603 CG2 ILE B 208 -2.278 -9.349 -3.195 1.00 19.41 C ANISOU 1603 CG2 ILE B 208 2258 1852 3265 -413 1005 381 C ATOM 1604 CD1 ILE B 208 -0.638 -6.863 -3.460 1.00 24.17 C ANISOU 1604 CD1 ILE B 208 2755 2821 3608 -278 1463 809 C ATOM 1605 N VAL B 209 -1.912 -11.079 -0.020 1.00 15.66 N ANISOU 1605 N VAL B 209 1476 1738 2738 472 537 794 N ATOM 1606 CA VAL B 209 -2.089 -12.497 0.126 1.00 15.65 C ANISOU 1606 CA VAL B 209 1636 1627 2682 415 635 607 C ATOM 1607 C VAL B 209 -3.158 -12.801 1.185 1.00 15.44 C ANISOU 1607 C VAL B 209 1734 1586 2545 181 408 478 C ATOM 1608 O VAL B 209 -3.935 -13.735 1.005 1.00 14.37 O ANISOU 1608 O VAL B 209 1393 1543 2523 117 610 308 O ATOM 1609 CB VAL B 209 -0.782 -13.172 0.426 1.00 13.44 C ANISOU 1609 CB VAL B 209 1178 1170 2759 334 1022 404 C ATOM 1610 CG1 VAL B 209 -0.990 -14.661 0.672 1.00 15.85 C ANISOU 1610 CG1 VAL B 209 1974 1335 2714 358 1034 639 C ATOM 1611 CG2 VAL B 209 0.165 -12.972 -0.812 1.00 17.29 C ANISOU 1611 CG2 VAL B 209 1843 1982 2742 -12 652 314 C ATOM 1612 N ARG B 210 -3.214 -11.982 2.244 1.00 14.21 N ANISOU 1612 N ARG B 210 1288 1503 2607 393 689 198 N ATOM 1613 CA ARG B 210 -4.389 -12.102 3.167 1.00 14.41 C ANISOU 1613 CA ARG B 210 948 1906 2622 387 892 -211 C ATOM 1614 C ARG B 210 -5.704 -12.019 2.412 1.00 14.70 C ANISOU 1614 C ARG B 210 1413 1555 2616 -3 591 469 C ATOM 1615 O ARG B 210 -6.633 -12.821 2.659 1.00 14.70 O ANISOU 1615 O ARG B 210 1365 1639 2581 40 567 510 O ATOM 1616 CB ARG B 210 -4.297 -11.069 4.270 1.00 13.87 C ANISOU 1616 CB ARG B 210 1100 1513 2658 299 1098 -174 C ATOM 1617 CG ARG B 210 -5.515 -11.202 5.247 1.00 14.28 C ANISOU 1617 CG ARG B 210 1182 1510 2735 432 1003 -3 C ATOM 1618 CD ARG B 210 -5.569 -10.070 6.304 1.00 15.33 C ANISOU 1618 CD ARG B 210 1723 1227 2875 160 938 131 C ATOM 1619 NE ARG B 210 -5.531 -8.743 5.669 1.00 15.74 N ANISOU 1619 NE ARG B 210 1439 1308 3233 273 679 331 N ATOM 1620 CZ ARG B 210 -6.444 -8.258 4.843 1.00 16.19 C ANISOU 1620 CZ ARG B 210 1157 1532 3460 84 1081 448 C ATOM 1621 NH1 ARG B 210 -7.586 -8.919 4.608 1.00 17.42 N ANISOU 1621 NH1 ARG B 210 1400 1784 3436 226 945 482 N ATOM 1622 NH2 ARG B 210 -6.245 -7.074 4.231 1.00 18.63 N ANISOU 1622 NH2 ARG B 210 1895 1630 3554 -190 944 566 N ATOM 1623 N ASP B 211 -5.795 -11.045 1.489 1.00 15.55 N ANISOU 1623 N ASP B 211 1763 1428 2718 498 607 708 N ATOM 1624 CA ASP B 211 -7.017 -10.915 0.745 1.00 17.19 C ANISOU 1624 CA ASP B 211 1891 1854 2787 637 454 782 C ATOM 1625 C ASP B 211 -7.301 -12.131 -0.153 1.00 16.86 C ANISOU 1625 C ASP B 211 1867 1895 2645 437 456 619 C ATOM 1626 O ASP B 211 -8.444 -12.601 -0.233 1.00 16.94 O ANISOU 1626 O ASP B 211 1785 2028 2623 193 443 593 O ATOM 1627 CB ASP B 211 -7.031 -9.589 -0.035 1.00 17.42 C ANISOU 1627 CB ASP B 211 1872 1730 3016 474 401 1108 C ATOM 1628 CG ASP B 211 -8.416 -9.239 -0.575 1.00 20.93 C ANISOU 1628 CG ASP B 211 2128 2504 3322 453 409 1207 C ATOM 1629 OD1 ASP B 211 -8.569 -9.191 -1.820 1.00 25.19 O ANISOU 1629 OD1 ASP B 211 2161 3727 3680 639 -100 1402 O ATOM 1630 OD2 ASP B 211 -9.355 -9.057 0.231 1.00 23.49 O ANISOU 1630 OD2 ASP B 211 2352 3077 3495 762 386 1159 O ATOM 1631 N ILE B 212 -6.270 -12.636 -0.842 1.00 15.76 N ANISOU 1631 N ILE B 212 1850 1582 2556 461 512 579 N ATOM 1632 CA ILE B 212 -6.436 -13.825 -1.647 1.00 15.69 C ANISOU 1632 CA ILE B 212 2199 1354 2408 535 603 506 C ATOM 1633 C ILE B 212 -6.950 -14.987 -0.781 1.00 15.31 C ANISOU 1633 C ILE B 212 1603 1949 2266 199 202 617 C ATOM 1634 O ILE B 212 -7.866 -15.718 -1.178 1.00 16.66 O ANISOU 1634 O ILE B 212 1839 2173 2317 186 146 368 O ATOM 1635 CB ILE B 212 -5.088 -14.268 -2.265 1.00 16.30 C ANISOU 1635 CB ILE B 212 1908 1788 2498 335 641 503 C ATOM 1636 CG1 ILE B 212 -4.583 -13.198 -3.249 1.00 18.96 C ANISOU 1636 CG1 ILE B 212 1849 2698 2658 59 564 668 C ATOM 1637 CG2 ILE B 212 -5.188 -15.605 -2.895 1.00 18.03 C ANISOU 1637 CG2 ILE B 212 2461 1924 2465 160 475 205 C ATOM 1638 CD1 ILE B 212 -3.134 -13.449 -3.783 1.00 19.45 C ANISOU 1638 CD1 ILE B 212 1548 3153 2688 -154 734 603 C ATOM 1639 N LYS B 213 -6.328 -15.130 0.401 1.00 15.38 N ANISOU 1639 N LYS B 213 1967 1747 2128 464 403 610 N ATOM 1640 CA LYS B 213 -6.710 -16.209 1.332 1.00 14.67 C ANISOU 1640 CA LYS B 213 1469 1776 2328 206 258 673 C ATOM 1641 C LYS B 213 -8.200 -16.099 1.665 1.00 13.76 C ANISOU 1641 C LYS B 213 1187 1451 2590 -300 322 346 C ATOM 1642 O LYS B 213 -8.941 -17.094 1.625 1.00 15.98 O ANISOU 1642 O LYS B 213 1719 1474 2878 -112 434 262 O ATOM 1643 CB LYS B 213 -5.865 -16.049 2.616 1.00 12.92 C ANISOU 1643 CB LYS B 213 866 1743 2302 270 -6 873 C ATOM 1644 CG LYS B 213 -6.245 -16.994 3.764 1.00 13.66 C ANISOU 1644 CG LYS B 213 1499 1378 2312 363 92 475 C ATOM 1645 CD LYS B 213 -5.593 -16.610 5.042 1.00 12.29 C ANISOU 1645 CD LYS B 213 1313 1051 2305 126 289 144 C ATOM 1646 CE LYS B 213 -6.159 -15.318 5.667 1.00 12.62 C ANISOU 1646 CE LYS B 213 1327 1044 2423 373 677 92 C ATOM 1647 NZ LYS B 213 -5.728 -15.121 7.092 1.00 13.55 N ANISOU 1647 NZ LYS B 213 1565 1347 2239 -11 567 169 N ATOM 1648 N GLU B 214 -8.613 -14.886 2.025 1.00 14.17 N ANISOU 1648 N GLU B 214 1248 1643 2491 269 177 282 N ATOM 1649 CA GLU B 214 -9.995 -14.673 2.441 1.00 15.28 C ANISOU 1649 CA GLU B 214 1425 1740 2641 81 107 -24 C ATOM 1650 C GLU B 214 -10.996 -14.873 1.312 1.00 18.53 C ANISOU 1650 C GLU B 214 1946 2235 2861 145 122 389 C ATOM 1651 O GLU B 214 -12.111 -15.289 1.572 1.00 20.85 O ANISOU 1651 O GLU B 214 1941 2985 2996 -318 -253 771 O ATOM 1652 CB GLU B 214 -10.185 -13.285 3.037 1.00 14.16 C ANISOU 1652 CB GLU B 214 1030 1607 2744 -17 207 69 C ATOM 1653 CG GLU B 214 -9.347 -13.037 4.264 1.00 13.93 C ANISOU 1653 CG GLU B 214 1154 1546 2593 320 286 230 C ATOM 1654 CD GLU B 214 -9.469 -11.623 4.814 1.00 15.66 C ANISOU 1654 CD GLU B 214 1373 1827 2750 564 280 169 C ATOM 1655 OE1 GLU B 214 -10.261 -10.800 4.259 1.00 17.88 O ANISOU 1655 OE1 GLU B 214 1705 2119 2971 620 47 34 O ATOM 1656 OE2 GLU B 214 -8.746 -11.312 5.773 1.00 15.57 O ANISOU 1656 OE2 GLU B 214 1392 1843 2681 258 485 377 O ATOM 1657 N LYS B 215 -10.593 -14.581 0.066 1.00 17.13 N ANISOU 1657 N LYS B 215 1692 2066 2751 168 54 556 N ATOM 1658 CA ALYS B 215 -11.513 -14.656 -1.072 0.50 19.24 C ANISOU 1658 CA ALYS B 215 2031 2350 2931 9 -54 469 C ATOM 1659 CA BLYS B 215 -11.529 -14.663 -1.052 0.50 18.03 C ANISOU 1659 CA BLYS B 215 1912 2101 2839 -93 -185 636 C ATOM 1660 C LYS B 215 -11.527 -16.017 -1.745 1.00 17.62 C ANISOU 1660 C LYS B 215 1636 2240 2819 17 -172 369 C ATOM 1661 O LYS B 215 -12.576 -16.437 -2.301 1.00 21.97 O ANISOU 1661 O LYS B 215 2389 2664 3293 -217 -477 14 O ATOM 1662 CB ALYS B 215 -11.145 -13.593 -2.110 0.50 21.70 C ANISOU 1662 CB ALYS B 215 2423 2577 3246 117 -97 571 C ATOM 1663 CB BLYS B 215 -11.239 -13.552 -2.063 0.50 17.85 C ANISOU 1663 CB BLYS B 215 2032 1769 2980 -127 -534 1071 C ATOM 1664 CG ALYS B 215 -11.340 -12.188 -1.592 0.50 26.72 C ANISOU 1664 CG ALYS B 215 3136 3357 3661 417 64 375 C ATOM 1665 CG BLYS B 215 -11.748 -12.194 -1.595 0.50 21.29 C ANISOU 1665 CG BLYS B 215 2510 2287 3292 423 -531 1022 C ATOM 1666 CD ALYS B 215 -12.805 -11.896 -1.417 0.50 29.58 C ANISOU 1666 CD ALYS B 215 3467 3782 3991 751 289 276 C ATOM 1667 CD BLYS B 215 -11.140 -11.085 -2.431 0.50 23.74 C ANISOU 1667 CD BLYS B 215 3257 2352 3410 640 -680 1303 C ATOM 1668 CE ALYS B 215 -12.994 -10.621 -0.636 0.50 29.72 C ANISOU 1668 CE ALYS B 215 3301 3843 4150 1028 448 302 C ATOM 1669 CE BLYS B 215 -11.789 -9.731 -2.107 0.50 28.16 C ANISOU 1669 CE BLYS B 215 3820 3236 3641 784 -785 1031 C ATOM 1670 NZ ALYS B 215 -12.069 -9.568 -1.114 0.50 29.46 N ANISOU 1670 NZ ALYS B 215 3457 3523 4212 751 637 376 N ATOM 1671 NZ BLYS B 215 -11.063 -8.632 -2.844 0.50 27.81 N ANISOU 1671 NZ BLYS B 215 3548 3270 3750 978 -1120 1135 N ATOM 1672 N LEU B 216 -10.392 -16.713 -1.741 1.00 17.81 N ANISOU 1672 N LEU B 216 2147 2019 2599 616 -176 367 N ATOM 1673 CA LEU B 216 -10.298 -17.933 -2.550 1.00 16.53 C ANISOU 1673 CA LEU B 216 1894 1893 2492 340 -152 719 C ATOM 1674 C LEU B 216 -10.023 -19.253 -1.823 1.00 15.45 C ANISOU 1674 C LEU B 216 1581 1849 2442 -133 -45 512 C ATOM 1675 O LEU B 216 -10.160 -20.317 -2.428 1.00 19.27 O ANISOU 1675 O LEU B 216 2487 2206 2628 -469 -16 326 O ATOM 1676 CB LEU B 216 -9.247 -17.707 -3.630 1.00 21.32 C ANISOU 1676 CB LEU B 216 3046 2606 2449 -80 78 858 C ATOM 1677 CG LEU B 216 -9.677 -16.690 -4.731 1.00 25.18 C ANISOU 1677 CG LEU B 216 3896 3090 2579 -35 -254 1070 C ATOM 1678 CD1 LEU B 216 -8.482 -16.604 -5.683 1.00 27.19 C ANISOU 1678 CD1 LEU B 216 4330 3018 2983 -507 -47 691 C ATOM 1679 CD2 LEU B 216 -11.022 -17.122 -5.396 1.00 28.64 C ANISOU 1679 CD2 LEU B 216 3951 3980 2949 -5 -210 1176 C ATOM 1680 N CYS B 217 -9.612 -19.179 -0.554 1.00 15.55 N ANISOU 1680 N CYS B 217 1528 1890 2489 -2 -71 580 N ATOM 1681 CA CYS B 217 -9.288 -20.427 0.147 1.00 14.79 C ANISOU 1681 CA CYS B 217 1284 1872 2464 -87 -71 418 C ATOM 1682 C CYS B 217 -10.544 -21.118 0.694 1.00 14.29 C ANISOU 1682 C CYS B 217 828 1962 2639 260 348 410 C ATOM 1683 O CYS B 217 -11.576 -20.482 0.976 1.00 17.00 O ANISOU 1683 O CYS B 217 1078 2279 3103 116 251 578 O ATOM 1684 CB CYS B 217 -8.295 -20.166 1.272 1.00 13.98 C ANISOU 1684 CB CYS B 217 727 2025 2560 217 -81 311 C ATOM 1685 SG CYS B 217 -6.622 -19.807 0.708 1.00 16.14 S ANISOU 1685 SG CYS B 217 1672 1774 2687 48 248 218 S ATOM 1686 N TYR B 218 -10.424 -22.440 0.835 1.00 15.97 N ANISOU 1686 N TYR B 218 1774 1986 2307 -37 100 522 N ATOM 1687 CA TYR B 218 -11.491 -23.252 1.383 1.00 16.55 C ANISOU 1687 CA TYR B 218 1800 2124 2363 -291 -220 552 C ATOM 1688 C TYR B 218 -10.918 -24.520 1.983 1.00 15.92 C ANISOU 1688 C TYR B 218 1534 2111 2406 -186 -26 542 C ATOM 1689 O TYR B 218 -9.766 -24.876 1.721 1.00 16.83 O ANISOU 1689 O TYR B 218 1939 1911 2546 -45 355 549 O ATOM 1690 CB TYR B 218 -12.524 -23.618 0.293 1.00 17.83 C ANISOU 1690 CB TYR B 218 1973 2479 2322 174 -281 306 C ATOM 1691 CG TYR B 218 -12.061 -24.576 -0.779 1.00 18.46 C ANISOU 1691 CG TYR B 218 1979 2477 2556 -558 -310 250 C ATOM 1692 CD1 TYR B 218 -12.276 -25.965 -0.661 1.00 19.12 C ANISOU 1692 CD1 TYR B 218 2014 2591 2660 -792 -83 71 C ATOM 1693 CD2 TYR B 218 -11.459 -24.089 -1.955 1.00 19.55 C ANISOU 1693 CD2 TYR B 218 2257 2664 2508 -130 -65 174 C ATOM 1694 CE1 TYR B 218 -11.857 -26.868 -1.645 1.00 21.76 C ANISOU 1694 CE1 TYR B 218 2635 2925 2707 -1089 -127 174 C ATOM 1695 CE2 TYR B 218 -11.042 -24.962 -2.949 1.00 20.64 C ANISOU 1695 CE2 TYR B 218 2540 2620 2684 -440 -116 104 C ATOM 1696 CZ TYR B 218 -11.252 -26.351 -2.804 1.00 22.48 C ANISOU 1696 CZ TYR B 218 2694 3120 2727 -882 -160 148 C ATOM 1697 OH TYR B 218 -10.847 -27.210 -3.792 1.00 22.68 O ANISOU 1697 OH TYR B 218 2288 3625 2704 -809 -160 87 O ATOM 1698 N VAL B 219 -11.721 -25.170 2.857 1.00 14.27 N ANISOU 1698 N VAL B 219 1647 1698 2076 -447 223 429 N ATOM 1699 CA VAL B 219 -11.294 -26.443 3.423 1.00 15.32 C ANISOU 1699 CA VAL B 219 2042 1503 2277 -491 191 486 C ATOM 1700 C VAL B 219 -11.903 -27.630 2.667 1.00 17.36 C ANISOU 1700 C VAL B 219 2441 1824 2333 -75 354 119 C ATOM 1701 O VAL B 219 -13.125 -27.682 2.514 1.00 18.21 O ANISOU 1701 O VAL B 219 2182 2164 2573 -298 325 48 O ATOM 1702 CB VAL B 219 -11.688 -26.505 4.906 1.00 15.88 C ANISOU 1702 CB VAL B 219 2220 1612 2202 -468 177 412 C ATOM 1703 CG1 VAL B 219 -11.401 -27.908 5.487 1.00 17.63 C ANISOU 1703 CG1 VAL B 219 2563 1801 2336 -383 124 691 C ATOM 1704 CG2 VAL B 219 -10.874 -25.452 5.675 1.00 16.34 C ANISOU 1704 CG2 VAL B 219 2273 1663 2271 -328 -74 -25 C ATOM 1705 N ALA B 220 -11.047 -28.520 2.171 1.00 17.61 N ANISOU 1705 N ALA B 220 2776 1528 2388 -292 586 -32 N ATOM 1706 CA ALA B 220 -11.504 -29.703 1.479 1.00 18.01 C ANISOU 1706 CA ALA B 220 2664 1526 2651 -232 827 -72 C ATOM 1707 C ALA B 220 -12.149 -30.672 2.487 1.00 19.73 C ANISOU 1707 C ALA B 220 2975 1763 2758 -706 494 150 C ATOM 1708 O ALA B 220 -11.681 -30.819 3.615 1.00 21.04 O ANISOU 1708 O ALA B 220 3301 1873 2821 -570 324 280 O ATOM 1709 CB ALA B 220 -10.351 -30.365 0.774 1.00 20.21 C ANISOU 1709 CB ALA B 220 2564 2283 2833 -319 1308 -185 C ATOM 1710 N LEU B 221 -13.226 -31.317 2.070 1.00 20.90 N ANISOU 1710 N LEU B 221 3033 2010 2896 -1072 415 -98 N ATOM 1711 CA LEU B 221 -13.805 -32.363 2.909 1.00 21.58 C ANISOU 1711 CA LEU B 221 3264 1962 2973 -1323 347 -105 C ATOM 1712 C LEU B 221 -12.896 -33.587 3.019 1.00 23.51 C ANISOU 1712 C LEU B 221 3693 2111 3128 -697 589 -264 C ATOM 1713 O LEU B 221 -12.796 -34.226 4.083 1.00 23.51 O ANISOU 1713 O LEU B 221 4003 2004 2927 -538 688 -5 O ATOM 1714 CB LEU B 221 -15.178 -32.751 2.348 1.00 22.10 C ANISOU 1714 CB LEU B 221 2847 2648 2901 -1502 426 -431 C ATOM 1715 CG LEU B 221 -16.028 -33.715 3.201 1.00 23.87 C ANISOU 1715 CG LEU B 221 3088 3004 2977 -2028 443 -404 C ATOM 1716 CD1 LEU B 221 -16.225 -33.155 4.589 1.00 25.03 C ANISOU 1716 CD1 LEU B 221 2961 3407 3140 -1313 313 -560 C ATOM 1717 CD2 LEU B 221 -17.357 -33.927 2.519 1.00 26.79 C ANISOU 1717 CD2 LEU B 221 3514 3612 3053 -2037 279 -335 C ATOM 1718 N ASP B 222 -12.256 -33.944 1.911 1.00 24.36 N ANISOU 1718 N ASP B 222 3766 2184 3304 -730 967 -383 N ATOM 1719 CA ASP B 222 -11.341 -35.070 1.852 1.00 25.29 C ANISOU 1719 CA ASP B 222 3259 2608 3741 -1024 1162 -543 C ATOM 1720 C ASP B 222 -10.075 -34.505 1.193 1.00 25.65 C ANISOU 1720 C ASP B 222 3634 2508 3602 -622 1270 -432 C ATOM 1721 O ASP B 222 -10.020 -34.346 -0.041 1.00 26.88 O ANISOU 1721 O ASP B 222 3788 2673 3752 -902 1312 -456 O ATOM 1722 CB ASP B 222 -11.966 -36.193 1.004 1.00 27.61 C ANISOU 1722 CB ASP B 222 3797 2382 4314 -744 1132 -776 C ATOM 1723 CG ASP B 222 -11.052 -37.407 0.828 1.00 32.41 C ANISOU 1723 CG ASP B 222 4839 2586 4889 -1291 758 -721 C ATOM 1724 OD1 ASP B 222 -9.812 -37.320 0.969 1.00 32.34 O ANISOU 1724 OD1 ASP B 222 4724 2638 4924 -715 1228 -494 O ATOM 1725 OD2 ASP B 222 -11.613 -38.492 0.536 1.00 35.48 O ANISOU 1725 OD2 ASP B 222 5385 2818 5279 -1367 581 -560 O ATOM 1726 N PHE B 223 -9.085 -34.172 2.010 1.00 22.38 N ANISOU 1726 N PHE B 223 3244 1766 3494 -297 1052 -332 N ATOM 1727 CA PHE B 223 -7.915 -33.470 1.488 1.00 21.63 C ANISOU 1727 CA PHE B 223 3222 1604 3394 -241 749 -550 C ATOM 1728 C PHE B 223 -7.142 -34.279 0.445 1.00 22.44 C ANISOU 1728 C PHE B 223 3359 1711 3458 -513 1086 -411 C ATOM 1729 O PHE B 223 -6.756 -33.746 -0.597 1.00 22.84 O ANISOU 1729 O PHE B 223 2942 2246 3490 -807 1250 -309 O ATOM 1730 CB PHE B 223 -6.962 -33.099 2.607 1.00 20.59 C ANISOU 1730 CB PHE B 223 2954 1654 3214 -514 559 -227 C ATOM 1731 CG PHE B 223 -5.699 -32.482 2.130 1.00 20.26 C ANISOU 1731 CG PHE B 223 2823 1791 3084 -243 839 -89 C ATOM 1732 CD1 PHE B 223 -5.691 -31.151 1.659 1.00 18.84 C ANISOU 1732 CD1 PHE B 223 2796 1484 2877 -101 810 -59 C ATOM 1733 CD2 PHE B 223 -4.524 -33.191 2.219 1.00 22.18 C ANISOU 1733 CD2 PHE B 223 2917 2301 3209 165 911 121 C ATOM 1734 CE1 PHE B 223 -4.498 -30.575 1.221 1.00 19.12 C ANISOU 1734 CE1 PHE B 223 2739 1550 2976 85 620 -114 C ATOM 1735 CE2 PHE B 223 -3.346 -32.647 1.772 1.00 20.72 C ANISOU 1735 CE2 PHE B 223 2858 1766 3249 152 1035 120 C ATOM 1736 CZ PHE B 223 -3.328 -31.317 1.294 1.00 20.43 C ANISOU 1736 CZ PHE B 223 2898 1802 3062 298 800 87 C ATOM 1737 N GLU B 224 -6.898 -35.550 0.751 1.00 25.29 N ANISOU 1737 N GLU B 224 4121 1825 3664 -259 1275 -612 N ATOM 1738 CA GLU B 224 -6.064 -36.379 -0.123 1.00 27.93 C ANISOU 1738 CA GLU B 224 4566 2083 3963 -299 1477 -638 C ATOM 1739 C GLU B 224 -6.771 -36.538 -1.458 1.00 28.29 C ANISOU 1739 C GLU B 224 4359 2434 3955 -790 1724 -654 C ATOM 1740 O GLU B 224 -6.121 -36.513 -2.535 1.00 29.84 O ANISOU 1740 O GLU B 224 4615 2730 3992 -513 1796 -814 O ATOM 1741 CB GLU B 224 -5.803 -37.724 0.552 1.00 31.92 C ANISOU 1741 CB GLU B 224 5554 2199 4376 383 1387 -473 C ATOM 1742 CG GLU B 224 -4.735 -37.650 1.668 1.00 38.24 C ANISOU 1742 CG GLU B 224 6317 3467 4744 606 1191 -591 C ATOM 1743 CD GLU B 224 -3.354 -37.235 1.160 1.00 46.21 C ANISOU 1743 CD GLU B 224 7442 5007 5110 976 932 -746 C ATOM 1744 OE1 GLU B 224 -2.907 -37.813 0.133 1.00 50.29 O ANISOU 1744 OE1 GLU B 224 7703 6167 5237 977 977 -711 O ATOM 1745 OE2 GLU B 224 -2.700 -36.349 1.789 1.00 46.84 O ANISOU 1745 OE2 GLU B 224 7712 4814 5270 1310 756 -820 O ATOM 1746 N ASN B 225 -8.090 -36.662 -1.418 1.00 29.58 N ANISOU 1746 N ASN B 225 4617 2620 4001 -1111 1267 -720 N ATOM 1747 CA ASN B 225 -8.847 -36.756 -2.640 1.00 32.43 C ANISOU 1747 CA ASN B 225 5040 3216 4065 -1665 1001 -687 C ATOM 1748 C ASN B 225 -8.828 -35.457 -3.419 1.00 31.53 C ANISOU 1748 C ASN B 225 5131 3024 3826 -1682 720 -804 C ATOM 1749 O ASN B 225 -8.719 -35.465 -4.649 1.00 32.61 O ANISOU 1749 O ASN B 225 5022 3598 3771 -1546 614 -763 O ATOM 1750 CB ASN B 225 -10.296 -37.209 -2.425 1.00 37.35 C ANISOU 1750 CB ASN B 225 5573 4183 4433 -1895 691 -772 C ATOM 1751 CG ASN B 225 -10.957 -37.633 -3.733 1.00 43.33 C ANISOU 1751 CG ASN B 225 6514 5148 4802 -1639 582 -507 C ATOM 1752 OD1 ASN B 225 -10.470 -38.543 -4.423 1.00 45.07 O ANISOU 1752 OD1 ASN B 225 7063 5266 4796 -2168 563 -473 O ATOM 1753 ND2 ASN B 225 -12.033 -36.955 -4.100 1.00 46.05 N ANISOU 1753 ND2 ASN B 225 6769 5726 5002 -1293 450 -266 N ATOM 1754 N GLU B 226 -8.927 -34.339 -2.704 1.00 28.24 N ANISOU 1754 N GLU B 226 4536 2635 3559 -1464 793 -628 N ATOM 1755 CA GLU B 226 -8.870 -33.040 -3.355 1.00 27.75 C ANISOU 1755 CA GLU B 226 4359 2740 3447 -1173 639 -441 C ATOM 1756 C GLU B 226 -7.512 -32.814 -4.021 1.00 26.76 C ANISOU 1756 C GLU B 226 4221 2701 3246 -681 649 -186 C ATOM 1757 O GLU B 226 -7.444 -32.222 -5.101 1.00 27.37 O ANISOU 1757 O GLU B 226 4203 2936 3259 -857 451 -177 O ATOM 1758 CB GLU B 226 -9.149 -31.937 -2.338 1.00 26.50 C ANISOU 1758 CB GLU B 226 4067 2553 3451 -1301 482 -113 C ATOM 1759 CG GLU B 226 -9.658 -30.637 -2.965 1.00 27.14 C ANISOU 1759 CG GLU B 226 3700 3090 3523 -844 626 152 C ATOM 1760 CD GLU B 226 -11.141 -30.673 -3.215 1.00 29.95 C ANISOU 1760 CD GLU B 226 4237 3474 3671 -1105 552 -128 C ATOM 1761 OE1 GLU B 226 -11.737 -31.754 -3.023 1.00 33.52 O ANISOU 1761 OE1 GLU B 226 4881 3762 4092 -1233 448 -62 O ATOM 1762 OE2 GLU B 226 -11.730 -29.650 -3.599 1.00 28.71 O ANISOU 1762 OE2 GLU B 226 3946 3412 3550 -1144 631 -473 O ATOM 1763 N MET B 227 -6.439 -33.270 -3.390 1.00 26.12 N ANISOU 1763 N MET B 227 3901 2837 3187 -753 1012 -447 N ATOM 1764 CA MET B 227 -5.112 -33.187 -3.999 1.00 25.78 C ANISOU 1764 CA MET B 227 3775 2827 3194 -776 1219 -763 C ATOM 1765 C MET B 227 -5.013 -34.078 -5.248 1.00 31.20 C ANISOU 1765 C MET B 227 4897 3683 3274 -1035 1293 -827 C ATOM 1766 O MET B 227 -4.576 -33.610 -6.305 1.00 35.09 O ANISOU 1766 O MET B 227 5674 4354 3305 -1033 1130 -963 O ATOM 1767 CB MET B 227 -4.059 -33.595 -3.001 1.00 24.66 C ANISOU 1767 CB MET B 227 3542 2445 3384 -317 1255 -528 C ATOM 1768 CG MET B 227 -3.852 -32.600 -1.891 1.00 24.09 C ANISOU 1768 CG MET B 227 3651 2011 3493 -294 1285 -113 C ATOM 1769 SD MET B 227 -3.097 -31.085 -2.491 1.00 24.35 S ANISOU 1769 SD MET B 227 3582 2147 3523 -150 1277 -84 S ATOM 1770 CE MET B 227 -1.450 -31.680 -2.830 1.00 27.20 C ANISOU 1770 CE MET B 227 3393 3035 3909 -555 1344 98 C ATOM 1771 N ALA B 228 -5.429 -35.342 -5.105 1.00 33.83 N ANISOU 1771 N ALA B 228 5565 3964 3325 -1353 955 -1003 N ATOM 1772 CA ALA B 228 -5.360 -36.329 -6.189 1.00 37.86 C ANISOU 1772 CA ALA B 228 6087 5004 3296 -1162 792 -1251 C ATOM 1773 C ALA B 228 -6.169 -35.894 -7.415 1.00 42.36 C ANISOU 1773 C ALA B 228 6465 6184 3444 -1066 152 -1156 C ATOM 1774 O ALA B 228 -5.837 -36.285 -8.554 1.00 45.68 O ANISOU 1774 O ALA B 228 7116 6619 3622 -834 188 -1379 O ATOM 1775 CB ALA B 228 -5.794 -37.721 -5.695 1.00 37.66 C ANISOU 1775 CB ALA B 228 6124 4884 3301 -1416 1029 -1345 C ATOM 1776 N THR B 229 -7.171 -35.058 -7.156 1.00 42.79 N ANISOU 1776 N THR B 229 5900 6771 3588 -1051 -53 -906 N ATOM 1777 CA THR B 229 -8.156 -34.467 -8.079 1.00 46.48 C ANISOU 1777 CA THR B 229 6401 7413 3847 -793 -242 -339 C ATOM 1778 C THR B 229 -7.740 -33.137 -8.714 1.00 48.34 C ANISOU 1778 C THR B 229 6879 7770 3719 -677 76 -453 C ATOM 1779 O THR B 229 -8.211 -32.783 -9.805 1.00 49.31 O ANISOU 1779 O THR B 229 7035 7933 3769 -638 -28 -884 O ATOM 1780 CB THR B 229 -9.439 -34.101 -7.250 1.00 48.34 C ANISOU 1780 CB THR B 229 6584 7546 4237 -473 -897 -90 C ATOM 1781 OG1 THR B 229 -10.225 -35.268 -7.025 1.00 50.79 O ANISOU 1781 OG1 THR B 229 6654 8242 4404 -6 -1114 391 O ATOM 1782 CG2 THR B 229 -10.311 -33.011 -7.911 1.00 49.59 C ANISOU 1782 CG2 THR B 229 7073 7399 4369 -736 -1024 -326 C ATOM 1783 N ALA B 230 -6.870 -32.403 -8.122 1.00 47.54 N ANISOU 1783 N ALA B 230 6896 7492 3676 -614 558 -498 N ATOM 1784 CA ALA B 230 -6.724 -31.057 -8.417 1.00 47.65 C ANISOU 1784 CA ALA B 230 7191 7141 3774 -176 653 -370 C ATOM 1785 C ALA B 230 -5.992 -31.117 -9.665 1.00 48.64 C ANISOU 1785 C ALA B 230 7615 6734 4131 372 884 -222 C ATOM 1786 O ALA B 230 -6.042 -30.311 -10.514 1.00 49.29 O ANISOU 1786 O ALA B 230 8335 6499 3895 807 846 -40 O ATOM 1787 CB ALA B 230 -5.861 -30.523 -7.517 1.00 47.89 C ANISOU 1787 CB ALA B 230 6857 7490 3850 -306 654 -213 C ATOM 1788 N ALA B 231 -5.115 -32.027 -9.534 1.00 48.29 N ANISOU 1788 N ALA B 231 7408 6425 4516 330 947 -284 N ATOM 1789 CA ALA B 231 -4.215 -32.549 -10.411 1.00 46.54 C ANISOU 1789 CA ALA B 231 6919 6122 4641 227 986 -676 C ATOM 1790 C ALA B 231 -4.856 -32.913 -11.721 1.00 46.43 C ANISOU 1790 C ALA B 231 6725 6128 4788 63 884 -830 C ATOM 1791 O ALA B 231 -4.136 -33.200 -12.599 0.50 45.45 O ANISOU 1791 O ALA B 231 6484 6115 4670 256 1287 -1006 O ATOM 1792 CB ALA B 231 -3.505 -33.734 -9.677 1.00 45.56 C ANISOU 1792 CB ALA B 231 6710 5889 4711 600 896 -787 C ATOM 1793 N SER B 232 -6.167 -32.754 -11.871 0.50 44.16 N ANISOU 1793 N SER B 232 6166 5725 4889 93 754 -747 N ATOM 1794 CA SER B 232 -7.008 -33.285 -12.964 0.50 43.45 C ANISOU 1794 CA SER B 232 6009 5514 4987 19 497 -513 C ATOM 1795 C SER B 232 -7.733 -32.111 -13.373 0.50 43.16 C ANISOU 1795 C SER B 232 6068 5414 4919 65 456 -326 C ATOM 1796 O SER B 232 -7.267 -31.332 -14.036 0.50 43.36 O ANISOU 1796 O SER B 232 6408 5250 4816 175 411 -444 O ATOM 1797 CB SER B 232 -7.949 -34.392 -12.396 0.50 43.44 C ANISOU 1797 CB SER B 232 5975 5393 5136 -10 231 -645 C ATOM 1798 OG SER B 232 -9.195 -34.578 -12.967 0.50 43.00 O ANISOU 1798 OG SER B 232 5939 5188 5213 -41 4 -761 O ATOM 1799 N SER B 233 -8.808 -31.917 -12.703 0.50 43.81 N ANISOU 1799 N SER B 233 6162 5491 4993 26 200 -23 N ATOM 1800 CA SER B 233 -9.940 -31.121 -12.999 0.50 42.01 C ANISOU 1800 CA SER B 233 5697 5288 4975 136 177 97 C ATOM 1801 C SER B 233 -9.737 -29.688 -13.330 0.50 41.74 C ANISOU 1801 C SER B 233 5692 5302 4866 225 372 -44 C ATOM 1802 O SER B 233 -8.674 -29.160 -13.706 0.50 41.52 O ANISOU 1802 O SER B 233 5665 5198 4913 249 447 -181 O ATOM 1803 CB SER B 233 -10.809 -31.217 -11.805 0.50 40.82 C ANISOU 1803 CB SER B 233 5462 5082 4966 -24 -60 395 C ATOM 1804 OG SER B 233 -10.959 -30.035 -11.042 0.50 40.98 O ANISOU 1804 OG SER B 233 5387 5128 5055 -175 -28 713 O ATOM 1805 N SER B 234 -10.819 -29.025 -13.106 0.50 41.00 N ANISOU 1805 N SER B 234 5499 5386 4693 102 404 -28 N ATOM 1806 CA SER B 234 -10.666 -27.801 -12.497 0.50 39.89 C ANISOU 1806 CA SER B 234 5287 5380 4490 -333 276 -276 C ATOM 1807 C SER B 234 -11.878 -27.140 -12.742 0.50 42.24 C ANISOU 1807 C SER B 234 5360 5998 4690 -284 159 -214 C ATOM 1808 O SER B 234 -12.175 -26.769 -13.752 0.50 42.17 O ANISOU 1808 O SER B 234 5002 6300 4722 -334 -66 -90 O ATOM 1809 CB SER B 234 -9.466 -27.002 -13.006 0.50 37.65 C ANISOU 1809 CB SER B 234 5147 4963 4196 -670 296 -455 C ATOM 1810 OG SER B 234 -9.589 -25.760 -12.631 0.50 34.33 O ANISOU 1810 OG SER B 234 4794 4349 3900 -1328 516 -690 O ATOM 1811 N SER B 235 -12.627 -27.055 -11.755 1.00 45.28 N ANISOU 1811 N SER B 235 5842 6410 4951 -141 240 -143 N ATOM 1812 CA SER B 235 -13.110 -25.869 -11.351 1.00 44.68 C ANISOU 1812 CA SER B 235 5806 6193 4978 -28 241 -160 C ATOM 1813 C SER B 235 -12.197 -25.567 -10.304 1.00 41.27 C ANISOU 1813 C SER B 235 5243 5740 4699 -120 -168 -179 C ATOM 1814 O SER B 235 -12.438 -24.631 -9.703 1.00 44.61 O ANISOU 1814 O SER B 235 5261 6582 5106 343 -644 -55 O ATOM 1815 CB SER B 235 -14.537 -25.908 -10.799 1.00 45.77 C ANISOU 1815 CB SER B 235 5878 6433 5080 200 398 -330 C ATOM 1816 N LEU B 236 -11.104 -26.243 -10.071 1.00 34.02 N ANISOU 1816 N LEU B 236 4607 4163 4156 -564 5 -85 N ATOM 1817 CA LEU B 236 -10.355 -25.742 -8.906 1.00 30.06 C ANISOU 1817 CA LEU B 236 4088 3712 3622 -527 -191 -188 C ATOM 1818 C LEU B 236 -9.583 -24.386 -9.022 1.00 29.29 C ANISOU 1818 C LEU B 236 3803 3893 3432 -599 -162 -230 C ATOM 1819 O LEU B 236 -9.497 -23.638 -8.167 1.00 26.22 O ANISOU 1819 O LEU B 236 2930 3847 3184 27 -282 -377 O ATOM 1820 CB LEU B 236 -9.386 -26.796 -8.544 1.00 29.61 C ANISOU 1820 CB LEU B 236 4051 3664 3536 -901 218 -299 C ATOM 1821 CG LEU B 236 -8.229 -26.487 -7.667 0.50 26.11 C ANISOU 1821 CG LEU B 236 3499 3075 3347 -709 752 -286 C ATOM 1822 CD1 LEU B 236 -8.758 -26.275 -6.290 0.50 27.49 C ANISOU 1822 CD1 LEU B 236 4065 3061 3320 -799 816 -564 C ATOM 1823 CD2 LEU B 236 -7.282 -27.604 -7.718 0.50 22.57 C ANISOU 1823 CD2 LEU B 236 2962 2344 3270 -760 1152 -127 C ATOM 1824 N GLU B 237 -8.986 -24.180 -10.165 1.00 28.14 N ANISOU 1824 N GLU B 237 3429 3796 3468 -1122 -461 -93 N ATOM 1825 CA GLU B 237 -8.181 -23.012 -10.410 1.00 28.88 C ANISOU 1825 CA GLU B 237 3459 3710 3803 -1328 -592 70 C ATOM 1826 C GLU B 237 -8.952 -21.779 -10.437 1.00 29.84 C ANISOU 1826 C GLU B 237 3463 3678 4196 -1027 -1189 -3 C ATOM 1827 O GLU B 237 -9.961 -21.749 -11.049 1.00 32.71 O ANISOU 1827 O GLU B 237 4404 3460 4563 -848 -1563 -127 O ATOM 1828 CB GLU B 237 -7.334 -23.127 -11.672 1.00 34.63 C ANISOU 1828 CB GLU B 237 4328 4633 4198 -1002 14 70 C ATOM 1829 CG GLU B 237 -6.319 -24.029 -11.485 1.00 39.77 C ANISOU 1829 CG GLU B 237 4917 5660 4532 -897 279 -36 C ATOM 1830 CD GLU B 237 -5.463 -24.145 -12.602 1.00 45.82 C ANISOU 1830 CD GLU B 237 5921 6635 4855 -746 131 110 C ATOM 1831 OE1 GLU B 237 -5.780 -23.591 -13.540 1.00 46.13 O ANISOU 1831 OE1 GLU B 237 5847 6986 4694 -1156 105 198 O ATOM 1832 OE2 GLU B 237 -4.433 -24.720 -12.498 1.00 48.60 O ANISOU 1832 OE2 GLU B 237 6410 6942 5113 -273 407 -53 O ATOM 1833 N LYS B 238 -8.502 -20.725 -9.783 1.00 27.09 N ANISOU 1833 N LYS B 238 3033 2975 4286 -896 -1070 416 N ATOM 1834 CA LYS B 238 -9.229 -19.464 -9.735 1.00 29.99 C ANISOU 1834 CA LYS B 238 2795 3852 4746 -744 -1352 428 C ATOM 1835 C LYS B 238 -8.255 -18.358 -9.924 1.00 32.30 C ANISOU 1835 C LYS B 238 3312 3876 5086 -635 -1404 479 C ATOM 1836 O LYS B 238 -7.103 -18.475 -9.513 1.00 32.78 O ANISOU 1836 O LYS B 238 3541 3500 5415 -203 -1585 334 O ATOM 1837 CB LYS B 238 -9.904 -19.244 -8.384 1.00 33.64 C ANISOU 1837 CB LYS B 238 3295 4520 4967 -493 -1371 312 C ATOM 1838 CG LYS B 238 -10.984 -20.225 -8.036 1.00 36.41 C ANISOU 1838 CG LYS B 238 3487 5114 5235 -1059 -1190 355 C ATOM 1839 CD LYS B 238 -12.107 -20.190 -9.065 1.00 39.44 C ANISOU 1839 CD LYS B 238 3802 5693 5492 -1013 -1258 508 C ATOM 1840 CE LYS B 238 -13.017 -21.401 -8.928 1.00 41.09 C ANISOU 1840 CE LYS B 238 3857 6084 5670 -1676 -1120 661 C ATOM 1841 NZ LYS B 238 -13.885 -21.566 -10.135 1.00 43.05 N ANISOU 1841 NZ LYS B 238 4061 6541 5754 -1634 -1114 720 N ATOM 1842 N SER B 239 -8.709 -17.278 -10.537 1.00 32.40 N ANISOU 1842 N SER B 239 3133 4100 5079 -1282 -1128 521 N ATOM 1843 CA ASER B 239 -7.842 -16.135 -10.763 0.50 32.44 C ANISOU 1843 CA ASER B 239 2976 4281 5070 -1104 -996 527 C ATOM 1844 CA BSER B 239 -7.858 -16.124 -10.773 0.50 32.66 C ANISOU 1844 CA BSER B 239 3126 4220 5062 -1078 -1056 415 C ATOM 1845 C SER B 239 -8.166 -15.013 -9.780 1.00 31.27 C ANISOU 1845 C SER B 239 2885 4064 4933 -903 -922 603 C ATOM 1846 O SER B 239 -9.287 -14.896 -9.268 1.00 31.00 O ANISOU 1846 O SER B 239 2648 3978 5154 -453 -811 560 O ATOM 1847 CB ASER B 239 -7.916 -15.660 -12.215 0.50 34.35 C ANISOU 1847 CB ASER B 239 2978 4906 5168 -1047 -916 494 C ATOM 1848 CB BSER B 239 -7.999 -15.636 -12.212 0.50 34.93 C ANISOU 1848 CB BSER B 239 3386 4737 5147 -969 -1100 158 C ATOM 1849 OG ASER B 239 -9.223 -15.247 -12.548 0.50 34.83 O ANISOU 1849 OG ASER B 239 2729 5273 5234 -1177 -784 687 O ATOM 1850 OG BSER B 239 -7.376 -16.546 -13.096 0.50 35.77 O ANISOU 1850 OG BSER B 239 3352 5035 5205 -1001 -1099 84 O ATOM 1851 N TYR B 240 -7.160 -14.207 -9.485 1.00 28.78 N ANISOU 1851 N TYR B 240 3014 3507 4415 -905 -908 836 N ATOM 1852 CA TYR B 240 -7.352 -13.118 -8.579 1.00 27.59 C ANISOU 1852 CA TYR B 240 2875 3533 4076 -322 -504 1281 C ATOM 1853 C TYR B 240 -6.695 -11.891 -9.193 1.00 24.88 C ANISOU 1853 C TYR B 240 2416 3160 3876 -212 -286 1467 C ATOM 1854 O TYR B 240 -5.527 -11.933 -9.601 1.00 25.23 O ANISOU 1854 O TYR B 240 2662 3351 3571 -816 -316 1211 O ATOM 1855 CB TYR B 240 -6.711 -13.460 -7.237 1.00 25.43 C ANISOU 1855 CB TYR B 240 2428 3314 3922 -251 -210 1406 C ATOM 1856 CG TYR B 240 -6.695 -12.339 -6.242 1.00 25.13 C ANISOU 1856 CG TYR B 240 2297 3546 3706 -395 130 1279 C ATOM 1857 CD1 TYR B 240 -7.703 -12.209 -5.269 1.00 24.17 C ANISOU 1857 CD1 TYR B 240 1700 3770 3713 -319 371 1238 C ATOM 1858 CD2 TYR B 240 -5.685 -11.382 -6.274 1.00 24.56 C ANISOU 1858 CD2 TYR B 240 2708 2954 3669 -404 102 1216 C ATOM 1859 CE1 TYR B 240 -7.679 -11.168 -4.341 1.00 26.74 C ANISOU 1859 CE1 TYR B 240 2494 3876 3790 72 309 1327 C ATOM 1860 CE2 TYR B 240 -5.651 -10.342 -5.359 1.00 25.57 C ANISOU 1860 CE2 TYR B 240 2695 3385 3635 -172 129 1218 C ATOM 1861 CZ TYR B 240 -6.642 -10.247 -4.384 1.00 26.28 C ANISOU 1861 CZ TYR B 240 2724 3516 3745 54 72 1255 C ATOM 1862 OH TYR B 240 -6.578 -9.222 -3.494 1.00 27.63 O ANISOU 1862 OH TYR B 240 2958 3737 3801 -128 86 1171 O ATOM 1863 N GLU B 241 -7.442 -10.800 -9.255 1.00 26.55 N ANISOU 1863 N GLU B 241 2325 3499 4264 44 -252 1750 N ATOM 1864 CA GLU B 241 -6.889 -9.623 -9.867 1.00 26.44 C ANISOU 1864 CA GLU B 241 1688 3553 4806 284 -46 1950 C ATOM 1865 C GLU B 241 -6.223 -8.746 -8.839 1.00 27.58 C ANISOU 1865 C GLU B 241 1952 3452 5077 199 254 1569 C ATOM 1866 O GLU B 241 -6.831 -8.361 -7.857 1.00 30.83 O ANISOU 1866 O GLU B 241 2900 3566 5248 -60 -36 1257 O ATOM 1867 CB GLU B 241 -7.964 -8.871 -10.640 1.00 32.61 C ANISOU 1867 CB GLU B 241 2812 4336 5241 524 -660 2155 C ATOM 1868 CG GLU B 241 -7.363 -7.860 -11.599 1.00 38.65 C ANISOU 1868 CG GLU B 241 3971 5045 5669 407 -964 2302 C ATOM 1869 CD GLU B 241 -8.414 -7.206 -12.474 1.00 45.40 C ANISOU 1869 CD GLU B 241 5210 5864 6176 425 -1166 1955 C ATOM 1870 OE1 GLU B 241 -9.262 -7.929 -13.046 1.00 48.91 O ANISOU 1870 OE1 GLU B 241 5585 6634 6366 -5 -1226 1735 O ATOM 1871 OE2 GLU B 241 -8.369 -5.968 -12.593 1.00 47.21 O ANISOU 1871 OE2 GLU B 241 5840 5689 6408 706 -1123 1875 O ATOM 1872 N LEU B 242 -4.952 -8.451 -9.063 1.00 30.06 N ANISOU 1872 N LEU B 242 2463 3578 5382 293 679 1645 N ATOM 1873 CA LEU B 242 -4.186 -7.616 -8.150 1.00 29.17 C ANISOU 1873 CA LEU B 242 2142 3272 5668 1471 504 1476 C ATOM 1874 C LEU B 242 -4.627 -6.144 -8.240 1.00 37.48 C ANISOU 1874 C LEU B 242 4019 4113 6109 1051 527 1370 C ATOM 1875 O LEU B 242 -5.291 -5.759 -9.214 1.00 37.44 O ANISOU 1875 O LEU B 242 4349 3678 6200 1177 506 1455 O ATOM 1876 CB LEU B 242 -2.687 -7.759 -8.452 1.00 30.05 C ANISOU 1876 CB LEU B 242 1995 3747 5674 846 260 1331 C ATOM 1877 CG LEU B 242 -2.152 -9.187 -8.303 1.00 31.87 C ANISOU 1877 CG LEU B 242 2385 4080 5645 722 120 1697 C ATOM 1878 CD1 LEU B 242 -0.779 -9.301 -8.944 1.00 32.42 C ANISOU 1878 CD1 LEU B 242 2691 4102 5525 799 430 1788 C ATOM 1879 CD2 LEU B 242 -2.070 -9.556 -6.857 1.00 33.65 C ANISOU 1879 CD2 LEU B 242 2773 4360 5654 -82 239 1753 C ATOM 1880 N PRO B 243 -4.257 -5.321 -7.230 1.00 41.18 N ANISOU 1880 N PRO B 243 5057 4131 6460 1027 505 1273 N ATOM 1881 CA PRO B 243 -4.705 -3.916 -7.273 1.00 44.45 C ANISOU 1881 CA PRO B 243 5831 4382 6678 739 470 1548 C ATOM 1882 C PRO B 243 -4.320 -3.229 -8.583 1.00 47.75 C ANISOU 1882 C PRO B 243 6436 4789 6919 651 624 1684 C ATOM 1883 O PRO B 243 -5.085 -2.410 -9.093 1.00 50.26 O ANISOU 1883 O PRO B 243 6861 5151 7084 787 684 1589 O ATOM 1884 CB PRO B 243 -3.975 -3.274 -6.093 1.00 43.11 C ANISOU 1884 CB PRO B 243 5701 4081 6596 690 321 1605 C ATOM 1885 CG PRO B 243 -3.774 -4.441 -5.114 1.00 42.19 C ANISOU 1885 CG PRO B 243 5452 3999 6581 727 256 1494 C ATOM 1886 CD PRO B 243 -3.512 -5.628 -5.988 1.00 40.95 C ANISOU 1886 CD PRO B 243 5040 4007 6512 1026 417 1420 C ATOM 1887 N ASP B 244 -3.171 -3.607 -9.139 1.00 46.88 N ANISOU 1887 N ASP B 244 6324 4517 6973 623 866 1657 N ATOM 1888 CA ASP B 244 -2.616 -2.925 -10.299 1.00 47.99 C ANISOU 1888 CA ASP B 244 6511 4662 7062 750 824 1651 C ATOM 1889 C ASP B 244 -3.138 -3.474 -11.620 1.00 47.39 C ANISOU 1889 C ASP B 244 6505 4599 6903 629 902 1894 C ATOM 1890 O ASP B 244 -2.704 -3.027 -12.683 1.00 48.04 O ANISOU 1890 O ASP B 244 6892 4398 6961 824 1141 2037 O ATOM 1891 CB ASP B 244 -1.080 -2.971 -10.256 1.00 48.92 C ANISOU 1891 CB ASP B 244 6542 4723 7321 928 735 1530 C ATOM 1892 CG ASP B 244 -0.528 -4.405 -10.213 1.00 50.47 C ANISOU 1892 CG ASP B 244 6628 4997 7550 882 646 1290 C ATOM 1893 OD1 ASP B 244 0.641 -4.581 -9.793 1.00 52.92 O ANISOU 1893 OD1 ASP B 244 7169 5312 7624 827 662 1039 O ATOM 1894 OD2 ASP B 244 -1.248 -5.353 -10.607 1.00 49.10 O ANISOU 1894 OD2 ASP B 244 6178 4851 7628 467 595 1457 O ATOM 1895 N GLY B 245 -4.040 -4.455 -11.556 1.00 44.81 N ANISOU 1895 N GLY B 245 5969 4393 6663 556 735 2051 N ATOM 1896 CA GLY B 245 -4.638 -5.035 -12.755 1.00 41.80 C ANISOU 1896 CA GLY B 245 5189 4354 6338 418 525 2275 C ATOM 1897 C GLY B 245 -4.076 -6.361 -13.248 1.00 39.67 C ANISOU 1897 C GLY B 245 4474 4564 6033 138 367 2450 C ATOM 1898 O GLY B 245 -4.718 -7.047 -14.057 1.00 40.96 O ANISOU 1898 O GLY B 245 4580 4943 6040 282 108 2498 O ATOM 1899 N GLN B 246 -2.875 -6.738 -12.797 1.00 35.43 N ANISOU 1899 N GLN B 246 3716 3981 5762 31 502 2491 N ATOM 1900 CA AGLN B 246 -2.362 -8.045 -13.204 0.50 34.50 C ANISOU 1900 CA AGLN B 246 3362 4187 5562 -449 325 2135 C ATOM 1901 CA BGLN B 246 -2.288 -8.049 -13.106 0.50 34.14 C ANISOU 1901 CA BGLN B 246 3407 3934 5629 -615 375 2335 C ATOM 1902 C GLN B 246 -3.102 -9.160 -12.440 1.00 32.00 C ANISOU 1902 C GLN B 246 2966 3875 5319 -278 109 2120 C ATOM 1903 O GLN B 246 -3.740 -8.917 -11.413 1.00 32.39 O ANISOU 1903 O GLN B 246 2607 4184 5514 -285 -120 1661 O ATOM 1904 CB AGLN B 246 -0.833 -8.136 -13.069 0.50 33.82 C ANISOU 1904 CB AGLN B 246 2771 4558 5520 -601 375 1813 C ATOM 1905 CB BGLN B 246 -0.843 -8.136 -12.598 0.50 33.06 C ANISOU 1905 CB BGLN B 246 2994 3840 5726 -1183 525 2399 C ATOM 1906 CG AGLN B 246 -0.035 -7.378 -14.199 0.50 34.79 C ANISOU 1906 CG AGLN B 246 2654 5149 5417 -599 241 1363 C ATOM 1907 CG BGLN B 246 0.195 -7.374 -13.433 0.50 36.06 C ANISOU 1907 CG BGLN B 246 3436 4344 5919 -1160 381 2111 C ATOM 1908 CD AGLN B 246 0.247 -8.233 -15.439 0.50 34.56 C ANISOU 1908 CD AGLN B 246 2090 5671 5370 -445 155 929 C ATOM 1909 CD BGLN B 246 0.767 -6.200 -12.691 0.50 37.76 C ANISOU 1909 CD BGLN B 246 3613 4682 6053 -1056 358 1831 C ATOM 1910 OE1AGLN B 246 1.024 -9.181 -15.390 0.50 32.26 O ANISOU 1910 OE1AGLN B 246 1096 5817 5343 -503 49 635 O ATOM 1911 OE1BGLN B 246 0.560 -5.049 -13.082 0.50 41.98 O ANISOU 1911 OE1BGLN B 246 4155 5557 6236 -693 279 1464 O ATOM 1912 NE2AGLN B 246 -0.380 -7.881 -16.559 0.50 35.71 N ANISOU 1912 NE2AGLN B 246 2386 5846 5337 -454 241 672 N ATOM 1913 NE2BGLN B 246 1.482 -6.476 -11.602 0.50 35.36 N ANISOU 1913 NE2BGLN B 246 2982 4472 5979 -1219 506 1679 N ATOM 1914 N VAL B 247 -3.061 -10.368 -12.992 1.00 29.02 N ANISOU 1914 N VAL B 247 2549 3778 4701 288 -279 1928 N ATOM 1915 CA VAL B 247 -3.791 -11.478 -12.405 1.00 25.57 C ANISOU 1915 CA VAL B 247 2313 3052 4349 674 -594 1325 C ATOM 1916 C VAL B 247 -2.841 -12.585 -11.964 1.00 25.77 C ANISOU 1916 C VAL B 247 2773 2781 4240 -669 -260 929 C ATOM 1917 O VAL B 247 -1.800 -12.816 -12.581 1.00 26.82 O ANISOU 1917 O VAL B 247 3018 2871 4300 -643 -185 907 O ATOM 1918 CB VAL B 247 -4.867 -11.992 -13.377 1.00 32.35 C ANISOU 1918 CB VAL B 247 3426 4437 4428 530 -480 746 C ATOM 1919 CG1 VAL B 247 -5.551 -13.147 -12.838 1.00 35.23 C ANISOU 1919 CG1 VAL B 247 4175 4713 4500 931 -428 810 C ATOM 1920 CG2 VAL B 247 -5.910 -10.925 -13.610 1.00 34.63 C ANISOU 1920 CG2 VAL B 247 3901 4880 4376 561 -604 766 C ATOM 1921 N ILE B 248 -3.201 -13.244 -10.868 1.00 26.03 N ANISOU 1921 N ILE B 248 2859 2994 4036 -424 -497 1021 N ATOM 1922 CA ILE B 248 -2.517 -14.474 -10.486 1.00 27.33 C ANISOU 1922 CA ILE B 248 3138 3033 4214 -721 -611 768 C ATOM 1923 C ILE B 248 -3.533 -15.602 -10.550 1.00 28.89 C ANISOU 1923 C ILE B 248 3512 3218 4245 -709 -486 739 C ATOM 1924 O ILE B 248 -4.728 -15.332 -10.522 1.00 31.47 O ANISOU 1924 O ILE B 248 3796 3619 4541 -798 -795 726 O ATOM 1925 CB ILE B 248 -1.830 -14.351 -9.083 1.00 28.42 C ANISOU 1925 CB ILE B 248 3078 3462 4259 -582 -552 813 C ATOM 1926 CG1 ILE B 248 -2.848 -14.076 -7.963 1.00 27.57 C ANISOU 1926 CG1 ILE B 248 2378 3688 4411 -992 -60 771 C ATOM 1927 CG2 ILE B 248 -0.760 -13.250 -9.095 1.00 27.95 C ANISOU 1927 CG2 ILE B 248 2753 3529 4337 -372 -681 657 C ATOM 1928 CD1 ILE B 248 -3.376 -15.339 -7.269 1.00 34.04 C ANISOU 1928 CD1 ILE B 248 3977 4386 4571 -138 -24 560 C ATOM 1929 N THR B 249 -3.082 -16.846 -10.676 1.00 27.73 N ANISOU 1929 N THR B 249 3753 2888 3896 -1035 -268 560 N ATOM 1930 CA ATHR B 249 -3.996 -17.990 -10.605 0.60 29.15 C ANISOU 1930 CA ATHR B 249 4433 2922 3720 -902 -25 753 C ATOM 1931 CA BTHR B 249 -4.016 -17.956 -10.582 0.40 27.25 C ANISOU 1931 CA BTHR B 249 3864 2847 3643 -750 -36 845 C ATOM 1932 C THR B 249 -3.513 -18.963 -9.540 1.00 26.94 C ANISOU 1932 C THR B 249 3730 2988 3516 -442 56 607 C ATOM 1933 O THR B 249 -2.331 -19.160 -9.361 1.00 27.53 O ANISOU 1933 O THR B 249 3609 3340 3512 -566 325 827 O ATOM 1934 CB ATHR B 249 -4.317 -18.677 -12.000 0.60 33.59 C ANISOU 1934 CB ATHR B 249 5517 3365 3880 -1298 116 497 C ATOM 1935 CB BTHR B 249 -4.383 -18.534 -11.988 0.40 27.35 C ANISOU 1935 CB BTHR B 249 3785 2988 3618 -846 91 959 C ATOM 1936 OG1ATHR B 249 -4.690 -20.055 -11.810 0.60 36.56 O ANISOU 1936 OG1ATHR B 249 6090 3968 3831 -1249 144 494 O ATOM 1937 OG1BTHR B 249 -4.866 -17.465 -12.812 0.40 26.34 O ANISOU 1937 OG1BTHR B 249 3412 3123 3474 -604 180 1247 O ATOM 1938 CG2ATHR B 249 -3.166 -18.592 -12.993 0.60 34.34 C ANISOU 1938 CG2ATHR B 249 5507 3585 3956 -990 136 335 C ATOM 1939 CG2BTHR B 249 -5.495 -19.593 -11.908 0.40 26.67 C ANISOU 1939 CG2BTHR B 249 3491 3057 3586 -532 187 1013 C ATOM 1940 N ILE B 250 -4.453 -19.518 -8.811 1.00 22.05 N ANISOU 1940 N ILE B 250 2573 2542 3262 -280 194 588 N ATOM 1941 CA ILE B 250 -4.177 -20.351 -7.666 1.00 22.37 C ANISOU 1941 CA ILE B 250 2647 2807 3046 -325 323 311 C ATOM 1942 C ILE B 250 -4.970 -21.626 -7.859 1.00 21.30 C ANISOU 1942 C ILE B 250 2482 2756 2857 -29 168 153 C ATOM 1943 O ILE B 250 -6.089 -21.557 -8.351 1.00 20.67 O ANISOU 1943 O ILE B 250 1882 2818 3154 -297 -36 190 O ATOM 1944 CB ILE B 250 -4.607 -19.553 -6.381 1.00 24.01 C ANISOU 1944 CB ILE B 250 2692 3225 3207 -555 240 -101 C ATOM 1945 CG1 ILE B 250 -4.351 -20.308 -5.116 1.00 27.68 C ANISOU 1945 CG1 ILE B 250 3471 3572 3475 -608 467 -76 C ATOM 1946 CG2 ILE B 250 -6.096 -19.068 -6.437 1.00 24.21 C ANISOU 1946 CG2 ILE B 250 2732 3263 3204 22 504 -148 C ATOM 1947 CD1 ILE B 250 -4.719 -19.452 -3.924 1.00 25.68 C ANISOU 1947 CD1 ILE B 250 3406 3111 3240 -457 978 -656 C ATOM 1948 N GLY B 251 -4.421 -22.771 -7.473 1.00 22.03 N ANISOU 1948 N GLY B 251 3182 2475 2715 -345 552 75 N ATOM 1949 CA GLY B 251 -5.113 -24.026 -7.611 1.00 22.63 C ANISOU 1949 CA GLY B 251 3573 2501 2527 -479 582 -4 C ATOM 1950 C GLY B 251 -5.218 -24.721 -6.261 1.00 21.26 C ANISOU 1950 C GLY B 251 3259 2561 2259 -42 589 -5 C ATOM 1951 O GLY B 251 -6.027 -24.317 -5.376 1.00 22.41 O ANISOU 1951 O GLY B 251 3352 2938 2223 -404 703 -131 O ATOM 1952 N ASN B 252 -4.421 -25.770 -6.098 1.00 19.75 N ANISOU 1952 N ASN B 252 2910 2275 2318 -472 444 29 N ATOM 1953 CA ASN B 252 -4.496 -26.538 -4.852 1.00 20.20 C ANISOU 1953 CA ASN B 252 2985 2125 2565 -318 491 -68 C ATOM 1954 C ASN B 252 -4.089 -25.739 -3.621 1.00 20.34 C ANISOU 1954 C ASN B 252 3046 2127 2554 -53 514 132 C ATOM 1955 O ASN B 252 -4.442 -26.100 -2.487 1.00 18.84 O ANISOU 1955 O ASN B 252 2949 1883 2328 214 730 254 O ATOM 1956 CB ASN B 252 -3.837 -27.933 -4.958 1.00 20.27 C ANISOU 1956 CB ASN B 252 2856 1951 2894 229 516 -282 C ATOM 1957 CG ASN B 252 -2.346 -27.886 -5.137 1.00 24.09 C ANISOU 1957 CG ASN B 252 3601 2619 2933 423 768 -252 C ATOM 1958 OD1 ASN B 252 -1.712 -28.901 -5.515 1.00 28.08 O ANISOU 1958 OD1 ASN B 252 4284 3225 3161 407 588 -296 O ATOM 1959 ND2 ASN B 252 -1.764 -26.763 -4.850 1.00 21.45 N ANISOU 1959 ND2 ASN B 252 3517 1975 2656 -174 1048 -218 N ATOM 1960 N GLU B 253 -3.427 -24.599 -3.828 1.00 17.68 N ANISOU 1960 N GLU B 253 2121 2042 2556 -224 686 36 N ATOM 1961 CA GLU B 253 -3.067 -23.710 -2.712 1.00 18.63 C ANISOU 1961 CA GLU B 253 2221 2367 2492 -447 861 190 C ATOM 1962 C GLU B 253 -4.331 -23.205 -2.001 1.00 16.64 C ANISOU 1962 C GLU B 253 1783 1933 2606 -606 372 332 C ATOM 1963 O GLU B 253 -4.280 -22.845 -0.814 1.00 17.14 O ANISOU 1963 O GLU B 253 2015 1883 2615 -210 653 439 O ATOM 1964 CB GLU B 253 -2.235 -22.513 -3.204 1.00 18.51 C ANISOU 1964 CB GLU B 253 2199 2376 2460 -341 946 346 C ATOM 1965 CG GLU B 253 -0.930 -22.942 -3.888 1.00 20.82 C ANISOU 1965 CG GLU B 253 2760 2493 2659 -418 1080 -14 C ATOM 1966 CD GLU B 253 -1.050 -23.274 -5.383 1.00 24.18 C ANISOU 1966 CD GLU B 253 2860 3271 3058 -441 1169 47 C ATOM 1967 OE1 GLU B 253 0.012 -23.532 -5.995 1.00 26.07 O ANISOU 1967 OE1 GLU B 253 2660 3811 3434 -328 1139 -378 O ATOM 1968 OE2 GLU B 253 -2.153 -23.284 -5.952 1.00 22.43 O ANISOU 1968 OE2 GLU B 253 2965 2643 2914 -686 999 422 O ATOM 1969 N ARG B 254 -5.446 -23.163 -2.736 1.00 15.98 N ANISOU 1969 N ARG B 254 1902 1637 2533 -72 356 347 N ATOM 1970 CA ARG B 254 -6.725 -22.719 -2.196 1.00 17.35 C ANISOU 1970 CA ARG B 254 2281 1902 2410 -69 109 450 C ATOM 1971 C ARG B 254 -7.092 -23.517 -0.957 1.00 16.21 C ANISOU 1971 C ARG B 254 2061 1597 2502 -3 -25 300 C ATOM 1972 O ARG B 254 -7.589 -22.951 0.024 1.00 15.61 O ANISOU 1972 O ARG B 254 1886 1481 2565 -359 278 146 O ATOM 1973 CB ARG B 254 -7.840 -22.848 -3.216 1.00 17.14 C ANISOU 1973 CB ARG B 254 2475 1788 2250 -59 -67 380 C ATOM 1974 CG ARG B 254 -7.689 -21.844 -4.345 1.00 19.80 C ANISOU 1974 CG ARG B 254 2956 2166 2400 14 -178 659 C ATOM 1975 CD ARG B 254 -8.787 -22.033 -5.367 1.00 17.48 C ANISOU 1975 CD ARG B 254 1500 2705 2436 -210 277 423 C ATOM 1976 NE ARG B 254 -10.085 -21.719 -4.792 1.00 19.72 N ANISOU 1976 NE ARG B 254 1943 2881 2669 200 293 673 N ATOM 1977 CZ ARG B 254 -11.262 -22.172 -5.225 1.00 22.49 C ANISOU 1977 CZ ARG B 254 2659 3018 2870 -288 143 427 C ATOM 1978 NH1 ARG B 254 -11.346 -22.997 -6.253 1.00 23.46 N ANISOU 1978 NH1 ARG B 254 2982 3022 2910 -427 -71 43 N ATOM 1979 NH2 ARG B 254 -12.375 -21.805 -4.605 1.00 24.73 N ANISOU 1979 NH2 ARG B 254 3027 3341 3030 -97 -6 522 N ATOM 1980 N PHE B 255 -6.884 -24.820 -1.034 1.00 15.91 N ANISOU 1980 N PHE B 255 2203 1405 2439 -165 39 439 N ATOM 1981 CA PHE B 255 -7.268 -25.659 0.129 1.00 16.37 C ANISOU 1981 CA PHE B 255 2508 1162 2549 -249 136 341 C ATOM 1982 C PHE B 255 -6.081 -26.178 0.939 1.00 14.38 C ANISOU 1982 C PHE B 255 1617 1164 2683 -62 509 134 C ATOM 1983 O PHE B 255 -6.256 -26.562 2.103 1.00 16.47 O ANISOU 1983 O PHE B 255 1797 1859 2603 -139 426 533 O ATOM 1984 CB PHE B 255 -8.216 -26.784 -0.299 1.00 17.11 C ANISOU 1984 CB PHE B 255 2258 1661 2581 -439 364 28 C ATOM 1985 CG PHE B 255 -7.619 -27.742 -1.289 1.00 17.86 C ANISOU 1985 CG PHE B 255 2087 2062 2636 -300 512 -14 C ATOM 1986 CD1 PHE B 255 -7.807 -27.541 -2.672 1.00 19.59 C ANISOU 1986 CD1 PHE B 255 2364 2357 2720 -547 658 -373 C ATOM 1987 CD2 PHE B 255 -6.910 -28.865 -0.864 1.00 17.57 C ANISOU 1987 CD2 PHE B 255 1903 1968 2804 194 220 -374 C ATOM 1988 CE1 PHE B 255 -7.262 -28.433 -3.603 1.00 20.34 C ANISOU 1988 CE1 PHE B 255 2695 2471 2562 -678 183 -119 C ATOM 1989 CE2 PHE B 255 -6.314 -29.741 -1.835 1.00 20.64 C ANISOU 1989 CE2 PHE B 255 2841 2213 2789 -127 323 -167 C ATOM 1990 CZ PHE B 255 -6.544 -29.507 -3.200 1.00 21.18 C ANISOU 1990 CZ PHE B 255 3065 2257 2726 -490 434 -222 C ATOM 1991 N ARG B 256 -4.860 -26.139 0.395 1.00 14.44 N ANISOU 1991 N ARG B 256 1076 1599 2811 116 623 174 N ATOM 1992 CA ARG B 256 -3.680 -26.508 1.160 1.00 15.01 C ANISOU 1992 CA ARG B 256 1296 1723 2682 245 456 -283 C ATOM 1993 C ARG B 256 -3.446 -25.508 2.266 1.00 13.69 C ANISOU 1993 C ARG B 256 962 1655 2586 221 412 -24 C ATOM 1994 O ARG B 256 -2.985 -25.865 3.323 1.00 16.42 O ANISOU 1994 O ARG B 256 1926 1866 2447 367 318 200 O ATOM 1995 CB ARG B 256 -2.441 -26.609 0.271 1.00 16.21 C ANISOU 1995 CB ARG B 256 2030 1416 2714 50 375 -94 C ATOM 1996 CG ARG B 256 -2.536 -27.808 -0.636 1.00 17.24 C ANISOU 1996 CG ARG B 256 2421 1378 2751 -13 1048 -167 C ATOM 1997 CD ARG B 256 -1.497 -27.663 -1.806 1.00 18.56 C ANISOU 1997 CD ARG B 256 2169 1922 2959 -530 1056 105 C ATOM 1998 NE ARG B 256 -0.162 -27.474 -1.283 1.00 19.22 N ANISOU 1998 NE ARG B 256 2028 2124 3149 219 1049 269 N ATOM 1999 CZ ARG B 256 0.846 -26.913 -1.958 1.00 20.37 C ANISOU 1999 CZ ARG B 256 2482 2037 3222 322 838 78 C ATOM 2000 NH1 ARG B 256 0.643 -26.399 -3.178 1.00 21.15 N ANISOU 2000 NH1 ARG B 256 2548 2272 3218 -308 728 -121 N ATOM 2001 NH2 ARG B 256 2.018 -26.787 -1.374 1.00 20.24 N ANISOU 2001 NH2 ARG B 256 2180 2105 3403 631 976 176 N ATOM 2002 N CYS B 257 -3.779 -24.239 2.025 1.00 14.77 N ANISOU 2002 N CYS B 257 1767 1195 2648 185 603 200 N ATOM 2003 CA CYS B 257 -3.489 -23.211 3.022 1.00 13.36 C ANISOU 2003 CA CYS B 257 1281 1299 2497 -91 512 202 C ATOM 2004 C CYS B 257 -4.263 -23.498 4.352 1.00 13.98 C ANISOU 2004 C CYS B 257 1455 1389 2469 342 374 131 C ATOM 2005 O CYS B 257 -3.621 -23.718 5.372 1.00 15.35 O ANISOU 2005 O CYS B 257 1932 1469 2432 -6 549 248 O ATOM 2006 CB CYS B 257 -3.745 -21.832 2.420 1.00 14.91 C ANISOU 2006 CB CYS B 257 1759 1299 2607 -83 468 56 C ATOM 2007 SG CYS B 257 -3.870 -20.535 3.650 1.00 16.23 S ANISOU 2007 SG CYS B 257 1854 1512 2799 -6 490 189 S ATOM 2008 N PRO B 258 -5.596 -23.573 4.290 1.00 12.68 N ANISOU 2008 N PRO B 258 1030 1507 2280 194 197 -24 N ATOM 2009 CA PRO B 258 -6.284 -23.814 5.582 1.00 13.42 C ANISOU 2009 CA PRO B 258 1117 1479 2503 417 551 130 C ATOM 2010 C PRO B 258 -6.210 -25.272 6.037 1.00 12.76 C ANISOU 2010 C PRO B 258 1311 1171 2366 384 696 207 C ATOM 2011 O PRO B 258 -6.588 -25.564 7.198 1.00 14.11 O ANISOU 2011 O PRO B 258 1631 1430 2302 -54 669 163 O ATOM 2012 CB PRO B 258 -7.745 -23.395 5.323 1.00 13.96 C ANISOU 2012 CB PRO B 258 1087 1921 2295 139 283 141 C ATOM 2013 CG PRO B 258 -7.911 -23.457 3.818 1.00 15.11 C ANISOU 2013 CG PRO B 258 1181 2101 2459 -374 300 158 C ATOM 2014 CD PRO B 258 -6.540 -23.159 3.222 1.00 12.79 C ANISOU 2014 CD PRO B 258 547 1816 2496 -443 -7 135 C ATOM 2015 N GLU B 259 -5.789 -26.210 5.158 1.00 13.20 N ANISOU 2015 N GLU B 259 1412 1188 2415 501 470 -8 N ATOM 2016 CA GLU B 259 -5.617 -27.597 5.617 1.00 12.33 C ANISOU 2016 CA GLU B 259 1217 970 2499 556 497 86 C ATOM 2017 C GLU B 259 -4.651 -27.576 6.807 1.00 14.05 C ANISOU 2017 C GLU B 259 1491 1276 2572 298 288 277 C ATOM 2018 O GLU B 259 -4.675 -28.484 7.641 1.00 14.53 O ANISOU 2018 O GLU B 259 1701 1432 2387 510 626 401 O ATOM 2019 CB GLU B 259 -5.038 -28.478 4.503 1.00 15.18 C ANISOU 2019 CB GLU B 259 2064 987 2716 634 869 207 C ATOM 2020 CG GLU B 259 -4.814 -29.905 4.910 1.00 16.76 C ANISOU 2020 CG GLU B 259 2291 1161 2915 335 1113 325 C ATOM 2021 CD GLU B 259 -6.105 -30.645 5.178 1.00 18.51 C ANISOU 2021 CD GLU B 259 2376 1908 2751 289 1002 333 C ATOM 2022 OE1 GLU B 259 -7.159 -30.155 4.778 1.00 17.99 O ANISOU 2022 OE1 GLU B 259 2570 1575 2689 93 783 12 O ATOM 2023 OE2 GLU B 259 -6.039 -31.766 5.765 1.00 17.73 O ANISOU 2023 OE2 GLU B 259 2204 1721 2812 81 881 422 O ATOM 2024 N THR B 260 -3.759 -26.605 6.859 1.00 15.24 N ANISOU 2024 N THR B 260 1691 1452 2647 233 158 113 N ATOM 2025 CA THR B 260 -2.790 -26.451 7.928 1.00 14.04 C ANISOU 2025 CA THR B 260 1308 1524 2501 186 468 112 C ATOM 2026 C THR B 260 -3.483 -26.479 9.311 1.00 14.39 C ANISOU 2026 C THR B 260 1552 1565 2350 89 441 308 C ATOM 2027 O THR B 260 -2.871 -26.926 10.329 1.00 14.26 O ANISOU 2027 O THR B 260 1534 1512 2372 355 547 279 O ATOM 2028 CB THR B 260 -2.038 -25.127 7.768 1.00 14.80 C ANISOU 2028 CB THR B 260 1191 1801 2631 -65 330 288 C ATOM 2029 OG1 THR B 260 -1.426 -25.150 6.460 1.00 17.66 O ANISOU 2029 OG1 THR B 260 1861 2177 2672 170 801 226 O ATOM 2030 CG2 THR B 260 -0.939 -24.923 8.818 1.00 15.18 C ANISOU 2030 CG2 THR B 260 1343 1689 2736 -5 446 150 C ATOM 2031 N LEU B 261 -4.709 -25.962 9.370 1.00 14.18 N ANISOU 2031 N LEU B 261 1641 1402 2343 61 518 332 N ATOM 2032 CA LEU B 261 -5.446 -25.991 10.675 1.00 13.16 C ANISOU 2032 CA LEU B 261 923 1548 2530 406 492 632 C ATOM 2033 C LEU B 261 -5.645 -27.429 11.147 1.00 14.67 C ANISOU 2033 C LEU B 261 1433 1611 2532 495 587 412 C ATOM 2034 O LEU B 261 -5.616 -27.692 12.388 1.00 14.10 O ANISOU 2034 O LEU B 261 1449 1438 2470 371 707 355 O ATOM 2035 CB LEU B 261 -6.805 -25.346 10.567 1.00 11.98 C ANISOU 2035 CB LEU B 261 691 1259 2600 183 349 399 C ATOM 2036 CG LEU B 261 -6.785 -23.840 10.307 1.00 13.09 C ANISOU 2036 CG LEU B 261 1333 904 2735 -200 8 138 C ATOM 2037 CD1 LEU B 261 -8.170 -23.427 9.824 1.00 14.44 C ANISOU 2037 CD1 LEU B 261 1532 1102 2852 396 -366 217 C ATOM 2038 CD2 LEU B 261 -6.337 -23.096 11.564 1.00 15.26 C ANISOU 2038 CD2 LEU B 261 1727 1208 2864 -156 -60 -16 C ATOM 2039 N PHE B 262 -5.837 -28.336 10.189 1.00 13.49 N ANISOU 2039 N PHE B 262 1366 1268 2493 -76 449 407 N ATOM 2040 CA PHE B 262 -6.037 -29.784 10.492 1.00 14.11 C ANISOU 2040 CA PHE B 262 1607 1138 2616 85 362 392 C ATOM 2041 C PHE B 262 -4.730 -30.552 10.520 1.00 16.27 C ANISOU 2041 C PHE B 262 1897 1608 2677 435 544 291 C ATOM 2042 O PHE B 262 -4.650 -31.624 11.151 1.00 17.23 O ANISOU 2042 O PHE B 262 2155 1588 2804 656 709 513 O ATOM 2043 CB PHE B 262 -7.020 -30.377 9.487 1.00 13.48 C ANISOU 2043 CB PHE B 262 1261 1329 2531 -194 582 107 C ATOM 2044 CG PHE B 262 -8.362 -29.753 9.570 1.00 14.45 C ANISOU 2044 CG PHE B 262 1273 1593 2624 320 473 15 C ATOM 2045 CD1 PHE B 262 -8.667 -28.622 8.803 1.00 16.25 C ANISOU 2045 CD1 PHE B 262 1948 1600 2625 333 97 161 C ATOM 2046 CD2 PHE B 262 -9.307 -30.248 10.465 1.00 15.24 C ANISOU 2046 CD2 PHE B 262 1527 1625 2639 183 508 0 C ATOM 2047 CE1 PHE B 262 -9.933 -28.003 8.903 1.00 14.84 C ANISOU 2047 CE1 PHE B 262 1437 1479 2722 -17 -213 83 C ATOM 2048 CE2 PHE B 262 -10.562 -29.638 10.597 1.00 15.90 C ANISOU 2048 CE2 PHE B 262 1789 1565 2688 48 212 -162 C ATOM 2049 CZ PHE B 262 -10.866 -28.484 9.822 1.00 15.32 C ANISOU 2049 CZ PHE B 262 1616 1545 2660 85 -69 -7 C ATOM 2050 N GLN B 263 -3.710 -29.999 9.829 1.00 15.41 N ANISOU 2050 N GLN B 263 1501 1596 2758 419 446 235 N ATOM 2051 CA GLN B 263 -2.377 -30.621 9.730 1.00 16.80 C ANISOU 2051 CA GLN B 263 1635 1864 2883 409 495 -9 C ATOM 2052 C GLN B 263 -1.293 -29.592 9.994 1.00 17.73 C ANISOU 2052 C GLN B 263 1774 2022 2940 671 873 111 C ATOM 2053 O GLN B 263 -0.650 -29.084 9.057 1.00 17.71 O ANISOU 2053 O GLN B 263 1469 2203 3056 530 856 403 O ATOM 2054 CB GLN B 263 -2.147 -31.254 8.362 1.00 17.31 C ANISOU 2054 CB GLN B 263 1875 1677 3026 606 305 -126 C ATOM 2055 CG GLN B 263 -3.206 -32.245 7.992 1.00 17.60 C ANISOU 2055 CG GLN B 263 1677 1939 3070 43 682 -118 C ATOM 2056 CD GLN B 263 -2.771 -33.154 6.859 1.00 20.03 C ANISOU 2056 CD GLN B 263 2401 1927 3284 902 621 -65 C ATOM 2057 OE1 GLN B 263 -1.676 -33.785 6.876 1.00 23.18 O ANISOU 2057 OE1 GLN B 263 2746 2589 3474 1323 340 67 O ATOM 2058 NE2 GLN B 263 -3.605 -33.214 5.854 1.00 22.39 N ANISOU 2058 NE2 GLN B 263 3174 1943 3391 254 610 11 N ATOM 2059 N PRO B 264 -1.082 -29.243 11.263 1.00 17.22 N ANISOU 2059 N PRO B 264 1776 1804 2963 737 777 404 N ATOM 2060 CA PRO B 264 -0.112 -28.185 11.555 1.00 18.21 C ANISOU 2060 CA PRO B 264 1730 2109 3080 446 578 443 C ATOM 2061 C PRO B 264 1.322 -28.503 11.128 1.00 18.33 C ANISOU 2061 C PRO B 264 1578 1955 3430 540 588 706 C ATOM 2062 O PRO B 264 2.156 -27.586 11.109 1.00 20.00 O ANISOU 2062 O PRO B 264 1661 2428 3510 380 715 871 O ATOM 2063 CB PRO B 264 -0.208 -28.018 13.073 1.00 17.31 C ANISOU 2063 CB PRO B 264 1118 2496 2962 175 986 692 C ATOM 2064 CG PRO B 264 -1.663 -28.415 13.338 1.00 17.80 C ANISOU 2064 CG PRO B 264 1685 2087 2991 370 753 529 C ATOM 2065 CD PRO B 264 -1.897 -29.589 12.450 1.00 16.78 C ANISOU 2065 CD PRO B 264 1434 1979 2964 401 803 613 C ATOM 2066 N SER B 265 1.584 -29.774 10.837 1.00 19.56 N ANISOU 2066 N SER B 265 1941 2050 3439 962 876 692 N ATOM 2067 CA SER B 265 2.896 -30.173 10.314 1.00 21.27 C ANISOU 2067 CA SER B 265 1972 2411 3699 1067 965 776 C ATOM 2068 C SER B 265 3.185 -29.445 9.021 1.00 21.84 C ANISOU 2068 C SER B 265 1621 2886 3793 907 1261 816 C ATOM 2069 O SER B 265 4.353 -29.284 8.644 1.00 24.88 O ANISOU 2069 O SER B 265 1706 3648 4099 919 1351 1077 O ATOM 2070 CB SER B 265 2.946 -31.681 10.108 1.00 21.99 C ANISOU 2070 CB SER B 265 1907 2537 3911 1102 645 191 C ATOM 2071 OG SER B 265 1.999 -32.106 9.156 1.00 24.63 O ANISOU 2071 OG SER B 265 2324 3015 4021 518 498 8 O ATOM 2072 N PHE B 266 2.144 -28.989 8.324 1.00 20.03 N ANISOU 2072 N PHE B 266 1653 2412 3544 792 886 744 N ATOM 2073 CA PHE B 266 2.387 -28.206 7.076 1.00 21.14 C ANISOU 2073 CA PHE B 266 1886 2547 3600 716 912 689 C ATOM 2074 C PHE B 266 3.294 -27.014 7.300 1.00 21.69 C ANISOU 2074 C PHE B 266 1860 2767 3614 635 979 802 C ATOM 2075 O PHE B 266 3.997 -26.615 6.364 1.00 22.14 O ANISOU 2075 O PHE B 266 1747 2927 3740 868 1181 512 O ATOM 2076 CB PHE B 266 1.095 -27.719 6.432 1.00 21.07 C ANISOU 2076 CB PHE B 266 1901 2497 3609 398 692 547 C ATOM 2077 CG PHE B 266 0.337 -28.778 5.709 1.00 20.21 C ANISOU 2077 CG PHE B 266 1594 2492 3592 92 978 511 C ATOM 2078 CD1 PHE B 266 -0.763 -28.440 4.906 1.00 20.61 C ANISOU 2078 CD1 PHE B 266 1615 2607 3611 69 962 536 C ATOM 2079 CD2 PHE B 266 0.652 -30.128 5.871 1.00 20.79 C ANISOU 2079 CD2 PHE B 266 1719 2662 3519 551 1377 371 C ATOM 2080 CE1 PHE B 266 -1.504 -29.413 4.237 1.00 20.30 C ANISOU 2080 CE1 PHE B 266 1768 2372 3573 410 957 400 C ATOM 2081 CE2 PHE B 266 -0.080 -31.093 5.227 1.00 23.00 C ANISOU 2081 CE2 PHE B 266 2256 2929 3552 461 1200 418 C ATOM 2082 CZ PHE B 266 -1.142 -30.772 4.402 1.00 20.39 C ANISOU 2082 CZ PHE B 266 1913 2255 3579 775 1199 311 C ATOM 2083 N ILE B 267 3.230 -26.388 8.474 1.00 21.81 N ANISOU 2083 N ILE B 267 2114 2597 3577 575 913 601 N ATOM 2084 CA ILE B 267 4.130 -25.309 8.806 1.00 23.55 C ANISOU 2084 CA ILE B 267 2406 2913 3628 631 698 671 C ATOM 2085 C ILE B 267 5.165 -25.734 9.864 1.00 25.98 C ANISOU 2085 C ILE B 267 2395 3436 4041 988 341 573 C ATOM 2086 O ILE B 267 5.722 -24.906 10.591 1.00 26.20 O ANISOU 2086 O ILE B 267 2441 3216 4299 763 127 508 O ATOM 2087 CB ILE B 267 3.402 -24.013 9.204 1.00 22.53 C ANISOU 2087 CB ILE B 267 2101 3092 3366 448 898 782 C ATOM 2088 CG1 ILE B 267 2.548 -24.222 10.476 1.00 22.99 C ANISOU 2088 CG1 ILE B 267 2016 3352 3369 862 1337 538 C ATOM 2089 CG2 ILE B 267 2.555 -23.492 8.053 1.00 21.07 C ANISOU 2089 CG2 ILE B 267 1890 2693 3423 46 417 1014 C ATOM 2090 CD1 ILE B 267 2.070 -22.900 11.017 1.00 24.72 C ANISOU 2090 CD1 ILE B 267 2040 3900 3455 424 1408 424 C ATOM 2091 N GLY B 268 5.395 -27.046 9.944 1.00 24.57 N ANISOU 2091 N GLY B 268 1412 3854 4069 1144 604 820 N ATOM 2092 CA GLY B 268 6.437 -27.571 10.816 1.00 27.62 C ANISOU 2092 CA GLY B 268 1925 4317 4252 773 -28 836 C ATOM 2093 C GLY B 268 6.068 -27.519 12.281 1.00 28.20 C ANISOU 2093 C GLY B 268 1791 4462 4461 1089 -215 725 C ATOM 2094 O GLY B 268 6.941 -27.594 13.152 1.00 31.69 O ANISOU 2094 O GLY B 268 2007 5423 4609 581 -270 512 O ATOM 2095 N MET B 269 4.772 -27.392 12.583 1.00 27.11 N ANISOU 2095 N MET B 269 1350 4351 4600 450 -2 803 N ATOM 2096 CA MET B 269 4.325 -27.436 13.965 1.00 28.18 C ANISOU 2096 CA MET B 269 1571 4447 4687 415 -199 1014 C ATOM 2097 C MET B 269 3.974 -28.861 14.354 1.00 30.49 C ANISOU 2097 C MET B 269 2320 4727 4538 948 -43 1516 C ATOM 2098 O MET B 269 3.350 -29.580 13.575 1.00 29.29 O ANISOU 2098 O MET B 269 2417 4384 4329 581 514 1689 O ATOM 2099 CB MET B 269 3.097 -26.562 14.147 1.00 29.79 C ANISOU 2099 CB MET B 269 1596 4662 5061 513 4 895 C ATOM 2100 CG MET B 269 3.408 -25.119 14.256 1.00 32.76 C ANISOU 2100 CG MET B 269 2133 4981 5332 960 424 956 C ATOM 2101 SD MET B 269 1.874 -24.206 14.515 1.00 36.95 S ANISOU 2101 SD MET B 269 3149 5294 5596 1684 388 1028 S ATOM 2102 CE MET B 269 1.359 -24.924 16.066 1.00 38.38 C ANISOU 2102 CE MET B 269 3996 5043 5542 1330 545 1342 C ATOM 2103 N GLU B 270 4.367 -29.218 15.552 1.00 32.75 N ANISOU 2103 N GLU B 270 2556 5139 4751 1292 -45 1507 N ATOM 2104 CA GLU B 270 4.096 -30.524 16.040 1.00 33.40 C ANISOU 2104 CA GLU B 270 2496 5316 4877 1376 -343 1574 C ATOM 2105 C GLU B 270 2.661 -30.755 16.612 1.00 34.84 C ANISOU 2105 C GLU B 270 3327 5036 4874 1360 134 1432 C ATOM 2106 O GLU B 270 2.214 -31.790 16.827 1.00 39.03 O ANISOU 2106 O GLU B 270 3860 5925 5044 1198 335 1271 O ATOM 2107 CB GLU B 270 5.219 -30.933 17.046 1.00 38.11 C ANISOU 2107 CB GLU B 270 3375 5965 5140 1696 -499 1388 C ATOM 2108 CG GLU B 270 6.233 -31.943 16.481 0.50 40.23 C ANISOU 2108 CG GLU B 270 3439 6561 5286 1814 -531 1138 C ATOM 2109 CD GLU B 270 7.737 -31.735 16.950 0.50 42.39 C ANISOU 2109 CD GLU B 270 3703 6993 5410 1625 -463 1033 C ATOM 2110 OE1 GLU B 270 7.999 -31.364 18.077 0.50 42.91 O ANISOU 2110 OE1 GLU B 270 3770 7125 5409 1442 -579 1076 O ATOM 2111 OE2 GLU B 270 8.662 -31.893 16.121 0.50 42.80 O ANISOU 2111 OE2 GLU B 270 3617 7116 5531 1668 -470 1047 O ATOM 2112 N SER B 271 1.948 -29.741 16.723 1.00 30.88 N ANISOU 2112 N SER B 271 2774 4405 4553 1198 -239 1361 N ATOM 2113 CA SER B 271 0.626 -29.811 17.329 1.00 27.63 C ANISOU 2113 CA SER B 271 2642 3584 4273 869 -203 1002 C ATOM 2114 C SER B 271 -0.388 -30.724 16.613 1.00 24.17 C ANISOU 2114 C SER B 271 2207 3174 3802 851 148 911 C ATOM 2115 O SER B 271 -0.352 -30.870 15.392 1.00 23.10 O ANISOU 2115 O SER B 271 2077 3079 3620 707 258 951 O ATOM 2116 CB SER B 271 0.041 -28.402 17.392 1.00 29.49 C ANISOU 2116 CB SER B 271 3738 2967 4499 886 -277 628 C ATOM 2117 OG SER B 271 -1.297 -28.439 17.864 1.00 31.76 O ANISOU 2117 OG SER B 271 4436 3088 4544 753 -453 264 O ATOM 2118 N ALA B 272 -1.323 -31.306 17.374 1.00 22.59 N ANISOU 2118 N ALA B 272 2018 2971 3595 752 0 1096 N ATOM 2119 CA ALA B 272 -2.511 -31.867 16.783 1.00 21.43 C ANISOU 2119 CA ALA B 272 1939 2789 3416 195 129 1578 C ATOM 2120 C ALA B 272 -3.323 -30.774 16.041 1.00 20.16 C ANISOU 2120 C ALA B 272 2129 2311 3218 422 439 1111 C ATOM 2121 O ALA B 272 -3.249 -29.593 16.395 1.00 20.27 O ANISOU 2121 O ALA B 272 2331 2215 3156 440 606 748 O ATOM 2122 CB ALA B 272 -3.388 -32.504 17.850 1.00 24.91 C ANISOU 2122 CB ALA B 272 2401 3457 3607 -115 62 1904 C ATOM 2123 N GLY B 273 -4.089 -31.206 15.049 1.00 17.17 N ANISOU 2123 N GLY B 273 1529 2192 2805 708 509 1025 N ATOM 2124 CA GLY B 273 -4.948 -30.282 14.288 1.00 16.77 C ANISOU 2124 CA GLY B 273 1348 2307 2716 551 696 910 C ATOM 2125 C GLY B 273 -6.197 -29.916 15.095 1.00 15.54 C ANISOU 2125 C GLY B 273 1315 1875 2715 174 404 655 C ATOM 2126 O GLY B 273 -6.470 -30.508 16.154 1.00 15.28 O ANISOU 2126 O GLY B 273 1663 1493 2651 199 504 576 O ATOM 2127 N ILE B 274 -6.974 -28.978 14.581 1.00 14.49 N ANISOU 2127 N ILE B 274 1197 1681 2629 551 562 462 N ATOM 2128 CA ILE B 274 -8.054 -28.410 15.365 1.00 13.82 C ANISOU 2128 CA ILE B 274 1193 1350 2707 143 582 668 C ATOM 2129 C ILE B 274 -9.168 -29.387 15.631 1.00 13.65 C ANISOU 2129 C ILE B 274 1440 1009 2737 212 445 358 C ATOM 2130 O ILE B 274 -9.915 -29.184 16.614 1.00 13.56 O ANISOU 2130 O ILE B 274 1298 1282 2573 184 673 456 O ATOM 2131 CB ILE B 274 -8.639 -27.109 14.705 1.00 14.64 C ANISOU 2131 CB ILE B 274 1716 1176 2670 60 507 366 C ATOM 2132 CG1 ILE B 274 -9.052 -27.348 13.250 1.00 14.68 C ANISOU 2132 CG1 ILE B 274 1792 1281 2506 614 321 392 C ATOM 2133 CG2 ILE B 274 -7.683 -25.898 14.859 1.00 16.10 C ANISOU 2133 CG2 ILE B 274 1705 1657 2754 -611 731 103 C ATOM 2134 CD1 ILE B 274 -9.871 -26.184 12.725 1.00 14.71 C ANISOU 2134 CD1 ILE B 274 1420 1354 2815 679 602 297 C ATOM 2135 N HIS B 275 -9.328 -30.422 14.799 1.00 15.30 N ANISOU 2135 N HIS B 275 2173 832 2811 90 606 404 N ATOM 2136 CA HIS B 275 -10.347 -31.447 15.100 1.00 14.79 C ANISOU 2136 CA HIS B 275 2050 848 2722 25 605 200 C ATOM 2137 C HIS B 275 -9.894 -32.271 16.309 1.00 15.20 C ANISOU 2137 C HIS B 275 1858 1139 2779 -2 764 328 C ATOM 2138 O HIS B 275 -10.701 -32.654 17.177 1.00 14.93 O ANISOU 2138 O HIS B 275 1759 1138 2775 45 721 275 O ATOM 2139 CB HIS B 275 -10.536 -32.387 13.913 1.00 15.96 C ANISOU 2139 CB HIS B 275 1938 1226 2899 255 746 -339 C ATOM 2140 CG HIS B 275 -9.268 -33.019 13.442 1.00 15.28 C ANISOU 2140 CG HIS B 275 1533 1224 3050 -119 775 -178 C ATOM 2141 ND1 HIS B 275 -8.160 -32.284 13.075 1.00 15.43 N ANISOU 2141 ND1 HIS B 275 1751 1188 2925 67 469 181 N ATOM 2142 CD2 HIS B 275 -8.962 -34.319 13.188 1.00 18.07 C ANISOU 2142 CD2 HIS B 275 2167 1410 3291 -156 742 2 C ATOM 2143 CE1 HIS B 275 -7.204 -33.108 12.664 1.00 16.63 C ANISOU 2143 CE1 HIS B 275 1885 1386 3048 465 513 147 C ATOM 2144 NE2 HIS B 275 -7.662 -34.347 12.734 1.00 17.97 N ANISOU 2144 NE2 HIS B 275 1793 1694 3341 -256 473 277 N ATOM 2145 N GLU B 276 -8.610 -32.590 16.314 1.00 15.58 N ANISOU 2145 N GLU B 276 1835 1105 2979 575 328 466 N ATOM 2146 CA AGLU B 276 -8.045 -33.393 17.408 0.40 16.22 C ANISOU 2146 CA AGLU B 276 2066 996 3101 737 566 386 C ATOM 2147 CA BGLU B 276 -7.945 -33.393 17.408 0.60 17.61 C ANISOU 2147 CA BGLU B 276 2419 1096 3175 1040 645 496 C ATOM 2148 C GLU B 276 -7.999 -32.609 18.716 1.00 16.89 C ANISOU 2148 C GLU B 276 2102 1298 3016 771 701 285 C ATOM 2149 O GLU B 276 -8.229 -33.159 19.811 1.00 16.33 O ANISOU 2149 O GLU B 276 1744 1455 3004 290 907 458 O ATOM 2150 CB AGLU B 276 -6.635 -33.894 17.071 0.40 17.52 C ANISOU 2150 CB AGLU B 276 2118 1188 3351 1160 524 523 C ATOM 2151 CB BGLU B 276 -6.535 -33.894 17.071 0.60 22.12 C ANISOU 2151 CB BGLU B 276 3092 1733 3580 1834 567 892 C ATOM 2152 CG AGLU B 276 -6.645 -34.919 16.000 0.40 19.74 C ANISOU 2152 CG AGLU B 276 2556 1403 3540 1310 667 377 C ATOM 2153 CG BGLU B 276 -5.965 -34.733 18.152 0.60 28.77 C ANISOU 2153 CG BGLU B 276 4484 2523 3925 2057 762 912 C ATOM 2154 CD AGLU B 276 -5.309 -35.678 15.916 0.40 24.91 C ANISOU 2154 CD AGLU B 276 3227 2406 3831 1022 512 534 C ATOM 2155 CD BGLU B 276 -5.178 -35.933 17.596 0.60 34.10 C ANISOU 2155 CD BGLU B 276 5196 3588 4172 2110 976 584 C ATOM 2156 OE1AGLU B 276 -4.505 -35.604 16.870 0.40 28.99 O ANISOU 2156 OE1AGLU B 276 3874 3057 4086 783 405 551 O ATOM 2157 OE1BGLU B 276 -4.826 -35.928 16.397 0.60 37.14 O ANISOU 2157 OE1BGLU B 276 5690 3945 4477 1973 829 406 O ATOM 2158 OE2AGLU B 276 -5.063 -36.316 14.879 0.40 24.94 O ANISOU 2158 OE2AGLU B 276 3116 2428 3932 1180 893 614 O ATOM 2159 OE2BGLU B 276 -4.948 -36.886 18.359 0.60 35.99 O ANISOU 2159 OE2BGLU B 276 5333 4026 4317 2521 927 504 O ATOM 2160 N THR B 277 -7.697 -31.314 18.628 1.00 14.89 N ANISOU 2160 N THR B 277 1511 1317 2830 168 316 155 N ATOM 2161 CA THR B 277 -7.662 -30.523 19.839 1.00 14.31 C ANISOU 2161 CA THR B 277 894 1776 2767 -368 451 359 C ATOM 2162 C THR B 277 -9.076 -30.365 20.400 1.00 12.65 C ANISOU 2162 C THR B 277 721 1342 2743 -96 429 631 C ATOM 2163 O THR B 277 -9.237 -30.295 21.632 1.00 15.08 O ANISOU 2163 O THR B 277 1457 1563 2710 110 764 631 O ATOM 2164 CB THR B 277 -6.936 -29.157 19.663 1.00 15.99 C ANISOU 2164 CB THR B 277 1217 2160 2700 -25 793 298 C ATOM 2165 OG1 THR B 277 -7.620 -28.387 18.671 1.00 15.52 O ANISOU 2165 OG1 THR B 277 1501 1738 2660 -71 543 476 O ATOM 2166 CG2 THR B 277 -5.471 -29.388 19.182 1.00 19.14 C ANISOU 2166 CG2 THR B 277 1640 2696 2935 -464 665 170 C ATOM 2167 N THR B 278 -10.070 -30.259 19.513 1.00 12.53 N ANISOU 2167 N THR B 278 915 1096 2751 166 148 406 N ATOM 2168 CA THR B 278 -11.478 -30.164 19.969 1.00 13.00 C ANISOU 2168 CA THR B 278 1072 1155 2713 -27 332 488 C ATOM 2169 C THR B 278 -11.794 -31.450 20.756 1.00 12.82 C ANISOU 2169 C THR B 278 1446 694 2729 10 436 78 C ATOM 2170 O THR B 278 -12.312 -31.398 21.876 1.00 13.92 O ANISOU 2170 O THR B 278 1318 1460 2513 195 452 325 O ATOM 2171 CB THR B 278 -12.440 -30.062 18.769 1.00 12.85 C ANISOU 2171 CB THR B 278 869 1262 2752 88 387 154 C ATOM 2172 OG1 THR B 278 -12.204 -28.827 18.075 1.00 14.77 O ANISOU 2172 OG1 THR B 278 1546 1220 2846 -37 292 445 O ATOM 2173 CG2 THR B 278 -13.929 -30.053 19.235 1.00 15.08 C ANISOU 2173 CG2 THR B 278 1409 1419 2903 148 849 237 C ATOM 2174 N TYR B 279 -11.459 -32.584 20.156 1.00 14.95 N ANISOU 2174 N TYR B 279 1994 741 2943 139 691 -2 N ATOM 2175 CA TYR B 279 -11.725 -33.881 20.815 1.00 15.61 C ANISOU 2175 CA TYR B 279 2008 958 2965 526 671 -32 C ATOM 2176 C TYR B 279 -10.948 -33.969 22.128 1.00 15.18 C ANISOU 2176 C TYR B 279 1605 1171 2992 440 806 247 C ATOM 2177 O TYR B 279 -11.508 -34.369 23.190 1.00 15.75 O ANISOU 2177 O TYR B 279 1990 1149 2844 277 669 458 O ATOM 2178 CB TYR B 279 -11.343 -35.004 19.842 1.00 15.38 C ANISOU 2178 CB TYR B 279 2133 660 3050 206 856 17 C ATOM 2179 CG TYR B 279 -11.460 -36.391 20.468 1.00 16.38 C ANISOU 2179 CG TYR B 279 2270 792 3162 -57 1269 258 C ATOM 2180 CD1 TYR B 279 -12.713 -36.971 20.679 1.00 16.62 C ANISOU 2180 CD1 TYR B 279 1952 1005 3359 -101 1322 242 C ATOM 2181 CD2 TYR B 279 -10.338 -37.088 20.821 1.00 18.48 C ANISOU 2181 CD2 TYR B 279 2734 925 3362 510 1209 282 C ATOM 2182 CE1 TYR B 279 -12.839 -38.235 21.280 1.00 19.52 C ANISOU 2182 CE1 TYR B 279 2372 1312 3733 56 1373 150 C ATOM 2183 CE2 TYR B 279 -10.437 -38.366 21.434 1.00 18.65 C ANISOU 2183 CE2 TYR B 279 2605 935 3545 526 1254 512 C ATOM 2184 CZ TYR B 279 -11.694 -38.917 21.643 1.00 18.90 C ANISOU 2184 CZ TYR B 279 2438 882 3862 -159 1240 255 C ATOM 2185 OH TYR B 279 -11.791 -40.193 22.221 1.00 21.24 O ANISOU 2185 OH TYR B 279 2843 1060 4165 -39 1430 253 O ATOM 2186 N ASN B 280 -9.659 -33.616 22.093 1.00 14.74 N ANISOU 2186 N ASN B 280 1094 1392 3114 526 691 270 N ATOM 2187 CA ASN B 280 -8.880 -33.714 23.317 1.00 16.15 C ANISOU 2187 CA ASN B 280 1558 1469 3111 673 752 360 C ATOM 2188 C ASN B 280 -9.475 -32.826 24.427 1.00 15.39 C ANISOU 2188 C ASN B 280 1442 1545 2860 770 782 443 C ATOM 2189 O ASN B 280 -9.416 -33.150 25.628 1.00 16.97 O ANISOU 2189 O ASN B 280 2128 1549 2770 532 722 575 O ATOM 2190 CB ASN B 280 -7.397 -33.329 23.097 1.00 18.20 C ANISOU 2190 CB ASN B 280 1468 2113 3334 603 802 830 C ATOM 2191 CG ASN B 280 -6.647 -34.320 22.177 1.00 20.57 C ANISOU 2191 CG ASN B 280 1955 2414 3444 849 966 884 C ATOM 2192 OD1 ASN B 280 -5.622 -33.958 21.572 1.00 25.81 O ANISOU 2192 OD1 ASN B 280 2292 3713 3802 907 948 622 O ATOM 2193 ND2 ASN B 280 -7.186 -35.501 22.007 1.00 18.80 N ANISOU 2193 ND2 ASN B 280 1735 2070 3339 1050 1161 902 N ATOM 2194 N SER B 281 -9.957 -31.642 24.028 1.00 14.15 N ANISOU 2194 N SER B 281 1217 1231 2929 757 487 404 N ATOM 2195 CA SER B 281 -10.522 -30.727 25.005 1.00 14.09 C ANISOU 2195 CA SER B 281 1425 1140 2787 453 827 551 C ATOM 2196 C SER B 281 -11.784 -31.350 25.660 1.00 14.67 C ANISOU 2196 C SER B 281 1342 1361 2871 431 392 438 C ATOM 2197 O SER B 281 -11.907 -31.307 26.896 1.00 14.65 O ANISOU 2197 O SER B 281 1592 1335 2638 82 685 460 O ATOM 2198 CB SER B 281 -10.881 -29.421 24.296 1.00 14.21 C ANISOU 2198 CB SER B 281 1930 733 2737 537 589 340 C ATOM 2199 OG SER B 281 -11.516 -28.481 25.172 1.00 16.51 O ANISOU 2199 OG SER B 281 1850 1409 3012 325 528 258 O ATOM 2200 N ILE B 282 -12.687 -31.879 24.823 1.00 13.31 N ANISOU 2200 N ILE B 282 820 1244 2993 116 691 298 N ATOM 2201 CA ILE B 282 -13.885 -32.561 25.308 1.00 14.14 C ANISOU 2201 CA ILE B 282 1051 1212 3111 -174 373 298 C ATOM 2202 C ILE B 282 -13.461 -33.709 26.261 1.00 14.55 C ANISOU 2202 C ILE B 282 1388 1041 3101 296 751 480 C ATOM 2203 O ILE B 282 -14.072 -33.863 27.315 1.00 16.81 O ANISOU 2203 O ILE B 282 1915 1354 3118 17 708 312 O ATOM 2204 CB ILE B 282 -14.672 -33.099 24.149 1.00 13.43 C ANISOU 2204 CB ILE B 282 1170 1022 2910 321 711 531 C ATOM 2205 CG1 ILE B 282 -15.277 -31.913 23.360 1.00 14.69 C ANISOU 2205 CG1 ILE B 282 1247 1401 2933 271 422 377 C ATOM 2206 CG2 ILE B 282 -15.817 -34.065 24.638 1.00 16.40 C ANISOU 2206 CG2 ILE B 282 1519 1721 2990 -204 889 288 C ATOM 2207 CD1 ILE B 282 -16.017 -32.339 22.170 1.00 17.99 C ANISOU 2207 CD1 ILE B 282 2113 1846 2878 285 390 210 C ATOM 2208 N MET B 283 -12.378 -34.430 25.908 1.00 14.89 N ANISOU 2208 N MET B 283 1490 1056 3114 364 716 478 N ATOM 2209 CA MET B 283 -11.951 -35.585 26.768 1.00 16.82 C ANISOU 2209 CA MET B 283 1953 1286 3151 508 877 397 C ATOM 2210 C MET B 283 -11.299 -35.154 28.077 1.00 18.79 C ANISOU 2210 C MET B 283 2637 1300 3203 920 619 395 C ATOM 2211 O MET B 283 -11.102 -35.977 28.988 1.00 22.03 O ANISOU 2211 O MET B 283 3360 1671 3339 771 499 859 O ATOM 2212 CB MET B 283 -11.036 -36.526 25.978 1.00 18.45 C ANISOU 2212 CB MET B 283 2272 1426 3311 418 846 406 C ATOM 2213 CG MET B 283 -11.814 -37.162 24.845 1.00 19.77 C ANISOU 2213 CG MET B 283 2484 1476 3553 228 1263 508 C ATOM 2214 SD MET B 283 -13.207 -38.225 25.388 1.00 21.34 S ANISOU 2214 SD MET B 283 2953 1446 3711 155 1171 484 S ATOM 2215 CE MET B 283 -12.284 -39.677 25.993 1.00 21.45 C ANISOU 2215 CE MET B 283 2735 1520 3896 51 996 712 C ATOM 2216 N LYS B 284 -10.910 -33.898 28.210 1.00 17.08 N ANISOU 2216 N LYS B 284 1843 1280 3368 404 507 342 N ATOM 2217 CA LYS B 284 -10.435 -33.390 29.480 1.00 18.04 C ANISOU 2217 CA LYS B 284 1709 1669 3478 156 509 467 C ATOM 2218 C LYS B 284 -11.577 -32.955 30.409 1.00 15.16 C ANISOU 2218 C LYS B 284 938 1415 3406 49 471 592 C ATOM 2219 O LYS B 284 -11.320 -32.580 31.564 1.00 20.96 O ANISOU 2219 O LYS B 284 1788 2584 3593 141 198 252 O ATOM 2220 CB LYS B 284 -9.449 -32.233 29.264 1.00 18.86 C ANISOU 2220 CB LYS B 284 1322 2230 3614 222 734 508 C ATOM 2221 CG LYS B 284 -8.124 -32.790 28.752 1.00 23.06 C ANISOU 2221 CG LYS B 284 1323 3374 4066 267 670 508 C ATOM 2222 CD LYS B 284 -7.060 -31.704 28.678 1.00 30.61 C ANISOU 2222 CD LYS B 284 2778 4333 4518 -345 1016 175 C ATOM 2223 CE LYS B 284 -5.677 -32.301 28.327 1.00 35.55 C ANISOU 2223 CE LYS B 284 3410 5274 4823 -628 935 238 C ATOM 2224 NZ LYS B 284 -4.743 -31.256 27.782 1.00 40.22 N ANISOU 2224 NZ LYS B 284 4397 5873 5014 -571 606 285 N ATOM 2225 N CYS B 285 -12.804 -32.945 29.876 1.00 14.30 N ANISOU 2225 N CYS B 285 647 1457 3331 167 430 482 N ATOM 2226 CA CYS B 285 -13.983 -32.510 30.651 1.00 13.83 C ANISOU 2226 CA CYS B 285 990 1083 3181 253 308 762 C ATOM 2227 C CYS B 285 -14.633 -33.729 31.248 1.00 15.52 C ANISOU 2227 C CYS B 285 1834 978 3084 385 654 429 C ATOM 2228 O CYS B 285 -14.473 -34.870 30.726 1.00 16.83 O ANISOU 2228 O CYS B 285 2208 1047 3141 273 951 631 O ATOM 2229 CB CYS B 285 -15.008 -31.863 29.735 1.00 15.90 C ANISOU 2229 CB CYS B 285 2030 818 3192 342 404 795 C ATOM 2230 SG CYS B 285 -14.398 -30.273 29.071 1.00 15.45 S ANISOU 2230 SG CYS B 285 1648 1261 2961 51 579 422 S ATOM 2231 N ASP B 286 -15.435 -33.485 32.285 1.00 17.16 N ANISOU 2231 N ASP B 286 1842 1636 3043 184 1158 619 N ATOM 2232 CA ASP B 286 -16.097 -34.613 32.957 1.00 17.92 C ANISOU 2232 CA ASP B 286 1898 1773 3137 -51 863 621 C ATOM 2233 C ASP B 286 -16.933 -35.359 31.966 1.00 15.95 C ANISOU 2233 C ASP B 286 1936 983 3141 386 932 572 C ATOM 2234 O ASP B 286 -17.640 -34.776 31.131 1.00 15.20 O ANISOU 2234 O ASP B 286 1528 1290 2958 206 876 554 O ATOM 2235 CB ASP B 286 -16.970 -34.097 34.065 1.00 20.14 C ANISOU 2235 CB ASP B 286 2474 2004 3176 -272 991 755 C ATOM 2236 CG ASP B 286 -17.610 -35.223 34.855 1.00 22.27 C ANISOU 2236 CG ASP B 286 2474 2659 3329 -278 791 575 C ATOM 2237 OD1 ASP B 286 -16.942 -35.691 35.781 1.00 24.36 O ANISOU 2237 OD1 ASP B 286 2883 2820 3553 35 898 493 O ATOM 2238 OD2 ASP B 286 -18.712 -35.660 34.479 1.00 22.28 O ANISOU 2238 OD2 ASP B 286 2004 3188 3274 -406 656 720 O ATOM 2239 N ILE B 287 -16.890 -36.689 32.055 1.00 18.63 N ANISOU 2239 N ILE B 287 2392 1172 3512 40 1218 301 N ATOM 2240 CA ILE B 287 -17.600 -37.470 31.083 1.00 20.31 C ANISOU 2240 CA ILE B 287 2851 1172 3695 -202 1499 136 C ATOM 2241 C ILE B 287 -19.086 -37.152 30.936 1.00 19.56 C ANISOU 2241 C ILE B 287 2686 1359 3385 -235 1375 -31 C ATOM 2242 O ILE B 287 -19.674 -37.307 29.874 1.00 21.11 O ANISOU 2242 O ILE B 287 3369 1354 3296 -664 1603 -122 O ATOM 2243 CB ILE B 287 -17.422 -38.999 31.382 1.00 23.66 C ANISOU 2243 CB ILE B 287 3512 1186 4292 -91 1979 646 C ATOM 2244 CG1 ILE B 287 -18.061 -39.815 30.277 1.00 25.22 C ANISOU 2244 CG1 ILE B 287 3731 1105 4745 331 2152 118 C ATOM 2245 CG2 ILE B 287 -17.919 -39.335 32.833 1.00 25.81 C ANISOU 2245 CG2 ILE B 287 4053 1424 4331 293 2196 1104 C ATOM 2246 CD1 ILE B 287 -17.645 -41.331 30.305 1.00 27.79 C ANISOU 2246 CD1 ILE B 287 3904 1443 5212 91 1958 -79 C ATOM 2247 N ASP B 288 -19.736 -36.722 32.040 1.00 17.31 N ANISOU 2247 N ASP B 288 2319 1134 3123 -18 1228 238 N ATOM 2248 CA ASP B 288 -21.165 -36.525 32.031 1.00 18.98 C ANISOU 2248 CA ASP B 288 2259 1938 3016 -50 1210 359 C ATOM 2249 C ASP B 288 -21.591 -35.227 31.389 1.00 18.36 C ANISOU 2249 C ASP B 288 2015 1813 3146 -120 874 111 C ATOM 2250 O ASP B 288 -22.804 -35.009 31.228 1.00 20.86 O ANISOU 2250 O ASP B 288 2165 2201 3560 31 765 635 O ATOM 2251 CB ASP B 288 -21.700 -36.589 33.466 1.00 20.89 C ANISOU 2251 CB ASP B 288 1617 3234 3088 -456 994 696 C ATOM 2252 CG ASP B 288 -21.544 -37.971 34.046 1.00 24.63 C ANISOU 2252 CG ASP B 288 2315 3934 3108 -990 624 1287 C ATOM 2253 OD1 ASP B 288 -21.239 -38.078 35.252 1.00 30.20 O ANISOU 2253 OD1 ASP B 288 2624 5673 3175 -1863 211 1544 O ATOM 2254 OD2 ASP B 288 -21.600 -38.935 33.269 1.00 25.29 O ANISOU 2254 OD2 ASP B 288 2947 3094 3566 -1083 260 1321 O ATOM 2255 N ILE B 289 -20.636 -34.382 30.966 1.00 15.44 N ANISOU 2255 N ILE B 289 1445 1422 3000 -47 796 33 N ATOM 2256 CA ILE B 289 -21.010 -33.175 30.234 1.00 16.13 C ANISOU 2256 CA ILE B 289 1651 1486 2993 -41 909 10 C ATOM 2257 C ILE B 289 -20.598 -33.290 28.772 1.00 14.89 C ANISOU 2257 C ILE B 289 1817 1007 2833 -173 950 191 C ATOM 2258 O ILE B 289 -20.874 -32.380 27.975 1.00 16.48 O ANISOU 2258 O ILE B 289 2274 1111 2877 -48 1098 200 O ATOM 2259 CB ILE B 289 -20.448 -31.852 30.856 1.00 16.03 C ANISOU 2259 CB ILE B 289 1563 1319 3209 -231 788 161 C ATOM 2260 CG1 ILE B 289 -18.955 -31.670 30.613 1.00 14.68 C ANISOU 2260 CG1 ILE B 289 1148 984 3445 -297 565 -243 C ATOM 2261 CG2 ILE B 289 -20.796 -31.790 32.370 1.00 20.17 C ANISOU 2261 CG2 ILE B 289 2356 2234 3075 144 1038 256 C ATOM 2262 CD1 ILE B 289 -18.526 -30.196 30.839 1.00 17.11 C ANISOU 2262 CD1 ILE B 289 1853 1018 3631 -96 471 -282 C ATOM 2263 N ARG B 290 -19.939 -34.392 28.398 1.00 15.73 N ANISOU 2263 N ARG B 290 2064 1074 2838 -3 1010 -90 N ATOM 2264 CA ARG B 290 -19.399 -34.441 27.016 1.00 16.37 C ANISOU 2264 CA ARG B 290 2169 1000 3051 -109 792 -17 C ATOM 2265 C ARG B 290 -20.465 -34.404 25.956 1.00 16.65 C ANISOU 2265 C ARG B 290 2125 1177 3024 -267 1038 127 C ATOM 2266 O ARG B 290 -20.264 -33.759 24.910 1.00 15.95 O ANISOU 2266 O ARG B 290 1738 1223 3100 102 1033 136 O ATOM 2267 CB ARG B 290 -18.460 -35.638 26.815 1.00 15.82 C ANISOU 2267 CB ARG B 290 1797 1078 3134 234 634 -93 C ATOM 2268 CG ARG B 290 -17.266 -35.521 27.630 1.00 15.57 C ANISOU 2268 CG ARG B 290 1573 1253 3090 476 976 172 C ATOM 2269 CD ARG B 290 -16.356 -36.755 27.486 1.00 17.87 C ANISOU 2269 CD ARG B 290 2326 1348 3116 562 662 306 C ATOM 2270 NE ARG B 290 -15.278 -36.679 28.468 1.00 18.13 N ANISOU 2270 NE ARG B 290 2208 1557 3123 555 899 353 N ATOM 2271 CZ ARG B 290 -14.665 -37.756 28.970 1.00 19.40 C ANISOU 2271 CZ ARG B 290 2397 1641 3335 27 843 93 C ATOM 2272 NH1 ARG B 290 -13.726 -37.635 29.902 1.00 19.17 N ANISOU 2272 NH1 ARG B 290 1965 1659 3658 141 557 222 N ATOM 2273 NH2 ARG B 290 -15.027 -38.959 28.505 1.00 17.61 N ANISOU 2273 NH2 ARG B 290 1999 1450 3241 35 1052 96 N ATOM 2274 N LYS B 291 -21.593 -35.064 26.199 1.00 17.39 N ANISOU 2274 N LYS B 291 1918 1467 3224 -145 864 -110 N ATOM 2275 CA ALYS B 291 -22.691 -35.056 25.191 0.30 17.22 C ANISOU 2275 CA ALYS B 291 1922 1354 3267 -642 860 -72 C ATOM 2276 CA BLYS B 291 -22.692 -35.070 25.240 0.70 19.40 C ANISOU 2276 CA BLYS B 291 2398 1558 3413 -915 790 166 C ATOM 2277 C LYS B 291 -23.164 -33.656 24.905 1.00 18.60 C ANISOU 2277 C LYS B 291 2000 1719 3349 -465 577 -95 C ATOM 2278 O LYS B 291 -23.484 -33.348 23.757 1.00 19.76 O ANISOU 2278 O LYS B 291 2182 1991 3334 -378 700 -7 O ATOM 2279 CB ALYS B 291 -23.895 -35.838 25.711 0.30 16.85 C ANISOU 2279 CB ALYS B 291 1711 1450 3240 -961 1088 -144 C ATOM 2280 CB BLYS B 291 -23.862 -35.901 25.773 0.70 25.60 C ANISOU 2280 CB BLYS B 291 3116 2951 3660 -1493 818 423 C ATOM 2281 CG ALYS B 291 -23.827 -37.279 25.495 0.30 16.64 C ANISOU 2281 CG ALYS B 291 1953 1072 3298 -1333 1306 -294 C ATOM 2282 CG BLYS B 291 -25.020 -36.040 24.798 0.70 33.08 C ANISOU 2282 CG BLYS B 291 4458 4022 4088 -1885 882 487 C ATOM 2283 CD ALYS B 291 -25.217 -37.828 25.808 0.30 18.73 C ANISOU 2283 CD ALYS B 291 2335 1381 3399 -1402 1209 -211 C ATOM 2284 CD BLYS B 291 -26.130 -36.901 25.379 0.70 38.28 C ANISOU 2284 CD BLYS B 291 5244 4967 4333 -1751 659 372 C ATOM 2285 CE ALYS B 291 -25.467 -39.115 25.099 0.30 20.68 C ANISOU 2285 CE ALYS B 291 2660 1787 3410 -327 1135 -332 C ATOM 2286 CE BLYS B 291 -27.321 -36.976 24.438 0.70 41.10 C ANISOU 2286 CE BLYS B 291 5628 5485 4504 -1766 723 403 C ATOM 2287 NZ ALYS B 291 -26.809 -39.633 25.477 0.30 20.75 N ANISOU 2287 NZ ALYS B 291 2592 1835 3459 -510 1089 -192 N ATOM 2288 NZ BLYS B 291 -28.428 -37.793 25.007 0.70 43.90 N ANISOU 2288 NZ BLYS B 291 6205 5888 4585 -1118 713 440 N ATOM 2289 N ASP B 292 -23.202 -32.801 25.921 1.00 17.47 N ANISOU 2289 N ASP B 292 1633 1607 3396 -109 781 -214 N ATOM 2290 CA ASP B 292 -23.630 -31.424 25.763 1.00 19.59 C ANISOU 2290 CA ASP B 292 1990 1841 3611 258 711 67 C ATOM 2291 C ASP B 292 -22.603 -30.626 24.970 1.00 19.85 C ANISOU 2291 C ASP B 292 1971 2054 3516 277 793 304 C ATOM 2292 O ASP B 292 -22.950 -29.691 24.227 1.00 22.53 O ANISOU 2292 O ASP B 292 1599 3051 3911 461 635 804 O ATOM 2293 CB ASP B 292 -23.846 -30.814 27.130 1.00 21.40 C ANISOU 2293 CB ASP B 292 1918 2323 3890 170 1226 -164 C ATOM 2294 CG ASP B 292 -25.163 -31.274 27.752 1.00 32.92 C ANISOU 2294 CG ASP B 292 4203 3888 4419 359 764 -339 C ATOM 2295 OD1 ASP B 292 -25.225 -31.393 28.991 1.00 39.54 O ANISOU 2295 OD1 ASP B 292 5812 4518 4694 -11 999 -42 O ATOM 2296 OD2 ASP B 292 -26.142 -31.518 26.993 1.00 37.00 O ANISOU 2296 OD2 ASP B 292 4379 4898 4780 518 581 -426 O ATOM 2297 N LEU B 293 -21.330 -30.976 25.142 1.00 15.57 N ANISOU 2297 N LEU B 293 1413 1445 3058 174 819 70 N ATOM 2298 CA LEU B 293 -20.278 -30.325 24.356 1.00 14.62 C ANISOU 2298 CA LEU B 293 1520 1037 2998 192 400 -56 C ATOM 2299 C LEU B 293 -20.342 -30.703 22.868 1.00 14.73 C ANISOU 2299 C LEU B 293 1631 1024 2943 183 254 9 C ATOM 2300 O LEU B 293 -20.322 -29.825 21.980 1.00 15.47 O ANISOU 2300 O LEU B 293 1741 1180 2958 -145 257 358 O ATOM 2301 CB LEU B 293 -18.895 -30.571 24.953 1.00 14.45 C ANISOU 2301 CB LEU B 293 1100 1336 3055 -315 -82 -169 C ATOM 2302 CG LEU B 293 -18.657 -30.145 26.399 1.00 14.38 C ANISOU 2302 CG LEU B 293 1488 967 3008 -108 37 -14 C ATOM 2303 CD1 LEU B 293 -17.267 -30.473 26.878 1.00 16.12 C ANISOU 2303 CD1 LEU B 293 2230 763 3130 105 37 -55 C ATOM 2304 CD2 LEU B 293 -18.956 -28.631 26.580 1.00 15.39 C ANISOU 2304 CD2 LEU B 293 1362 1329 3156 107 39 123 C ATOM 2305 N TYR B 294 -20.405 -32.009 22.577 1.00 14.43 N ANISOU 2305 N TYR B 294 1572 1012 2898 56 345 -253 N ATOM 2306 CA TYR B 294 -20.540 -32.446 21.208 1.00 13.80 C ANISOU 2306 CA TYR B 294 1474 746 3024 -243 324 21 C ATOM 2307 C TYR B 294 -21.705 -31.861 20.462 1.00 16.69 C ANISOU 2307 C TYR B 294 1759 1468 3113 -167 502 25 C ATOM 2308 O TYR B 294 -21.569 -31.606 19.267 1.00 16.52 O ANISOU 2308 O TYR B 294 1630 1714 2933 -218 150 153 O ATOM 2309 CB TYR B 294 -20.671 -33.962 21.169 1.00 15.78 C ANISOU 2309 CB TYR B 294 1971 847 3180 226 741 269 C ATOM 2310 CG TYR B 294 -19.367 -34.702 21.335 1.00 14.76 C ANISOU 2310 CG TYR B 294 1616 755 3237 323 932 138 C ATOM 2311 CD1 TYR B 294 -18.370 -34.646 20.336 1.00 14.72 C ANISOU 2311 CD1 TYR B 294 1172 1112 3307 163 1098 111 C ATOM 2312 CD2 TYR B 294 -19.135 -35.509 22.454 1.00 17.79 C ANISOU 2312 CD2 TYR B 294 2147 1089 3522 126 657 230 C ATOM 2313 CE1 TYR B 294 -17.172 -35.385 20.473 1.00 17.45 C ANISOU 2313 CE1 TYR B 294 1863 1329 3440 518 995 345 C ATOM 2314 CE2 TYR B 294 -17.929 -36.255 22.591 1.00 16.99 C ANISOU 2314 CE2 TYR B 294 1519 1264 3672 -241 1018 -31 C ATOM 2315 CZ TYR B 294 -16.956 -36.211 21.585 1.00 16.79 C ANISOU 2315 CZ TYR B 294 1112 1544 3725 173 1074 79 C ATOM 2316 OH TYR B 294 -15.784 -36.965 21.716 1.00 19.69 O ANISOU 2316 OH TYR B 294 1529 1972 3980 107 1104 -288 O ATOM 2317 N ALA B 295 -22.836 -31.668 21.143 1.00 15.22 N ANISOU 2317 N ALA B 295 1002 1169 3611 -170 371 -48 N ATOM 2318 CA ALA B 295 -24.065 -31.191 20.498 1.00 15.97 C ANISOU 2318 CA ALA B 295 1053 1311 3703 -214 526 109 C ATOM 2319 C ALA B 295 -24.054 -29.683 20.328 1.00 17.01 C ANISOU 2319 C ALA B 295 1300 1668 3496 -369 514 56 C ATOM 2320 O ALA B 295 -24.998 -29.129 19.751 1.00 18.39 O ANISOU 2320 O ALA B 295 1485 1765 3737 -588 277 11 O ATOM 2321 CB ALA B 295 -25.279 -31.617 21.315 1.00 18.73 C ANISOU 2321 CB ALA B 295 1283 1873 3960 -371 545 191 C ATOM 2322 N ASN B 296 -22.995 -29.030 20.844 1.00 15.57 N ANISOU 2322 N ASN B 296 1362 1218 3335 -117 450 145 N ATOM 2323 CA ASN B 296 -22.962 -27.560 20.877 1.00 15.93 C ANISOU 2323 CA ASN B 296 1567 1267 3218 -89 712 80 C ATOM 2324 C ASN B 296 -21.573 -27.011 20.590 1.00 14.89 C ANISOU 2324 C ASN B 296 1442 1144 3073 -21 624 279 C ATOM 2325 O ASN B 296 -21.025 -26.247 21.392 1.00 15.33 O ANISOU 2325 O ASN B 296 1409 1202 3213 -159 299 -38 O ATOM 2326 CB ASN B 296 -23.460 -27.104 22.270 1.00 16.29 C ANISOU 2326 CB ASN B 296 1197 1619 3373 19 835 94 C ATOM 2327 CG ASN B 296 -24.954 -27.430 22.492 1.00 16.70 C ANISOU 2327 CG ASN B 296 1296 1326 3725 447 112 104 C ATOM 2328 OD1 ASN B 296 -25.816 -26.802 21.890 1.00 18.76 O ANISOU 2328 OD1 ASN B 296 1475 1572 4082 163 24 -93 O ATOM 2329 ND2 ASN B 296 -25.239 -28.458 23.283 1.00 17.74 N ANISOU 2329 ND2 ASN B 296 1578 1279 3884 113 306 336 N ATOM 2330 N AASN B 297 -21.022 -27.382 19.480 0.50 14.15 N ANISOU 2330 N AASN B 297 935 1418 3024 77 382 112 N ATOM 2331 N BASN B 297 -21.020 -27.443 19.456 0.50 16.44 N ANISOU 2331 N BASN B 297 2136 1083 3028 -83 410 187 N ATOM 2332 CA AASN B 297 -19.697 -26.902 19.075 0.50 10.90 C ANISOU 2332 CA AASN B 297 72 1183 2887 150 343 -90 C ATOM 2333 CA BASN B 297 -19.722 -26.955 18.982 0.50 16.36 C ANISOU 2333 CA BASN B 297 2403 867 2945 -121 408 159 C ATOM 2334 C AASN B 297 -19.827 -25.653 18.229 0.50 13.05 C ANISOU 2334 C AASN B 297 313 1673 2973 -301 13 95 C ATOM 2335 C BASN B 297 -19.977 -25.663 18.245 0.50 17.15 C ANISOU 2335 C BASN B 297 2664 946 2906 -321 -173 271 C ATOM 2336 O AASN B 297 -20.165 -25.761 17.220 0.50 19.69 O ANISOU 2336 O AASN B 297 1516 2659 3308 369 -54 120 O ATOM 2337 O BASN B 297 -20.598 -25.701 17.175 0.50 20.36 O ANISOU 2337 O BASN B 297 3901 700 3137 -470 -1124 307 O ATOM 2338 CB AASN B 297 -18.950 -27.998 18.273 0.50 12.63 C ANISOU 2338 CB AASN B 297 381 1570 2848 64 10 -272 C ATOM 2339 CB BASN B 297 -19.120 -27.910 17.943 0.50 19.95 C ANISOU 2339 CB BASN B 297 2801 1719 3059 -206 402 17 C ATOM 2340 CG AASN B 297 -17.467 -27.622 17.940 0.50 14.02 C ANISOU 2340 CG AASN B 297 1355 1145 2827 174 312 -456 C ATOM 2341 CG BASN B 297 -18.494 -29.120 18.544 0.50 20.24 C ANISOU 2341 CG BASN B 297 2716 1919 3053 -252 344 142 C ATOM 2342 OD1AASN B 297 -16.858 -26.726 18.425 0.50 18.28 O ANISOU 2342 OD1AASN B 297 3103 992 2849 4 1013 53 O ATOM 2343 OD1BASN B 297 -19.146 -30.115 18.788 0.50 25.53 O ANISOU 2343 OD1BASN B 297 3045 3354 3303 77 340 242 O ATOM 2344 ND2AASN B 297 -16.936 -28.403 17.146 0.50 15.90 N ANISOU 2344 ND2AASN B 297 1724 1520 2798 180 -525 -519 N ATOM 2345 ND2BASN B 297 -17.196 -29.079 18.696 0.50 18.13 N ANISOU 2345 ND2BASN B 297 2347 1569 2973 137 342 -50 N ATOM 2346 N VAL B 298 -19.508 -24.540 18.789 1.00 12.73 N ANISOU 2346 N VAL B 298 1132 824 2882 -198 507 167 N ATOM 2347 CA VAL B 298 -19.678 -23.265 18.108 1.00 11.41 C ANISOU 2347 CA VAL B 298 762 920 2654 -105 623 276 C ATOM 2348 C VAL B 298 -18.357 -22.828 17.518 1.00 11.62 C ANISOU 2348 C VAL B 298 1028 865 2523 20 30 152 C ATOM 2349 O VAL B 298 -17.361 -22.870 18.206 1.00 12.74 O ANISOU 2349 O VAL B 298 743 1542 2556 25 -6 206 O ATOM 2350 CB VAL B 298 -20.244 -22.221 19.110 1.00 13.82 C ANISOU 2350 CB VAL B 298 1463 870 2919 192 937 119 C ATOM 2351 CG1 VAL B 298 -20.215 -20.806 18.506 1.00 16.87 C ANISOU 2351 CG1 VAL B 298 2279 1022 3111 682 1006 610 C ATOM 2352 CG2 VAL B 298 -21.684 -22.602 19.530 1.00 16.79 C ANISOU 2352 CG2 VAL B 298 1498 1693 3189 48 1015 272 C ATOM 2353 N MET B 299 -18.404 -22.363 16.272 1.00 12.08 N ANISOU 2353 N MET B 299 727 1276 2588 -152 346 277 N ATOM 2354 CA MET B 299 -17.192 -21.829 15.652 1.00 10.82 C ANISOU 2354 CA MET B 299 469 1218 2425 -40 37 -94 C ATOM 2355 C MET B 299 -17.282 -20.312 15.602 1.00 10.91 C ANISOU 2355 C MET B 299 825 973 2345 -19 123 6 C ATOM 2356 O MET B 299 -18.310 -19.773 15.213 1.00 13.13 O ANISOU 2356 O MET B 299 1262 1183 2542 139 39 112 O ATOM 2357 CB MET B 299 -17.046 -22.297 14.213 1.00 14.81 C ANISOU 2357 CB MET B 299 1771 1077 2779 -504 625 -230 C ATOM 2358 CG MET B 299 -16.790 -23.762 14.149 1.00 18.81 C ANISOU 2358 CG MET B 299 2399 1602 3146 -499 349 -553 C ATOM 2359 SD MET B 299 -16.350 -24.235 12.441 1.00 20.51 S ANISOU 2359 SD MET B 299 1892 2322 3578 96 268 -582 S ATOM 2360 CE MET B 299 -15.726 -25.865 12.674 1.00 24.28 C ANISOU 2360 CE MET B 299 3234 2118 3874 -582 51 -121 C ATOM 2361 N SER B 300 -16.188 -19.652 16.002 1.00 10.67 N ANISOU 2361 N SER B 300 858 952 2245 -275 221 284 N ATOM 2362 CA SER B 300 -16.176 -18.149 15.920 1.00 11.18 C ANISOU 2362 CA SER B 300 971 1065 2212 -295 238 115 C ATOM 2363 C SER B 300 -14.822 -17.640 15.533 1.00 9.62 C ANISOU 2363 C SER B 300 260 980 2416 318 36 430 C ATOM 2364 O SER B 300 -13.831 -18.323 15.719 1.00 12.12 O ANISOU 2364 O SER B 300 800 1264 2543 343 54 523 O ATOM 2365 CB SER B 300 -16.648 -17.547 17.251 1.00 16.61 C ANISOU 2365 CB SER B 300 1910 2179 2224 108 151 -28 C ATOM 2366 OG SER B 300 -15.814 -17.989 18.281 1.00 18.24 O ANISOU 2366 OG SER B 300 2426 1871 2632 -430 165 17 O ATOM 2367 N GLY B 301 -14.802 -16.436 14.968 1.00 10.45 N ANISOU 2367 N GLY B 301 350 1112 2508 277 458 418 N ATOM 2368 CA GLY B 301 -13.545 -15.801 14.603 1.00 10.98 C ANISOU 2368 CA GLY B 301 44 1706 2421 -15 292 117 C ATOM 2369 C GLY B 301 -13.279 -15.895 13.096 1.00 11.64 C ANISOU 2369 C GLY B 301 914 1217 2292 -41 441 283 C ATOM 2370 O GLY B 301 -13.811 -16.773 12.403 1.00 11.80 O ANISOU 2370 O GLY B 301 899 1325 2259 167 144 259 O ATOM 2371 N GLY B 302 -12.494 -14.940 12.600 1.00 11.08 N ANISOU 2371 N GLY B 302 900 1052 2259 8 435 374 N ATOM 2372 CA GLY B 302 -12.280 -14.852 11.134 1.00 12.33 C ANISOU 2372 CA GLY B 302 1308 1206 2172 388 602 322 C ATOM 2373 C GLY B 302 -11.699 -16.118 10.515 1.00 12.35 C ANISOU 2373 C GLY B 302 927 1411 2355 516 485 376 C ATOM 2374 O GLY B 302 -12.013 -16.448 9.385 1.00 13.33 O ANISOU 2374 O GLY B 302 1300 1361 2403 417 431 250 O ATOM 2375 N THR B 303 -10.849 -16.829 11.282 1.00 10.32 N ANISOU 2375 N THR B 303 354 1053 2513 352 411 374 N ATOM 2376 CA THR B 303 -10.188 -18.009 10.695 1.00 12.27 C ANISOU 2376 CA THR B 303 858 1204 2600 -90 243 175 C ATOM 2377 C THR B 303 -11.131 -19.219 10.616 1.00 11.18 C ANISOU 2377 C THR B 303 179 1510 2557 -104 195 145 C ATOM 2378 O THR B 303 -10.807 -20.224 9.974 1.00 13.38 O ANISOU 2378 O THR B 303 952 1432 2700 105 462 55 O ATOM 2379 CB THR B 303 -8.815 -18.214 11.366 1.00 11.56 C ANISOU 2379 CB THR B 303 877 1071 2446 58 20 -11 C ATOM 2380 OG1 THR B 303 -7.973 -17.111 10.974 1.00 11.84 O ANISOU 2380 OG1 THR B 303 714 1348 2437 64 440 341 O ATOM 2381 CG2 THR B 303 -8.144 -19.537 10.985 1.00 11.69 C ANISOU 2381 CG2 THR B 303 578 1310 2552 138 -241 -170 C ATOM 2382 N THR B 304 -12.350 -19.084 11.178 1.00 10.80 N ANISOU 2382 N THR B 304 445 1318 2339 -86 181 413 N ATOM 2383 CA THR B 304 -13.335 -20.139 10.965 1.00 13.97 C ANISOU 2383 CA THR B 304 1262 1753 2295 -163 426 182 C ATOM 2384 C THR B 304 -14.230 -19.854 9.737 1.00 11.75 C ANISOU 2384 C THR B 304 116 1942 2406 -158 464 129 C ATOM 2385 O THR B 304 -15.213 -20.549 9.517 1.00 13.88 O ANISOU 2385 O THR B 304 806 1984 2482 -287 171 2 O ATOM 2386 CB THR B 304 -14.240 -20.417 12.185 1.00 13.20 C ANISOU 2386 CB THR B 304 960 1625 2432 661 203 258 C ATOM 2387 OG1 THR B 304 -15.132 -19.302 12.368 1.00 12.73 O ANISOU 2387 OG1 THR B 304 752 1726 2358 -30 193 75 O ATOM 2388 CG2 THR B 304 -13.381 -20.680 13.421 1.00 14.51 C ANISOU 2388 CG2 THR B 304 1204 1840 2471 418 398 502 C ATOM 2389 N AMET B 305 -13.845 -18.853 8.928 0.60 13.63 N ANISOU 2389 N AMET B 305 910 1990 2279 269 235 504 N ATOM 2390 N BMET B 305 -13.909 -18.846 8.923 0.40 12.18 N ANISOU 2390 N BMET B 305 804 1551 2272 231 257 364 N ATOM 2391 CA AMET B 305 -14.704 -18.382 7.842 0.60 17.28 C ANISOU 2391 CA AMET B 305 1882 2088 2597 415 123 312 C ATOM 2392 CA BMET B 305 -14.848 -18.509 7.848 0.40 12.61 C ANISOU 2392 CA BMET B 305 1034 1339 2417 158 113 181 C ATOM 2393 C AMET B 305 -14.561 -19.166 6.531 0.60 16.01 C ANISOU 2393 C AMET B 305 1708 1936 2439 369 147 86 C ATOM 2394 C BMET B 305 -14.730 -19.415 6.625 0.40 14.46 C ANISOU 2394 C BMET B 305 1496 1671 2328 72 176 158 C ATOM 2395 O AMET B 305 -15.309 -18.886 5.561 0.60 16.25 O ANISOU 2395 O AMET B 305 1595 2185 2393 -33 83 102 O ATOM 2396 O BMET B 305 -15.656 -19.479 5.811 0.40 14.98 O ANISOU 2396 O BMET B 305 1635 1810 2248 -97 249 350 O ATOM 2397 CB AMET B 305 -14.415 -16.905 7.560 0.60 19.24 C ANISOU 2397 CB AMET B 305 1990 2342 2977 662 369 516 C ATOM 2398 CB BMET B 305 -14.698 -17.049 7.443 0.40 12.13 C ANISOU 2398 CB BMET B 305 628 1350 2629 578 222 112 C ATOM 2399 CG AMET B 305 -14.950 -15.924 8.593 0.60 19.44 C ANISOU 2399 CG AMET B 305 1576 2488 3321 889 284 628 C ATOM 2400 CG BMET B 305 -15.121 -16.090 8.538 0.40 13.54 C ANISOU 2400 CG BMET B 305 698 1680 2767 443 43 -65 C ATOM 2401 SD AMET B 305 -16.688 -16.155 9.034 0.60 21.41 S ANISOU 2401 SD AMET B 305 1535 3073 3524 1133 367 772 S ATOM 2402 SD BMET B 305 -14.877 -14.344 8.152 0.40 16.91 S ANISOU 2402 SD BMET B 305 1322 2315 2786 399 139 -55 S ATOM 2403 CE AMET B 305 -17.498 -16.136 7.475 0.60 23.10 C ANISOU 2403 CE AMET B 305 1134 3992 3650 863 378 686 C ATOM 2404 CE BMET B 305 -16.201 -14.046 6.973 0.40 19.00 C ANISOU 2404 CE BMET B 305 1957 2471 2792 866 -188 399 C ATOM 2405 N TYR B 306 -13.595 -20.093 6.475 1.00 14.35 N ANISOU 2405 N TYR B 306 1643 1424 2386 171 303 -68 N ATOM 2406 CA TYR B 306 -13.392 -20.884 5.256 1.00 13.63 C ANISOU 2406 CA TYR B 306 1102 1543 2535 126 19 -30 C ATOM 2407 C TYR B 306 -14.607 -21.709 4.861 1.00 15.34 C ANISOU 2407 C TYR B 306 1285 2035 2508 85 -156 3 C ATOM 2408 O TYR B 306 -15.177 -22.475 5.677 1.00 16.17 O ANISOU 2408 O TYR B 306 1338 2067 2740 62 17 250 O ATOM 2409 CB TYR B 306 -12.198 -21.828 5.405 1.00 12.91 C ANISOU 2409 CB TYR B 306 899 1406 2599 146 39 89 C ATOM 2410 CG TYR B 306 -10.939 -21.084 5.654 1.00 12.77 C ANISOU 2410 CG TYR B 306 1126 1214 2512 -120 202 159 C ATOM 2411 CD1 TYR B 306 -10.220 -20.548 4.573 1.00 12.65 C ANISOU 2411 CD1 TYR B 306 888 1423 2497 -22 534 359 C ATOM 2412 CD2 TYR B 306 -10.412 -20.905 6.942 1.00 13.98 C ANISOU 2412 CD2 TYR B 306 1278 1541 2493 242 -81 108 C ATOM 2413 CE1 TYR B 306 -9.071 -19.823 4.753 1.00 13.12 C ANISOU 2413 CE1 TYR B 306 1133 1355 2497 -60 329 242 C ATOM 2414 CE2 TYR B 306 -9.247 -20.191 7.150 1.00 13.16 C ANISOU 2414 CE2 TYR B 306 1104 1267 2631 222 418 168 C ATOM 2415 CZ TYR B 306 -8.566 -19.627 6.040 1.00 13.29 C ANISOU 2415 CZ TYR B 306 971 1509 2572 -83 244 314 C ATOM 2416 OH TYR B 306 -7.451 -18.877 6.209 1.00 14.34 O ANISOU 2416 OH TYR B 306 1426 1548 2475 -235 385 81 O ATOM 2417 N PRO B 307 -15.024 -21.598 3.582 1.00 15.15 N ANISOU 2417 N PRO B 307 1386 1866 2505 168 -442 280 N ATOM 2418 CA PRO B 307 -16.012 -22.555 3.098 1.00 17.96 C ANISOU 2418 CA PRO B 307 2011 2315 2499 -393 -421 284 C ATOM 2419 C PRO B 307 -15.535 -23.987 3.349 1.00 16.64 C ANISOU 2419 C PRO B 307 1974 1860 2490 -577 -119 263 C ATOM 2420 O PRO B 307 -14.351 -24.276 3.153 1.00 17.36 O ANISOU 2420 O PRO B 307 1953 1988 2653 -130 -25 315 O ATOM 2421 CB PRO B 307 -16.105 -22.252 1.582 1.00 18.27 C ANISOU 2421 CB PRO B 307 2102 2251 2590 -145 -219 664 C ATOM 2422 CG PRO B 307 -15.754 -20.773 1.504 1.00 17.98 C ANISOU 2422 CG PRO B 307 2022 2152 2659 78 -478 557 C ATOM 2423 CD PRO B 307 -14.684 -20.536 2.606 1.00 15.47 C ANISOU 2423 CD PRO B 307 1491 1945 2441 308 -622 540 C ATOM 2424 N GLY B 308 -16.455 -24.857 3.805 1.00 17.29 N ANISOU 2424 N GLY B 308 1972 2190 2408 -1079 -277 244 N ATOM 2425 CA GLY B 308 -16.127 -26.248 4.036 1.00 18.86 C ANISOU 2425 CA GLY B 308 2602 2083 2482 -714 12 303 C ATOM 2426 C GLY B 308 -15.641 -26.564 5.446 1.00 17.11 C ANISOU 2426 C GLY B 308 1923 2096 2481 -187 421 40 C ATOM 2427 O GLY B 308 -15.575 -27.738 5.831 1.00 18.45 O ANISOU 2427 O GLY B 308 2463 1771 2774 -420 338 370 O ATOM 2428 N ILE B 309 -15.245 -25.556 6.209 1.00 15.05 N ANISOU 2428 N ILE B 309 1356 1984 2380 103 -16 -45 N ATOM 2429 CA ILE B 309 -14.596 -25.899 7.499 1.00 16.19 C ANISOU 2429 CA ILE B 309 1734 2011 2408 -107 -130 58 C ATOM 2430 C ILE B 309 -15.627 -26.535 8.465 1.00 16.44 C ANISOU 2430 C ILE B 309 1512 2191 2545 0 116 115 C ATOM 2431 O ILE B 309 -15.281 -27.473 9.177 1.00 16.80 O ANISOU 2431 O ILE B 309 1848 2144 2392 73 384 170 O ATOM 2432 CB ILE B 309 -13.886 -24.689 8.133 1.00 15.26 C ANISOU 2432 CB ILE B 309 1653 1590 2554 180 -266 -217 C ATOM 2433 CG1 ILE B 309 -12.897 -25.154 9.225 1.00 16.52 C ANISOU 2433 CG1 ILE B 309 1815 1567 2894 7 -608 10 C ATOM 2434 CG2 ILE B 309 -14.901 -23.636 8.685 1.00 15.75 C ANISOU 2434 CG2 ILE B 309 1821 1692 2472 474 -35 225 C ATOM 2435 CD1 ILE B 309 -12.115 -24.010 9.888 1.00 17.96 C ANISOU 2435 CD1 ILE B 309 2122 1720 2982 -312 -945 159 C ATOM 2436 N ALA B 310 -16.876 -26.063 8.472 1.00 16.48 N ANISOU 2436 N ALA B 310 1241 2402 2619 -215 148 151 N ATOM 2437 CA ALA B 310 -17.837 -26.709 9.374 1.00 16.62 C ANISOU 2437 CA ALA B 310 1073 2373 2870 20 -33 50 C ATOM 2438 C ALA B 310 -18.094 -28.173 8.971 1.00 18.46 C ANISOU 2438 C ALA B 310 1715 2439 2861 -137 -140 175 C ATOM 2439 O ALA B 310 -18.144 -29.068 9.840 1.00 18.97 O ANISOU 2439 O ALA B 310 1817 2615 2775 -351 20 320 O ATOM 2440 CB ALA B 310 -19.130 -25.917 9.404 1.00 21.05 C ANISOU 2440 CB ALA B 310 1135 3686 3176 333 -95 422 C ATOM 2441 N ASP B 311 -18.255 -28.436 7.662 1.00 18.50 N ANISOU 2441 N ASP B 311 1274 2830 2926 -200 -160 -2 N ATOM 2442 CA ASP B 311 -18.460 -29.832 7.215 1.00 20.57 C ANISOU 2442 CA ASP B 311 1859 2958 2998 -579 -43 75 C ATOM 2443 C ASP B 311 -17.250 -30.701 7.513 1.00 18.74 C ANISOU 2443 C ASP B 311 1903 2439 2777 -610 320 55 C ATOM 2444 O ASP B 311 -17.365 -31.871 7.875 1.00 18.15 O ANISOU 2444 O ASP B 311 1830 2310 2755 -794 508 53 O ATOM 2445 CB ASP B 311 -18.754 -29.907 5.702 1.00 25.20 C ANISOU 2445 CB ASP B 311 2286 3956 3333 -426 -737 106 C ATOM 2446 CG ASP B 311 -20.044 -29.188 5.310 1.00 32.81 C ANISOU 2446 CG ASP B 311 3191 5376 3901 -223 -796 170 C ATOM 2447 OD1 ASP B 311 -20.101 -28.625 4.196 1.00 38.49 O ANISOU 2447 OD1 ASP B 311 4058 6235 4330 233 -1193 276 O ATOM 2448 OD2 ASP B 311 -20.997 -29.183 6.095 1.00 32.58 O ANISOU 2448 OD2 ASP B 311 2574 5578 4229 -648 -893 277 O ATOM 2449 N ARG B 312 -16.047 -30.149 7.333 1.00 17.00 N ANISOU 2449 N ARG B 312 1723 2140 2595 -300 263 -184 N ATOM 2450 CA ARG B 312 -14.847 -30.907 7.646 1.00 17.48 C ANISOU 2450 CA ARG B 312 2096 1977 2569 -263 307 83 C ATOM 2451 C ARG B 312 -14.750 -31.220 9.138 1.00 15.89 C ANISOU 2451 C ARG B 312 2029 1552 2458 -185 437 -99 C ATOM 2452 O ARG B 312 -14.394 -32.351 9.512 1.00 16.83 O ANISOU 2452 O ARG B 312 2242 1398 2756 -438 694 112 O ATOM 2453 CB ARG B 312 -13.589 -30.164 7.186 1.00 16.80 C ANISOU 2453 CB ARG B 312 1783 1787 2812 -614 227 111 C ATOM 2454 CG ARG B 312 -12.309 -30.875 7.494 1.00 16.49 C ANISOU 2454 CG ARG B 312 2046 1474 2746 -339 366 -76 C ATOM 2455 CD ARG B 312 -12.087 -32.184 6.663 1.00 16.60 C ANISOU 2455 CD ARG B 312 1943 1482 2883 -627 345 -250 C ATOM 2456 NE ARG B 312 -10.751 -32.656 7.030 1.00 17.16 N ANISOU 2456 NE ARG B 312 1495 2065 2960 -257 455 -160 N ATOM 2457 CZ ARG B 312 -9.604 -32.165 6.522 1.00 13.94 C ANISOU 2457 CZ ARG B 312 1205 1298 2795 307 554 158 C ATOM 2458 NH1 ARG B 312 -9.628 -31.241 5.537 1.00 16.64 N ANISOU 2458 NH1 ARG B 312 2356 1418 2548 -46 621 341 N ATOM 2459 NH2 ARG B 312 -8.430 -32.577 6.991 1.00 17.22 N ANISOU 2459 NH2 ARG B 312 2101 1432 3010 381 266 44 N ATOM 2460 N AMET B 313 -15.061 -30.244 9.990 0.50 15.41 N ANISOU 2460 N AMET B 313 1925 1507 2423 -492 433 -72 N ATOM 2461 N BMET B 313 -15.083 -30.243 9.982 0.50 17.18 N ANISOU 2461 N BMET B 313 2179 1838 2510 -330 257 -31 N ATOM 2462 CA AMET B 313 -15.041 -30.520 11.424 0.50 13.81 C ANISOU 2462 CA AMET B 313 1452 1391 2403 -483 593 -172 C ATOM 2463 CA BMET B 313 -15.081 -30.468 11.431 0.50 17.62 C ANISOU 2463 CA BMET B 313 2090 2014 2592 -184 167 -96 C ATOM 2464 C AMET B 313 -16.079 -31.588 11.762 0.50 16.00 C ANISOU 2464 C AMET B 313 1911 1647 2522 -506 582 118 C ATOM 2465 C BMET B 313 -16.119 -31.502 11.846 0.50 17.51 C ANISOU 2465 C BMET B 313 2203 1828 2625 -118 261 87 C ATOM 2466 O AMET B 313 -15.797 -32.537 12.495 0.50 16.38 O ANISOU 2466 O AMET B 313 2053 1576 2593 -777 465 82 O ATOM 2467 O BMET B 313 -15.890 -32.315 12.741 0.50 16.95 O ANISOU 2467 O BMET B 313 2273 1429 2738 127 -17 -9 O ATOM 2468 CB AMET B 313 -15.278 -29.246 12.232 0.50 12.01 C ANISOU 2468 CB AMET B 313 1371 753 2440 -311 642 -320 C ATOM 2469 CB BMET B 313 -15.337 -29.154 12.156 0.50 18.85 C ANISOU 2469 CB BMET B 313 2390 1990 2783 -46 64 -141 C ATOM 2470 CG AMET B 313 -15.181 -29.476 13.719 0.50 9.82 C ANISOU 2470 CG AMET B 313 181 1104 2445 175 260 -115 C ATOM 2471 CG BMET B 313 -14.161 -28.222 12.118 0.50 19.57 C ANISOU 2471 CG BMET B 313 2025 2416 2993 147 -208 -18 C ATOM 2472 SD AMET B 313 -13.507 -29.894 14.195 0.50 12.65 S ANISOU 2472 SD AMET B 313 975 1121 2712 -34 383 200 S ATOM 2473 SD BMET B 313 -12.898 -28.713 13.300 0.50 22.23 S ANISOU 2473 SD BMET B 313 2205 2936 3306 158 -308 -155 S ATOM 2474 CE AMET B 313 -12.605 -28.338 14.058 0.50 12.58 C ANISOU 2474 CE AMET B 313 1469 650 2662 536 491 350 C ATOM 2475 CE BMET B 313 -13.665 -28.255 14.819 0.50 22.15 C ANISOU 2475 CE BMET B 313 2454 2735 3226 307 -162 -39 C ATOM 2476 N GLN B 314 -17.286 -31.444 11.209 1.00 18.30 N ANISOU 2476 N GLN B 314 1962 2200 2789 -199 427 304 N ATOM 2477 CA GLN B 314 -18.323 -32.441 11.471 1.00 18.04 C ANISOU 2477 CA GLN B 314 1558 2239 3057 -174 335 -29 C ATOM 2478 C GLN B 314 -17.814 -33.839 11.152 1.00 17.93 C ANISOU 2478 C GLN B 314 1993 2004 2814 -286 386 -196 C ATOM 2479 O GLN B 314 -17.968 -34.768 11.951 1.00 19.53 O ANISOU 2479 O GLN B 314 2511 2063 2845 -798 480 155 O ATOM 2480 CB GLN B 314 -19.549 -32.165 10.615 1.00 19.42 C ANISOU 2480 CB GLN B 314 1529 2568 3281 -640 207 99 C ATOM 2481 CG GLN B 314 -20.720 -33.161 10.840 1.00 20.91 C ANISOU 2481 CG GLN B 314 1830 2636 3480 -1250 480 185 C ATOM 2482 CD GLN B 314 -21.516 -32.883 12.103 1.00 23.29 C ANISOU 2482 CD GLN B 314 2162 2943 3742 -1014 305 65 C ATOM 2483 OE1 GLN B 314 -21.542 -31.750 12.599 1.00 28.67 O ANISOU 2483 OE1 GLN B 314 3203 3709 3980 -1117 429 -166 O ATOM 2484 NE2 GLN B 314 -22.175 -33.922 12.638 1.00 25.75 N ANISOU 2484 NE2 GLN B 314 2565 3498 3721 -694 189 261 N ATOM 2485 N LYS B 315 -17.169 -33.985 9.993 1.00 17.05 N ANISOU 2485 N LYS B 315 1580 2189 2712 -396 391 -104 N ATOM 2486 CA LYS B 315 -16.661 -35.298 9.574 1.00 18.59 C ANISOU 2486 CA LYS B 315 2218 2099 2745 4 580 -291 C ATOM 2487 C LYS B 315 -15.590 -35.775 10.534 1.00 18.39 C ANISOU 2487 C LYS B 315 2541 1631 2814 -298 487 -3 C ATOM 2488 O LYS B 315 -15.602 -36.936 11.007 1.00 20.00 O ANISOU 2488 O LYS B 315 2802 1830 2968 -451 411 -11 O ATOM 2489 CB LYS B 315 -16.101 -35.197 8.146 1.00 20.04 C ANISOU 2489 CB LYS B 315 2721 2084 2812 -7 891 -505 C ATOM 2490 CG LYS B 315 -15.306 -36.394 7.687 1.00 23.18 C ANISOU 2490 CG LYS B 315 3464 2288 3057 -230 1009 -482 C ATOM 2491 CD LYS B 315 -14.657 -36.123 6.332 1.00 27.75 C ANISOU 2491 CD LYS B 315 4383 2910 3249 -128 1814 -559 C ATOM 2492 CE LYS B 315 -13.837 -37.332 5.896 1.00 33.17 C ANISOU 2492 CE LYS B 315 5238 3792 3572 -275 1755 -253 C ATOM 2493 NZ LYS B 315 -13.119 -37.079 4.599 1.00 35.39 N ANISOU 2493 NZ LYS B 315 5590 3916 3943 -1117 1577 -65 N ATOM 2494 N GLU B 316 -14.643 -34.903 10.873 1.00 18.41 N ANISOU 2494 N GLU B 316 2531 1763 2702 -541 504 29 N ATOM 2495 CA GLU B 316 -13.513 -35.325 11.685 1.00 16.68 C ANISOU 2495 CA GLU B 316 1963 1466 2910 -496 521 124 C ATOM 2496 C GLU B 316 -13.912 -35.637 13.124 1.00 17.86 C ANISOU 2496 C GLU B 316 2252 1633 2901 -190 782 -2 C ATOM 2497 O GLU B 316 -13.429 -36.626 13.699 1.00 18.81 O ANISOU 2497 O GLU B 316 2459 1666 3023 -367 561 180 O ATOM 2498 CB GLU B 316 -12.437 -34.269 11.701 1.00 15.36 C ANISOU 2498 CB GLU B 316 1133 1778 2924 -553 519 71 C ATOM 2499 CG GLU B 316 -11.876 -33.995 10.316 1.00 16.44 C ANISOU 2499 CG GLU B 316 1960 1352 2933 -144 955 -9 C ATOM 2500 CD GLU B 316 -11.071 -35.148 9.700 1.00 20.42 C ANISOU 2500 CD GLU B 316 2989 1650 3120 183 1028 7 C ATOM 2501 OE1 GLU B 316 -10.657 -35.000 8.525 1.00 24.05 O ANISOU 2501 OE1 GLU B 316 3926 1980 3233 -32 1305 126 O ATOM 2502 OE2 GLU B 316 -10.779 -36.167 10.385 1.00 22.23 O ANISOU 2502 OE2 GLU B 316 3513 1668 3267 215 1070 326 O ATOM 2503 N ILE B 317 -14.787 -34.809 13.697 1.00 18.00 N ANISOU 2503 N ILE B 317 2356 1692 2793 -130 931 -116 N ATOM 2504 CA AILE B 317 -15.239 -35.046 15.072 0.50 17.29 C ANISOU 2504 CA AILE B 317 2051 1686 2832 -369 835 -16 C ATOM 2505 CA BILE B 317 -15.193 -35.082 15.080 0.50 18.14 C ANISOU 2505 CA BILE B 317 2494 1599 2799 -17 915 66 C ATOM 2506 C ILE B 317 -16.081 -36.316 15.101 1.00 18.02 C ANISOU 2506 C ILE B 317 2279 1722 2847 -227 765 141 C ATOM 2507 O ILE B 317 -15.974 -37.119 16.000 1.00 19.44 O ANISOU 2507 O ILE B 317 2777 1752 2858 -258 687 288 O ATOM 2508 CB AILE B 317 -16.034 -33.830 15.598 0.50 14.90 C ANISOU 2508 CB AILE B 317 1126 1716 2819 -968 892 -247 C ATOM 2509 CB BILE B 317 -15.892 -33.883 15.752 0.50 18.39 C ANISOU 2509 CB BILE B 317 2668 1587 2731 -18 1066 -22 C ATOM 2510 CG1AILE B 317 -15.089 -32.641 15.760 0.50 16.63 C ANISOU 2510 CG1AILE B 317 1112 2271 2935 -1094 511 -341 C ATOM 2511 CG1BILE B 317 -14.993 -32.644 15.673 0.50 20.72 C ANISOU 2511 CG1BILE B 317 3196 1741 2936 70 913 -7 C ATOM 2512 CG2AILE B 317 -16.801 -34.155 16.924 0.50 16.22 C ANISOU 2512 CG2AILE B 317 1433 1819 2913 -774 892 -127 C ATOM 2513 CG2BILE B 317 -16.284 -34.227 17.232 0.50 18.67 C ANISOU 2513 CG2BILE B 317 2937 1514 2644 -122 1000 0 C ATOM 2514 CD1AILE B 317 -13.917 -32.927 16.687 0.50 16.70 C ANISOU 2514 CD1AILE B 317 1013 2360 2970 -1053 600 -282 C ATOM 2515 CD1BILE B 317 -15.614 -31.388 16.268 0.50 21.08 C ANISOU 2515 CD1BILE B 317 3451 1536 3021 25 928 -107 C ATOM 2516 N THR B 318 -16.937 -36.480 14.109 1.00 18.93 N ANISOU 2516 N THR B 318 2402 1757 3032 -551 780 44 N ATOM 2517 CA THR B 318 -17.727 -37.731 14.042 1.00 21.26 C ANISOU 2517 CA THR B 318 2611 2145 3320 -809 722 41 C ATOM 2518 C THR B 318 -16.808 -38.951 14.057 1.00 20.20 C ANISOU 2518 C THR B 318 2670 1798 3206 -700 910 111 C ATOM 2519 O THR B 318 -17.111 -39.956 14.730 1.00 21.13 O ANISOU 2519 O THR B 318 3225 1534 3269 -498 904 290 O ATOM 2520 CB THR B 318 -18.607 -37.730 12.811 1.00 21.67 C ANISOU 2520 CB THR B 318 2795 1839 3599 -1245 758 -158 C ATOM 2521 OG1 THR B 318 -19.554 -36.661 12.900 1.00 22.17 O ANISOU 2521 OG1 THR B 318 2749 2077 3597 -784 416 -56 O ATOM 2522 CG2 THR B 318 -19.344 -39.059 12.650 1.00 25.36 C ANISOU 2522 CG2 THR B 318 3631 2042 3964 -1192 994 -369 C ATOM 2523 N ALA B 319 -15.703 -38.897 13.314 1.00 21.32 N ANISOU 2523 N ALA B 319 2972 1878 3251 -234 922 -79 N ATOM 2524 CA ALA B 319 -14.804 -40.037 13.261 1.00 20.62 C ANISOU 2524 CA ALA B 319 2636 1988 3211 -322 1224 40 C ATOM 2525 C ALA B 319 -14.108 -40.359 14.588 1.00 21.84 C ANISOU 2525 C ALA B 319 3310 1656 3334 159 914 198 C ATOM 2526 O ALA B 319 -13.646 -41.482 14.785 1.00 24.62 O ANISOU 2526 O ALA B 319 4213 1520 3620 -170 1039 111 O ATOM 2527 CB ALA B 319 -13.735 -39.858 12.161 1.00 23.25 C ANISOU 2527 CB ALA B 319 3185 2444 3207 -315 1450 57 C ATOM 2528 N LEU B 320 -13.993 -39.375 15.480 1.00 19.78 N ANISOU 2528 N LEU B 320 2703 1685 3128 220 1016 240 N ATOM 2529 CA LEU B 320 -13.255 -39.527 16.737 1.00 19.60 C ANISOU 2529 CA LEU B 320 2535 1621 3291 -87 997 344 C ATOM 2530 C LEU B 320 -14.231 -39.908 17.870 1.00 18.95 C ANISOU 2530 C LEU B 320 2541 1366 3291 59 1073 495 C ATOM 2531 O LEU B 320 -13.845 -40.624 18.787 1.00 22.13 O ANISOU 2531 O LEU B 320 3609 1411 3386 180 1090 447 O ATOM 2532 CB LEU B 320 -12.534 -38.240 17.125 1.00 19.01 C ANISOU 2532 CB LEU B 320 2200 1664 3358 -221 972 -22 C ATOM 2533 CG LEU B 320 -11.259 -37.956 16.307 1.00 21.75 C ANISOU 2533 CG LEU B 320 2214 2496 3553 -313 955 54 C ATOM 2534 CD1 LEU B 320 -10.802 -36.494 16.448 1.00 21.49 C ANISOU 2534 CD1 LEU B 320 2495 2374 3296 -493 1071 -213 C ATOM 2535 CD2 LEU B 320 -10.111 -38.905 16.716 1.00 25.22 C ANISOU 2535 CD2 LEU B 320 2486 3244 3853 86 638 207 C ATOM 2536 N ALA B 321 -15.455 -39.409 17.782 1.00 19.38 N ANISOU 2536 N ALA B 321 2437 1550 3375 -50 876 257 N ATOM 2537 CA ALA B 321 -16.415 -39.467 18.875 1.00 20.42 C ANISOU 2537 CA ALA B 321 3121 1198 3439 -150 1360 350 C ATOM 2538 C ALA B 321 -17.099 -40.823 18.891 1.00 21.36 C ANISOU 2538 C ALA B 321 3594 1146 3377 247 1467 521 C ATOM 2539 O ALA B 321 -17.134 -41.515 17.859 1.00 21.02 O ANISOU 2539 O ALA B 321 3547 980 3459 -169 1619 135 O ATOM 2540 CB ALA B 321 -17.468 -38.404 18.664 1.00 21.50 C ANISOU 2540 CB ALA B 321 3703 1050 3415 263 1398 265 C ATOM 2541 N PRO B 322 -17.724 -41.171 20.042 1.00 21.24 N ANISOU 2541 N PRO B 322 3644 994 3433 26 1421 375 N ATOM 2542 CA PRO B 322 -18.557 -42.361 20.015 1.00 22.80 C ANISOU 2542 CA PRO B 322 3425 1572 3666 -174 1295 137 C ATOM 2543 C PRO B 322 -19.553 -42.372 18.874 1.00 24.54 C ANISOU 2543 C PRO B 322 3907 1486 3930 53 1374 99 C ATOM 2544 O PRO B 322 -20.123 -41.320 18.503 1.00 23.31 O ANISOU 2544 O PRO B 322 3382 1573 3900 -295 1170 314 O ATOM 2545 CB PRO B 322 -19.284 -42.289 21.366 1.00 22.27 C ANISOU 2545 CB PRO B 322 3502 1463 3497 -34 1529 196 C ATOM 2546 CG PRO B 322 -18.310 -41.639 22.262 1.00 24.46 C ANISOU 2546 CG PRO B 322 3923 2045 3328 -297 1564 637 C ATOM 2547 CD PRO B 322 -17.696 -40.531 21.370 1.00 23.41 C ANISOU 2547 CD PRO B 322 3958 1687 3250 45 1563 349 C ATOM 2548 N SER B 323 -19.794 -43.552 18.302 1.00 26.24 N ANISOU 2548 N SER B 323 3780 1769 4422 -268 1378 88 N ATOM 2549 CA SER B 323 -20.541 -43.589 17.046 1.00 31.80 C ANISOU 2549 CA SER B 323 4375 2338 5372 -492 477 -296 C ATOM 2550 C SER B 323 -22.026 -43.182 17.180 1.00 35.59 C ANISOU 2550 C SER B 323 5053 2543 5926 -960 -44 -176 C ATOM 2551 O SER B 323 -22.685 -42.868 16.197 1.00 39.12 O ANISOU 2551 O SER B 323 5902 2591 6371 -1298 -827 -231 O ATOM 2552 CB SER B 323 -20.351 -44.931 16.341 1.00 36.63 C ANISOU 2552 CB SER B 323 5307 2876 5734 -421 497 -85 C ATOM 2553 OG SER B 323 -21.325 -45.837 16.776 1.00 41.29 O ANISOU 2553 OG SER B 323 6450 3162 6078 -140 227 80 O ATOM 2554 N THR B 324 -22.508 -43.141 18.410 1.00 33.68 N ANISOU 2554 N THR B 324 4284 2395 6117 -1130 465 -43 N ATOM 2555 CA THR B 324 -23.894 -42.809 18.726 1.00 34.82 C ANISOU 2555 CA THR B 324 4152 2929 6148 26 451 164 C ATOM 2556 C THR B 324 -24.090 -41.322 18.995 1.00 31.28 C ANISOU 2556 C THR B 324 3381 2413 6092 -541 685 207 C ATOM 2557 O THR B 324 -25.217 -40.848 19.166 1.00 31.52 O ANISOU 2557 O THR B 324 3093 2263 6622 -498 675 419 O ATOM 2558 CB THR B 324 -24.325 -43.557 20.002 1.00 35.85 C ANISOU 2558 CB THR B 324 4157 3393 6072 311 420 105 C ATOM 2559 OG1 THR B 324 -23.207 -43.573 20.931 1.00 38.60 O ANISOU 2559 OG1 THR B 324 5637 3040 5987 119 -211 93 O ATOM 2560 CG2 THR B 324 -24.733 -44.972 19.653 1.00 38.10 C ANISOU 2560 CG2 THR B 324 3890 4545 6043 341 846 -453 C ATOM 2561 N MET B 325 -22.980 -40.597 19.061 1.00 26.95 N ANISOU 2561 N MET B 325 3062 1802 5377 -1164 966 382 N ATOM 2562 CA MET B 325 -22.985 -39.233 19.591 1.00 24.21 C ANISOU 2562 CA MET B 325 3063 1430 4705 -658 973 -69 C ATOM 2563 C MET B 325 -23.623 -38.253 18.621 1.00 23.94 C ANISOU 2563 C MET B 325 2874 1779 4445 -492 1055 -220 C ATOM 2564 O MET B 325 -23.329 -38.281 17.429 1.00 25.70 O ANISOU 2564 O MET B 325 3370 2020 4376 -467 1130 -290 O ATOM 2565 CB MET B 325 -21.536 -38.847 19.902 1.00 23.32 C ANISOU 2565 CB MET B 325 3066 1403 4393 -654 1054 -277 C ATOM 2566 CG MET B 325 -21.372 -37.508 20.548 1.00 22.70 C ANISOU 2566 CG MET B 325 3331 1197 4096 -159 1164 -227 C ATOM 2567 SD MET B 325 -22.083 -37.514 22.206 1.00 23.44 S ANISOU 2567 SD MET B 325 3138 1646 4122 69 1357 -2 S ATOM 2568 CE MET B 325 -20.978 -38.634 23.050 1.00 23.33 C ANISOU 2568 CE MET B 325 3207 1434 4222 -424 1062 331 C ATOM 2569 N LYS B 326 -24.503 -37.379 19.120 1.00 20.32 N ANISOU 2569 N LYS B 326 1971 1586 4166 -423 996 -103 N ATOM 2570 CA ALYS B 326 -25.078 -36.349 18.258 0.50 21.45 C ANISOU 2570 CA ALYS B 326 2071 1934 4143 -673 868 109 C ATOM 2571 CA BLYS B 326 -24.978 -36.349 18.258 0.50 22.96 C ANISOU 2571 CA BLYS B 326 2466 2056 4201 -334 790 91 C ATOM 2572 C LYS B 326 -24.056 -35.219 18.251 1.00 22.10 C ANISOU 2572 C LYS B 326 2596 1807 3995 -517 578 59 C ATOM 2573 O LYS B 326 -23.662 -34.721 19.301 1.00 21.66 O ANISOU 2573 O LYS B 326 2649 1664 3918 -354 417 19 O ATOM 2574 CB ALYS B 326 -26.423 -35.906 18.796 0.50 22.39 C ANISOU 2574 CB ALYS B 326 1915 2349 4242 -1126 612 377 C ATOM 2575 CB BLYS B 326 -26.323 -35.906 18.796 0.50 25.82 C ANISOU 2575 CB BLYS B 326 2763 2646 4399 -94 453 372 C ATOM 2576 CG ALYS B 326 -27.344 -37.121 19.048 0.50 26.08 C ANISOU 2576 CG ALYS B 326 2387 3115 4406 -611 418 286 C ATOM 2577 CG BLYS B 326 -26.958 -34.836 17.880 0.50 29.84 C ANISOU 2577 CG BLYS B 326 3313 3395 4628 733 313 392 C ATOM 2578 CD ALYS B 326 -28.768 -36.753 19.459 0.50 29.79 C ANISOU 2578 CD ALYS B 326 2924 3890 4507 -428 121 212 C ATOM 2579 CD BLYS B 326 -28.342 -34.370 18.328 0.50 34.96 C ANISOU 2579 CD BLYS B 326 4280 4193 4809 1037 203 362 C ATOM 2580 CE ALYS B 326 -29.715 -37.923 19.126 0.50 32.94 C ANISOU 2580 CE ALYS B 326 3549 4427 4540 -211 -61 241 C ATOM 2581 CE BLYS B 326 -28.858 -33.290 17.355 0.50 39.12 C ANISOU 2581 CE BLYS B 326 4897 5011 4955 1213 47 400 C ATOM 2582 NZ ALYS B 326 -29.576 -38.342 17.681 0.50 34.40 N ANISOU 2582 NZ ALYS B 326 3767 4751 4552 148 -368 201 N ATOM 2583 NZ BLYS B 326 -30.228 -32.800 17.763 0.50 42.63 N ANISOU 2583 NZ BLYS B 326 5508 5633 5054 977 44 348 N ATOM 2584 N ILE B 327 -23.595 -34.898 17.057 1.00 20.48 N ANISOU 2584 N ILE B 327 2105 1996 3681 -587 613 -25 N ATOM 2585 CA AILE B 327 -22.550 -33.889 16.821 0.50 20.34 C ANISOU 2585 CA AILE B 327 2196 1973 3558 -1039 362 224 C ATOM 2586 CA BILE B 327 -22.606 -33.835 16.923 0.50 20.28 C ANISOU 2586 CA BILE B 327 2382 1779 3545 -705 419 134 C ATOM 2587 C ILE B 327 -23.177 -32.725 16.081 1.00 20.37 C ANISOU 2587 C ILE B 327 2231 1886 3621 -679 77 208 C ATOM 2588 O ILE B 327 -23.787 -32.949 15.015 1.00 21.51 O ANISOU 2588 O ILE B 327 2259 2226 3689 -698 -289 27 O ATOM 2589 CB AILE B 327 -21.455 -34.469 15.875 0.50 20.37 C ANISOU 2589 CB AILE B 327 2334 2006 3400 -1023 295 175 C ATOM 2590 CB BILE B 327 -21.290 -34.355 16.323 0.50 20.84 C ANISOU 2590 CB BILE B 327 2887 1614 3419 -163 450 -111 C ATOM 2591 CG1AILE B 327 -20.832 -35.749 16.442 0.50 22.73 C ANISOU 2591 CG1AILE B 327 2561 2545 3530 -841 251 213 C ATOM 2592 CG1BILE B 327 -20.710 -35.460 17.204 0.50 20.48 C ANISOU 2592 CG1BILE B 327 3181 1372 3227 108 269 -318 C ATOM 2593 CG2AILE B 327 -20.359 -33.426 15.539 0.50 18.44 C ANISOU 2593 CG2AILE B 327 2113 1725 3171 -1165 -210 -31 C ATOM 2594 CG2BILE B 327 -20.270 -33.214 16.138 0.50 22.38 C ANISOU 2594 CG2BILE B 327 2998 2093 3413 -234 662 220 C ATOM 2595 CD1AILE B 327 -20.102 -35.521 17.707 0.50 24.29 C ANISOU 2595 CD1AILE B 327 2881 2811 3535 -558 343 68 C ATOM 2596 CD1BILE B 327 -19.758 -36.322 16.463 0.50 21.70 C ANISOU 2596 CD1BILE B 327 3493 1446 3308 230 371 -366 C ATOM 2597 N LYS B 328 -23.034 -31.509 16.592 1.00 19.08 N ANISOU 2597 N LYS B 328 1928 1609 3713 -509 -186 302 N ATOM 2598 CA LYS B 328 -23.582 -30.363 15.862 1.00 20.38 C ANISOU 2598 CA LYS B 328 2049 1748 3947 -341 -265 374 C ATOM 2599 C LYS B 328 -22.534 -29.273 15.890 1.00 19.85 C ANISOU 2599 C LYS B 328 1915 1864 3764 -580 -352 367 C ATOM 2600 O LYS B 328 -22.020 -28.927 16.967 1.00 17.82 O ANISOU 2600 O LYS B 328 1466 1694 3612 -286 -3 332 O ATOM 2601 CB LYS B 328 -24.843 -29.826 16.512 1.00 25.93 C ANISOU 2601 CB LYS B 328 3036 2461 4355 -148 -388 90 C ATOM 2602 CG LYS B 328 -25.580 -28.787 15.700 1.00 32.16 C ANISOU 2602 CG LYS B 328 4236 3299 4684 -660 -267 124 C ATOM 2603 CD LYS B 328 -26.794 -28.297 16.506 1.00 39.88 C ANISOU 2603 CD LYS B 328 5541 4639 4972 -451 16 289 C ATOM 2604 CE LYS B 328 -28.009 -28.001 15.635 1.00 44.34 C ANISOU 2604 CE LYS B 328 6329 5341 5176 -267 14 520 C ATOM 2605 NZ LYS B 328 -27.824 -26.769 14.793 1.00 47.69 N ANISOU 2605 NZ LYS B 328 6851 5896 5371 -354 -6 449 N ATOM 2606 N ILE B 329 -22.191 -28.793 14.697 1.00 21.61 N ANISOU 2606 N ILE B 329 2233 2378 3598 -699 -445 568 N ATOM 2607 CA ILE B 329 -21.312 -27.627 14.536 1.00 18.90 C ANISOU 2607 CA ILE B 329 1497 2202 3484 -626 -178 735 C ATOM 2608 C ILE B 329 -22.190 -26.429 14.209 1.00 20.25 C ANISOU 2608 C ILE B 329 1970 2359 3366 -210 -213 635 C ATOM 2609 O ILE B 329 -22.964 -26.480 13.238 1.00 22.34 O ANISOU 2609 O ILE B 329 2569 2497 3422 -363 -971 534 O ATOM 2610 CB ILE B 329 -20.249 -27.855 13.389 1.00 22.60 C ANISOU 2610 CB ILE B 329 2076 2805 3705 -1017 65 588 C ATOM 2611 CG1 ILE B 329 -19.534 -29.217 13.428 1.00 27.08 C ANISOU 2611 CG1 ILE B 329 3058 3423 3807 -624 -308 441 C ATOM 2612 CG2 ILE B 329 -19.272 -26.730 13.340 1.00 22.48 C ANISOU 2612 CG2 ILE B 329 1747 3034 3760 -1595 27 394 C ATOM 2613 CD1 ILE B 329 -18.867 -29.589 14.671 1.00 26.66 C ANISOU 2613 CD1 ILE B 329 2507 3904 3720 -446 -476 149 C ATOM 2614 N ILE B 330 -22.110 -25.392 15.036 1.00 18.52 N ANISOU 2614 N ILE B 330 2078 1578 3382 -276 -366 650 N ATOM 2615 CA ILE B 330 -22.868 -24.151 14.830 1.00 19.81 C ANISOU 2615 CA ILE B 330 2299 1882 3347 -175 28 552 C ATOM 2616 C ILE B 330 -21.856 -23.125 14.296 1.00 18.42 C ANISOU 2616 C ILE B 330 1922 1896 3183 -402 -243 757 C ATOM 2617 O ILE B 330 -20.910 -22.758 15.001 1.00 17.93 O ANISOU 2617 O ILE B 330 1715 1917 3180 -375 -322 599 O ATOM 2618 CB ILE B 330 -23.526 -23.653 16.144 1.00 23.17 C ANISOU 2618 CB ILE B 330 2525 2568 3709 -387 397 717 C ATOM 2619 CG1 ILE B 330 -24.521 -24.703 16.645 1.00 25.10 C ANISOU 2619 CG1 ILE B 330 2899 2732 3907 -881 51 919 C ATOM 2620 CG2 ILE B 330 -24.230 -22.317 15.941 1.00 23.90 C ANISOU 2620 CG2 ILE B 330 2436 2849 3795 -39 138 816 C ATOM 2621 CD1 ILE B 330 -23.953 -25.633 17.636 1.00 27.12 C ANISOU 2621 CD1 ILE B 330 2811 3202 4293 -1726 -63 879 C ATOM 2622 N ALA B 331 -22.043 -22.706 13.045 1.00 17.31 N ANISOU 2622 N ALA B 331 1544 1806 3225 -107 271 699 N ATOM 2623 CA ALA B 331 -21.094 -21.846 12.366 1.00 16.07 C ANISOU 2623 CA ALA B 331 1752 1199 3155 251 186 368 C ATOM 2624 C ALA B 331 -21.937 -20.756 11.694 1.00 14.68 C ANISOU 2624 C ALA B 331 933 1501 3145 324 -19 -100 C ATOM 2625 O ALA B 331 -22.311 -20.832 10.517 1.00 18.04 O ANISOU 2625 O ALA B 331 2064 1633 3159 159 -498 -152 O ATOM 2626 CB ALA B 331 -20.311 -22.643 11.345 1.00 18.72 C ANISOU 2626 CB ALA B 331 2239 1412 3463 551 66 122 C ATOM 2627 N PRO B 332 -22.255 -19.732 12.479 1.00 15.97 N ANISOU 2627 N PRO B 332 1477 1470 3122 -8 150 -32 N ATOM 2628 CA PRO B 332 -23.123 -18.688 11.952 1.00 18.70 C ANISOU 2628 CA PRO B 332 2298 1630 3179 341 430 -16 C ATOM 2629 C PRO B 332 -22.495 -17.874 10.834 1.00 17.82 C ANISOU 2629 C PRO B 332 1942 1721 3107 289 39 -111 C ATOM 2630 O PRO B 332 -21.297 -17.673 10.840 1.00 16.27 O ANISOU 2630 O PRO B 332 1834 1506 2843 168 -181 -95 O ATOM 2631 CB PRO B 332 -23.321 -17.768 13.184 1.00 22.11 C ANISOU 2631 CB PRO B 332 3339 1839 3222 837 732 4 C ATOM 2632 CG PRO B 332 -22.930 -18.520 14.324 1.00 21.87 C ANISOU 2632 CG PRO B 332 2171 2825 3314 52 209 -105 C ATOM 2633 CD PRO B 332 -21.928 -19.532 13.904 1.00 18.27 C ANISOU 2633 CD PRO B 332 2012 1896 3035 83 25 -294 C ATOM 2634 N PRO B 333 -23.326 -17.327 9.924 1.00 16.37 N ANISOU 2634 N PRO B 333 1142 1805 3273 -121 47 97 N ATOM 2635 CA PRO B 333 -22.706 -16.487 8.860 1.00 17.42 C ANISOU 2635 CA PRO B 333 948 2246 3426 -137 -389 358 C ATOM 2636 C PRO B 333 -21.980 -15.238 9.384 1.00 17.38 C ANISOU 2636 C PRO B 333 1440 1973 3191 68 -434 146 C ATOM 2637 O PRO B 333 -21.052 -14.757 8.716 1.00 18.36 O ANISOU 2637 O PRO B 333 1761 2125 3091 36 -629 583 O ATOM 2638 CB PRO B 333 -23.888 -16.150 7.902 1.00 21.32 C ANISOU 2638 CB PRO B 333 952 3520 3630 -88 -804 461 C ATOM 2639 CG PRO B 333 -25.089 -16.516 8.618 1.00 25.32 C ANISOU 2639 CG PRO B 333 2055 3751 3813 -33 -337 601 C ATOM 2640 CD PRO B 333 -24.773 -17.515 9.700 1.00 20.41 C ANISOU 2640 CD PRO B 333 1512 2628 3613 -16 -410 240 C ATOM 2641 N GLU B 334 -22.359 -14.747 10.568 1.00 16.62 N ANISOU 2641 N GLU B 334 1502 1687 3126 427 -462 95 N ATOM 2642 CA GLU B 334 -21.706 -13.564 11.143 1.00 16.29 C ANISOU 2642 CA GLU B 334 1112 1819 3260 585 -349 -134 C ATOM 2643 C GLU B 334 -20.560 -13.916 12.098 1.00 14.08 C ANISOU 2643 C GLU B 334 985 1518 2846 627 -245 18 C ATOM 2644 O GLU B 334 -20.128 -13.076 12.876 1.00 14.85 O ANISOU 2644 O GLU B 334 880 1912 2851 309 73 -106 O ATOM 2645 CB GLU B 334 -22.741 -12.697 11.888 1.00 19.54 C ANISOU 2645 CB GLU B 334 1410 2311 3702 381 -195 -701 C ATOM 2646 CG GLU B 334 -23.242 -13.259 13.199 1.00 18.75 C ANISOU 2646 CG GLU B 334 900 2422 3801 19 20 -1150 C ATOM 2647 CD GLU B 334 -24.329 -14.336 13.125 1.00 22.13 C ANISOU 2647 CD GLU B 334 1464 3168 3777 -25 -432 -1211 C ATOM 2648 OE1 GLU B 334 -24.827 -14.712 14.210 1.00 27.57 O ANISOU 2648 OE1 GLU B 334 2177 4235 4062 318 -152 -1425 O ATOM 2649 OE2 GLU B 334 -24.628 -14.884 12.028 1.00 20.42 O ANISOU 2649 OE2 GLU B 334 1471 2531 3757 451 -875 -584 O ATOM 2650 N ARG B 335 -20.082 -15.168 12.042 1.00 14.27 N ANISOU 2650 N ARG B 335 1396 1348 2678 696 -59 156 N ATOM 2651 CA ARG B 335 -19.166 -15.612 13.098 1.00 14.40 C ANISOU 2651 CA ARG B 335 1398 1292 2780 486 -145 -61 C ATOM 2652 C ARG B 335 -17.857 -14.866 13.191 1.00 14.53 C ANISOU 2652 C ARG B 335 1605 1250 2666 456 -221 -25 C ATOM 2653 O ARG B 335 -17.154 -14.968 14.229 1.00 14.95 O ANISOU 2653 O ARG B 335 1737 1369 2576 408 -164 -16 O ATOM 2654 CB ARG B 335 -18.927 -17.116 13.022 1.00 14.55 C ANISOU 2654 CB ARG B 335 1764 968 2796 321 189 -218 C ATOM 2655 CG ARG B 335 -18.255 -17.597 11.763 1.00 13.77 C ANISOU 2655 CG ARG B 335 1617 780 2835 605 20 -301 C ATOM 2656 CD ARG B 335 -18.354 -19.112 11.760 1.00 14.24 C ANISOU 2656 CD ARG B 335 1332 1136 2944 543 -250 -340 C ATOM 2657 NE ARG B 335 -17.731 -19.724 10.588 1.00 15.74 N ANISOU 2657 NE ARG B 335 1611 1210 3160 -123 -137 -464 N ATOM 2658 CZ ARG B 335 -18.351 -19.815 9.397 1.00 15.84 C ANISOU 2658 CZ ARG B 335 731 1904 3385 534 312 -738 C ATOM 2659 NH1 ARG B 335 -17.733 -20.404 8.340 1.00 19.51 N ANISOU 2659 NH1 ARG B 335 1510 2434 3467 458 721 -866 N ATOM 2660 NH2 ARG B 335 -19.585 -19.306 9.231 1.00 17.80 N ANISOU 2660 NH2 ARG B 335 1053 2075 3636 122 213 -593 N ATOM 2661 N LYS B 336 -17.469 -14.136 12.168 1.00 13.08 N ANISOU 2661 N LYS B 336 1066 1337 2568 376 70 -465 N ATOM 2662 CA ALYS B 336 -16.313 -13.262 12.255 0.50 18.26 C ANISOU 2662 CA ALYS B 336 1847 2295 2797 73 208 -406 C ATOM 2663 CA BLYS B 336 -16.306 -13.265 12.284 0.50 15.78 C ANISOU 2663 CA BLYS B 336 1412 1999 2585 -124 596 -260 C ATOM 2664 C LYS B 336 -16.491 -12.224 13.354 1.00 17.15 C ANISOU 2664 C LYS B 336 1281 2616 2617 -275 192 -542 C ATOM 2665 O LYS B 336 -15.543 -11.668 13.842 1.00 19.15 O ANISOU 2665 O LYS B 336 861 3341 3075 304 210 -786 O ATOM 2666 CB ALYS B 336 -16.122 -12.533 10.915 0.50 23.76 C ANISOU 2666 CB ALYS B 336 2808 3149 3071 -312 396 -382 C ATOM 2667 CB BLYS B 336 -16.028 -12.454 11.030 0.50 16.14 C ANISOU 2667 CB BLYS B 336 1361 2348 2424 -863 1504 -48 C ATOM 2668 CG ALYS B 336 -14.919 -11.741 10.611 0.50 29.06 C ANISOU 2668 CG ALYS B 336 3974 3652 3417 -89 41 -189 C ATOM 2669 CG BLYS B 336 -14.638 -11.957 11.126 0.50 21.24 C ANISOU 2669 CG BLYS B 336 2598 2809 2665 -511 876 234 C ATOM 2670 CD ALYS B 336 -15.195 -11.115 9.163 0.50 30.25 C ANISOU 2670 CD ALYS B 336 4220 3724 3551 -8 -49 -62 C ATOM 2671 CD BLYS B 336 -14.337 -10.991 10.065 0.50 21.50 C ANISOU 2671 CD BLYS B 336 2422 3030 2715 -976 708 639 C ATOM 2672 CE ALYS B 336 -13.956 -10.581 8.381 0.50 27.70 C ANISOU 2672 CE ALYS B 336 3752 3202 3569 872 -417 19 C ATOM 2673 CE BLYS B 336 -12.884 -10.594 10.133 0.50 22.02 C ANISOU 2673 CE BLYS B 336 2447 3070 2848 -463 505 232 C ATOM 2674 NZ ALYS B 336 -13.724 -10.744 6.923 0.50 20.64 N ANISOU 2674 NZ ALYS B 336 2405 2008 3431 1516 -843 -350 N ATOM 2675 NZ BLYS B 336 -12.836 -9.395 9.410 0.50 21.38 N ANISOU 2675 NZ BLYS B 336 2340 2761 3024 -806 227 142 N ATOM 2676 N TYR B 337 -17.731 -11.953 13.697 1.00 13.71 N ANISOU 2676 N TYR B 337 1671 1182 2356 284 320 37 N ATOM 2677 CA TYR B 337 -18.055 -10.923 14.718 1.00 12.92 C ANISOU 2677 CA TYR B 337 1694 985 2230 234 15 150 C ATOM 2678 C TYR B 337 -18.859 -11.503 15.903 1.00 13.17 C ANISOU 2678 C TYR B 337 1606 1121 2277 -79 125 136 C ATOM 2679 O TYR B 337 -19.396 -10.741 16.699 1.00 13.54 O ANISOU 2679 O TYR B 337 1439 1282 2422 40 432 -157 O ATOM 2680 CB TYR B 337 -18.902 -9.786 14.107 1.00 15.35 C ANISOU 2680 CB TYR B 337 2406 1091 2333 444 120 121 C ATOM 2681 CG TYR B 337 -18.201 -9.038 13.021 1.00 17.03 C ANISOU 2681 CG TYR B 337 2331 1735 2403 125 -252 129 C ATOM 2682 CD1 TYR B 337 -16.842 -8.788 13.097 1.00 17.07 C ANISOU 2682 CD1 TYR B 337 2173 1693 2619 -289 569 -132 C ATOM 2683 CD2 TYR B 337 -18.913 -8.490 11.968 1.00 21.71 C ANISOU 2683 CD2 TYR B 337 2892 2829 2527 -714 -282 654 C ATOM 2684 CE1 TYR B 337 -16.159 -8.081 12.084 1.00 17.50 C ANISOU 2684 CE1 TYR B 337 2577 1477 2595 -590 300 255 C ATOM 2685 CE2 TYR B 337 -18.253 -7.755 10.975 1.00 25.59 C ANISOU 2685 CE2 TYR B 337 3889 3171 2663 -1454 -275 1057 C ATOM 2686 CZ TYR B 337 -16.872 -7.595 11.048 1.00 24.73 C ANISOU 2686 CZ TYR B 337 3752 2931 2713 -1156 330 889 C ATOM 2687 OH TYR B 337 -16.193 -6.878 10.074 1.00 31.85 O ANISOU 2687 OH TYR B 337 5383 3901 2817 -1509 432 899 O ATOM 2688 N SER B 338 -18.979 -12.826 16.019 1.00 12.07 N ANISOU 2688 N SER B 338 1170 1099 2318 -103 127 179 N ATOM 2689 CA ASER B 338 -19.833 -13.408 17.071 0.50 11.66 C ANISOU 2689 CA ASER B 338 1363 907 2158 -411 249 81 C ATOM 2690 CA BSER B 338 -19.861 -13.362 17.061 0.50 13.25 C ANISOU 2690 CA BSER B 338 1494 1108 2431 -368 89 97 C ATOM 2691 C SER B 338 -19.401 -13.008 18.478 1.00 12.00 C ANISOU 2691 C SER B 338 1267 1002 2292 -354 -9 191 C ATOM 2692 O SER B 338 -20.230 -12.926 19.407 1.00 12.27 O ANISOU 2692 O SER B 338 820 1359 2483 -21 252 106 O ATOM 2693 CB ASER B 338 -19.890 -14.937 16.982 0.50 12.20 C ANISOU 2693 CB ASER B 338 1430 1059 2148 -563 246 81 C ATOM 2694 CB BSER B 338 -19.952 -14.858 16.944 0.50 16.84 C ANISOU 2694 CB BSER B 338 1869 1587 2942 -395 -168 67 C ATOM 2695 OG ASER B 338 -20.633 -15.378 15.856 0.50 10.41 O ANISOU 2695 OG ASER B 338 1176 865 1915 -7 444 77 O ATOM 2696 OG BSER B 338 -18.641 -15.342 17.025 0.50 19.16 O ANISOU 2696 OG BSER B 338 2026 1920 3332 43 -283 39 O ATOM 2697 N VAL B 339 -18.089 -12.875 18.710 1.00 12.41 N ANISOU 2697 N VAL B 339 1242 1213 2260 1 0 63 N ATOM 2698 CA VAL B 339 -17.642 -12.442 20.062 1.00 11.10 C ANISOU 2698 CA VAL B 339 1025 801 2392 129 397 39 C ATOM 2699 C VAL B 339 -18.248 -11.065 20.354 1.00 10.77 C ANISOU 2699 C VAL B 339 814 913 2366 251 236 84 C ATOM 2700 O VAL B 339 -18.867 -10.840 21.383 1.00 11.69 O ANISOU 2700 O VAL B 339 1161 972 2307 193 380 4 O ATOM 2701 CB VAL B 339 -16.120 -12.353 20.139 1.00 12.64 C ANISOU 2701 CB VAL B 339 1170 1183 2451 -26 302 -149 C ATOM 2702 CG1 VAL B 339 -15.725 -11.633 21.414 1.00 12.40 C ANISOU 2702 CG1 VAL B 339 1025 1378 2308 -283 339 78 C ATOM 2703 CG2 VAL B 339 -15.575 -13.782 20.067 1.00 15.87 C ANISOU 2703 CG2 VAL B 339 1384 1994 2653 636 -4 -16 C ATOM 2704 N TRP B 340 -18.057 -10.149 19.412 1.00 11.58 N ANISOU 2704 N TRP B 340 1285 899 2218 90 202 241 N ATOM 2705 CA TRP B 340 -18.576 -8.810 19.607 1.00 11.04 C ANISOU 2705 CA TRP B 340 920 960 2315 274 376 235 C ATOM 2706 C TRP B 340 -20.102 -8.862 19.792 1.00 10.35 C ANISOU 2706 C TRP B 340 887 766 2278 474 289 16 C ATOM 2707 O TRP B 340 -20.699 -8.189 20.669 1.00 12.14 O ANISOU 2707 O TRP B 340 1414 799 2398 184 456 -86 O ATOM 2708 CB TRP B 340 -18.219 -7.916 18.398 1.00 11.46 C ANISOU 2708 CB TRP B 340 1113 813 2428 25 232 38 C ATOM 2709 CG TRP B 340 -18.600 -6.497 18.711 1.00 13.06 C ANISOU 2709 CG TRP B 340 1580 921 2462 302 586 -228 C ATOM 2710 CD1 TRP B 340 -17.840 -5.549 19.368 1.00 13.65 C ANISOU 2710 CD1 TRP B 340 1702 953 2533 262 795 339 C ATOM 2711 CD2 TRP B 340 -19.889 -5.930 18.518 1.00 12.13 C ANISOU 2711 CD2 TRP B 340 1418 754 2438 -204 691 22 C ATOM 2712 NE1 TRP B 340 -18.611 -4.395 19.560 1.00 15.46 N ANISOU 2712 NE1 TRP B 340 1761 1402 2712 426 660 417 N ATOM 2713 CE2 TRP B 340 -19.855 -4.612 19.037 1.00 14.14 C ANISOU 2713 CE2 TRP B 340 1895 954 2525 281 366 350 C ATOM 2714 CE3 TRP B 340 -21.073 -6.407 17.957 1.00 13.41 C ANISOU 2714 CE3 TRP B 340 1447 1202 2446 232 650 193 C ATOM 2715 CZ2 TRP B 340 -20.995 -3.779 19.047 1.00 14.67 C ANISOU 2715 CZ2 TRP B 340 1691 1285 2598 251 73 446 C ATOM 2716 CZ3 TRP B 340 -22.226 -5.555 17.943 1.00 13.75 C ANISOU 2716 CZ3 TRP B 340 1494 1208 2523 583 610 453 C ATOM 2717 CH2 TRP B 340 -22.154 -4.261 18.484 1.00 14.58 C ANISOU 2717 CH2 TRP B 340 1687 1212 2639 549 539 393 C ATOM 2718 N ILE B 341 -20.761 -9.621 18.913 1.00 12.23 N ANISOU 2718 N ILE B 341 1062 1292 2293 51 198 281 N ATOM 2719 CA ILE B 341 -22.211 -9.729 18.968 1.00 12.75 C ANISOU 2719 CA ILE B 341 1326 1236 2282 140 34 64 C ATOM 2720 C ILE B 341 -22.695 -10.279 20.290 1.00 13.01 C ANISOU 2720 C ILE B 341 1590 1068 2286 373 51 -123 C ATOM 2721 O ILE B 341 -23.700 -9.795 20.865 1.00 12.96 O ANISOU 2721 O ILE B 341 1280 1162 2483 335 142 31 O ATOM 2722 CB ILE B 341 -22.746 -10.509 17.778 1.00 12.50 C ANISOU 2722 CB ILE B 341 583 1850 2315 76 45 -115 C ATOM 2723 CG1 ILE B 341 -22.477 -9.686 16.504 1.00 14.86 C ANISOU 2723 CG1 ILE B 341 1686 1774 2186 473 140 -124 C ATOM 2724 CG2 ILE B 341 -24.218 -10.853 17.970 1.00 13.71 C ANISOU 2724 CG2 ILE B 341 718 1989 2502 274 -258 -139 C ATOM 2725 CD1 ILE B 341 -22.737 -10.496 15.196 1.00 15.96 C ANISOU 2725 CD1 ILE B 341 1710 2253 2100 148 99 -452 C ATOM 2726 N GLY B 342 -21.999 -11.303 20.790 1.00 12.74 N ANISOU 2726 N GLY B 342 1427 1097 2317 89 346 207 N ATOM 2727 CA GLY B 342 -22.404 -11.829 22.107 1.00 11.98 C ANISOU 2727 CA GLY B 342 1210 1093 2250 11 435 126 C ATOM 2728 C GLY B 342 -22.223 -10.768 23.189 1.00 13.27 C ANISOU 2728 C GLY B 342 1348 1314 2379 75 244 85 C ATOM 2729 O GLY B 342 -23.027 -10.707 24.149 1.00 12.56 O ANISOU 2729 O GLY B 342 1119 1130 2522 165 43 -30 O ATOM 2730 N GLY B 343 -21.188 -9.936 23.042 1.00 11.25 N ANISOU 2730 N GLY B 343 1119 924 2233 237 5 -135 N ATOM 2731 CA GLY B 343 -21.058 -8.818 24.009 1.00 12.19 C ANISOU 2731 CA GLY B 343 1433 899 2299 371 146 -141 C ATOM 2732 C GLY B 343 -22.187 -7.812 23.889 1.00 12.24 C ANISOU 2732 C GLY B 343 1247 1180 2223 381 197 49 C ATOM 2733 O GLY B 343 -22.701 -7.306 24.900 1.00 13.70 O ANISOU 2733 O GLY B 343 1690 1132 2383 200 436 -78 O ATOM 2734 N SER B 344 -22.580 -7.517 22.659 1.00 13.06 N ANISOU 2734 N SER B 344 1154 1367 2440 289 149 502 N ATOM 2735 CA SER B 344 -23.683 -6.584 22.432 1.00 13.00 C ANISOU 2735 CA SER B 344 907 1572 2460 357 -75 397 C ATOM 2736 C SER B 344 -24.966 -7.121 23.031 1.00 13.11 C ANISOU 2736 C SER B 344 1144 1202 2636 477 271 89 C ATOM 2737 O SER B 344 -25.742 -6.381 23.666 1.00 15.41 O ANISOU 2737 O SER B 344 1548 1504 2804 778 709 115 O ATOM 2738 CB SER B 344 -23.860 -6.360 20.941 1.00 15.21 C ANISOU 2738 CB SER B 344 1554 1709 2517 495 -273 483 C ATOM 2739 OG SER B 344 -24.983 -5.515 20.692 1.00 16.07 O ANISOU 2739 OG SER B 344 1627 1745 2735 554 45 226 O ATOM 2740 N ILE B 345 -25.201 -8.424 22.857 1.00 13.21 N ANISOU 2740 N ILE B 345 1318 1015 2685 72 393 69 N ATOM 2741 CA ILE B 345 -26.389 -9.015 23.398 1.00 14.26 C ANISOU 2741 CA ILE B 345 1462 1400 2555 -72 276 -172 C ATOM 2742 C ILE B 345 -26.281 -8.960 24.943 1.00 13.13 C ANISOU 2742 C ILE B 345 1049 1458 2482 80 201 117 C ATOM 2743 O ILE B 345 -27.262 -8.552 25.643 1.00 14.35 O ANISOU 2743 O ILE B 345 1240 1683 2528 227 676 146 O ATOM 2744 CB ILE B 345 -26.493 -10.477 22.948 1.00 13.44 C ANISOU 2744 CB ILE B 345 1399 1073 2633 -278 22 -49 C ATOM 2745 CG1 ILE B 345 -26.934 -10.505 21.494 1.00 14.29 C ANISOU 2745 CG1 ILE B 345 1219 1540 2669 23 -199 -425 C ATOM 2746 CG2 ILE B 345 -27.550 -11.235 23.795 1.00 17.48 C ANISOU 2746 CG2 ILE B 345 1951 1675 3014 -272 228 16 C ATOM 2747 CD1 ILE B 345 -26.715 -11.880 20.829 1.00 16.04 C ANISOU 2747 CD1 ILE B 345 1719 1469 2908 -86 277 -540 C ATOM 2748 N LEU B 346 -25.169 -9.427 25.494 1.00 13.60 N ANISOU 2748 N LEU B 346 1444 1328 2398 222 -103 39 N ATOM 2749 CA LEU B 346 -25.078 -9.512 26.959 1.00 13.86 C ANISOU 2749 CA LEU B 346 1508 1329 2430 523 -174 98 C ATOM 2750 C LEU B 346 -25.199 -8.135 27.591 1.00 14.47 C ANISOU 2750 C LEU B 346 1726 1480 2292 290 351 112 C ATOM 2751 O LEU B 346 -25.955 -7.979 28.536 1.00 16.69 O ANISOU 2751 O LEU B 346 1941 1979 2422 548 499 107 O ATOM 2752 CB LEU B 346 -23.725 -10.109 27.331 1.00 14.28 C ANISOU 2752 CB LEU B 346 1296 1693 2436 79 114 365 C ATOM 2753 CG LEU B 346 -23.420 -10.320 28.816 1.00 14.03 C ANISOU 2753 CG LEU B 346 983 1851 2498 -150 548 375 C ATOM 2754 CD1 LEU B 346 -24.495 -11.280 29.433 1.00 15.47 C ANISOU 2754 CD1 LEU B 346 1410 1617 2853 -172 689 470 C ATOM 2755 CD2 LEU B 346 -21.933 -10.740 29.029 1.00 14.77 C ANISOU 2755 CD2 LEU B 346 1152 1904 2558 384 359 89 C ATOM 2756 N ALA B 347 -24.476 -7.152 27.065 1.00 13.11 N ANISOU 2756 N ALA B 347 1728 848 2406 277 56 -127 N ATOM 2757 CA ALA B 347 -24.480 -5.812 27.682 1.00 15.22 C ANISOU 2757 CA ALA B 347 2030 1200 2554 386 394 -35 C ATOM 2758 C ALA B 347 -25.869 -5.131 27.570 1.00 17.78 C ANISOU 2758 C ALA B 347 2324 1687 2745 532 575 -107 C ATOM 2759 O ALA B 347 -26.127 -4.155 28.315 1.00 18.28 O ANISOU 2759 O ALA B 347 2491 1574 2881 522 1025 -193 O ATOM 2760 CB ALA B 347 -23.434 -4.973 27.047 1.00 15.38 C ANISOU 2760 CB ALA B 347 1978 1426 2439 21 124 76 C ATOM 2761 N SER B 348 -26.715 -5.615 26.665 1.00 16.92 N ANISOU 2761 N SER B 348 1461 2117 2850 1182 574 430 N ATOM 2762 CA ASER B 348 -28.053 -5.087 26.442 0.50 17.79 C ANISOU 2762 CA ASER B 348 1449 2367 2941 771 387 369 C ATOM 2763 CA BSER B 348 -28.022 -5.011 26.490 0.50 16.43 C ANISOU 2763 CA BSER B 348 1378 2005 2860 682 450 71 C ATOM 2764 C SER B 348 -29.109 -5.768 27.280 1.00 18.75 C ANISOU 2764 C SER B 348 1913 2043 3168 607 483 -94 C ATOM 2765 O SER B 348 -30.280 -5.382 27.226 1.00 19.64 O ANISOU 2765 O SER B 348 1737 2290 3435 733 612 -59 O ATOM 2766 CB ASER B 348 -28.436 -5.309 24.987 0.50 23.07 C ANISOU 2766 CB ASER B 348 2129 3525 3113 1124 53 668 C ATOM 2767 CB BSER B 348 -28.357 -4.915 24.994 0.50 20.52 C ANISOU 2767 CB BSER B 348 2256 2641 2899 745 247 -27 C ATOM 2768 OG ASER B 348 -27.562 -4.593 24.179 0.50 25.59 O ANISOU 2768 OG ASER B 348 2330 4194 3198 1505 9 1024 O ATOM 2769 OG BSER B 348 -28.807 -6.169 24.511 0.50 22.76 O ANISOU 2769 OG BSER B 348 2757 2981 2909 1128 89 -458 O ATOM 2770 N LEU B 349 -28.739 -6.825 28.002 1.00 17.22 N ANISOU 2770 N LEU B 349 1997 1440 3108 373 501 -171 N ATOM 2771 CA LEU B 349 -29.775 -7.590 28.738 1.00 17.32 C ANISOU 2771 CA LEU B 349 1655 1448 3479 574 503 -206 C ATOM 2772 C LEU B 349 -30.070 -6.967 30.082 1.00 15.94 C ANISOU 2772 C LEU B 349 1070 1473 3514 296 667 -178 C ATOM 2773 O LEU B 349 -29.134 -6.592 30.807 1.00 15.68 O ANISOU 2773 O LEU B 349 1062 1459 3437 38 412 14 O ATOM 2774 CB LEU B 349 -29.311 -9.011 29.069 1.00 20.56 C ANISOU 2774 CB LEU B 349 2325 1856 3629 996 -95 -292 C ATOM 2775 CG LEU B 349 -29.227 -10.026 27.965 1.00 20.42 C ANISOU 2775 CG LEU B 349 2663 1576 3521 739 -381 -397 C ATOM 2776 CD1 LEU B 349 -28.732 -11.328 28.632 1.00 22.23 C ANISOU 2776 CD1 LEU B 349 3100 1764 3581 722 -451 -308 C ATOM 2777 CD2 LEU B 349 -30.561 -10.202 27.226 1.00 21.56 C ANISOU 2777 CD2 LEU B 349 2590 2016 3584 -269 -639 -595 C ATOM 2778 N SER B 350 -31.362 -6.928 30.454 1.00 18.64 N ANISOU 2778 N SER B 350 1385 1730 3970 308 558 217 N ATOM 2779 CA SER B 350 -31.710 -6.482 31.804 1.00 20.10 C ANISOU 2779 CA SER B 350 1525 1710 4403 191 679 268 C ATOM 2780 C SER B 350 -30.890 -7.235 32.834 1.00 20.51 C ANISOU 2780 C SER B 350 1834 1692 4265 777 1147 275 C ATOM 2781 O SER B 350 -30.379 -6.649 33.772 1.00 21.88 O ANISOU 2781 O SER B 350 2057 1998 4260 449 1470 177 O ATOM 2782 CB SER B 350 -33.207 -6.704 32.083 1.00 21.08 C ANISOU 2782 CB SER B 350 1239 1683 5089 252 465 208 C ATOM 2783 OG SER B 350 -33.571 -8.028 31.738 1.00 25.40 O ANISOU 2783 OG SER B 350 2085 2082 5482 238 495 630 O ATOM 2784 N THR B 351 -30.760 -8.559 32.616 1.00 18.65 N ANISOU 2784 N THR B 351 1633 1480 3972 409 1093 303 N ATOM 2785 CA THR B 351 -30.068 -9.444 33.561 1.00 18.32 C ANISOU 2785 CA THR B 351 1733 1696 3533 784 846 28 C ATOM 2786 C THR B 351 -28.621 -9.057 33.856 1.00 17.47 C ANISOU 2786 C THR B 351 1902 1455 3281 391 758 8 C ATOM 2787 O THR B 351 -28.100 -9.322 34.927 1.00 20.07 O ANISOU 2787 O THR B 351 2092 2436 3099 224 863 286 O ATOM 2788 CB THR B 351 -30.134 -10.907 33.009 1.00 17.05 C ANISOU 2788 CB THR B 351 2176 1161 3140 -58 462 -115 C ATOM 2789 OG1 THR B 351 -31.401 -11.106 32.349 1.00 18.57 O ANISOU 2789 OG1 THR B 351 2299 1837 2921 101 598 -239 O ATOM 2790 CG2 THR B 351 -29.919 -11.931 34.157 1.00 18.94 C ANISOU 2790 CG2 THR B 351 2171 1842 3182 -93 395 146 C ATOM 2791 N PHE B 352 -27.958 -8.444 32.875 1.00 15.82 N ANISOU 2791 N PHE B 352 1487 1471 3052 438 698 52 N ATOM 2792 CA PHE B 352 -26.573 -8.084 33.007 1.00 15.13 C ANISOU 2792 CA PHE B 352 1247 1812 2691 242 937 -71 C ATOM 2793 C PHE B 352 -26.349 -6.778 33.767 1.00 15.49 C ANISOU 2793 C PHE B 352 1647 1451 2787 358 749 -278 C ATOM 2794 O PHE B 352 -25.242 -6.497 34.191 1.00 18.01 O ANISOU 2794 O PHE B 352 2039 2038 2764 270 599 -142 O ATOM 2795 CB PHE B 352 -25.974 -7.959 31.585 1.00 14.09 C ANISOU 2795 CB PHE B 352 1042 1845 2465 275 982 -31 C ATOM 2796 CG PHE B 352 -24.516 -7.676 31.561 1.00 12.87 C ANISOU 2796 CG PHE B 352 809 1653 2427 210 660 -55 C ATOM 2797 CD1 PHE B 352 -23.559 -8.665 31.929 1.00 15.03 C ANISOU 2797 CD1 PHE B 352 1477 1840 2394 597 493 -17 C ATOM 2798 CD2 PHE B 352 -24.045 -6.434 31.236 1.00 15.42 C ANISOU 2798 CD2 PHE B 352 1805 1788 2266 3 462 -3 C ATOM 2799 CE1 PHE B 352 -22.162 -8.422 31.944 1.00 14.81 C ANISOU 2799 CE1 PHE B 352 1458 1752 2417 50 473 -379 C ATOM 2800 CE2 PHE B 352 -22.662 -6.202 31.217 1.00 16.28 C ANISOU 2800 CE2 PHE B 352 2036 1839 2310 288 259 -97 C ATOM 2801 CZ PHE B 352 -21.721 -7.189 31.584 1.00 16.21 C ANISOU 2801 CZ PHE B 352 1809 1903 2449 -120 308 107 C ATOM 2802 N GLN B 353 -27.370 -5.916 33.854 1.00 16.32 N ANISOU 2802 N GLN B 353 1962 1432 2809 210 668 -182 N ATOM 2803 CA GLN B 353 -27.089 -4.557 34.363 1.00 16.92 C ANISOU 2803 CA GLN B 353 1717 1779 2934 261 558 7 C ATOM 2804 C GLN B 353 -26.571 -4.582 35.799 1.00 18.21 C ANISOU 2804 C GLN B 353 2190 1854 2877 155 985 -175 C ATOM 2805 O GLN B 353 -25.764 -3.751 36.179 1.00 19.32 O ANISOU 2805 O GLN B 353 2515 2029 2796 -4 812 -78 O ATOM 2806 CB GLN B 353 -28.308 -3.653 34.218 1.00 18.17 C ANISOU 2806 CB GLN B 353 1567 2155 3180 435 828 -46 C ATOM 2807 CG GLN B 353 -28.840 -3.590 32.794 1.00 18.97 C ANISOU 2807 CG GLN B 353 1600 2422 3186 323 880 239 C ATOM 2808 CD GLN B 353 -27.730 -3.267 31.805 1.00 15.73 C ANISOU 2808 CD GLN B 353 1472 1408 3097 525 850 57 C ATOM 2809 OE1 GLN B 353 -27.047 -2.249 31.961 1.00 18.12 O ANISOU 2809 OE1 GLN B 353 2197 1376 3312 292 703 -299 O ATOM 2810 NE2 GLN B 353 -27.508 -4.160 30.811 1.00 15.90 N ANISOU 2810 NE2 GLN B 353 1478 1555 3008 471 944 -58 N ATOM 2811 N GLN B 354 -27.061 -5.540 36.602 1.00 18.63 N ANISOU 2811 N GLN B 354 2214 1900 2963 -39 1112 62 N ATOM 2812 CA GLN B 354 -26.549 -5.691 37.955 1.00 19.18 C ANISOU 2812 CA GLN B 354 2412 1953 2922 -630 953 -130 C ATOM 2813 C GLN B 354 -25.106 -6.175 38.025 1.00 18.46 C ANISOU 2813 C GLN B 354 2291 1973 2748 -289 716 -213 C ATOM 2814 O GLN B 354 -24.496 -6.200 39.090 1.00 22.98 O ANISOU 2814 O GLN B 354 3505 2560 2666 -236 715 -391 O ATOM 2815 CB GLN B 354 -27.453 -6.634 38.758 1.00 21.15 C ANISOU 2815 CB GLN B 354 3073 1978 2985 -613 890 -279 C ATOM 2816 CG GLN B 354 -27.455 -8.004 38.146 1.00 22.04 C ANISOU 2816 CG GLN B 354 3270 2020 3083 -617 910 72 C ATOM 2817 CD GLN B 354 -28.598 -8.849 38.605 1.00 25.38 C ANISOU 2817 CD GLN B 354 3651 2954 3038 -1139 991 56 C ATOM 2818 OE1 GLN B 354 -28.932 -8.855 39.799 1.00 30.37 O ANISOU 2818 OE1 GLN B 354 4162 4137 3241 -1614 1025 298 O ATOM 2819 NE2 GLN B 354 -29.194 -9.606 37.675 1.00 24.17 N ANISOU 2819 NE2 GLN B 354 3601 2640 2940 -853 1108 166 N ATOM 2820 N MET B 355 -24.551 -6.607 36.877 1.00 17.54 N ANISOU 2820 N MET B 355 2225 1684 2754 -260 872 -102 N ATOM 2821 CA MET B 355 -23.243 -7.239 36.828 1.00 16.92 C ANISOU 2821 CA MET B 355 2202 1450 2776 -255 355 -189 C ATOM 2822 C MET B 355 -22.095 -6.282 36.540 1.00 16.81 C ANISOU 2822 C MET B 355 2265 1370 2751 -516 435 -225 C ATOM 2823 O MET B 355 -20.932 -6.626 36.808 1.00 19.35 O ANISOU 2823 O MET B 355 2832 1682 2839 -480 34 -155 O ATOM 2824 CB MET B 355 -23.233 -8.349 35.776 1.00 14.46 C ANISOU 2824 CB MET B 355 1061 1439 2994 -321 554 -387 C ATOM 2825 CG MET B 355 -24.281 -9.358 36.069 1.00 17.21 C ANISOU 2825 CG MET B 355 2059 1344 3137 -607 216 -261 C ATOM 2826 SD MET B 355 -24.186 -10.759 34.985 1.00 22.01 S ANISOU 2826 SD MET B 355 3273 1586 3503 -505 93 -51 S ATOM 2827 CE MET B 355 -25.591 -11.690 35.668 1.00 22.22 C ANISOU 2827 CE MET B 355 3019 1798 3627 -788 -547 -210 C ATOM 2828 N TRP B 356 -22.409 -5.099 35.977 1.00 15.87 N ANISOU 2828 N TRP B 356 2213 1197 2621 -169 538 -56 N ATOM 2829 CA TRP B 356 -21.320 -4.141 35.728 1.00 16.19 C ANISOU 2829 CA TRP B 356 2026 1509 2616 -670 250 -24 C ATOM 2830 C TRP B 356 -20.517 -3.892 37.019 1.00 16.05 C ANISOU 2830 C TRP B 356 2065 1597 2438 -533 395 -152 C ATOM 2831 O TRP B 356 -21.102 -3.854 38.119 1.00 18.85 O ANISOU 2831 O TRP B 356 2501 2054 2607 -477 842 -373 O ATOM 2832 CB TRP B 356 -21.861 -2.798 35.305 1.00 17.95 C ANISOU 2832 CB TRP B 356 2864 1169 2786 105 322 112 C ATOM 2833 CG TRP B 356 -22.587 -2.752 34.000 1.00 15.02 C ANISOU 2833 CG TRP B 356 1904 1059 2745 -228 266 -14 C ATOM 2834 CD1 TRP B 356 -23.922 -2.645 33.798 1.00 15.74 C ANISOU 2834 CD1 TRP B 356 1947 1203 2830 -216 425 121 C ATOM 2835 CD2 TRP B 356 -21.986 -2.789 32.714 1.00 15.98 C ANISOU 2835 CD2 TRP B 356 2199 1205 2668 -586 218 341 C ATOM 2836 NE1 TRP B 356 -24.210 -2.621 32.434 1.00 14.94 N ANISOU 2836 NE1 TRP B 356 1418 1375 2885 -14 658 51 N ATOM 2837 CE2 TRP B 356 -23.017 -2.695 31.757 1.00 14.29 C ANISOU 2837 CE2 TRP B 356 1429 1331 2670 -202 472 116 C ATOM 2838 CE3 TRP B 356 -20.658 -2.885 32.286 1.00 16.56 C ANISOU 2838 CE3 TRP B 356 2640 1022 2631 -129 413 311 C ATOM 2839 CZ2 TRP B 356 -22.760 -2.680 30.375 1.00 14.84 C ANISOU 2839 CZ2 TRP B 356 1556 1259 2825 367 422 224 C ATOM 2840 CZ3 TRP B 356 -20.380 -2.878 30.898 1.00 16.42 C ANISOU 2840 CZ3 TRP B 356 2577 972 2691 -40 279 266 C ATOM 2841 CH2 TRP B 356 -21.432 -2.778 29.976 1.00 14.40 C ANISOU 2841 CH2 TRP B 356 1373 1346 2751 277 189 -2 C ATOM 2842 N ILE B 357 -19.208 -3.714 36.892 1.00 16.66 N ANISOU 2842 N ILE B 357 2335 1548 2446 -375 -206 -185 N ATOM 2843 CA ILE B 357 -18.389 -3.163 37.983 1.00 17.64 C ANISOU 2843 CA ILE B 357 2776 1347 2579 -153 -163 -60 C ATOM 2844 C ILE B 357 -18.620 -1.637 37.915 1.00 16.72 C ANISOU 2844 C ILE B 357 2312 1472 2568 -260 -44 -38 C ATOM 2845 O ILE B 357 -18.411 -1.022 36.866 1.00 16.04 O ANISOU 2845 O ILE B 357 2171 1473 2452 -229 298 -50 O ATOM 2846 CB ILE B 357 -16.877 -3.414 37.810 1.00 19.40 C ANISOU 2846 CB ILE B 357 3008 1466 2897 11 -168 -163 C ATOM 2847 CG1 ILE B 357 -16.525 -4.905 37.679 1.00 21.73 C ANISOU 2847 CG1 ILE B 357 3077 1988 3189 512 -58 134 C ATOM 2848 CG2 ILE B 357 -16.102 -2.783 38.997 1.00 19.37 C ANISOU 2848 CG2 ILE B 357 2958 1659 2744 101 -375 -307 C ATOM 2849 CD1 ILE B 357 -15.109 -5.110 37.154 1.00 23.05 C ANISOU 2849 CD1 ILE B 357 3174 2171 3412 586 306 -43 C ATOM 2850 N THR B 358 -19.056 -1.025 39.016 1.00 16.84 N ANISOU 2850 N THR B 358 1996 1621 2780 208 340 -347 N ATOM 2851 CA THR B 358 -19.248 0.415 38.996 1.00 17.09 C ANISOU 2851 CA THR B 358 1992 1708 2793 -187 490 -411 C ATOM 2852 C THR B 358 -17.999 1.120 39.462 1.00 16.53 C ANISOU 2852 C THR B 358 1995 1574 2710 263 329 -212 C ATOM 2853 O THR B 358 -17.151 0.526 40.127 1.00 17.01 O ANISOU 2853 O THR B 358 1958 1796 2708 115 -157 -207 O ATOM 2854 CB THR B 358 -20.409 0.859 39.907 1.00 19.73 C ANISOU 2854 CB THR B 358 1911 2506 3079 -116 512 -715 C ATOM 2855 OG1 THR B 358 -20.085 0.547 41.269 1.00 22.47 O ANISOU 2855 OG1 THR B 358 3236 2493 2808 -298 701 -545 O ATOM 2856 CG2 THR B 358 -21.711 0.183 39.471 1.00 21.72 C ANISOU 2856 CG2 THR B 358 1902 2824 3525 -474 477 -766 C ATOM 2857 N LYS B 359 -17.865 2.406 39.137 1.00 18.02 N ANISOU 2857 N LYS B 359 2575 1494 2778 49 296 -178 N ATOM 2858 CA ALYS B 359 -16.714 3.178 39.611 0.50 19.32 C ANISOU 2858 CA ALYS B 359 2877 1513 2950 -271 169 -345 C ATOM 2859 CA BLYS B 359 -16.711 3.174 39.608 0.50 20.66 C ANISOU 2859 CA BLYS B 359 3097 1834 2920 -283 198 -330 C ATOM 2860 C LYS B 359 -16.668 3.178 41.144 1.00 20.15 C ANISOU 2860 C LYS B 359 2974 1818 2862 -374 199 -303 C ATOM 2861 O LYS B 359 -15.618 3.048 41.711 1.00 20.44 O ANISOU 2861 O LYS B 359 2978 2005 2784 -305 -65 -489 O ATOM 2862 CB ALYS B 359 -16.756 4.614 39.069 0.50 18.16 C ANISOU 2862 CB ALYS B 359 2522 1111 3268 -108 -6 -417 C ATOM 2863 CB BLYS B 359 -16.736 4.606 39.051 0.50 22.48 C ANISOU 2863 CB BLYS B 359 3255 2112 3176 -205 78 -410 C ATOM 2864 CG ALYS B 359 -15.707 5.558 39.618 0.50 20.34 C ANISOU 2864 CG ALYS B 359 2484 1651 3594 35 55 -401 C ATOM 2865 CG BLYS B 359 -15.538 5.473 39.396 0.50 26.73 C ANISOU 2865 CG BLYS B 359 3651 3048 3457 -82 137 -428 C ATOM 2866 CD ALYS B 359 -14.308 5.035 39.377 0.50 22.63 C ANISOU 2866 CD ALYS B 359 2799 1919 3882 -314 -41 -250 C ATOM 2867 CD BLYS B 359 -14.222 4.817 39.019 0.50 29.55 C ANISOU 2867 CD BLYS B 359 3876 3694 3659 -255 106 -329 C ATOM 2868 CE ALYS B 359 -13.268 6.169 39.329 0.50 25.56 C ANISOU 2868 CE ALYS B 359 3512 2132 4066 -694 -122 -240 C ATOM 2869 CE BLYS B 359 -12.999 5.684 39.398 0.50 31.71 C ANISOU 2869 CE BLYS B 359 4137 4102 3810 -434 133 -226 C ATOM 2870 NZ ALYS B 359 -13.055 6.834 40.644 0.50 25.52 N ANISOU 2870 NZ ALYS B 359 3496 2071 4130 -449 -166 -622 N ATOM 2871 NZ BLYS B 359 -12.915 6.970 38.642 0.50 32.29 N ANISOU 2871 NZ BLYS B 359 4100 4334 3835 -597 227 -89 N ATOM 2872 N GLN B 360 -17.838 3.314 41.793 1.00 19.06 N ANISOU 2872 N GLN B 360 2514 2065 2664 -256 687 -397 N ATOM 2873 CA GLN B 360 -17.885 3.233 43.269 1.00 20.30 C ANISOU 2873 CA GLN B 360 2428 2497 2788 -164 379 -518 C ATOM 2874 C GLN B 360 -17.285 1.896 43.769 1.00 21.31 C ANISOU 2874 C GLN B 360 3100 2263 2734 1 90 -489 C ATOM 2875 O GLN B 360 -16.493 1.867 44.689 1.00 22.70 O ANISOU 2875 O GLN B 360 3391 2568 2665 217 -324 -634 O ATOM 2876 CB GLN B 360 -19.297 3.444 43.809 1.00 23.68 C ANISOU 2876 CB GLN B 360 2812 3176 3011 54 835 -538 C ATOM 2877 CG GLN B 360 -19.288 3.375 45.360 1.00 26.62 C ANISOU 2877 CG GLN B 360 2953 3924 3236 19 907 -686 C ATOM 2878 CD GLN B 360 -20.623 3.717 45.990 1.00 31.83 C ANISOU 2878 CD GLN B 360 3521 4910 3663 317 805 -493 C ATOM 2879 OE1 GLN B 360 -21.625 3.860 45.299 1.00 34.79 O ANISOU 2879 OE1 GLN B 360 3539 5685 3993 708 839 -403 O ATOM 2880 NE2 GLN B 360 -20.641 3.852 47.321 1.00 34.52 N ANISOU 2880 NE2 GLN B 360 4026 5162 3928 20 866 -109 N ATOM 2881 N GLU B 361 -17.654 0.779 43.142 1.00 20.27 N ANISOU 2881 N GLU B 361 2850 2095 2759 211 535 -569 N ATOM 2882 CA GLU B 361 -17.085 -0.510 43.544 1.00 22.34 C ANISOU 2882 CA GLU B 361 3282 2342 2865 -82 72 -70 C ATOM 2883 C GLU B 361 -15.580 -0.566 43.352 1.00 21.80 C ANISOU 2883 C GLU B 361 3042 2387 2852 343 -177 -88 C ATOM 2884 O GLU B 361 -14.825 -1.115 44.167 1.00 23.82 O ANISOU 2884 O GLU B 361 3330 2741 2980 442 0 -337 O ATOM 2885 CB GLU B 361 -17.731 -1.666 42.787 1.00 23.50 C ANISOU 2885 CB GLU B 361 3455 2539 2935 -974 -160 -27 C ATOM 2886 CG GLU B 361 -19.125 -2.003 43.260 1.00 27.05 C ANISOU 2886 CG GLU B 361 4048 3149 3080 -883 152 -33 C ATOM 2887 CD GLU B 361 -19.826 -3.012 42.348 1.00 30.97 C ANISOU 2887 CD GLU B 361 4553 3834 3379 -1125 398 145 C ATOM 2888 OE1 GLU B 361 -20.514 -3.906 42.868 1.00 35.85 O ANISOU 2888 OE1 GLU B 361 5618 4213 3792 -1398 415 206 O ATOM 2889 OE2 GLU B 361 -19.709 -2.928 41.118 1.00 28.99 O ANISOU 2889 OE2 GLU B 361 4299 3465 3252 -1080 581 245 O ATOM 2890 N TYR B 362 -15.130 -0.028 42.225 1.00 20.67 N ANISOU 2890 N TYR B 362 2834 2324 2696 473 -332 -153 N ATOM 2891 CA TYR B 362 -13.708 0.006 41.924 1.00 21.73 C ANISOU 2891 CA TYR B 362 2721 2830 2703 503 -273 -445 C ATOM 2892 C TYR B 362 -12.980 0.856 42.980 1.00 23.08 C ANISOU 2892 C TYR B 362 3081 2761 2926 640 -441 -500 C ATOM 2893 O TYR B 362 -11.900 0.499 43.451 1.00 22.66 O ANISOU 2893 O TYR B 362 2706 3083 2821 717 -796 -835 O ATOM 2894 CB TYR B 362 -13.452 0.560 40.512 1.00 20.98 C ANISOU 2894 CB TYR B 362 2234 2837 2901 834 -95 -565 C ATOM 2895 CG TYR B 362 -11.975 0.714 40.225 1.00 20.72 C ANISOU 2895 CG TYR B 362 1794 2979 3099 283 -202 -604 C ATOM 2896 CD1 TYR B 362 -11.216 -0.387 39.826 1.00 23.23 C ANISOU 2896 CD1 TYR B 362 2614 3040 3170 -94 -480 -367 C ATOM 2897 CD2 TYR B 362 -11.319 1.933 40.425 1.00 21.40 C ANISOU 2897 CD2 TYR B 362 2015 2891 3227 89 -149 -308 C ATOM 2898 CE1 TYR B 362 -9.878 -0.266 39.582 1.00 23.83 C ANISOU 2898 CE1 TYR B 362 2740 3047 3266 -558 -479 -605 C ATOM 2899 CE2 TYR B 362 -9.972 2.057 40.187 1.00 22.24 C ANISOU 2899 CE2 TYR B 362 2198 2940 3311 94 84 -579 C ATOM 2900 CZ TYR B 362 -9.245 0.958 39.783 1.00 25.19 C ANISOU 2900 CZ TYR B 362 2917 3226 3429 -248 -83 -703 C ATOM 2901 OH TYR B 362 -7.899 1.126 39.561 1.00 26.51 O ANISOU 2901 OH TYR B 362 2900 3696 3477 -223 -55 -637 O ATOM 2902 N ASP B 363 -13.565 1.995 43.331 1.00 23.88 N ANISOU 2902 N ASP B 363 3274 2683 3116 265 -244 -1037 N ATOM 2903 CA ASP B 363 -12.918 2.874 44.300 1.00 25.84 C ANISOU 2903 CA ASP B 363 3613 2699 3505 406 -582 -1048 C ATOM 2904 C ASP B 363 -12.735 2.171 45.643 1.00 27.05 C ANISOU 2904 C ASP B 363 3803 2944 3533 366 -810 -941 C ATOM 2905 O ASP B 363 -11.715 2.355 46.331 1.00 28.86 O ANISOU 2905 O ASP B 363 3660 3614 3692 -44 -907 -872 O ATOM 2906 CB ASP B 363 -13.750 4.137 44.496 1.00 24.97 C ANISOU 2906 CB ASP B 363 3303 2189 3996 305 -606 -945 C ATOM 2907 CG ASP B 363 -13.561 5.128 43.399 1.00 28.39 C ANISOU 2907 CG ASP B 363 3390 2892 4503 390 -776 -721 C ATOM 2908 OD1 ASP B 363 -14.384 6.062 43.285 1.00 30.09 O ANISOU 2908 OD1 ASP B 363 3684 2914 4836 542 -865 -711 O ATOM 2909 OD2 ASP B 363 -12.601 4.999 42.632 1.00 27.48 O ANISOU 2909 OD2 ASP B 363 2903 2965 4575 -47 -708 -747 O ATOM 2910 N GLU B 364 -13.719 1.377 46.018 1.00 28.60 N ANISOU 2910 N GLU B 364 4354 3174 3340 444 -759 -738 N ATOM 2911 CA GLU B 364 -13.710 0.741 47.326 1.00 31.26 C ANISOU 2911 CA GLU B 364 5046 3458 3373 753 -645 -534 C ATOM 2912 C GLU B 364 -12.814 -0.495 47.364 1.00 32.49 C ANISOU 2912 C GLU B 364 5259 3731 3355 728 -790 -627 C ATOM 2913 O GLU B 364 -12.228 -0.818 48.403 1.00 35.78 O ANISOU 2913 O GLU B 364 5816 4352 3426 671 -1134 -732 O ATOM 2914 CB GLU B 364 -15.148 0.482 47.783 1.00 35.23 C ANISOU 2914 CB GLU B 364 5451 4360 3573 536 -489 -433 C ATOM 2915 CG GLU B 364 -15.871 1.831 48.037 1.00 38.84 C ANISOU 2915 CG GLU B 364 5820 4966 3973 594 -229 -443 C ATOM 2916 CD GLU B 364 -17.376 1.752 48.344 1.00 43.32 C ANISOU 2916 CD GLU B 364 6420 5734 4305 350 -66 -371 C ATOM 2917 OE1 GLU B 364 -17.959 0.643 48.368 1.00 44.94 O ANISOU 2917 OE1 GLU B 364 6587 5922 4568 -190 -47 -278 O ATOM 2918 OE2 GLU B 364 -17.979 2.841 48.551 1.00 44.25 O ANISOU 2918 OE2 GLU B 364 6458 6208 4148 382 225 -502 O ATOM 2919 N ALA B 365 -12.667 -1.173 46.220 1.00 29.40 N ANISOU 2919 N ALA B 365 4630 3219 3323 733 -452 -562 N ATOM 2920 CA ALA B 365 -12.019 -2.492 46.210 1.00 27.09 C ANISOU 2920 CA ALA B 365 4110 2804 3381 714 -647 -335 C ATOM 2921 C ALA B 365 -10.718 -2.553 45.413 1.00 27.36 C ANISOU 2921 C ALA B 365 3993 2795 3609 399 -863 -264 C ATOM 2922 O ALA B 365 -9.887 -3.443 45.632 1.00 29.96 O ANISOU 2922 O ALA B 365 4268 3290 3827 865 -1290 -166 O ATOM 2923 CB ALA B 365 -13.001 -3.557 45.727 1.00 27.30 C ANISOU 2923 CB ALA B 365 4063 2885 3424 0 -317 -333 C ATOM 2924 N GLY B 366 -10.529 -1.616 44.490 1.00 26.37 N ANISOU 2924 N GLY B 366 3610 2881 3529 -257 -668 -410 N ATOM 2925 CA GLY B 366 -9.349 -1.594 43.623 1.00 24.95 C ANISOU 2925 CA GLY B 366 3282 2606 3592 -8 -380 -668 C ATOM 2926 C GLY B 366 -9.456 -2.578 42.443 1.00 25.30 C ANISOU 2926 C GLY B 366 3056 2937 3621 -152 -434 -367 C ATOM 2927 O GLY B 366 -10.463 -3.263 42.300 1.00 24.73 O ANISOU 2927 O GLY B 366 3089 2808 3497 86 -433 -189 O ATOM 2928 N PRO B 367 -8.398 -2.666 41.611 1.00 24.83 N ANISOU 2928 N PRO B 367 2537 3170 3727 -31 -365 -725 N ATOM 2929 CA PRO B 367 -8.486 -3.516 40.390 1.00 23.90 C ANISOU 2929 CA PRO B 367 2392 2911 3780 -282 -490 -789 C ATOM 2930 C PRO B 367 -8.830 -4.980 40.619 1.00 25.62 C ANISOU 2930 C PRO B 367 3036 3042 3655 129 -604 -629 C ATOM 2931 O PRO B 367 -9.379 -5.608 39.725 1.00 25.42 O ANISOU 2931 O PRO B 367 3005 3042 3612 -32 -622 -863 O ATOM 2932 CB PRO B 367 -7.077 -3.434 39.774 1.00 26.60 C ANISOU 2932 CB PRO B 367 2437 3649 4020 -41 -570 -773 C ATOM 2933 CG PRO B 367 -6.443 -2.221 40.385 1.00 28.19 C ANISOU 2933 CG PRO B 367 2689 3992 4028 -660 -659 -918 C ATOM 2934 CD PRO B 367 -7.055 -2.069 41.762 1.00 27.00 C ANISOU 2934 CD PRO B 367 2512 3801 3944 -318 -444 -1005 C ATOM 2935 N SER B 368 -8.521 -5.538 41.785 1.00 26.60 N ANISOU 2935 N SER B 368 3620 2947 3540 91 -860 -535 N ATOM 2936 CA SER B 368 -8.787 -6.958 42.028 1.00 27.47 C ANISOU 2936 CA SER B 368 3653 3272 3512 -275 -912 -338 C ATOM 2937 C SER B 368 -10.294 -7.253 42.055 1.00 27.64 C ANISOU 2937 C SER B 368 3809 3286 3405 -135 -543 -357 C ATOM 2938 O SER B 368 -10.700 -8.418 42.027 1.00 29.02 O ANISOU 2938 O SER B 368 3979 3654 3393 -642 -413 -242 O ATOM 2939 CB SER B 368 -8.097 -7.419 43.331 1.00 31.26 C ANISOU 2939 CB SER B 368 4404 3886 3590 91 -1006 -162 C ATOM 2940 OG SER B 368 -8.766 -6.878 44.458 1.00 35.83 O ANISOU 2940 OG SER B 368 5284 4666 3664 20 -1226 -98 O ATOM 2941 N ILE B 369 -11.133 -6.217 42.126 1.00 24.63 N ANISOU 2941 N ILE B 369 3220 2835 3304 -157 -418 -391 N ATOM 2942 CA ILE B 369 -12.567 -6.444 42.068 1.00 23.91 C ANISOU 2942 CA ILE B 369 2801 2909 3377 28 -284 -680 C ATOM 2943 C ILE B 369 -12.978 -7.185 40.775 1.00 23.85 C ANISOU 2943 C ILE B 369 2654 3149 3261 -451 -48 -543 C ATOM 2944 O ILE B 369 -14.046 -7.781 40.729 1.00 23.44 O ANISOU 2944 O ILE B 369 2818 2823 3266 -495 -169 -340 O ATOM 2945 CB ILE B 369 -13.371 -5.136 42.207 1.00 28.08 C ANISOU 2945 CB ILE B 369 3018 3720 3933 143 -445 -999 C ATOM 2946 CG1 ILE B 369 -14.793 -5.494 42.682 1.00 33.51 C ANISOU 2946 CG1 ILE B 369 3562 4631 4539 183 -690 -1118 C ATOM 2947 CG2 ILE B 369 -13.237 -4.260 40.943 1.00 27.61 C ANISOU 2947 CG2 ILE B 369 2842 3652 3999 366 -936 -1296 C ATOM 2948 CD1 ILE B 369 -15.724 -4.369 42.834 1.00 39.77 C ANISOU 2948 CD1 ILE B 369 4681 5515 4915 274 -539 -917 C ATOM 2949 N VAL B 370 -12.174 -7.168 39.774 1.00 22.40 N ANISOU 2949 N VAL B 370 2726 2668 3118 -306 -254 -290 N ATOM 2950 CA VAL B 370 -12.471 -7.834 38.529 1.00 21.13 C ANISOU 2950 CA VAL B 370 2559 2378 3090 -333 -126 -254 C ATOM 2951 C VAL B 370 -12.626 -9.315 38.673 1.00 23.81 C ANISOU 2951 C VAL B 370 2991 2763 3292 -97 -223 -67 C ATOM 2952 O VAL B 370 -13.357 -9.880 38.025 1.00 22.67 O ANISOU 2952 O VAL B 370 2590 2701 3321 -401 -106 -99 O ATOM 2953 CB VAL B 370 -11.487 -7.439 37.420 1.00 21.80 C ANISOU 2953 CB VAL B 370 2886 2348 3050 -297 -351 -408 C ATOM 2954 CG1 VAL B 370 -10.223 -7.999 37.583 1.00 23.48 C ANISOU 2954 CG1 VAL B 370 3069 2721 3131 -350 -92 -693 C ATOM 2955 CG2 VAL B 370 -11.947 -7.885 36.077 1.00 21.61 C ANISOU 2955 CG2 VAL B 370 2885 2128 3199 -757 -503 -203 C ATOM 2956 N HIS B 371 -11.883 -9.887 39.576 1.00 23.50 N ANISOU 2956 N HIS B 371 3086 2420 3423 -175 -130 50 N ATOM 2957 CA HIS B 371 -11.936 -11.315 39.780 1.00 26.66 C ANISOU 2957 CA HIS B 371 3432 2950 3746 2 -244 278 C ATOM 2958 C HIS B 371 -13.194 -11.751 40.484 1.00 28.94 C ANISOU 2958 C HIS B 371 3975 3288 3734 255 -71 463 C ATOM 2959 O HIS B 371 -13.702 -12.694 40.258 1.00 29.94 O ANISOU 2959 O HIS B 371 4107 3354 3916 -115 276 643 O ATOM 2960 CB HIS B 371 -10.723 -11.833 40.510 1.00 27.46 C ANISOU 2960 CB HIS B 371 3042 3335 4056 -175 -278 76 C ATOM 2961 CG HIS B 371 -9.438 -11.318 40.010 1.00 29.65 C ANISOU 2961 CG HIS B 371 3210 3919 4138 302 -170 -193 C ATOM 2962 ND1 HIS B 371 -8.979 -11.539 38.747 1.00 31.12 N ANISOU 2962 ND1 HIS B 371 3183 4370 4273 -256 -537 -157 N ATOM 2963 CD2 HIS B 371 -8.499 -10.594 40.637 1.00 30.40 C ANISOU 2963 CD2 HIS B 371 3221 4207 4121 747 -250 -195 C ATOM 2964 CE1 HIS B 371 -7.832 -10.941 38.629 1.00 31.93 C ANISOU 2964 CE1 HIS B 371 3345 4487 4298 518 -113 -41 C ATOM 2965 NE2 HIS B 371 -7.522 -10.376 39.772 1.00 30.62 N ANISOU 2965 NE2 HIS B 371 3100 4395 4139 303 -418 -219 N ATOM 2966 N ARG B 372 -13.701 -10.926 41.315 1.00 28.67 N ANISOU 2966 N ARG B 372 3708 3666 3518 382 -146 312 N ATOM 2967 CA ARG B 372 -14.864 -11.270 41.929 1.00 28.66 C ANISOU 2967 CA ARG B 372 3797 3645 3446 226 -126 173 C ATOM 2968 C ARG B 372 -16.155 -10.959 41.198 1.00 26.59 C ANISOU 2968 C ARG B 372 3602 3100 3402 -22 -132 338 C ATOM 2969 O ARG B 372 -17.124 -11.544 41.359 1.00 26.69 O ANISOU 2969 O ARG B 372 3560 3011 3570 -66 11 485 O ATOM 2970 CB ARG B 372 -14.770 -10.746 43.287 1.00 33.50 C ANISOU 2970 CB ARG B 372 4613 4492 3622 162 -113 74 C ATOM 2971 CG ARG B 372 -15.448 -9.658 43.602 0.50 35.71 C ANISOU 2971 CG ARG B 372 5177 4694 3698 90 -263 3 C ATOM 2972 CD ARG B 372 -15.555 -9.575 45.158 0.50 38.07 C ANISOU 2972 CD ARG B 372 5740 4892 3834 12 -334 -4 C ATOM 2973 NE ARG B 372 -14.980 -8.446 45.848 0.50 39.89 N ANISOU 2973 NE ARG B 372 6261 4863 4032 133 -324 27 N ATOM 2974 CZ ARG B 372 -13.685 -8.172 46.079 0.50 40.97 C ANISOU 2974 CZ ARG B 372 6594 4864 4110 418 -408 -63 C ATOM 2975 NH1 ARG B 372 -12.627 -8.836 45.638 0.50 42.22 N ANISOU 2975 NH1 ARG B 372 6795 5173 4073 552 -339 -113 N ATOM 2976 NH2 ARG B 372 -13.430 -7.112 46.729 0.50 40.31 N ANISOU 2976 NH2 ARG B 372 6766 4424 4128 276 -490 -207 N ATOM 2977 N LYS B 373 -16.057 -10.010 40.308 1.00 21.09 N ANISOU 2977 N LYS B 373 2796 2258 2959 -133 -66 496 N ATOM 2978 CA LYS B 373 -17.204 -9.605 39.549 1.00 22.53 C ANISOU 2978 CA LYS B 373 3355 2110 3096 349 106 277 C ATOM 2979 C LYS B 373 -17.333 -10.150 38.097 1.00 22.73 C ANISOU 2979 C LYS B 373 3536 2154 2945 -118 100 409 C ATOM 2980 O LYS B 373 -18.347 -10.252 37.665 1.00 24.09 O ANISOU 2980 O LYS B 373 3728 2439 2985 -64 -41 174 O ATOM 2981 CB LYS B 373 -17.234 -8.073 39.456 1.00 23.66 C ANISOU 2981 CB LYS B 373 3508 2165 3317 428 327 -22 C ATOM 2982 CG LYS B 373 -17.493 -7.376 40.762 1.00 28.62 C ANISOU 2982 CG LYS B 373 3998 3478 3399 722 393 -104 C ATOM 2983 CD LYS B 373 -18.921 -7.180 41.036 1.00 32.05 C ANISOU 2983 CD LYS B 373 4274 4274 3629 794 286 81 C ATOM 2984 CE LYS B 373 -19.592 -6.137 40.214 1.00 34.54 C ANISOU 2984 CE LYS B 373 5014 4373 3736 530 440 236 C ATOM 2985 NZ LYS B 373 -20.913 -5.528 40.469 1.00 34.88 N ANISOU 2985 NZ LYS B 373 5055 4406 3792 72 416 70 N ATOM 2986 N CYS B 374 -16.235 -10.464 37.503 1.00 20.58 N ANISOU 2986 N CYS B 374 2692 2214 2913 -293 292 334 N ATOM 2987 CA CYS B 374 -16.221 -10.910 36.105 1.00 21.09 C ANISOU 2987 CA CYS B 374 3196 1871 2947 -535 -55 -126 C ATOM 2988 C CYS B 374 -15.829 -12.364 36.038 1.00 22.79 C ANISOU 2988 C CYS B 374 3275 2078 3306 -441 -118 30 C ATOM 2989 O CYS B 374 -14.634 -12.690 36.120 1.00 22.53 O ANISOU 2989 O CYS B 374 3112 1839 3610 -279 -34 182 O ATOM 2990 CB CYS B 374 -15.237 -10.091 35.289 1.00 20.35 C ANISOU 2990 CB CYS B 374 3057 1628 3048 -160 60 171 C ATOM 2991 SG CYS B 374 -15.713 -8.348 35.339 1.00 20.93 S ANISOU 2991 SG CYS B 374 3176 1813 2963 -174 5 143 S ATOM 2992 N PHE B 375 -16.821 -13.229 35.854 1.00 21.04 N ANISOU 2992 N PHE B 375 2958 1528 3508 -222 247 -169 N ATOM 2993 CA PHE B 375 -16.562 -14.675 35.824 1.00 23.38 C ANISOU 2993 CA PHE B 375 3153 1949 3782 -641 281 -252 C ATOM 2994 C PHE B 375 -17.765 -15.329 35.208 1.00 23.96 C ANISOU 2994 C PHE B 375 2904 2023 4177 -342 398 -411 C ATOM 2995 O PHE B 375 -18.846 -14.707 35.193 1.00 24.51 O ANISOU 2995 O PHE B 375 2682 2256 4375 -408 251 -97 O ATOM 2996 CB PHE B 375 -16.342 -15.235 37.247 1.00 28.29 C ANISOU 2996 CB PHE B 375 4321 2658 3769 -505 252 329 C ATOM 2997 CG PHE B 375 -17.562 -15.124 38.119 1.00 31.40 C ANISOU 2997 CG PHE B 375 5249 3105 3577 -760 690 512 C ATOM 2998 CD1 PHE B 375 -17.783 -13.991 38.908 1.00 34.40 C ANISOU 2998 CD1 PHE B 375 5750 3638 3681 -743 805 482 C ATOM 2999 CD2 PHE B 375 -18.532 -16.130 38.110 1.00 33.31 C ANISOU 2999 CD2 PHE B 375 5457 3705 3495 -1066 873 521 C ATOM 3000 CE1 PHE B 375 -18.940 -13.869 39.691 1.00 35.34 C ANISOU 3000 CE1 PHE B 375 5903 3748 3778 -915 797 324 C ATOM 3001 CE2 PHE B 375 -19.694 -16.011 38.879 1.00 34.90 C ANISOU 3001 CE2 PHE B 375 5667 3871 3722 -1149 963 292 C ATOM 3002 CZ PHE B 375 -19.890 -14.880 39.678 1.00 34.44 C ANISOU 3002 CZ PHE B 375 5628 3689 3770 -1315 1003 208 C ATOM 3003 OXT PHE B 375 -17.662 -16.490 34.766 1.00 25.51 O ANISOU 3003 OXT PHE B 375 2976 2427 4290 -354 464 -670 O TER 3004 PHE B 375 ATOM 3005 N ARG M 111 -26.977 -15.988 14.913 1.00 28.38 N ANISOU 3005 N ARG M 111 2617 4318 3847 412 348 -260 N ATOM 3006 CA AARG M 111 -27.428 -15.432 16.144 0.50 30.34 C ANISOU 3006 CA AARG M 111 3303 4355 3869 665 327 -145 C ATOM 3007 CA BARG M 111 -27.497 -15.454 16.163 0.50 30.22 C ANISOU 3007 CA BARG M 111 3298 4328 3859 714 287 -124 C ATOM 3008 C ARG M 111 -28.673 -16.229 16.627 1.00 28.36 C ANISOU 3008 C ARG M 111 2861 4064 3852 789 56 199 C ATOM 3009 O ARG M 111 -29.336 -16.779 15.871 1.00 28.36 O ANISOU 3009 O ARG M 111 2211 4550 4016 -236 -132 865 O ATOM 3010 CB AARG M 111 -27.789 -13.942 15.986 0.50 35.05 C ANISOU 3010 CB AARG M 111 4239 5025 4053 584 509 -166 C ATOM 3011 CB BARG M 111 -27.916 -13.992 15.999 0.50 34.98 C ANISOU 3011 CB BARG M 111 4292 4961 4038 816 371 -121 C ATOM 3012 CG AARG M 111 -27.606 -13.094 17.218 0.50 38.05 C ANISOU 3012 CG AARG M 111 4721 5491 4246 388 527 -111 C ATOM 3013 CG BARG M 111 -27.586 -13.210 17.126 0.50 38.05 C ANISOU 3013 CG BARG M 111 4888 5344 4226 820 267 -47 C ATOM 3014 CD AARG M 111 -28.654 -11.983 17.178 0.50 39.85 C ANISOU 3014 CD AARG M 111 5037 5744 4359 300 532 -19 C ATOM 3015 CD BARG M 111 -27.827 -11.799 16.695 0.50 40.61 C ANISOU 3015 CD BARG M 111 5374 5720 4336 851 95 101 C ATOM 3016 NE AARG M 111 -28.127 -10.625 17.060 0.50 41.12 N ANISOU 3016 NE AARG M 111 5037 6164 4424 87 459 164 N ATOM 3017 NE BARG M 111 -28.558 -10.922 17.468 0.50 42.88 N ANISOU 3017 NE BARG M 111 5723 6123 4448 985 -200 159 N ATOM 3018 CZ AARG M 111 -28.421 -9.647 17.922 0.50 41.90 C ANISOU 3018 CZ AARG M 111 5146 6309 4467 -343 391 406 C ATOM 3019 CZ BARG M 111 -29.282 -11.278 18.513 0.50 43.75 C ANISOU 3019 CZ BARG M 111 5816 6367 4439 983 -466 120 C ATOM 3020 NH1AARG M 111 -29.234 -9.899 18.956 0.50 42.64 N ANISOU 3020 NH1AARG M 111 5247 6453 4501 -261 361 474 N ATOM 3021 NH1BARG M 111 -29.437 -12.525 18.792 0.50 43.73 N ANISOU 3021 NH1BARG M 111 5777 6424 4415 885 -632 131 N ATOM 3022 NH2AARG M 111 -27.920 -8.418 17.761 0.50 41.05 N ANISOU 3022 NH2AARG M 111 4870 6281 4449 -916 470 604 N ATOM 3023 NH2BARG M 111 -29.948 -10.408 19.228 0.50 44.54 N ANISOU 3023 NH2BARG M 111 5924 6494 4503 1128 -562 89 N ATOM 3024 N ALA M 112 -28.846 -16.286 17.930 1.00 27.56 N ANISOU 3024 N ALA M 112 2557 4153 3762 926 229 605 N ATOM 3025 CA ALA M 112 -30.034 -16.962 18.444 1.00 30.89 C ANISOU 3025 CA ALA M 112 3734 4395 3608 1071 308 1019 C ATOM 3026 C ALA M 112 -31.298 -16.234 17.978 1.00 32.46 C ANISOU 3026 C ALA M 112 3865 4768 3699 776 274 868 C ATOM 3027 O ALA M 112 -31.323 -14.997 17.905 1.00 32.27 O ANISOU 3027 O ALA M 112 3924 4644 3695 549 178 741 O ATOM 3028 CB ALA M 112 -30.006 -16.991 19.967 1.00 32.22 C ANISOU 3028 CB ALA M 112 4059 4879 3303 1482 459 1182 C ATOM 3029 N ARG M 113 -32.347 -17.009 17.714 1.00 31.49 N ANISOU 3029 N ARG M 113 3521 4647 3796 632 144 882 N ATOM 3030 CA ARG M 113 -33.685 -16.480 17.405 1.00 32.84 C ANISOU 3030 CA ARG M 113 3552 4952 3974 441 284 868 C ATOM 3031 C ARG M 113 -34.315 -15.672 18.559 1.00 32.01 C ANISOU 3031 C ARG M 113 2915 5138 4108 665 327 910 C ATOM 3032 O ARG M 113 -35.090 -14.751 18.293 1.00 34.47 O ANISOU 3032 O ARG M 113 3197 5725 4176 1462 347 848 O ATOM 3033 CB ARG M 113 -34.615 -17.608 16.960 1.00 33.29 C ANISOU 3033 CB ARG M 113 3953 4656 4040 532 -2 728 C ATOM 3034 N THR M 114 -33.997 -16.016 19.815 1.00 30.36 N ANISOU 3034 N THR M 114 2509 4941 4085 -183 128 903 N ATOM 3035 CA THR M 114 -34.430 -15.241 21.001 1.00 32.25 C ANISOU 3035 CA THR M 114 3043 4955 4256 -510 73 413 C ATOM 3036 C THR M 114 -33.317 -15.165 22.003 1.00 28.52 C ANISOU 3036 C THR M 114 2384 4423 4032 -184 41 532 C ATOM 3037 O THR M 114 -32.473 -16.041 22.041 1.00 28.22 O ANISOU 3037 O THR M 114 2213 4534 3975 -249 659 343 O ATOM 3038 CB THR M 114 -35.454 -15.967 21.937 1.00 35.48 C ANISOU 3038 CB THR M 114 3145 5575 4762 -1196 -190 126 C ATOM 3039 OG1 THR M 114 -35.823 -17.257 21.446 1.00 39.12 O ANISOU 3039 OG1 THR M 114 3270 6456 5139 -1418 277 8 O ATOM 3040 CG2 THR M 114 -36.596 -15.086 22.315 1.00 35.66 C ANISOU 3040 CG2 THR M 114 3794 4958 4795 -1309 12 182 C ATOM 3041 N GLU M 115 -33.349 -14.133 22.852 1.00 29.69 N ANISOU 3041 N GLU M 115 2727 4645 3906 -32 -248 844 N ATOM 3042 CA GLU M 115 -32.491 -14.056 24.045 1.00 31.16 C ANISOU 3042 CA GLU M 115 2964 4927 3948 -914 -265 671 C ATOM 3043 C GLU M 115 -33.200 -14.629 25.275 1.00 29.90 C ANISOU 3043 C GLU M 115 2735 4811 3816 -509 322 435 C ATOM 3044 O GLU M 115 -32.628 -14.643 26.368 1.00 28.15 O ANISOU 3044 O GLU M 115 2761 4237 3699 -314 206 446 O ATOM 3045 CB GLU M 115 -32.135 -12.606 24.369 1.00 32.00 C ANISOU 3045 CB GLU M 115 2860 4888 4409 -1129 -33 537 C ATOM 3046 CG GLU M 115 -31.227 -11.931 23.376 0.70 36.97 C ANISOU 3046 CG GLU M 115 3499 5804 4745 -404 150 430 C ATOM 3047 CD GLU M 115 -31.540 -10.461 23.257 0.50 41.32 C ANISOU 3047 CD GLU M 115 4260 6389 5052 -83 314 360 C ATOM 3048 OE1 GLU M 115 -32.443 -9.999 23.988 0.50 44.03 O ANISOU 3048 OE1 GLU M 115 4870 6740 5121 -102 302 80 O ATOM 3049 OE2 GLU M 115 -30.898 -9.772 22.439 0.50 43.95 O ANISOU 3049 OE2 GLU M 115 4744 6727 5227 181 205 514 O ATOM 3050 N ASP M 116 -34.448 -15.065 25.104 1.00 29.40 N ANISOU 3050 N ASP M 116 2731 4717 3722 -370 630 285 N ATOM 3051 CA ASP M 116 -35.278 -15.520 26.246 1.00 29.48 C ANISOU 3051 CA ASP M 116 2758 4622 3820 -285 528 457 C ATOM 3052 C ASP M 116 -34.636 -16.643 27.040 1.00 28.32 C ANISOU 3052 C ASP M 116 3145 4039 3576 -183 456 240 C ATOM 3053 O ASP M 116 -34.628 -16.566 28.272 1.00 28.13 O ANISOU 3053 O ASP M 116 2868 4146 3676 -337 609 311 O ATOM 3054 CB ASP M 116 -36.690 -15.926 25.800 1.00 30.81 C ANISOU 3054 CB ASP M 116 2456 5138 4112 -469 493 606 C ATOM 3055 CG ASP M 116 -37.583 -14.721 25.453 0.50 35.16 C ANISOU 3055 CG ASP M 116 3049 5894 4417 -166 178 400 C ATOM 3056 OD1 ASP M 116 -37.201 -13.553 25.720 0.50 35.92 O ANISOU 3056 OD1 ASP M 116 3312 5780 4555 34 136 277 O ATOM 3057 OD2 ASP M 116 -38.685 -14.951 24.896 0.50 36.33 O ANISOU 3057 OD2 ASP M 116 2961 6352 4490 350 -99 344 O ATOM 3058 N TYR M 117 -34.075 -17.664 26.365 1.00 24.07 N ANISOU 3058 N TYR M 117 2681 3256 3210 287 266 -49 N ATOM 3059 CA TYR M 117 -33.525 -18.805 27.087 1.00 22.59 C ANISOU 3059 CA TYR M 117 2561 2724 3300 -583 133 -296 C ATOM 3060 C TYR M 117 -32.168 -18.396 27.678 1.00 23.85 C ANISOU 3060 C TYR M 117 1925 3747 3391 -13 -26 156 C ATOM 3061 O TYR M 117 -31.812 -18.790 28.771 1.00 24.86 O ANISOU 3061 O TYR M 117 2059 4124 3264 -585 179 -72 O ATOM 3062 CB TYR M 117 -33.506 -20.093 26.226 1.00 24.79 C ANISOU 3062 CB TYR M 117 3322 2706 3391 -1152 18 113 C ATOM 3063 CG TYR M 117 -34.862 -20.430 25.648 0.60 23.68 C ANISOU 3063 CG TYR M 117 3085 2475 3439 -1109 -223 220 C ATOM 3064 CD1 TYR M 117 -35.068 -20.457 24.268 0.60 25.14 C ANISOU 3064 CD1 TYR M 117 3319 2759 3475 -1106 -410 470 C ATOM 3065 CD2 TYR M 117 -35.936 -20.731 26.484 0.60 21.28 C ANISOU 3065 CD2 TYR M 117 2524 1999 3561 -1245 -532 200 C ATOM 3066 CE1 TYR M 117 -36.314 -20.769 23.745 0.60 25.57 C ANISOU 3066 CE1 TYR M 117 3237 2983 3493 -1380 -328 630 C ATOM 3067 CE2 TYR M 117 -37.195 -21.041 25.972 0.60 22.14 C ANISOU 3067 CE2 TYR M 117 2959 2011 3443 -1424 -679 332 C ATOM 3068 CZ TYR M 117 -37.370 -21.070 24.604 0.60 25.43 C ANISOU 3068 CZ TYR M 117 3244 2859 3558 -1335 -590 685 C ATOM 3069 OH TYR M 117 -38.606 -21.378 24.095 0.60 27.79 O ANISOU 3069 OH TYR M 117 3398 3464 3695 -1266 -770 747 O ATOM 3070 N LEU M 118 -31.448 -17.543 26.977 1.00 25.93 N ANISOU 3070 N LEU M 118 2535 3669 3649 66 139 285 N ATOM 3071 CA LEU M 118 -30.195 -17.057 27.514 1.00 24.34 C ANISOU 3071 CA LEU M 118 2134 3463 3652 331 238 663 C ATOM 3072 C LEU M 118 -30.418 -16.317 28.853 1.00 22.10 C ANISOU 3072 C LEU M 118 1393 3464 3540 84 296 617 C ATOM 3073 O LEU M 118 -29.719 -16.611 29.845 1.00 21.73 O ANISOU 3073 O LEU M 118 1359 3502 3396 -455 165 904 O ATOM 3074 CB LEU M 118 -29.490 -16.153 26.487 1.00 26.47 C ANISOU 3074 CB LEU M 118 2650 3415 3991 692 499 1007 C ATOM 3075 CG LEU M 118 -28.168 -15.544 26.930 1.00 24.23 C ANISOU 3075 CG LEU M 118 2421 2578 4206 128 634 1228 C ATOM 3076 CD1 LEU M 118 -27.150 -16.650 27.231 1.00 23.17 C ANISOU 3076 CD1 LEU M 118 2154 2431 4217 724 664 1455 C ATOM 3077 CD2 LEU M 118 -27.624 -14.567 25.873 1.00 24.18 C ANISOU 3077 CD2 LEU M 118 2162 2618 4407 700 1074 872 C ATOM 3078 N ALYS M 119 -31.422 -15.422 28.908 0.60 21.68 N ANISOU 3078 N ALYS M 119 1631 3121 3484 -217 410 600 N ATOM 3079 N BLYS M 119 -31.393 -15.447 28.896 0.40 22.06 N ANISOU 3079 N BLYS M 119 1705 3115 3561 -177 318 589 N ATOM 3080 CA ALYS M 119 -31.743 -14.711 30.154 0.60 21.94 C ANISOU 3080 CA ALYS M 119 1975 2780 3579 54 167 447 C ATOM 3081 CA BLYS M 119 -31.697 -14.766 30.094 0.40 22.24 C ANISOU 3081 CA BLYS M 119 1967 2804 3678 -26 140 457 C ATOM 3082 C ALYS M 119 -32.114 -15.716 31.239 0.60 19.71 C ANISOU 3082 C ALYS M 119 2023 2055 3410 -78 230 330 C ATOM 3083 C BLYS M 119 -32.096 -15.734 31.220 0.40 20.05 C ANISOU 3083 C BLYS M 119 2028 2117 3474 -90 239 316 C ATOM 3084 O ALYS M 119 -31.696 -15.592 32.375 0.60 19.44 O ANISOU 3084 O ALYS M 119 2476 1758 3152 -2 -198 230 O ATOM 3085 O BLYS M 119 -31.708 -15.592 32.310 0.40 19.98 O ANISOU 3085 O BLYS M 119 2476 1810 3305 -49 -83 261 O ATOM 3086 CB ALYS M 119 -32.932 -13.764 30.018 0.60 23.22 C ANISOU 3086 CB ALYS M 119 2270 2775 3776 -566 -236 620 C ATOM 3087 CB BLYS M 119 -32.835 -13.851 29.793 0.40 24.59 C ANISOU 3087 CB BLYS M 119 2409 2966 3967 -391 -257 557 C ATOM 3088 CG ALYS M 119 -32.602 -12.508 29.285 0.60 25.35 C ANISOU 3088 CG ALYS M 119 2397 3315 3921 -836 78 805 C ATOM 3089 CG BLYS M 119 -33.139 -12.998 30.812 0.40 28.11 C ANISOU 3089 CG BLYS M 119 2845 3643 4194 -196 -84 626 C ATOM 3090 CD ALYS M 119 -33.842 -11.770 28.839 0.60 31.13 C ANISOU 3090 CD ALYS M 119 3339 4184 4305 -186 107 591 C ATOM 3091 CD BLYS M 119 -34.368 -12.179 30.458 0.40 32.37 C ANISOU 3091 CD BLYS M 119 3432 4455 4412 -57 -77 455 C ATOM 3092 CE ALYS M 119 -34.493 -11.116 30.008 0.60 34.40 C ANISOU 3092 CE ALYS M 119 3976 4587 4507 218 32 511 C ATOM 3093 CE BLYS M 119 -34.156 -11.105 29.516 0.40 34.51 C ANISOU 3093 CE BLYS M 119 3838 4682 4594 224 40 350 C ATOM 3094 NZ ALYS M 119 -35.560 -10.152 29.592 0.60 35.08 N ANISOU 3094 NZ ALYS M 119 3895 4726 4709 579 17 262 N ATOM 3095 NZ BLYS M 119 -35.438 -10.308 29.479 0.40 35.28 N ANISOU 3095 NZ BLYS M 119 3941 4745 4718 562 -11 259 N ATOM 3096 N ARG M 120 -32.906 -16.715 30.892 1.00 18.72 N ANISOU 3096 N ARG M 120 1505 2192 3416 -198 603 103 N ATOM 3097 CA AARG M 120 -33.320 -17.656 31.928 0.50 19.60 C ANISOU 3097 CA AARG M 120 1736 2230 3479 -624 574 -117 C ATOM 3098 CA BARG M 120 -33.340 -17.725 31.871 0.50 17.88 C ANISOU 3098 CA BARG M 120 1560 1796 3438 -650 439 -141 C ATOM 3099 C ARG M 120 -32.143 -18.480 32.409 1.00 18.44 C ANISOU 3099 C ARG M 120 1812 1908 3286 -454 691 -133 C ATOM 3100 O ARG M 120 -32.087 -18.801 33.595 1.00 19.37 O ANISOU 3100 O ARG M 120 2324 1880 3155 -303 460 -96 O ATOM 3101 CB AARG M 120 -34.505 -18.510 31.480 0.50 23.79 C ANISOU 3101 CB AARG M 120 1955 3333 3753 -330 552 -515 C ATOM 3102 CB BARG M 120 -34.325 -18.705 31.221 0.50 19.15 C ANISOU 3102 CB BARG M 120 1465 2182 3631 -258 99 -590 C ATOM 3103 CG AARG M 120 -35.859 -17.798 31.672 0.50 26.64 C ANISOU 3103 CG AARG M 120 2169 3957 3995 -1112 726 -238 C ATOM 3104 CG BARG M 120 -35.710 -18.119 30.918 0.50 20.16 C ANISOU 3104 CG BARG M 120 1682 2218 3759 -246 261 -405 C ATOM 3105 CD AARG M 120 -36.984 -18.807 31.555 0.50 31.96 C ANISOU 3105 CD AARG M 120 3262 4568 4313 -1269 882 -192 C ATOM 3106 CD BARG M 120 -36.716 -19.212 30.534 0.50 22.57 C ANISOU 3106 CD BARG M 120 2329 2399 3849 -7 447 -514 C ATOM 3107 NE AARG M 120 -36.466 -19.998 30.918 0.50 33.91 N ANISOU 3107 NE AARG M 120 3505 4855 4526 -1366 1003 -141 N ATOM 3108 NE BARG M 120 -37.977 -18.663 30.032 0.50 26.38 N ANISOU 3108 NE BARG M 120 2927 3115 3982 -650 605 -197 N ATOM 3109 CZ AARG M 120 -36.257 -20.096 29.616 0.50 34.76 C ANISOU 3109 CZ AARG M 120 3386 5152 4668 -1602 1032 -193 C ATOM 3110 CZ BARG M 120 -39.087 -18.564 30.749 0.50 28.12 C ANISOU 3110 CZ BARG M 120 3205 3509 3969 -335 534 13 C ATOM 3111 NH1AARG M 120 -36.552 -19.074 28.811 0.50 33.91 N ANISOU 3111 NH1AARG M 120 3145 5100 4639 -1901 1247 55 N ATOM 3112 NH1BARG M 120 -39.106 -18.987 32.009 0.50 27.94 N ANISOU 3112 NH1BARG M 120 3307 3485 3823 -572 431 94 N ATOM 3113 NH2AARG M 120 -35.765 -21.215 29.121 0.50 36.55 N ANISOU 3113 NH2AARG M 120 3403 5601 4882 -1310 773 -216 N ATOM 3114 NH2BARG M 120 -40.184 -18.064 30.196 0.50 28.11 N ANISOU 3114 NH2BARG M 120 3132 3559 3992 -422 282 185 N ATOM 3115 N ALYS M 121 -31.201 -18.774 31.527 0.70 17.48 N ANISOU 3115 N ALYS M 121 1377 2048 3216 -118 908 -177 N ATOM 3116 N BLYS M 121 -31.193 -18.769 31.531 0.30 18.19 N ANISOU 3116 N BLYS M 121 1566 2075 3270 -143 786 -238 N ATOM 3117 CA ALYS M 121 -30.064 -19.540 31.897 0.70 18.51 C ANISOU 3117 CA ALYS M 121 1739 2140 3153 55 949 -386 C ATOM 3118 CA BLYS M 121 -30.032 -19.524 31.906 0.30 19.34 C ANISOU 3118 CA BLYS M 121 1943 2150 3255 19 770 -435 C ATOM 3119 C ALYS M 121 -29.128 -18.747 32.769 0.70 18.47 C ANISOU 3119 C ALYS M 121 2310 1613 3094 -123 738 -227 C ATOM 3120 C BLYS M 121 -29.117 -18.737 32.792 0.30 18.88 C ANISOU 3120 C BLYS M 121 2325 1710 3138 -133 645 -270 C ATOM 3121 O ALYS M 121 -28.587 -19.243 33.674 0.70 19.86 O ANISOU 3121 O ALYS M 121 2303 1946 3296 -177 454 -238 O ATOM 3122 O BLYS M 121 -28.556 -19.226 33.685 0.30 19.56 O ANISOU 3122 O BLYS M 121 2322 1907 3201 -143 477 -267 O ATOM 3123 CB ALYS M 121 -29.369 -20.131 30.643 0.70 21.22 C ANISOU 3123 CB ALYS M 121 2384 2332 3348 65 449 -1093 C ATOM 3124 CB BLYS M 121 -29.236 -19.950 30.659 0.30 22.31 C ANISOU 3124 CB BLYS M 121 2530 2523 3425 90 568 -912 C ATOM 3125 CG ALYS M 121 -30.194 -21.299 30.031 0.70 26.21 C ANISOU 3125 CG ALYS M 121 3182 3188 3588 182 449 -1295 C ATOM 3126 CG BLYS M 121 -29.973 -20.682 29.643 0.30 27.05 C ANISOU 3126 CG BLYS M 121 3313 3333 3631 287 587 -969 C ATOM 3127 CD ALYS M 121 -29.525 -22.091 29.002 0.70 31.55 C ANISOU 3127 CD ALYS M 121 4159 3999 3831 252 331 -883 C ATOM 3128 CD BLYS M 121 -30.409 -21.863 30.180 0.30 30.99 C ANISOU 3128 CD BLYS M 121 4098 3839 3838 96 548 -829 C ATOM 3129 CE ALYS M 121 -29.403 -21.339 27.679 0.70 33.23 C ANISOU 3129 CE ALYS M 121 4574 4056 3997 97 590 -365 C ATOM 3130 CE BLYS M 121 -29.416 -22.882 29.919 0.30 33.73 C ANISOU 3130 CE BLYS M 121 4586 4224 4004 -15 621 -462 C ATOM 3131 NZ ALYS M 121 -29.727 -22.038 26.379 0.70 32.61 N ANISOU 3131 NZ ALYS M 121 4572 3920 3898 -267 878 -170 N ATOM 3132 NZ BLYS M 121 -29.393 -23.892 31.004 0.30 34.42 N ANISOU 3132 NZ BLYS M 121 4742 4248 4089 -215 645 -260 N ATOM 3133 N ILE M 122 -28.991 -17.467 32.494 1.00 18.04 N ANISOU 3133 N ILE M 122 2445 1376 3035 -393 559 -138 N ATOM 3134 CA ILE M 122 -28.102 -16.613 33.305 1.00 17.73 C ANISOU 3134 CA ILE M 122 2233 1369 3133 -777 458 230 C ATOM 3135 C ILE M 122 -28.707 -16.427 34.704 1.00 17.42 C ANISOU 3135 C ILE M 122 2188 1218 3213 -146 456 130 C ATOM 3136 O ILE M 122 -28.016 -16.558 35.720 1.00 18.00 O ANISOU 3136 O ILE M 122 2114 1764 2962 -192 420 165 O ATOM 3137 CB ILE M 122 -27.848 -15.259 32.590 1.00 17.22 C ANISOU 3137 CB ILE M 122 1865 1622 3055 -667 461 477 C ATOM 3138 CG1 ILE M 122 -26.977 -15.537 31.363 1.00 17.75 C ANISOU 3138 CG1 ILE M 122 1605 2045 3094 -444 922 835 C ATOM 3139 CG2 ILE M 122 -27.184 -14.260 33.566 1.00 17.54 C ANISOU 3139 CG2 ILE M 122 1979 1427 3257 -334 -249 231 C ATOM 3140 CD1 ILE M 122 -26.929 -14.318 30.433 1.00 22.18 C ANISOU 3140 CD1 ILE M 122 2529 2447 3451 -260 459 828 C ATOM 3141 N ARG M 123 -30.033 -16.254 34.706 1.00 18.00 N ANISOU 3141 N ARG M 123 1746 1648 3444 164 763 -47 N ATOM 3142 CA AARG M 123 -30.745 -16.044 35.974 0.50 18.34 C ANISOU 3142 CA AARG M 123 1699 1903 3367 203 759 123 C ATOM 3143 CA BARG M 123 -30.790 -16.056 35.967 0.50 16.34 C ANISOU 3143 CA BARG M 123 999 1784 3424 169 895 8 C ATOM 3144 C ARG M 123 -30.661 -17.268 36.889 1.00 18.66 C ANISOU 3144 C ARG M 123 1832 1908 3352 448 528 28 C ATOM 3145 O ARG M 123 -30.707 -17.138 38.110 1.00 21.07 O ANISOU 3145 O ARG M 123 2738 1926 3341 511 742 94 O ATOM 3146 CB AARG M 123 -32.197 -15.679 35.715 0.50 21.63 C ANISOU 3146 CB AARG M 123 2412 2408 3397 622 569 253 C ATOM 3147 CB BARG M 123 -32.278 -15.769 35.689 0.50 17.26 C ANISOU 3147 CB BARG M 123 944 2039 3576 454 729 -62 C ATOM 3148 CG AARG M 123 -32.910 -15.256 36.946 0.50 23.24 C ANISOU 3148 CG AARG M 123 3192 2362 3277 682 555 381 C ATOM 3149 CG BARG M 123 -32.537 -14.423 35.032 0.50 19.26 C ANISOU 3149 CG BARG M 123 1986 1750 3581 374 625 -107 C ATOM 3150 CD AARG M 123 -34.364 -15.148 36.595 0.50 20.20 C ANISOU 3150 CD AARG M 123 2996 1574 3104 590 731 425 C ATOM 3151 CD BARG M 123 -34.039 -14.223 34.785 0.50 18.27 C ANISOU 3151 CD BARG M 123 2449 1060 3432 375 515 -317 C ATOM 3152 NE AARG M 123 -34.544 -14.138 35.566 0.50 19.06 N ANISOU 3152 NE AARG M 123 2873 1532 2838 477 917 136 N ATOM 3153 NE BARG M 123 -34.374 -12.910 34.247 0.50 18.42 N ANISOU 3153 NE BARG M 123 2618 1139 3240 170 657 -384 N ATOM 3154 CZ AARG M 123 -35.191 -14.311 34.418 0.50 20.49 C ANISOU 3154 CZ AARG M 123 3630 1466 2690 802 791 -112 C ATOM 3155 CZ BARG M 123 -35.440 -12.654 33.496 0.50 20.25 C ANISOU 3155 CZ BARG M 123 2826 1761 3106 -225 579 -386 C ATOM 3156 NH1AARG M 123 -35.806 -15.473 34.110 0.50 22.64 N ANISOU 3156 NH1AARG M 123 4051 1843 2710 1805 742 -132 N ATOM 3157 NH1BARG M 123 -36.283 -13.618 33.144 0.50 22.58 N ANISOU 3157 NH1BARG M 123 2986 2486 3108 -375 180 -147 N ATOM 3158 NH2AARG M 123 -35.251 -13.276 33.579 0.50 21.27 N ANISOU 3158 NH2AARG M 123 3923 1500 2659 193 858 -356 N ATOM 3159 NH2BARG M 123 -35.656 -11.421 33.092 0.50 23.14 N ANISOU 3159 NH2BARG M 123 3088 2628 3075 -601 582 -537 N ATOM 3160 N SER M 124 -30.539 -18.461 36.294 1.00 17.19 N ANISOU 3160 N SER M 124 1733 1547 3254 59 480 163 N ATOM 3161 CA SER M 124 -30.449 -19.689 37.115 1.00 17.35 C ANISOU 3161 CA SER M 124 1902 1423 3266 -126 346 54 C ATOM 3162 C SER M 124 -29.070 -20.320 37.093 1.00 18.18 C ANISOU 3162 C SER M 124 2109 1623 3176 -161 415 38 C ATOM 3163 O SER M 124 -28.904 -21.489 37.404 1.00 18.99 O ANISOU 3163 O SER M 124 2242 1799 3175 -386 466 -38 O ATOM 3164 CB SER M 124 -31.476 -20.697 36.647 1.00 18.98 C ANISOU 3164 CB SER M 124 2193 1650 3370 -331 478 -310 C ATOM 3165 OG SER M 124 -31.345 -21.002 35.272 1.00 21.61 O ANISOU 3165 OG SER M 124 2765 2030 3417 -416 549 -78 O ATOM 3166 N ARG M 125 -28.061 -19.529 36.728 1.00 16.96 N ANISOU 3166 N ARG M 125 1845 1566 3032 74 854 110 N ATOM 3167 CA ARG M 125 -26.681 -20.034 36.610 1.00 16.37 C ANISOU 3167 CA ARG M 125 1542 1538 3139 305 877 338 C ATOM 3168 C ARG M 125 -26.193 -20.620 37.936 1.00 16.52 C ANISOU 3168 C ARG M 125 1684 1611 2983 189 933 343 C ATOM 3169 O ARG M 125 -26.359 -19.990 38.993 1.00 19.19 O ANISOU 3169 O ARG M 125 2101 2355 2836 24 896 103 O ATOM 3170 CB ARG M 125 -25.752 -18.896 36.187 1.00 17.28 C ANISOU 3170 CB ARG M 125 1355 1790 3423 -110 730 398 C ATOM 3171 CG ARG M 125 -24.309 -19.291 35.965 1.00 16.45 C ANISOU 3171 CG ARG M 125 1261 1575 3413 -165 539 130 C ATOM 3172 CD ARG M 125 -23.514 -18.042 35.629 1.00 17.25 C ANISOU 3172 CD ARG M 125 1775 1230 3551 -222 987 76 C ATOM 3173 NE ARG M 125 -22.204 -18.458 35.122 1.00 18.90 N ANISOU 3173 NE ARG M 125 2206 1439 3535 -60 1023 126 N ATOM 3174 CZ ARG M 125 -21.126 -17.683 35.121 1.00 18.87 C ANISOU 3174 CZ ARG M 125 2215 1259 3697 134 863 157 C ATOM 3175 NH1 ARG M 125 -21.204 -16.405 35.536 1.00 21.53 N ANISOU 3175 NH1 ARG M 125 2935 1279 3966 74 475 -221 N ATOM 3176 NH2 ARG M 125 -19.966 -18.149 34.678 1.00 19.59 N ANISOU 3176 NH2 ARG M 125 2551 1460 3434 330 828 409 N ATOM 3177 N PRO M 126 -25.588 -21.820 37.888 1.00 18.58 N ANISOU 3177 N PRO M 126 2648 1396 3016 87 778 110 N ATOM 3178 CA PRO M 126 -25.047 -22.374 39.128 1.00 19.97 C ANISOU 3178 CA PRO M 126 2803 1686 3098 -8 732 173 C ATOM 3179 C PRO M 126 -23.893 -21.566 39.667 1.00 21.43 C ANISOU 3179 C PRO M 126 3152 2113 2879 174 299 261 C ATOM 3180 O PRO M 126 -23.171 -20.889 38.897 1.00 19.84 O ANISOU 3180 O PRO M 126 2436 2273 2830 57 445 233 O ATOM 3181 CB PRO M 126 -24.511 -23.746 38.711 1.00 21.17 C ANISOU 3181 CB PRO M 126 2960 1833 3248 67 676 13 C ATOM 3182 CG PRO M 126 -25.070 -24.037 37.356 1.00 25.11 C ANISOU 3182 CG PRO M 126 3980 2239 3323 783 738 -84 C ATOM 3183 CD PRO M 126 -25.495 -22.740 36.731 1.00 20.48 C ANISOU 3183 CD PRO M 126 3346 1220 3215 439 764 96 C ATOM 3184 N GLU M 127 -23.718 -21.614 40.931 1.00 21.87 N ANISOU 3184 N GLU M 127 3288 2220 2803 409 609 233 N ATOM 3185 CA GLU M 127 -22.531 -21.058 41.568 1.00 23.82 C ANISOU 3185 CA GLU M 127 3741 2602 2708 350 361 -233 C ATOM 3186 C GLU M 127 -21.285 -21.859 41.209 1.00 19.95 C ANISOU 3186 C GLU M 127 2725 1981 2874 280 239 -180 C ATOM 3187 O GLU M 127 -21.387 -23.001 41.029 1.00 19.99 O ANISOU 3187 O GLU M 127 2478 2086 3033 -64 213 -161 O ATOM 3188 CB GLU M 127 -22.710 -21.016 43.087 1.00 29.22 C ANISOU 3188 CB GLU M 127 4296 3835 2973 268 114 -428 C ATOM 3189 N ARG M 128 -20.130 -21.220 41.155 1.00 22.07 N ANISOU 3189 N ARG M 128 3057 2264 3063 -410 481 99 N ATOM 3190 CA ARG M 128 -18.904 -21.913 40.813 1.00 22.56 C ANISOU 3190 CA ARG M 128 2885 2365 3322 -271 586 154 C ATOM 3191 C ARG M 128 -18.672 -23.102 41.727 1.00 22.20 C ANISOU 3191 C ARG M 128 3007 2323 3105 -355 527 106 C ATOM 3192 O ARG M 128 -18.245 -24.183 41.259 1.00 20.63 O ANISOU 3192 O ARG M 128 2771 2122 2946 -123 468 -211 O ATOM 3193 CB ARG M 128 -17.698 -20.945 40.848 1.00 22.54 C ANISOU 3193 CB ARG M 128 2216 2553 3794 -967 498 159 C ATOM 3194 CG ARG M 128 -16.511 -21.422 40.021 1.00 26.97 C ANISOU 3194 CG ARG M 128 2231 3552 4466 -1210 615 -81 C ATOM 3195 CD ARG M 128 -15.268 -20.521 40.162 1.00 30.54 C ANISOU 3195 CD ARG M 128 2135 4496 4971 -858 671 -334 C ATOM 3196 NE ARG M 128 -14.132 -21.116 39.450 1.00 36.34 N ANISOU 3196 NE ARG M 128 3126 5376 5305 -642 644 -251 N ATOM 3197 CZ ARG M 128 -13.389 -22.130 39.905 1.00 40.82 C ANISOU 3197 CZ ARG M 128 3953 6092 5466 -599 514 -200 C ATOM 3198 NH1 ARG M 128 -12.381 -22.594 39.175 1.00 42.68 N ANISOU 3198 NH1 ARG M 128 4361 6243 5614 -196 659 -273 N ATOM 3199 NH2 ARG M 128 -13.646 -22.705 41.073 1.00 42.17 N ANISOU 3199 NH2 ARG M 128 4226 6328 5469 -624 257 9 N ATOM 3200 N ALA M 129 -18.937 -22.912 43.030 1.00 22.14 N ANISOU 3200 N ALA M 129 3127 2278 3008 -579 359 140 N ATOM 3201 CA ALA M 129 -18.743 -23.967 44.028 1.00 22.20 C ANISOU 3201 CA ALA M 129 3305 1932 3197 -699 80 -94 C ATOM 3202 C ALA M 129 -19.541 -25.212 43.676 1.00 21.05 C ANISOU 3202 C ALA M 129 2824 1949 3224 -617 132 3 C ATOM 3203 O ALA M 129 -19.075 -26.326 43.981 1.00 21.69 O ANISOU 3203 O ALA M 129 3189 1853 3198 -443 217 243 O ATOM 3204 CB ALA M 129 -19.101 -23.466 45.462 1.00 24.00 C ANISOU 3204 CB ALA M 129 3734 2192 3194 -1050 96 -271 C ATOM 3205 N AGLU M 130 -20.662 -25.065 43.074 0.50 18.91 N ANISOU 3205 N AGLU M 130 2321 1656 3209 -408 236 -21 N ATOM 3206 N BGLU M 130 -20.562 -25.066 43.081 0.50 21.37 N ANISOU 3206 N BGLU M 130 2914 1868 3338 -420 248 -135 N ATOM 3207 CA AGLU M 130 -21.422 -26.243 42.648 0.50 20.50 C ANISOU 3207 CA AGLU M 130 2309 2159 3323 -244 -16 203 C ATOM 3208 CA BGLU M 130 -21.343 -26.229 42.668 0.50 23.19 C ANISOU 3208 CA BGLU M 130 2891 2360 3561 -179 56 -72 C ATOM 3209 C AGLU M 130 -20.753 -26.999 41.539 0.50 20.91 C ANISOU 3209 C AGLU M 130 2520 2129 3297 -43 -174 190 C ATOM 3210 C BGLU M 130 -20.671 -26.992 41.538 0.50 22.15 C ANISOU 3210 C BGLU M 130 2755 2251 3409 76 -233 67 C ATOM 3211 O AGLU M 130 -20.781 -28.134 41.532 0.50 20.60 O ANISOU 3211 O AGLU M 130 2531 1944 3352 -294 -332 566 O ATOM 3212 O BGLU M 130 -20.682 -28.138 41.538 0.50 21.78 O ANISOU 3212 O BGLU M 130 2669 2159 3449 130 -614 420 O ATOM 3213 CB AGLU M 130 -22.759 -25.913 42.136 0.50 22.89 C ANISOU 3213 CB AGLU M 130 2520 2673 3504 -759 228 369 C ATOM 3214 CB BGLU M 130 -22.721 -25.808 42.278 0.50 26.68 C ANISOU 3214 CB BGLU M 130 3306 2876 3956 -363 420 -197 C ATOM 3215 CG AGLU M 130 -23.643 -25.852 43.051 0.50 25.90 C ANISOU 3215 CG AGLU M 130 2930 3331 3580 -712 193 367 C ATOM 3216 CG BGLU M 130 -23.638 -26.803 41.912 0.50 30.34 C ANISOU 3216 CG BGLU M 130 3817 3453 4258 -452 557 -442 C ATOM 3217 CD AGLU M 130 -23.878 -27.173 43.842 0.50 29.12 C ANISOU 3217 CD AGLU M 130 3594 3755 3716 -1066 277 83 C ATOM 3218 CD BGLU M 130 -25.020 -26.289 41.579 0.50 34.44 C ANISOU 3218 CD BGLU M 130 4501 3954 4631 -1149 744 -317 C ATOM 3219 OE1AGLU M 130 -23.881 -27.045 44.970 0.50 30.15 O ANISOU 3219 OE1AGLU M 130 4048 3683 3726 -1882 504 295 O ATOM 3220 OE1BGLU M 130 -25.604 -25.504 42.251 0.50 35.32 O ANISOU 3220 OE1BGLU M 130 4417 4144 4859 -908 1260 56 O ATOM 3221 OE2AGLU M 130 -23.970 -28.289 43.411 0.50 32.28 O ANISOU 3221 OE2AGLU M 130 3883 4528 3854 -921 43 -238 O ATOM 3222 OE2BGLU M 130 -25.559 -26.719 40.594 0.50 37.10 O ANISOU 3222 OE2BGLU M 130 4707 4546 4844 -1384 392 -157 O ATOM 3223 N LEU M 131 -20.203 -26.303 40.587 1.00 20.32 N ANISOU 3223 N LEU M 131 2296 2283 3142 41 -203 205 N ATOM 3224 CA LEU M 131 -19.490 -26.989 39.510 1.00 19.73 C ANISOU 3224 CA LEU M 131 2596 1790 3109 -303 43 370 C ATOM 3225 C LEU M 131 -18.283 -27.720 40.077 1.00 20.30 C ANISOU 3225 C LEU M 131 2832 1974 2908 156 205 262 C ATOM 3226 O LEU M 131 -17.928 -28.784 39.589 1.00 21.08 O ANISOU 3226 O LEU M 131 3358 1752 2898 477 441 171 O ATOM 3227 CB LEU M 131 -18.992 -25.994 38.444 1.00 21.20 C ANISOU 3227 CB LEU M 131 2864 2005 3186 -221 87 259 C ATOM 3228 CG LEU M 131 -19.895 -25.731 37.259 1.00 24.23 C ANISOU 3228 CG LEU M 131 3081 2535 3592 -361 248 178 C ATOM 3229 CD1 LEU M 131 -21.127 -25.040 37.694 1.00 24.64 C ANISOU 3229 CD1 LEU M 131 3400 2367 3596 -455 -173 582 C ATOM 3230 CD2 LEU M 131 -19.148 -24.900 36.214 1.00 24.99 C ANISOU 3230 CD2 LEU M 131 2699 3091 3706 755 662 -725 C ATOM 3231 N VAL M 132 -17.633 -27.147 41.093 1.00 21.70 N ANISOU 3231 N VAL M 132 3020 2404 2819 -659 -147 383 N ATOM 3232 CA VAL M 132 -16.498 -27.799 41.730 1.00 22.32 C ANISOU 3232 CA VAL M 132 2880 2649 2950 -421 -207 321 C ATOM 3233 C VAL M 132 -16.980 -29.050 42.467 1.00 23.45 C ANISOU 3233 C VAL M 132 3303 2477 3128 -285 -132 414 C ATOM 3234 O VAL M 132 -16.398 -30.124 42.313 1.00 24.87 O ANISOU 3234 O VAL M 132 3849 2404 3198 2 -348 480 O ATOM 3235 CB VAL M 132 -15.753 -26.818 42.669 1.00 22.82 C ANISOU 3235 CB VAL M 132 2906 2884 2880 -310 -169 223 C ATOM 3236 CG1 VAL M 132 -14.609 -27.514 43.420 1.00 25.35 C ANISOU 3236 CG1 VAL M 132 3329 3277 3024 97 -291 522 C ATOM 3237 CG2 VAL M 132 -15.205 -25.633 41.879 1.00 21.61 C ANISOU 3237 CG2 VAL M 132 2680 2543 2986 -61 -76 95 C ATOM 3238 N ARG M 133 -18.076 -28.931 43.214 1.00 24.48 N ANISOU 3238 N ARG M 133 3432 2628 3241 -410 110 247 N ATOM 3239 CA AARG M 133 -18.604 -30.101 43.915 0.50 24.93 C ANISOU 3239 CA AARG M 133 3698 2450 3325 -539 409 453 C ATOM 3240 CA BARG M 133 -18.616 -30.096 43.915 0.50 24.58 C ANISOU 3240 CA BARG M 133 3687 2332 3321 -680 222 408 C ATOM 3241 C ARG M 133 -18.970 -31.207 42.918 1.00 24.03 C ANISOU 3241 C ARG M 133 3697 2010 3425 -214 266 463 C ATOM 3242 O ARG M 133 -18.807 -32.407 43.200 1.00 26.53 O ANISOU 3242 O ARG M 133 4304 2087 3691 -60 44 588 O ATOM 3243 CB AARG M 133 -19.819 -29.720 44.759 0.50 26.73 C ANISOU 3243 CB AARG M 133 3891 2825 3441 -697 885 285 C ATOM 3244 CB BARG M 133 -19.862 -29.699 44.700 0.50 25.63 C ANISOU 3244 CB BARG M 133 3837 2471 3429 -1172 327 135 C ATOM 3245 CG AARG M 133 -19.466 -28.970 46.042 0.50 28.11 C ANISOU 3245 CG AARG M 133 4137 3054 3490 -689 1178 418 C ATOM 3246 CG BARG M 133 -20.343 -30.751 45.687 0.50 25.91 C ANISOU 3246 CG BARG M 133 3833 2547 3466 -1501 151 94 C ATOM 3247 CD AARG M 133 -20.668 -28.818 46.973 0.50 29.96 C ANISOU 3247 CD AARG M 133 4532 3263 3590 -441 1265 431 C ATOM 3248 CD BARG M 133 -21.736 -30.416 46.186 0.50 28.77 C ANISOU 3248 CD BARG M 133 3866 3476 3591 -1653 99 -117 C ATOM 3249 NE AARG M 133 -21.556 -27.742 46.553 0.50 30.30 N ANISOU 3249 NE AARG M 133 4599 3189 3724 -524 1264 494 N ATOM 3250 NE BARG M 133 -22.625 -30.057 45.079 0.50 30.62 N ANISOU 3250 NE BARG M 133 3589 4310 3734 -1800 135 -357 N ATOM 3251 CZ AARG M 133 -21.392 -26.465 46.890 0.50 32.09 C ANISOU 3251 CZ AARG M 133 5066 3313 3816 -208 1054 353 C ATOM 3252 CZ BARG M 133 -22.957 -30.875 44.078 0.50 30.29 C ANISOU 3252 CZ BARG M 133 2932 4784 3794 -1650 483 -584 C ATOM 3253 NH1AARG M 133 -20.371 -26.106 47.656 0.50 33.82 N ANISOU 3253 NH1AARG M 133 5519 3549 3783 -436 956 224 N ATOM 3254 NH1BARG M 133 -22.500 -32.111 44.036 0.50 27.31 N ANISOU 3254 NH1BARG M 133 1997 4522 3859 -1649 688 -779 N ATOM 3255 NH2AARG M 133 -22.246 -25.547 46.461 0.50 30.00 N ANISOU 3255 NH2AARG M 133 4899 2697 3801 71 1019 724 N ATOM 3256 NH2BARG M 133 -23.764 -30.452 43.123 0.50 30.94 N ANISOU 3256 NH2BARG M 133 2796 5172 3787 -1770 420 -767 N ATOM 3257 N MET M 134 -19.452 -30.857 41.773 1.00 23.35 N ANISOU 3257 N MET M 134 3592 1806 3474 -510 201 249 N ATOM 3258 CA MET M 134 -19.781 -31.805 40.744 1.00 23.30 C ANISOU 3258 CA MET M 134 3240 2090 3524 -386 226 323 C ATOM 3259 C MET M 134 -18.628 -32.338 39.923 1.00 26.11 C ANISOU 3259 C MET M 134 4310 2031 3582 154 71 439 C ATOM 3260 O MET M 134 -18.840 -33.143 39.145 1.00 28.04 O ANISOU 3260 O MET M 134 4730 2109 3816 118 -336 216 O ATOM 3261 CB MET M 134 -20.863 -31.308 39.824 1.00 22.60 C ANISOU 3261 CB MET M 134 2774 2044 3769 -715 357 196 C ATOM 3262 CG MET M 134 -22.136 -30.992 40.359 1.00 23.22 C ANISOU 3262 CG MET M 134 2355 2565 3903 -512 263 322 C ATOM 3263 SD MET M 134 -23.359 -30.529 39.178 1.00 26.58 S ANISOU 3263 SD MET M 134 2978 3098 4025 -619 429 -96 S ATOM 3264 CE MET M 134 -24.364 -29.729 40.065 1.00 33.05 C ANISOU 3264 CE MET M 134 4604 3662 4291 -298 213 -5 C ATOM 3265 N HIS M 135 -17.485 -31.853 40.157 1.00 25.65 N ANISOU 3265 N HIS M 135 4264 1951 3529 30 261 864 N ATOM 3266 CA HIS M 135 -16.316 -32.172 39.443 1.00 27.93 C ANISOU 3266 CA HIS M 135 4806 2021 3785 585 -30 841 C ATOM 3267 C HIS M 135 -16.265 -31.750 38.013 1.00 28.12 C ANISOU 3267 C HIS M 135 4809 2260 3616 542 149 554 C ATOM 3268 O HIS M 135 -15.573 -32.252 37.266 1.00 28.71 O ANISOU 3268 O HIS M 135 4832 2390 3685 571 -88 524 O ATOM 3269 CB HIS M 135 -16.045 -33.675 39.545 1.00 31.35 C ANISOU 3269 CB HIS M 135 5092 2656 4161 967 -273 1036 C ATOM 3270 CG HIS M 135 -15.950 -34.118 40.947 1.00 38.06 C ANISOU 3270 CG HIS M 135 6125 3855 4481 316 -689 1338 C ATOM 3271 ND1 HIS M 135 -16.824 -34.997 41.532 1.00 42.56 N ANISOU 3271 ND1 HIS M 135 7049 4515 4605 17 -973 1519 N ATOM 3272 CD2 HIS M 135 -15.119 -33.738 41.897 1.00 40.97 C ANISOU 3272 CD2 HIS M 135 6609 4390 4567 -435 -701 1438 C ATOM 3273 CE1 HIS M 135 -16.523 -35.124 42.796 1.00 43.60 C ANISOU 3273 CE1 HIS M 135 7319 4539 4708 -354 -851 1588 C ATOM 3274 NE2 HIS M 135 -15.447 -34.421 43.020 1.00 43.22 N ANISOU 3274 NE2 HIS M 135 7025 4656 4740 -736 -828 1493 N ATOM 3275 N ILE M 136 -16.988 -30.719 37.725 1.00 23.62 N ANISOU 3275 N ILE M 136 4040 1693 3240 448 487 575 N ATOM 3276 CA ILE M 136 -16.981 -30.085 36.412 1.00 24.56 C ANISOU 3276 CA ILE M 136 4337 1934 3062 297 530 403 C ATOM 3277 C ILE M 136 -15.861 -29.085 36.333 1.00 27.21 C ANISOU 3277 C ILE M 136 4624 2413 3304 336 855 267 C ATOM 3278 O ILE M 136 -15.192 -28.984 35.347 1.00 27.53 O ANISOU 3278 O ILE M 136 4730 2251 3478 464 705 26 O ATOM 3279 CB ILE M 136 -18.330 -29.544 36.058 1.00 23.63 C ANISOU 3279 CB ILE M 136 4144 1927 2906 -202 398 403 C ATOM 3280 CG1 ILE M 136 -19.336 -30.666 35.920 1.00 26.84 C ANISOU 3280 CG1 ILE M 136 4704 2444 3049 -196 332 594 C ATOM 3281 CG2 ILE M 136 -18.337 -28.663 34.753 1.00 21.87 C ANISOU 3281 CG2 ILE M 136 3899 1704 2706 250 152 397 C ATOM 3282 CD1 ILE M 136 -20.623 -30.388 35.729 1.00 27.94 C ANISOU 3282 CD1 ILE M 136 4955 2538 3124 -213 241 640 C ATOM 3283 N LEU M 137 -15.643 -28.392 37.410 1.00 26.91 N ANISOU 3283 N LEU M 137 4418 2410 3396 442 532 170 N ATOM 3284 CA LEU M 137 -14.496 -27.510 37.563 1.00 26.78 C ANISOU 3284 CA LEU M 137 4008 2498 3670 419 650 158 C ATOM 3285 C LEU M 137 -13.530 -28.044 38.593 1.00 29.48 C ANISOU 3285 C LEU M 137 3652 3428 4122 512 622 370 C ATOM 3286 O LEU M 137 -13.960 -28.672 39.560 1.00 31.90 O ANISOU 3286 O LEU M 137 4043 4030 4046 277 532 587 O ATOM 3287 CB LEU M 137 -14.946 -26.153 38.077 1.00 26.94 C ANISOU 3287 CB LEU M 137 4150 2528 3557 455 482 138 C ATOM 3288 CG LEU M 137 -15.369 -25.126 37.064 1.00 27.28 C ANISOU 3288 CG LEU M 137 3786 3109 3468 687 358 385 C ATOM 3289 CD1 LEU M 137 -15.888 -23.891 37.768 1.00 25.90 C ANISOU 3289 CD1 LEU M 137 3724 2621 3497 315 325 428 C ATOM 3290 CD2 LEU M 137 -14.191 -24.753 36.139 1.00 28.93 C ANISOU 3290 CD2 LEU M 137 3907 3605 3479 899 288 293 C ATOM 3291 N GLU M 138 -12.233 -27.773 38.440 1.00 35.15 N ANISOU 3291 N GLU M 138 4273 4490 4592 -212 780 468 N ATOM 3292 CA GLU M 138 -11.276 -28.120 39.492 1.00 39.58 C ANISOU 3292 CA GLU M 138 4342 5603 5092 120 621 256 C ATOM 3293 C GLU M 138 -11.409 -27.096 40.617 1.00 43.49 C ANISOU 3293 C GLU M 138 4598 6566 5358 -306 363 8 C ATOM 3294 O GLU M 138 -11.868 -25.957 40.383 1.00 44.57 O ANISOU 3294 O GLU M 138 4728 6880 5327 -652 427 -404 O ATOM 3295 CB GLU M 138 -9.838 -28.119 38.965 1.00 41.96 C ANISOU 3295 CB GLU M 138 4646 5959 5336 370 778 233 C ATOM 3296 CG GLU M 138 -9.433 -29.393 38.244 1.00 46.48 C ANISOU 3296 CG GLU M 138 5461 6590 5607 496 807 290 C ATOM 3297 CD GLU M 138 -8.151 -29.215 37.425 1.00 50.14 C ANISOU 3297 CD GLU M 138 6186 7093 5771 678 706 155 C ATOM 3298 OE1 GLU M 138 -7.661 -28.058 37.319 1.00 51.03 O ANISOU 3298 OE1 GLU M 138 6201 7377 5812 432 572 -7 O ATOM 3299 OE2 GLU M 138 -7.650 -30.229 36.872 1.00 51.79 O ANISOU 3299 OE2 GLU M 138 6576 7240 5861 1032 639 284 O ATOM 3300 N GLU M 139 -11.028 -27.498 41.835 1.00 46.98 N ANISOU 3300 N GLU M 139 4905 7244 5703 -352 259 14 N ATOM 3301 CA GLU M 139 -10.915 -26.539 42.937 1.00 49.89 C ANISOU 3301 CA GLU M 139 5375 7573 6009 -522 197 40 C ATOM 3302 C GLU M 139 -9.837 -25.534 42.536 1.00 54.30 C ANISOU 3302 C GLU M 139 6181 8110 6341 -760 70 -86 C ATOM 3303 O GLU M 139 -8.937 -25.870 41.741 1.00 56.02 O ANISOU 3303 O GLU M 139 6274 8547 6462 -749 87 -58 O ATOM 3304 CB GLU M 139 -10.550 -27.242 44.262 1.00 48.98 C ANISOU 3304 CB GLU M 139 5171 7408 6032 -273 57 121 C ATOM 3305 N THR M 140 -9.925 -24.302 43.037 1.00 55.43 N ANISOU 3305 N THR M 140 6631 7941 6488 -1070 -183 -303 N ATOM 3306 CA THR M 140 -8.946 -23.296 42.626 1.00 57.30 C ANISOU 3306 CA THR M 140 7164 7942 6665 -1179 -387 -257 C ATOM 3307 C THR M 140 -8.660 -22.234 43.685 1.00 59.01 C ANISOU 3307 C THR M 140 7512 8064 6846 -1078 -518 -179 C ATOM 3308 O THR M 140 -7.572 -21.611 43.655 1.00 60.33 O ANISOU 3308 O THR M 140 7759 8232 6932 -887 -632 -132 O ATOM 3309 CB THR M 140 -9.352 -22.654 41.310 1.00 57.39 C ANISOU 3309 CB THR M 140 7241 7866 6698 -1426 -407 -190 C TER 3310 THR M 140 HETATM 3311 O5 LAB B 401 -3.313 -12.428 7.788 1.00 17.02 O ANISOU 3311 O5 LAB B 401 1864 1623 2978 315 619 402 O HETATM 3312 C18 LAB B 401 -2.702 -11.438 8.192 1.00 16.46 C ANISOU 3312 C18 LAB B 401 1284 1904 3067 394 1016 27 C HETATM 3313 N1 LAB B 401 -2.883 -10.882 9.375 1.00 16.60 N ANISOU 3313 N1 LAB B 401 1706 1577 3022 134 748 56 N HETATM 3314 C16 LAB B 401 -2.272 -9.603 9.604 1.00 15.88 C ANISOU 3314 C16 LAB B 401 1132 1752 3150 46 792 3 C HETATM 3315 C17 LAB B 401 -1.083 -9.476 8.591 1.00 15.91 C ANISOU 3315 C17 LAB B 401 1153 1851 3041 17 761 -165 C HETATM 3316 S1 LAB B 401 -1.541 -10.559 7.266 1.00 18.28 S ANISOU 3316 S1 LAB B 401 1900 1973 3072 36 897 171 S HETATM 3317 C15 LAB B 401 -3.279 -8.462 9.444 1.00 15.10 C ANISOU 3317 C15 LAB B 401 811 1801 3124 -65 930 -113 C HETATM 3318 O4 LAB B 401 -3.717 -8.273 8.090 1.00 15.97 O ANISOU 3318 O4 LAB B 401 1560 1618 2891 -66 250 283 O HETATM 3319 C14 LAB B 401 -4.579 -8.795 10.217 1.00 14.62 C ANISOU 3319 C14 LAB B 401 600 1737 3220 -321 942 -116 C HETATM 3320 C13 LAB B 401 -5.429 -7.559 10.544 1.00 16.32 C ANISOU 3320 C13 LAB B 401 1386 1549 3267 -78 662 63 C HETATM 3321 O2 LAB B 401 -6.100 -7.053 9.392 1.00 17.75 O ANISOU 3321 O2 LAB B 401 1736 1629 3378 156 789 142 O HETATM 3322 C12 LAB B 401 -4.571 -6.413 11.094 1.00 17.35 C ANISOU 3322 C12 LAB B 401 1640 1640 3312 -531 1094 -18 C HETATM 3323 C11 LAB B 401 -3.496 -6.141 10.039 1.00 17.70 C ANISOU 3323 C11 LAB B 401 1534 1676 3517 -214 1010 150 C HETATM 3324 O3 LAB B 401 -2.631 -7.298 9.967 1.00 18.14 O ANISOU 3324 O3 LAB B 401 1843 1611 3437 -165 908 -84 O HETATM 3325 C10 LAB B 401 -2.728 -4.864 10.358 1.00 19.38 C ANISOU 3325 C10 LAB B 401 2059 1642 3662 -531 1250 300 C HETATM 3326 C9 LAB B 401 -1.875 -4.443 9.141 1.00 21.40 C ANISOU 3326 C9 LAB B 401 2547 1935 3648 -433 1295 193 C HETATM 3327 C8 LAB B 401 -2.682 -4.020 7.908 1.00 20.81 C ANISOU 3327 C8 LAB B 401 2355 1934 3618 -390 1323 219 C HETATM 3328 C20 LAB B 401 -1.671 -3.365 6.923 1.00 23.14 C ANISOU 3328 C20 LAB B 401 2936 2205 3651 -1175 1237 204 C HETATM 3329 C7 LAB B 401 -3.794 -3.065 8.210 1.00 20.94 C ANISOU 3329 C7 LAB B 401 2348 1876 3731 -723 1002 192 C HETATM 3330 C6 LAB B 401 -5.088 -3.205 7.925 1.00 20.25 C ANISOU 3330 C6 LAB B 401 1999 1952 3742 -1189 1047 437 C HETATM 3331 C5 LAB B 401 -5.756 -4.375 7.223 1.00 20.22 C ANISOU 3331 C5 LAB B 401 2055 1817 3810 -342 1030 361 C HETATM 3332 C4 LAB B 401 -6.989 -4.702 8.096 1.00 20.40 C ANISOU 3332 C4 LAB B 401 2059 1844 3849 41 959 313 C HETATM 3333 C3 LAB B 401 -7.839 -5.741 7.397 1.00 17.72 C ANISOU 3333 C3 LAB B 401 1386 1686 3659 222 274 355 C HETATM 3334 C19 LAB B 401 -8.641 -5.374 6.176 1.00 18.64 C ANISOU 3334 C19 LAB B 401 1488 1852 3741 337 443 469 C HETATM 3335 C2 LAB B 401 -7.957 -7.046 7.757 1.00 17.14 C ANISOU 3335 C2 LAB B 401 1374 1688 3451 445 486 91 C HETATM 3336 C1 LAB B 401 -7.270 -7.684 8.877 1.00 17.58 C ANISOU 3336 C1 LAB B 401 1637 1753 3288 178 823 -88 C HETATM 3337 O1 LAB B 401 -7.644 -8.744 9.335 1.00 17.47 O ANISOU 3337 O1 LAB B 401 1992 1388 3257 -52 470 200 O HETATM 3338 PG ATP B 402 -7.365 -13.115 17.811 0.80 12.11 P ANISOU 3338 PG ATP B 402 792 1140 2671 26 469 163 P HETATM 3339 O1G ATP B 402 -8.745 -13.457 18.344 0.80 11.52 O ANISOU 3339 O1G ATP B 402 324 1402 2651 -348 220 -28 O HETATM 3340 O2G ATP B 402 -6.627 -14.256 17.237 0.80 12.85 O ANISOU 3340 O2G ATP B 402 1115 1278 2490 219 239 388 O HETATM 3341 O3G ATP B 402 -6.610 -12.292 18.786 0.80 14.14 O ANISOU 3341 O3G ATP B 402 1447 1304 2620 -424 185 65 O HETATM 3342 PB ATP B 402 -8.743 -11.263 16.037 1.00 12.59 P ANISOU 3342 PB ATP B 402 1004 1211 2569 37 343 -15 P HETATM 3343 O1B ATP B 402 -9.909 -11.275 16.956 1.00 12.50 O ANISOU 3343 O1B ATP B 402 1006 1124 2622 153 641 89 O HETATM 3344 O2B ATP B 402 -8.190 -9.928 15.686 1.00 12.86 O ANISOU 3344 O2B ATP B 402 1013 1128 2746 4 195 -27 O HETATM 3345 O3B ATP B 402 -7.584 -12.192 16.555 1.00 13.18 O ANISOU 3345 O3B ATP B 402 865 1388 2755 144 380 235 O HETATM 3346 PA ATP B 402 -10.562 -11.900 13.893 1.00 13.19 P ANISOU 3346 PA ATP B 402 819 1476 2715 57 130 -172 P HETATM 3347 O1A ATP B 402 -10.949 -10.487 13.853 1.00 14.52 O ANISOU 3347 O1A ATP B 402 1379 1530 2609 15 386 89 O HETATM 3348 O2A ATP B 402 -11.485 -12.944 14.427 1.00 13.82 O ANISOU 3348 O2A ATP B 402 1091 1331 2827 -28 242 -452 O HETATM 3349 O3A ATP B 402 -9.170 -12.005 14.664 1.00 12.11 O ANISOU 3349 O3A ATP B 402 700 1257 2645 -177 313 -335 O HETATM 3350 O5' ATP B 402 -10.125 -12.467 12.457 1.00 14.26 O ANISOU 3350 O5' ATP B 402 921 1776 2720 74 143 -65 O HETATM 3351 C5' ATP B 402 -9.096 -11.792 11.684 1.00 14.36 C ANISOU 3351 C5' ATP B 402 1222 1723 2510 0 579 -252 C HETATM 3352 C4' ATP B 402 -8.402 -12.933 10.961 1.00 12.68 C ANISOU 3352 C4' ATP B 402 467 1859 2491 -386 573 -152 C HETATM 3353 O4' ATP B 402 -9.402 -13.704 10.302 1.00 14.14 O ANISOU 3353 O4' ATP B 402 1068 1825 2481 -63 764 134 O HETATM 3354 C3' ATP B 402 -7.394 -12.526 9.877 1.00 14.48 C ANISOU 3354 C3' ATP B 402 1273 1581 2648 526 373 -10 C HETATM 3355 O3' ATP B 402 -6.325 -13.482 9.852 1.00 13.60 O ANISOU 3355 O3' ATP B 402 1161 1281 2725 166 599 138 O HETATM 3356 C2' ATP B 402 -8.194 -12.588 8.617 1.00 14.34 C ANISOU 3356 C2' ATP B 402 1033 1778 2638 241 702 137 C HETATM 3357 O2' ATP B 402 -7.364 -12.794 7.462 1.00 13.98 O ANISOU 3357 O2' ATP B 402 905 1628 2780 72 393 205 O HETATM 3358 C1' ATP B 402 -9.033 -13.827 8.925 1.00 13.79 C ANISOU 3358 C1' ATP B 402 952 1631 2656 -100 363 211 C HETATM 3359 N9 ATP B 402 -10.194 -13.864 8.044 1.00 13.02 N ANISOU 3359 N9 ATP B 402 1087 1125 2736 -52 321 -133 N HETATM 3360 C8 ATP B 402 -11.117 -12.852 7.943 1.00 16.04 C ANISOU 3360 C8 ATP B 402 1113 1867 3114 -201 4 -103 C HETATM 3361 N7 ATP B 402 -12.069 -13.165 7.036 1.00 13.72 N ANISOU 3361 N7 ATP B 402 529 1428 3257 206 270 -346 N HETATM 3362 C5 ATP B 402 -11.751 -14.382 6.559 1.00 15.03 C ANISOU 3362 C5 ATP B 402 1519 1290 2900 254 404 265 C HETATM 3363 C6 ATP B 402 -12.336 -15.254 5.563 1.00 15.53 C ANISOU 3363 C6 ATP B 402 1542 1664 2695 109 300 411 C HETATM 3364 N6 ATP B 402 -13.455 -14.872 4.851 1.00 16.62 N ANISOU 3364 N6 ATP B 402 1351 2295 2670 -164 -244 582 N HETATM 3365 N1 ATP B 402 -11.684 -16.446 5.344 1.00 14.48 N ANISOU 3365 N1 ATP B 402 1366 1650 2488 317 321 178 N HETATM 3366 C2 ATP B 402 -10.590 -16.803 6.036 1.00 15.53 C ANISOU 3366 C2 ATP B 402 1844 1762 2292 -123 301 -161 C HETATM 3367 N3 ATP B 402 -10.005 -16.029 6.942 1.00 13.56 N ANISOU 3367 N3 ATP B 402 1593 1138 2421 -45 421 203 N HETATM 3368 C4 ATP B 402 -10.546 -14.827 7.232 1.00 13.24 C ANISOU 3368 C4 ATP B 402 1602 790 2637 85 560 202 C HETATM 3369 MG MG B 403 -10.671 -12.573 18.441 1.00 13.25 MG ANISOU 3369 MG MG B 403 997 940 3096 101 561 65 MG HETATM 3370 C1 GOL B 404 -22.930 -13.838 32.431 1.00 37.86 C ANISOU 3370 C1 GOL B 404 4669 4404 5313 243 -48 293 C HETATM 3371 O1 GOL B 404 -23.588 -14.747 33.303 1.00 34.37 O ANISOU 3371 O1 GOL B 404 2213 5418 5429 111 324 -439 O HETATM 3372 C2 GOL B 404 -21.427 -14.022 32.569 1.00 36.79 C ANISOU 3372 C2 GOL B 404 4109 4622 5249 -150 258 -65 C HETATM 3373 O2 GOL B 404 -21.008 -15.195 31.887 1.00 35.94 O ANISOU 3373 O2 GOL B 404 4530 4095 5033 -22 258 -561 O HETATM 3374 C3 GOL B 404 -20.652 -12.839 32.044 1.00 35.97 C ANISOU 3374 C3 GOL B 404 3547 4810 5310 51 178 -192 C HETATM 3375 O3 GOL B 404 -19.250 -13.141 32.063 1.00 37.86 O ANISOU 3375 O3 GOL B 404 5043 3912 5428 16 -60 506 O HETATM 3376 C1 GOL B 405 -31.149 -27.345 32.787 1.00 46.90 C ANISOU 3376 C1 GOL B 405 5573 6103 6146 -367 492 226 C HETATM 3377 O1 GOL B 405 -30.347 -27.761 31.702 1.00 46.95 O ANISOU 3377 O1 GOL B 405 5727 5941 6172 -380 343 318 O HETATM 3378 C2 GOL B 405 -30.312 -26.614 33.794 1.00 49.34 C ANISOU 3378 C2 GOL B 405 5904 6615 6229 -45 510 22 C HETATM 3379 O2 GOL B 405 -31.056 -26.725 34.938 1.00 51.34 O ANISOU 3379 O2 GOL B 405 6232 7036 6239 9 462 63 O HETATM 3380 C3 GOL B 405 -29.024 -27.184 34.290 1.00 50.99 C ANISOU 3380 C3 GOL B 405 6083 6972 6318 86 493 -271 C HETATM 3381 O3 GOL B 405 -28.855 -26.553 35.564 1.00 51.96 O ANISOU 3381 O3 GOL B 405 6264 7077 6402 410 615 -605 O HETATM 3382 O HOH B 501 -10.642 -0.166 9.016 1.00 56.65 O ANISOU 3382 O HOH B 501 8393 6046 7087 -1283 1943 2157 O HETATM 3383 O HOH B 502 -3.983 -35.850 19.951 1.00 44.67 O ANISOU 3383 O HOH B 502 6157 4616 6202 2642 3454 691 O HETATM 3384 O HOH B 503 0.001 -17.117 15.681 1.00 26.92 O ANISOU 3384 O HOH B 503 1894 4494 3841 509 -469 -481 O HETATM 3385 O HOH B 504 -29.781 -8.259 24.431 1.00 35.66 O ANISOU 3385 O HOH B 504 4252 4220 5077 1203 1093 1250 O HETATM 3386 O HOH B 505 -8.677 3.666 12.435 1.00 38.51 O ANISOU 3386 O HOH B 505 5335 4509 4788 180 1162 146 O HETATM 3387 O HOH B 506 5.858 -25.879 1.392 1.00 51.82 O ANISOU 3387 O HOH B 506 1581 9263 8843 754 449 4311 O HETATM 3388 O HOH B 507 -2.963 -35.720 4.049 1.00 47.80 O ANISOU 3388 O HOH B 507 5753 5177 7233 2099 -878 323 O HETATM 3389 O HOH B 508 -26.483 -1.728 28.305 1.00 53.79 O ANISOU 3389 O HOH B 508 4472 6126 9840 -1585 2984 -2204 O HETATM 3390 O HOH B 509 -14.681 -34.924 36.503 1.00 34.36 O ANISOU 3390 O HOH B 509 5080 3525 4448 318 -55 1054 O HETATM 3391 O HOH B 510 -13.889 -6.986 9.115 1.00 41.43 O ANISOU 3391 O HOH B 510 5531 6191 4021 1077 1011 189 O HETATM 3392 O HOH B 511 -25.036 -8.793 12.566 1.00 36.55 O ANISOU 3392 O HOH B 511 5229 4392 4267 506 25 122 O HETATM 3393 O HOH B 512 -28.348 -32.009 28.100 1.00 62.67 O ANISOU 3393 O HOH B 512 4339 11505 7969 -935 3379 -5442 O HETATM 3394 O HOH B 513 -13.053 0.404 9.538 1.00 44.76 O ANISOU 3394 O HOH B 513 3881 8207 4919 820 722 2356 O HETATM 3395 O HOH B 514 -22.171 -17.806 17.997 1.00 18.41 O ANISOU 3395 O HOH B 514 970 3307 2717 303 -291 -718 O HETATM 3396 O HOH B 515 -6.489 8.513 19.664 1.00 54.13 O ANISOU 3396 O HOH B 515 6755 4496 9317 -2873 -647 10 O HETATM 3397 O HOH B 516 -15.725 -38.724 23.536 1.00 24.93 O ANISOU 3397 O HOH B 516 3741 1754 3979 452 848 163 O HETATM 3398 O HOH B 517 -10.843 -14.619 32.523 1.00 48.04 O ANISOU 3398 O HOH B 517 8335 4091 5826 164 -2033 147 O HETATM 3399 O HOH B 518 -25.817 -20.140 32.774 1.00 30.52 O ANISOU 3399 O HOH B 518 2855 4586 4155 401 381 768 O HETATM 3400 O HOH B 519 -18.712 -16.255 32.070 1.00 39.54 O ANISOU 3400 O HOH B 519 6250 3737 5038 -1607 -79 713 O HETATM 3401 O HOH B 520 4.389 -27.565 4.043 1.00 43.44 O ANISOU 3401 O HOH B 520 5917 4274 6316 753 259 -746 O HETATM 3402 O HOH B 521 -10.943 -13.986 -7.562 1.00 59.14 O ANISOU 3402 O HOH B 521 5637 8198 8634 124 218 3672 O HETATM 3403 O HOH B 522 -22.516 -47.958 17.536 1.00 37.00 O ANISOU 3403 O HOH B 522 2862 3030 8166 195 574 832 O HETATM 3404 O HOH B 523 -28.884 2.502 20.293 1.00 50.93 O ANISOU 3404 O HOH B 523 8752 4563 6037 -197 129 -561 O HETATM 3405 O HOH B 524 -24.766 6.181 17.224 1.00 44.29 O ANISOU 3405 O HOH B 524 6344 4588 5895 -1407 1273 -1482 O HETATM 3406 O HOH B 525 -4.566 -16.164 24.071 1.00 39.96 O ANISOU 3406 O HOH B 525 5062 4800 5320 -2639 -22 -745 O HETATM 3407 O HOH B 526 3.796 -27.001 1.798 1.00 54.60 O ANISOU 3407 O HOH B 526 10192 3633 6922 2853 3559 878 O HETATM 3408 O HOH B 527 -10.447 9.744 28.298 1.00 39.75 O ANISOU 3408 O HOH B 527 6645 3143 5316 -52 1163 1127 O HETATM 3409 O HOH B 528 -13.677 -14.497 17.612 1.00 20.87 O ANISOU 3409 O HOH B 528 2217 2413 3299 -242 286 144 O HETATM 3410 O HOH B 529 -4.319 -33.862 14.602 1.00 31.06 O ANISOU 3410 O HOH B 529 2826 3465 5510 142 58 169 O HETATM 3411 O HOH B 530 -3.461 -33.798 11.873 1.00 62.34 O ANISOU 3411 O HOH B 530 9319 4758 9609 3662 5538 1977 O HETATM 3412 O HOH B 531 -1.642 -16.541 13.321 1.00 23.18 O ANISOU 3412 O HOH B 531 2403 2742 3661 62 232 28 O HETATM 3413 O HOH B 532 -24.157 -4.672 41.161 1.00 56.20 O ANISOU 3413 O HOH B 532 5776 8100 7477 -490 2139 -3900 O HETATM 3414 O HOH B 533 6.074 -9.436 -6.135 1.00 55.07 O ANISOU 3414 O HOH B 533 10168 6085 4669 913 -1787 -538 O HETATM 3415 O AHOH B 534 3.955 -11.262 17.846 0.70 46.82 O ANISOU 3415 O AHOH B 534 6450 5813 5527 2983 -2874 -1212 O HETATM 3416 O HOH B 535 -6.536 -36.569 11.973 1.00 51.68 O ANISOU 3416 O HOH B 535 5353 4759 9523 1759 2184 -1215 O HETATM 3417 O HOH B 536 -22.428 4.156 42.838 1.00 41.89 O ANISOU 3417 O HOH B 536 4755 5715 5445 -1475 1261 -2359 O HETATM 3418 O HOH B 537 -8.359 -36.973 9.850 1.00 46.46 O ANISOU 3418 O HOH B 537 4657 6088 6907 2983 1218 985 O HETATM 3419 O HOH B 538 8.745 -18.359 -7.071 1.00 46.41 O ANISOU 3419 O HOH B 538 5392 7328 4913 324 -667 1415 O HETATM 3420 O HOH B 539 -9.284 -15.698 22.882 1.00 31.70 O ANISOU 3420 O HOH B 539 3722 3202 5120 592 -750 -390 O HETATM 3421 O HOH B 540 -23.217 -14.857 16.262 1.00 26.66 O ANISOU 3421 O HOH B 540 3150 2866 4113 -397 235 -684 O HETATM 3422 O HOH B 541 -14.103 6.175 36.258 1.00 31.79 O ANISOU 3422 O HOH B 541 4566 3478 4034 -258 -18 -97 O HETATM 3423 O HOH B 542 -22.204 -1.071 17.066 1.00 22.59 O ANISOU 3423 O HOH B 542 3152 1989 3443 419 -141 427 O HETATM 3424 O HOH B 543 7.758 -9.603 -4.363 1.00 48.43 O ANISOU 3424 O HOH B 543 3313 8431 6657 -603 98 -3857 O HETATM 3425 O HOH B 544 -5.669 -25.650 29.641 1.00 43.27 O ANISOU 3425 O HOH B 544 4010 6909 5522 2422 541 912 O HETATM 3426 O HOH B 545 -25.729 -26.716 30.788 1.00 39.92 O ANISOU 3426 O HOH B 545 2543 7940 4685 -737 1473 1011 O HETATM 3427 O HOH B 546 -26.776 -16.379 12.234 1.00 27.01 O ANISOU 3427 O HOH B 546 2893 2950 4419 163 -48 174 O HETATM 3428 O HOH B 547 -21.987 0.464 43.079 1.00 37.86 O ANISOU 3428 O HOH B 547 3631 6184 4572 195 661 -1359 O HETATM 3429 O HOH B 548 -24.780 -31.479 31.580 1.00 33.18 O ANISOU 3429 O HOH B 548 4248 2867 5490 1082 -920 -1059 O HETATM 3430 O HOH B 549 -11.447 -10.119 2.013 1.00 37.01 O ANISOU 3430 O HOH B 549 4192 3837 6031 1607 -1135 -267 O HETATM 3431 O HOH B 550 -0.236 -34.835 4.940 1.00 50.04 O ANISOU 3431 O HOH B 550 6548 4486 7980 1524 3447 -838 O HETATM 3432 O HOH B 551 -13.174 -18.860 -0.343 1.00 33.99 O ANISOU 3432 O HOH B 551 3889 4006 5019 919 1279 1652 O HETATM 3433 O HOH B 552 -11.360 -13.923 19.871 1.00 13.35 O ANISOU 3433 O HOH B 552 875 1218 2979 -47 644 184 O HETATM 3434 O HOH B 553 -13.628 -11.601 15.651 1.00 20.13 O ANISOU 3434 O HOH B 553 1463 3509 2676 730 -43 -238 O HETATM 3435 O HOH B 554 -8.195 -15.455 33.602 1.00 42.12 O ANISOU 3435 O HOH B 554 3795 6085 6122 157 344 647 O HETATM 3436 O HOH B 555 -23.025 -41.470 22.520 1.00 35.57 O ANISOU 3436 O HOH B 555 4359 3000 6155 -1448 2463 -943 O HETATM 3437 O HOH B 556 -28.368 -22.038 33.974 1.00 31.39 O ANISOU 3437 O HOH B 556 6002 2640 3286 -35 759 -59 O HETATM 3438 O HOH B 557 -9.514 -15.523 30.637 1.00 38.22 O ANISOU 3438 O HOH B 557 3384 4764 6373 1191 1318 2060 O HETATM 3439 O HOH B 558 -7.652 -9.934 23.591 1.00 22.71 O ANISOU 3439 O HOH B 558 1365 3554 3709 -427 -173 1518 O HETATM 3440 O HOH B 559 -21.457 -45.442 21.610 1.00 33.17 O ANISOU 3440 O HOH B 559 5464 3937 3201 1229 -360 352 O HETATM 3441 O HOH B 560 -8.066 -11.792 20.943 1.00 18.32 O ANISOU 3441 O HOH B 560 1696 1856 3410 27 544 245 O HETATM 3442 O HOH B 561 -11.004 -9.069 6.124 1.00 31.07 O ANISOU 3442 O HOH B 561 3566 3449 4791 1023 818 -998 O HETATM 3443 O HOH B 562 -18.159 -35.728 38.136 1.00 39.38 O ANISOU 3443 O HOH B 562 4063 6195 4705 1170 959 1499 O HETATM 3444 O HOH B 563 3.123 -6.140 21.407 1.00 29.02 O ANISOU 3444 O HOH B 563 2471 4036 4521 -679 138 -151 O HETATM 3445 O HOH B 564 -25.834 4.056 30.159 1.00 32.05 O ANISOU 3445 O HOH B 564 4956 2738 4485 92 1418 580 O HETATM 3446 O HOH B 565 -22.049 -39.419 15.396 1.00 29.72 O ANISOU 3446 O HOH B 565 3885 2821 4584 -1045 1602 -445 O HETATM 3447 O HOH B 566 4.575 -15.515 -2.616 1.00 28.16 O ANISOU 3447 O HOH B 566 3685 3384 3632 160 686 1244 O HETATM 3448 O HOH B 567 -0.135 -9.813 17.097 1.00 21.98 O ANISOU 3448 O HOH B 567 2314 2333 3704 -273 404 9 O HETATM 3449 O HOH B 568 -0.514 8.489 18.546 1.00 57.04 O ANISOU 3449 O HOH B 568 5104 6291 10279 -2564 726 -2242 O HETATM 3450 O HOH B 569 -27.168 -24.694 29.559 1.00 52.21 O ANISOU 3450 O HOH B 569 8625 5829 5383 2547 854 1265 O HETATM 3451 O HOH B 570 -23.390 -29.835 12.403 1.00 31.38 O ANISOU 3451 O HOH B 570 4123 3714 4086 -412 -1089 -708 O HETATM 3452 O HOH B 571 -17.773 -21.641 5.967 1.00 43.40 O ANISOU 3452 O HOH B 571 5698 6635 4157 608 181 -1937 O HETATM 3453 O HOH B 572 0.840 -7.293 6.475 1.00 23.37 O ANISOU 3453 O HOH B 572 2365 2813 3701 -571 855 227 O HETATM 3454 O HOH B 573 -30.832 -10.642 40.422 1.00 40.12 O ANISOU 3454 O HOH B 573 4572 3588 7082 -895 1155 -116 O HETATM 3455 O HOH B 574 -11.332 -13.989 16.894 1.00 14.73 O ANISOU 3455 O HOH B 574 1320 1095 3183 261 -229 -365 O HETATM 3456 O HOH B 575 -12.600 -11.742 18.071 1.00 13.42 O ANISOU 3456 O HOH B 575 1109 1334 2654 59 589 194 O HETATM 3457 O HOH B 576 -10.854 -37.318 12.813 1.00 22.66 O ANISOU 3457 O HOH B 576 3091 1541 3976 -142 1249 351 O HETATM 3458 O HOH B 577 -19.950 -17.926 16.373 1.00 19.41 O ANISOU 3458 O HOH B 577 2288 1777 3309 831 436 -14 O HETATM 3459 O HOH B 578 -14.435 -27.424 17.032 1.00 26.91 O ANISOU 3459 O HOH B 578 2234 2373 5619 272 1075 353 O HETATM 3460 O HOH B 579 -29.883 -6.356 36.398 1.00 22.57 O ANISOU 3460 O HOH B 579 2065 2734 3777 367 834 -134 O HETATM 3461 O HOH B 580 -6.543 -37.783 20.330 1.00 45.55 O ANISOU 3461 O HOH B 580 4749 4408 8151 2587 2013 562 O HETATM 3462 O HOH B 581 5.381 -3.419 -1.052 1.00 56.00 O ANISOU 3462 O HOH B 581 3607 9042 8628 635 2346 5161 O HETATM 3463 O HOH B 582 -9.243 -33.521 32.998 1.00 58.11 O ANISOU 3463 O HOH B 582 7379 8494 6207 1762 -1918 1487 O HETATM 3464 O HOH B 583 -16.678 -39.077 9.776 1.00 27.94 O ANISOU 3464 O HOH B 583 4522 2530 3562 -1506 960 -447 O HETATM 3465 O HOH B 584 -2.071 -17.425 29.552 1.00 43.01 O ANISOU 3465 O HOH B 584 2447 7133 6761 511 -433 -2012 O HETATM 3466 O HOH B 585 1.288 -9.615 28.976 1.00 34.48 O ANISOU 3466 O HOH B 585 1146 6257 5699 -144 -925 -2 O HETATM 3467 O HOH B 586 -24.481 -35.007 21.876 1.00 20.42 O ANISOU 3467 O HOH B 586 1567 1524 4667 -269 349 269 O HETATM 3468 O HOH B 587 5.189 -16.935 9.930 1.00 50.49 O ANISOU 3468 O HOH B 587 6522 7382 5279 1694 -1344 1526 O HETATM 3469 O HOH B 588 1.632 -31.660 13.715 1.00 36.11 O ANISOU 3469 O HOH B 588 4568 4055 5097 -71 845 353 O HETATM 3470 O HOH B 589 -9.171 -7.681 2.549 1.00 32.57 O ANISOU 3470 O HOH B 589 3104 5007 4264 1838 93 936 O HETATM 3471 O HOH B 590 -28.118 -2.897 14.403 1.00 48.48 O ANISOU 3471 O HOH B 590 6764 5180 6475 1985 -563 -1850 O HETATM 3472 O HOH B 591 -4.243 -9.508 28.135 1.00 22.97 O ANISOU 3472 O HOH B 591 1943 3337 3447 -18 6 -385 O HETATM 3473 O HOH B 592 -23.579 -14.654 36.012 1.00 33.22 O ANISOU 3473 O HOH B 592 3146 2096 7380 463 698 -413 O HETATM 3474 O HOH B 593 -19.463 -40.386 16.009 1.00 30.80 O ANISOU 3474 O HOH B 593 4334 3777 3592 -1609 1142 837 O HETATM 3475 O HOH B 594 -11.775 -17.087 22.827 1.00 17.52 O ANISOU 3475 O HOH B 594 1664 1645 3348 211 94 131 O HETATM 3476 O HOH B 595 -13.965 12.629 27.435 1.00 28.38 O ANISOU 3476 O HOH B 595 5133 1464 4186 -473 1574 68 O HETATM 3477 O HOH B 596 -2.640 -5.972 18.247 1.00 22.81 O ANISOU 3477 O HOH B 596 1741 3132 3792 -850 192 -30 O HETATM 3478 O HOH B 597 -14.392 -16.505 0.724 1.00 39.26 O ANISOU 3478 O HOH B 597 2121 8066 4729 -1200 117 627 O HETATM 3479 O HOH B 598 -21.266 13.786 24.729 1.00 31.17 O ANISOU 3479 O HOH B 598 4492 2872 4480 -187 573 944 O HETATM 3480 O HOH B 599 -13.473 12.752 33.372 1.00 36.86 O ANISOU 3480 O HOH B 599 4430 5338 4239 -1228 -530 -553 O HETATM 3481 O HOH B 600 4.994 1.349 15.874 1.00 41.83 O ANISOU 3481 O HOH B 600 6366 3884 5645 -2562 2172 -617 O HETATM 3482 O HOH B 601 -9.244 -17.200 20.990 1.00 26.68 O ANISOU 3482 O HOH B 601 1368 3527 5242 587 381 2244 O HETATM 3483 O HOH B 602 -4.702 -17.972 26.062 1.00 30.07 O ANISOU 3483 O HOH B 602 3977 3319 4128 1239 -336 115 O HETATM 3484 O HOH B 603 -14.023 -20.680 34.963 1.00 40.48 O ANISOU 3484 O HOH B 603 6943 4267 4172 228 58 -1755 O HETATM 3485 O HOH B 604 -0.643 -12.546 17.517 1.00 22.18 O ANISOU 3485 O HOH B 604 1728 2758 3941 -338 -178 131 O HETATM 3486 O HOH B 605 -19.868 9.419 34.332 1.00 26.53 O ANISOU 3486 O HOH B 605 4564 2233 3283 453 868 -70 O HETATM 3487 O HOH B 606 -23.288 -39.317 31.151 1.00 25.33 O ANISOU 3487 O HOH B 606 3170 2237 4218 440 118 139 O HETATM 3488 O HOH B 607 -20.452 9.916 24.232 1.00 20.73 O ANISOU 3488 O HOH B 607 2814 1588 3475 582 430 184 O HETATM 3489 O HOH B 608 -17.398 8.110 35.110 1.00 29.19 O ANISOU 3489 O HOH B 608 3711 2365 5016 701 634 -540 O HETATM 3490 O HOH B 609 -7.144 -4.950 19.741 1.00 21.96 O ANISOU 3490 O HOH B 609 2672 2114 3558 134 977 -109 O HETATM 3491 O HOH B 610 -20.714 -8.836 38.414 1.00 33.04 O ANISOU 3491 O HOH B 610 4393 4200 3960 1231 302 241 O HETATM 3492 O HOH B 611 -8.829 -1.457 7.490 1.00 52.40 O ANISOU 3492 O HOH B 611 5946 3433 10529 1002 -3059 -208 O HETATM 3493 O HOH B 612 -18.680 -13.676 9.567 1.00 24.96 O ANISOU 3493 O HOH B 612 2170 4658 2655 -409 -410 726 O HETATM 3494 O HOH B 613 -12.116 10.167 30.198 1.00 42.84 O ANISOU 3494 O HOH B 613 5793 5732 4751 2808 1848 1262 O HETATM 3495 O HOH B 614 -7.856 -14.568 22.132 1.00 40.78 O ANISOU 3495 O HOH B 614 2775 4909 7809 -499 1272 -574 O HETATM 3496 O HOH B 615 -11.318 -6.280 24.550 1.00 19.93 O ANISOU 3496 O HOH B 615 1823 2406 3343 -202 620 211 O HETATM 3497 O HOH B 616 -12.563 -18.087 3.324 1.00 25.14 O ANISOU 3497 O HOH B 616 4428 1889 3235 -387 -1213 500 O HETATM 3498 O HOH B 617 -25.620 -26.110 12.638 1.00 48.89 O ANISOU 3498 O HOH B 617 1871 10024 6680 -349 -839 1702 O HETATM 3499 O HOH B 618 -6.936 10.511 32.129 1.00 53.93 O ANISOU 3499 O HOH B 618 7870 4335 8284 -2287 -2890 190 O HETATM 3500 O HOH B 619 -10.117 -9.728 8.650 1.00 21.66 O ANISOU 3500 O HOH B 619 3281 1327 3622 277 195 -244 O HETATM 3501 O HOH B 620 5.892 -16.709 4.245 1.00 32.95 O ANISOU 3501 O HOH B 620 1717 4915 5889 -542 12 966 O HETATM 3502 O HOH B 621 -7.599 -17.024 8.237 1.00 13.17 O ANISOU 3502 O HOH B 621 1175 1309 2522 -58 329 336 O HETATM 3503 O HOH B 622 0.756 -28.315 1.173 1.00 34.08 O ANISOU 3503 O HOH B 622 3487 5370 4091 1472 -275 -489 O HETATM 3504 O HOH B 623 -14.284 -41.120 22.935 1.00 34.89 O ANISOU 3504 O HOH B 623 4108 1515 7632 2 3010 461 O HETATM 3505 O HOH B 624 5.937 -24.924 5.382 1.00 41.14 O ANISOU 3505 O HOH B 624 2569 5692 7371 755 1079 2262 O HETATM 3506 O HOH B 625 -27.529 0.296 20.275 1.00 41.53 O ANISOU 3506 O HOH B 625 5202 4263 6316 2015 -465 -1193 O HETATM 3507 O HOH B 626 -22.128 -37.439 13.504 1.00 36.75 O ANISOU 3507 O HOH B 626 5562 3797 4603 -335 629 -205 O HETATM 3508 O HOH B 627 -2.677 -31.617 -6.452 1.00 30.84 O ANISOU 3508 O HOH B 627 4805 3459 3453 147 1274 -607 O HETATM 3509 O HOH B 628 -7.599 -4.363 44.395 1.00 40.03 O ANISOU 3509 O HOH B 628 6505 4260 4444 941 -2537 -936 O HETATM 3510 O HOH B 629 -9.836 -5.559 47.404 1.00 55.84 O ANISOU 3510 O HOH B 629 8243 6431 6542 482 -992 2064 O HETATM 3511 O HOH B 630 -28.088 -26.373 23.402 1.00 44.12 O ANISOU 3511 O HOH B 630 2684 5831 8249 -33 1619 1275 O HETATM 3512 O HOH B 631 1.735 -6.825 9.040 1.00 24.27 O ANISOU 3512 O HOH B 631 2604 2854 3764 -648 874 317 O HETATM 3513 O HOH B 632 -11.233 -26.280 36.198 1.00 48.34 O ANISOU 3513 O HOH B 632 4386 3558 10421 -247 1223 2457 O HETATM 3514 O HOH B 633 -13.355 -9.888 12.628 1.00 21.61 O ANISOU 3514 O HOH B 633 2443 2311 3457 548 123 428 O HETATM 3515 O HOH B 634 -5.215 7.975 17.558 1.00 41.49 O ANISOU 3515 O HOH B 634 4056 3433 8275 -951 2402 -1408 O HETATM 3516 O HOH B 635 -13.207 14.332 29.686 1.00 28.99 O ANISOU 3516 O HOH B 635 3553 1787 5676 69 -398 -786 O HETATM 3517 O HOH B 636 -1.470 -4.052 0.202 1.00 33.52 O ANISOU 3517 O HOH B 636 3923 3035 5779 274 2077 1208 O HETATM 3518 O HOH B 637 -13.382 -26.436 19.911 1.00 24.30 O ANISOU 3518 O HOH B 637 3771 1814 3648 -68 726 323 O HETATM 3519 O HOH B 638 0.062 -25.863 -7.513 1.00 56.08 O ANISOU 3519 O HOH B 638 10906 4970 5432 -1786 4584 -101 O HETATM 3520 O HOH B 639 -1.106 -31.487 20.142 1.00 42.33 O ANISOU 3520 O HOH B 639 5603 6992 3487 1115 381 394 O HETATM 3521 O HOH B 640 -12.972 -33.043 -0.881 1.00 34.01 O ANISOU 3521 O HOH B 640 6101 3571 3251 -1508 356 -63 O HETATM 3522 O HOH B 641 -6.715 -11.237 26.698 1.00 20.53 O ANISOU 3522 O HOH B 641 1048 3470 3282 -694 40 -852 O HETATM 3523 O HOH B 642 -26.764 0.307 26.972 1.00 29.41 O ANISOU 3523 O HOH B 642 2335 2678 6161 -168 678 545 O HETATM 3524 O HOH B 643 0.729 -23.496 19.866 1.00 40.61 O ANISOU 3524 O HOH B 643 3056 6977 5396 2888 693 2618 O HETATM 3525 O HOH B 644 -8.935 -16.254 18.654 1.00 17.82 O ANISOU 3525 O HOH B 644 1233 2263 3274 -10 312 600 O HETATM 3526 O HOH B 645 -8.141 -7.989 25.586 1.00 25.37 O ANISOU 3526 O HOH B 645 2905 2344 4390 -300 558 -154 O HETATM 3527 O HOH B 646 2.188 -15.181 11.540 1.00 33.74 O ANISOU 3527 O HOH B 646 2836 4485 5497 -482 -522 -771 O HETATM 3528 O HOH B 647 -11.766 2.292 10.506 1.00 46.19 O ANISOU 3528 O HOH B 647 9310 3808 4434 100 541 319 O HETATM 3529 O HOH B 648 -15.966 -10.200 17.348 1.00 12.48 O ANISOU 3529 O HOH B 648 883 1336 2521 359 331 -41 O HETATM 3530 O HOH B 649 3.069 -19.884 8.609 1.00 21.75 O ANISOU 3530 O HOH B 649 1616 2863 3787 569 136 543 O HETATM 3531 O HOH B 650 -25.461 -2.698 13.755 1.00 41.52 O ANISOU 3531 O HOH B 650 3157 7026 5592 777 -167 -923 O HETATM 3532 O HOH B 651 -15.152 -29.434 3.638 1.00 21.90 O ANISOU 3532 O HOH B 651 3399 2248 2673 -569 200 54 O HETATM 3533 O HOH B 652 7.490 -15.248 -0.198 1.00 49.45 O ANISOU 3533 O HOH B 652 3996 5819 8976 465 -391 -341 O HETATM 3534 O HOH B 653 -22.352 -26.869 10.523 1.00 47.87 O ANISOU 3534 O HOH B 653 3405 10518 4266 1796 121 501 O HETATM 3535 O HOH B 654 -20.335 1.096 10.679 1.00 52.36 O ANISOU 3535 O HOH B 654 6471 9598 3824 2822 -917 -737 O HETATM 3536 O HOH B 655 -15.464 -12.805 32.796 1.00 38.98 O ANISOU 3536 O HOH B 655 6315 3937 4557 335 -837 145 O HETATM 3537 O HOH B 656 -14.864 -37.898 33.595 1.00 32.92 O ANISOU 3537 O HOH B 656 3763 2910 5835 1247 1381 1973 O HETATM 3538 O HOH B 657 -26.138 -25.606 25.613 1.00 23.49 O ANISOU 3538 O HOH B 657 1780 2921 4224 -126 1003 -228 O HETATM 3539 O HOH B 658 -13.279 -43.569 12.907 1.00 46.50 O ANISOU 3539 O HOH B 658 8130 4460 5080 922 2081 -488 O HETATM 3540 O HOH B 659 -21.133 4.665 37.879 1.00 31.84 O ANISOU 3540 O HOH B 659 4011 4636 3453 1251 584 -1261 O HETATM 3541 O BHOH B 660 3.825 -12.333 17.052 0.30 29.75 O ANISOU 3541 O BHOH B 660 173 4196 6935 474 585 -2020 O HETATM 3542 O HOH B 661 -8.341 -28.216 3.083 1.00 17.20 O ANISOU 3542 O HOH B 661 1683 1897 2955 -609 71 584 O HETATM 3543 O HOH B 662 -10.445 -36.564 6.170 1.00 52.43 O ANISOU 3543 O HOH B 662 10699 3067 6154 -1868 3358 -498 O HETATM 3544 O HOH B 663 -4.186 3.724 34.493 1.00 52.41 O ANISOU 3544 O HOH B 663 3150 7948 8817 -1057 375 -2337 O HETATM 3545 O HOH B 664 -3.223 -17.904 32.879 1.00 70.34 O ANISOU 3545 O HOH B 664 9060 8037 9629 -1049 -6583 1209 O HETATM 3546 O HOH B 665 8.325 -12.130 3.484 1.00 50.21 O ANISOU 3546 O HOH B 665 4800 9744 4533 47 -941 2492 O HETATM 3547 O HOH B 666 -29.686 -7.224 22.021 1.00 41.38 O ANISOU 3547 O HOH B 666 4522 6694 4506 1342 -396 417 O HETATM 3548 O HOH B 667 -11.371 -17.252 -11.539 1.00 42.84 O ANISOU 3548 O HOH B 667 3486 5518 7274 -1169 -2202 3208 O HETATM 3549 O HOH B 668 -6.511 -34.571 5.780 1.00 42.74 O ANISOU 3549 O HOH B 668 6526 5491 4221 -585 1158 657 O HETATM 3550 O HOH B 669 8.423 -7.189 -3.462 1.00 43.85 O ANISOU 3550 O HOH B 669 2459 9574 4628 -1736 -230 619 O HETATM 3551 O HOH B 670 -14.513 12.088 19.346 1.00 34.01 O ANISOU 3551 O HOH B 670 6145 1835 4941 802 1389 848 O HETATM 3552 O HOH B 671 -22.302 -36.617 28.484 1.00 35.52 O ANISOU 3552 O HOH B 671 5594 4059 3842 -3099 907 311 O HETATM 3553 O HOH B 672 -10.137 -18.506 31.037 1.00 41.83 O ANISOU 3553 O HOH B 672 2722 7397 5774 -505 255 -1448 O HETATM 3554 O HOH B 673 -27.634 2.522 17.512 1.00 53.52 O ANISOU 3554 O HOH B 673 5177 8470 6687 -646 289 -1785 O HETATM 3555 O HOH B 674 -10.082 -10.919 -8.146 1.00 48.93 O ANISOU 3555 O HOH B 674 3161 7082 8347 -688 -2409 2063 O HETATM 3556 O HOH B 675 -2.835 -15.268 36.568 1.00 42.78 O ANISOU 3556 O HOH B 675 8490 3758 4006 1713 -1042 787 O HETATM 3557 O HOH B 676 5.270 -13.069 5.850 1.00 52.31 O ANISOU 3557 O HOH B 676 3572 11399 4904 -1157 275 1377 O HETATM 3558 O HOH B 677 -6.033 -28.544 28.372 1.00 35.24 O ANISOU 3558 O HOH B 677 4230 3906 5255 306 1152 1353 O HETATM 3559 O HOH B 678 -24.316 -17.828 32.434 1.00 31.35 O ANISOU 3559 O HOH B 678 3545 5162 3205 1380 377 51 O HETATM 3560 O HOH B 679 -15.315 -18.648 32.916 1.00 37.19 O ANISOU 3560 O HOH B 679 4620 3663 5847 -1013 1051 -111 O HETATM 3561 O HOH B 680 -14.553 -12.252 4.403 1.00 51.16 O ANISOU 3561 O HOH B 680 6106 3595 9738 2782 -2947 -989 O HETATM 3562 O HOH B 681 -19.538 -33.590 7.100 1.00 34.70 O ANISOU 3562 O HOH B 681 3599 4648 4936 -1958 69 -580 O HETATM 3563 O HOH B 682 -25.632 -37.554 21.762 1.00 29.11 O ANISOU 3563 O HOH B 682 3415 2433 5212 -356 1971 -13 O HETATM 3564 O HOH B 683 2.508 -2.431 20.227 1.00 41.13 O ANISOU 3564 O HOH B 683 3796 4782 7048 -1820 2094 -1726 O HETATM 3565 O HOH B 684 -7.514 -35.222 26.274 1.00 25.93 O ANISOU 3565 O HOH B 684 2647 3485 3719 831 379 924 O HETATM 3566 O HOH B 685 -1.012 -12.462 36.695 1.00 35.90 O ANISOU 3566 O HOH B 685 4597 4123 4922 1136 -1179 -206 O HETATM 3567 O HOH B 686 -10.547 -11.161 19.967 1.00 15.13 O ANISOU 3567 O HOH B 686 1287 1611 2849 -296 -150 656 O HETATM 3568 O HOH B 687 -2.585 -26.656 -8.148 1.00 35.71 O ANISOU 3568 O HOH B 687 5651 4326 3592 837 1705 900 O HETATM 3569 O HOH B 688 -12.777 -14.379 37.556 1.00 49.99 O ANISOU 3569 O HOH B 688 4976 6025 7992 1523 852 1747 O HETATM 3570 O HOH B 689 8.713 -22.565 -8.880 1.00 45.55 O ANISOU 3570 O HOH B 689 4213 7078 6016 -1110 -2625 2330 O HETATM 3571 O HOH B 690 -7.676 -37.059 3.098 1.00 42.46 O ANISOU 3571 O HOH B 690 7135 3555 5442 579 3480 1155 O HETATM 3572 O HOH B 691 -7.706 -37.246 24.267 1.00 39.19 O ANISOU 3572 O HOH B 691 5685 3917 5289 1228 2420 711 O HETATM 3573 O HOH B 692 -20.746 -12.377 36.511 1.00 49.13 O ANISOU 3573 O HOH B 692 6372 5442 6855 -995 584 -2238 O HETATM 3574 O HOH B 693 -18.675 -26.285 5.754 1.00 24.86 O ANISOU 3574 O HOH B 693 2585 3695 3168 533 -141 961 O HETATM 3575 O HOH B 694 -7.632 11.483 19.575 1.00 52.40 O ANISOU 3575 O HOH B 694 5926 5905 8077 -1117 645 2012 O HETATM 3576 O HOH B 695 2.922 -10.771 -16.915 1.00 28.57 O ANISOU 3576 O HOH B 695 2441 5223 3192 1713 375 -144 O HETATM 3577 O HOH B 696 -8.911 -35.215 4.723 1.00 37.13 O ANISOU 3577 O HOH B 696 7756 2865 3486 -1171 932 223 O HETATM 3578 O HOH B 697 -27.749 -29.701 24.085 1.00 55.74 O ANISOU 3578 O HOH B 697 4520 6652 10006 -2562 4274 -3225 O HETATM 3579 O HOH B 698 -11.350 -23.242 -13.130 1.00 57.70 O ANISOU 3579 O HOH B 698 6524 6824 8575 -2420 -2652 -2080 O HETATM 3580 O HOH B 699 -0.079 -32.442 11.177 1.00 25.05 O ANISOU 3580 O HOH B 699 2001 2381 5134 379 1257 772 O HETATM 3581 O HOH B 700 3.961 -2.970 28.160 1.00 49.14 O ANISOU 3581 O HOH B 700 2810 8685 7176 -1292 170 -2640 O HETATM 3582 O HOH B 701 3.200 -32.622 6.539 1.00 52.18 O ANISOU 3582 O HOH B 701 6500 6755 6572 3329 1120 987 O HETATM 3583 O HOH B 702 -23.894 -2.901 38.263 1.00 28.69 O ANISOU 3583 O HOH B 702 4235 3447 3219 -566 186 -545 O HETATM 3584 O HOH B 703 -16.017 -13.417 16.714 1.00 16.21 O ANISOU 3584 O HOH B 703 1251 2218 2688 20 441 2 O HETATM 3585 O HOH B 704 -27.619 -27.820 19.724 1.00 53.61 O ANISOU 3585 O HOH B 704 4772 4417 11179 431 -4765 -2191 O HETATM 3586 O HOH B 705 -18.369 -2.633 10.489 1.00 51.07 O ANISOU 3586 O HOH B 705 5314 9081 5008 -358 11 1996 O HETATM 3587 O HOH B 706 1.701 -7.715 30.751 1.00 49.00 O ANISOU 3587 O HOH B 706 7907 4910 5799 1859 -2079 -700 O HETATM 3588 O HOH B 707 -20.932 -46.986 19.449 1.00 45.25 O ANISOU 3588 O HOH B 707 7786 4868 4539 -2162 666 1442 O HETATM 3589 O HOH B 708 -9.450 -9.066 -6.730 1.00 55.33 O ANISOU 3589 O HOH B 708 4119 8821 8084 -225 -244 2333 O HETATM 3590 O HOH B 709 -4.754 -31.264 22.367 1.00 29.06 O ANISOU 3590 O HOH B 709 3050 3583 4409 70 645 668 O HETATM 3591 O HOH B 710 -24.137 -23.787 11.280 1.00 34.07 O ANISOU 3591 O HOH B 710 2824 5231 4892 -1704 -1210 504 O HETATM 3592 O HOH B 711 5.087 -2.865 2.267 1.00 30.27 O ANISOU 3592 O HOH B 711 3050 3141 5308 -503 1222 877 O HETATM 3593 O HOH B 712 -19.637 12.972 11.654 1.00 51.72 O ANISOU 3593 O HOH B 712 7988 6241 5423 -2359 -1919 471 O HETATM 3594 O HOH B 713 -3.145 -25.603 25.491 1.00 49.55 O ANISOU 3594 O HOH B 713 1973 7495 9359 1739 1181 5248 O HETATM 3595 O HOH B 714 -28.013 -1.317 24.871 0.50 32.88 O ANISOU 3595 O HOH B 714 1705 4416 6371 1147 881 -3093 O HETATM 3596 O HOH B 715 -26.412 -29.442 31.549 1.00 58.74 O ANISOU 3596 O HOH B 715 2975 10490 8853 -92 1684 1264 O HETATM 3597 O HOH B 716 -20.127 6.274 16.306 1.00 57.62 O ANISOU 3597 O HOH B 716 7565 4574 9756 332 -1193 1169 O HETATM 3598 O HOH B 717 -23.286 -0.918 13.781 1.00 39.57 O ANISOU 3598 O HOH B 717 4353 4481 6202 22 -1797 1538 O HETATM 3599 O HOH B 718 -11.200 -41.731 19.531 1.00 43.79 O ANISOU 3599 O HOH B 718 5867 2157 8616 852 1883 122 O HETATM 3600 O HOH B 719 -23.832 -34.096 28.603 1.00 27.02 O ANISOU 3600 O HOH B 719 2912 3369 3986 849 1256 93 O HETATM 3601 O HOH B 720 3.884 -18.773 10.762 1.00 53.94 O ANISOU 3601 O HOH B 720 2061 12965 5470 -539 -220 -1481 O HETATM 3602 O HOH B 721 -0.579 -24.176 24.301 1.00 46.12 O ANISOU 3602 O HOH B 721 2860 9098 5565 1397 -763 1319 O HETATM 3603 O HOH B 722 -27.326 -23.689 27.021 1.00 22.64 O ANISOU 3603 O HOH B 722 2230 1818 4552 -1159 544 -107 O HETATM 3604 O HOH B 723 -4.471 -4.017 3.963 1.00 33.21 O ANISOU 3604 O HOH B 723 4640 3408 4569 912 1730 776 O HETATM 3605 O HOH B 724 -3.370 4.644 36.562 1.00 59.91 O ANISOU 3605 O HOH B 724 4189 7641 10933 -2595 -635 -2180 O HETATM 3606 O HOH B 725 -7.294 -34.508 8.974 1.00 37.11 O ANISOU 3606 O HOH B 725 5981 3360 4758 -143 -737 1518 O HETATM 3607 O HOH B 726 -9.302 1.932 43.841 1.00 44.26 O ANISOU 3607 O HOH B 726 7239 4444 5135 -95 -869 -775 O HETATM 3608 O HOH B 727 -5.380 -6.419 0.525 1.00 48.06 O ANISOU 3608 O HOH B 727 5879 3770 8612 -110 1537 -1235 O HETATM 3609 O HOH B 728 -15.447 -0.032 10.475 1.00 50.77 O ANISOU 3609 O HOH B 728 8808 5732 4751 3794 2426 848 O HETATM 3610 O HOH B 729 -18.166 -23.876 6.862 1.00 33.59 O ANISOU 3610 O HOH B 729 5348 3933 3482 1352 -1516 53 O HETATM 3611 O HOH B 730 4.210 -6.604 16.923 1.00 43.47 O ANISOU 3611 O HOH B 730 3183 6458 6875 45 2405 -974 O HETATM 3612 O HOH B 731 -9.342 -41.164 23.691 1.00 58.19 O ANISOU 3612 O HOH B 731 1739 8123 12246 685 1519 3459 O HETATM 3613 O HOH B 732 -19.271 -23.815 3.504 1.00 37.53 O ANISOU 3613 O HOH B 732 2816 6144 5298 -328 -742 2292 O HETATM 3614 O HOH B 733 5.932 -27.260 17.233 1.00 50.08 O ANISOU 3614 O HOH B 733 6069 7221 5736 -1364 -1632 -166 O HETATM 3615 O HOH B 734 -28.764 0.072 32.847 1.00 52.29 O ANISOU 3615 O HOH B 734 8052 2435 9381 -704 2554 -1780 O HETATM 3616 O HOH B 735 -16.847 -14.444 30.777 1.00 28.23 O ANISOU 3616 O HOH B 735 4336 2284 4107 -911 174 184 O HETATM 3617 O HOH B 736 -0.035 5.722 25.604 1.00 59.88 O ANISOU 3617 O HOH B 736 8865 4317 9569 -1413 -2094 -2134 O HETATM 3618 O HOH B 737 -24.451 -36.353 14.540 1.00 30.54 O ANISOU 3618 O HOH B 737 4109 3081 4412 -963 452 -334 O HETATM 3619 O HOH B 738 5.774 -3.341 9.732 1.00 41.34 O ANISOU 3619 O HOH B 738 4188 4527 6990 -1470 1119 -490 O HETATM 3620 O HOH B 739 -15.261 12.183 21.783 1.00 25.33 O ANISOU 3620 O HOH B 739 3406 2093 4127 41 136 175 O HETATM 3621 O HOH B 740 -11.749 -38.642 8.918 1.00 55.05 O ANISOU 3621 O HOH B 740 10990 5648 4279 -687 609 -1296 O HETATM 3622 O HOH B 741 -4.668 7.715 26.835 1.00 61.55 O ANISOU 3622 O HOH B 741 10406 6839 6142 -4710 2562 -539 O HETATM 3623 O HOH B 742 -28.114 10.301 22.185 1.00 36.74 O ANISOU 3623 O HOH B 742 4067 4903 4990 -409 230 288 O HETATM 3624 O HOH B 743 -15.252 -27.324 0.361 1.00 56.99 O ANISOU 3624 O HOH B 743 5618 11778 4256 -4774 131 413 O HETATM 3625 O HOH B 744 -14.066 1.203 11.333 1.00 37.36 O ANISOU 3625 O HOH B 744 5375 4135 4686 257 1411 1251 O HETATM 3626 O HOH B 745 -33.419 -7.434 28.257 1.00 36.88 O ANISOU 3626 O HOH B 745 2592 3142 8277 1141 -1470 -2640 O HETATM 3627 O HOH B 746 -2.513 -18.895 27.386 1.00 36.15 O ANISOU 3627 O HOH B 746 3021 6083 4630 -719 449 636 O HETATM 3628 O HOH B 747 -11.385 12.427 16.232 1.00 46.97 O ANISOU 3628 O HOH B 747 9267 3029 5551 526 837 976 O HETATM 3629 O HOH B 748 10.100 -20.116 -6.996 1.00 51.46 O ANISOU 3629 O HOH B 748 7141 5636 6775 445 1585 1962 O HETATM 3630 O HOH B 749 -14.499 -30.403 -0.578 1.00 45.80 O ANISOU 3630 O HOH B 749 8160 6119 3122 -1721 -1643 533 O HETATM 3631 O HOH B 750 -15.248 -16.807 3.255 1.00 26.69 O ANISOU 3631 O HOH B 750 2727 3062 4351 291 -209 495 O HETATM 3632 O HOH B 751 -7.735 -5.334 2.157 1.00 49.69 O ANISOU 3632 O HOH B 751 8697 3403 6779 244 -376 604 O HETATM 3633 O HOH B 752 -4.575 7.260 20.201 1.00 38.99 O ANISOU 3633 O HOH B 752 5037 4661 5118 -589 2125 -145 O HETATM 3634 O HOH B 753 -16.531 -3.021 45.929 1.00 48.12 O ANISOU 3634 O HOH B 753 7544 6253 4489 -1154 -918 1929 O HETATM 3635 O HOH B 754 4.268 -0.784 27.290 1.00 45.50 O ANISOU 3635 O HOH B 754 5134 4452 7703 -1683 -209 -1034 O HETATM 3636 O HOH B 755 -28.155 6.627 24.656 1.00 42.28 O ANISOU 3636 O HOH B 755 4625 5382 6059 153 484 1689 O HETATM 3637 O HOH B 756 -7.953 12.897 25.459 1.00 49.43 O ANISOU 3637 O HOH B 756 5384 3414 9982 -1124 531 -1590 O HETATM 3638 O HOH B 757 -15.046 -18.122 35.264 1.00 40.73 O ANISOU 3638 O HOH B 757 4181 4714 6580 -413 711 -953 O HETATM 3639 O HOH B 758 3.589 -10.198 12.363 1.00 37.07 O ANISOU 3639 O HOH B 758 2081 7430 4575 -930 480 -1113 O HETATM 3640 O HOH B 759 1.486 -13.750 24.057 1.00 36.37 O ANISOU 3640 O HOH B 759 4093 4715 5013 321 -157 -355 O HETATM 3641 O HOH B 760 -28.762 -23.511 16.660 1.00 53.09 O ANISOU 3641 O HOH B 760 6530 6759 6882 -801 -1072 546 O HETATM 3642 O HOH B 761 2.663 -9.240 16.502 1.00 30.73 O ANISOU 3642 O HOH B 761 1628 4966 5083 -415 212 -965 O HETATM 3643 O HOH B 762 5.477 -7.819 7.834 1.00 53.34 O ANISOU 3643 O HOH B 762 5835 6471 7959 195 1428 618 O HETATM 3644 O HOH B 763 -24.648 3.836 46.203 1.00 40.63 O ANISOU 3644 O HOH B 763 4731 4940 5768 -68 324 332 O HETATM 3645 O HOH B 764 -9.440 4.941 42.498 1.00 58.54 O ANISOU 3645 O HOH B 764 7756 7962 6524 2274 -1858 -2834 O HETATM 3646 O HOH B 765 -27.922 -26.077 38.554 1.00 52.86 O ANISOU 3646 O HOH B 765 6149 3715 10220 678 1434 -1963 O HETATM 3647 O HOH B 766 -26.027 -0.132 29.828 1.00 36.98 O ANISOU 3647 O HOH B 766 4014 4903 5133 367 1098 195 O HETATM 3648 O HOH B 767 6.379 0.231 24.525 1.00 57.99 O ANISOU 3648 O HOH B 767 5159 8432 8442 -1486 841 -251 O HETATM 3649 O HOH B 768 8.071 -4.748 4.084 1.00 47.29 O ANISOU 3649 O HOH B 768 3106 9813 5049 -3187 377 593 O HETATM 3650 O HOH B 769 -27.502 -32.518 24.265 1.00 56.34 O ANISOU 3650 O HOH B 769 6255 6808 8343 -1347 2801 25 O HETATM 3651 O HOH B 770 -15.541 -37.288 2.466 1.00 49.75 O ANISOU 3651 O HOH B 770 7142 3841 7919 -1185 830 -1454 O HETATM 3652 O HOH B 771 4.612 -4.150 20.519 1.00 40.41 O ANISOU 3652 O HOH B 771 4381 5827 5148 -265 795 -374 O HETATM 3653 O HOH B 772 5.725 -9.868 5.453 1.00 51.98 O ANISOU 3653 O HOH B 772 2617 8671 8462 -862 -747 480 O HETATM 3654 O HOH B 773 -25.376 -40.073 22.319 1.00 45.12 O ANISOU 3654 O HOH B 773 6903 2406 7834 1370 3962 1536 O HETATM 3655 O HOH B 774 -0.185 1.874 29.985 1.00 52.16 O ANISOU 3655 O HOH B 774 7105 5610 7104 -1345 502 -2521 O HETATM 3656 O HOH B 775 -17.217 -39.873 26.229 1.00 33.99 O ANISOU 3656 O HOH B 775 6800 1264 4852 -273 2177 -9 O HETATM 3657 O HOH B 776 6.233 -5.789 23.757 1.00 68.37 O ANISOU 3657 O HOH B 776 7847 8279 9851 877 -1868 4363 O HETATM 3658 O HOH B 777 -26.918 11.978 28.055 1.00 51.27 O ANISOU 3658 O HOH B 777 6854 4710 7917 2219 3226 860 O HETATM 3659 O HOH B 778 -31.648 -20.018 22.584 1.00 49.40 O ANISOU 3659 O HOH B 778 2810 6242 9718 -753 943 -909 O HETATM 3660 O HOH B 779 0.742 -21.758 23.144 1.00 55.49 O ANISOU 3660 O HOH B 779 6983 8136 5964 2461 507 1220 O HETATM 3661 O HOH B 780 3.664 -19.377 17.015 1.00 74.08 O ANISOU 3661 O HOH B 780 4108 11063 12975 -3221 3968 50 O HETATM 3662 O HOH B 781 -3.583 -24.299 27.482 1.00 53.79 O ANISOU 3662 O HOH B 781 8343 5908 6186 3487 -113 148 O HETATM 3663 O HOH B 782 -27.919 12.749 22.078 1.00 61.51 O ANISOU 3663 O HOH B 782 9425 4607 9337 2345 -3635 764 O HETATM 3664 O HOH B 783 0.741 -7.274 33.461 1.00 63.98 O ANISOU 3664 O HOH B 783 8697 7680 7933 2210 1449 2224 O HETATM 3665 O HOH B 784 -6.703 -8.674 27.624 1.00 24.34 O ANISOU 3665 O HOH B 784 2448 2348 4451 -192 -256 427 O HETATM 3666 O HOH B 785 -19.818 -35.947 8.980 1.00 40.45 O ANISOU 3666 O HOH B 785 3931 5458 5982 -110 149 -674 O HETATM 3667 O HOH B 786 -23.902 4.774 48.129 1.00 66.68 O ANISOU 3667 O HOH B 786 7715 8869 8754 -2218 536 -513 O HETATM 3668 O HOH B 787 -17.381 -29.664 2.232 1.00 32.59 O ANISOU 3668 O HOH B 787 2691 5034 4658 -249 -423 -361 O HETATM 3669 O HOH B 788 -15.522 -14.783 -1.317 1.00 60.71 O ANISOU 3669 O HOH B 788 5176 8749 9143 -1981 -3057 1587 O HETATM 3670 O HOH B 789 7.371 -28.944 6.752 1.00 66.27 O ANISOU 3670 O HOH B 789 8405 8127 8647 1844 150 385 O HETATM 3671 O HOH B 790 6.340 -31.041 12.258 1.00 49.12 O ANISOU 3671 O HOH B 790 3725 3999 10941 594 -760 -396 O HETATM 3672 O HOH B 791 7.234 -16.642 1.907 1.00 51.42 O ANISOU 3672 O HOH B 791 2583 7653 9302 211 1790 4110 O HETATM 3673 O HOH B 792 -20.927 0.292 45.833 1.00 58.13 O ANISOU 3673 O HOH B 792 9986 6689 5412 -843 1876 -1157 O HETATM 3674 O HOH B 793 -5.013 -34.272 25.699 1.00 41.66 O ANISOU 3674 O HOH B 793 3592 5930 6308 581 -839 88 O HETATM 3675 O HOH B 794 4.813 -20.497 6.581 1.00 28.53 O ANISOU 3675 O HOH B 794 2331 4521 3988 1091 495 609 O HETATM 3676 O HOH B 795 -17.248 13.970 10.883 1.00 53.07 O ANISOU 3676 O HOH B 795 10467 3701 5995 -3050 1706 -94 O HETATM 3677 O HOH B 796 -7.441 -36.559 28.725 1.00 47.69 O ANISOU 3677 O HOH B 796 5102 5540 7479 1709 2021 2756 O HETATM 3678 O HOH B 797 -29.673 -26.839 28.164 1.00 51.62 O ANISOU 3678 O HOH B 797 5165 6139 8309 -525 1135 1291 O HETATM 3679 O HOH B 798 -4.961 -36.504 4.757 1.00 50.32 O ANISOU 3679 O HOH B 798 5577 5747 7797 397 299 153 O HETATM 3680 O HOH B 799 -28.791 -13.299 38.073 1.00 49.98 O ANISOU 3680 O HOH B 799 6216 3948 8826 -620 788 28 O HETATM 3681 O HOH B 800 -22.385 -29.173 10.017 1.00 64.06 O ANISOU 3681 O HOH B 800 8062 8372 7905 1082 -1814 -946 O HETATM 3682 O HOH B 801 0.319 -14.325 15.440 1.00 38.36 O ANISOU 3682 O HOH B 801 4867 3244 6466 612 -423 -440 O HETATM 3683 O HOH B 802 6.548 -18.638 5.997 1.00 40.94 O ANISOU 3683 O HOH B 802 3008 6165 6382 -976 528 1985 O HETATM 3684 O HOH B 803 -20.047 -39.471 26.776 1.00 45.65 O ANISOU 3684 O HOH B 803 5078 4835 7432 -657 1889 1791 O HETATM 3685 O HOH B 804 -23.202 -16.978 40.059 1.00 64.80 O ANISOU 3685 O HOH B 804 9152 6918 8551 -2624 3861 453 O HETATM 3686 O HOH B 805 -12.502 -35.824 33.879 1.00 54.68 O ANISOU 3686 O HOH B 805 4820 8159 7797 1549 -1875 -82 O HETATM 3687 O HOH B 806 -20.470 -22.856 7.023 1.00 61.65 O ANISOU 3687 O HOH B 806 7924 9427 6072 4623 -3364 -404 O HETATM 3688 O HOH B 807 -3.038 7.428 24.810 1.00 54.03 O ANISOU 3688 O HOH B 807 4659 6646 9225 -624 1288 -1572 O HETATM 3689 O HOH B 808 -5.608 -17.514 35.227 1.00 64.40 O ANISOU 3689 O HOH B 808 6655 8489 9326 -1746 2423 175 O HETATM 3690 O HOH B 809 -2.498 -29.887 21.337 1.00 54.29 O ANISOU 3690 O HOH B 809 3477 9313 7840 -795 -145 -643 O HETATM 3691 O HOH B 810 -1.462 -9.411 40.153 1.00 60.54 O ANISOU 3691 O HOH B 810 7573 7931 7498 1018 -1730 658 O HETATM 3692 O HOH B 811 2.019 -30.435 -3.092 1.00 59.39 O ANISOU 3692 O HOH B 811 4856 6920 10789 -1341 1348 -1951 O HETATM 3693 O HOH B 812 -6.981 9.688 27.969 1.00 60.54 O ANISOU 3693 O HOH B 812 10002 4606 8394 -2181 -925 721 O HETATM 3694 O HOH B 813 4.137 -5.821 9.962 1.00 37.66 O ANISOU 3694 O HOH B 813 3625 4386 6296 -19 -163 -30 O HETATM 3695 O HOH B 814 -27.293 -34.323 22.560 1.00 43.56 O ANISOU 3695 O HOH B 814 3736 3408 9406 -1284 3114 -959 O HETATM 3696 O HOH B 815 -11.626 -11.965 -11.869 1.00 74.74 O ANISOU 3696 O HOH B 815 10007 8901 9491 -1004 1168 84 O HETATM 3697 O HOH B 816 -15.754 -22.228 -2.208 1.00 58.85 O ANISOU 3697 O HOH B 816 8424 10629 3308 -1589 1422 -1048 O HETATM 3698 O HOH B 817 -23.255 -25.256 9.227 1.00 56.48 O ANISOU 3698 O HOH B 817 7767 8257 5437 -2997 -1220 1843 O HETATM 3699 O HOH B 818 -12.547 -16.072 34.219 1.00 45.69 O ANISOU 3699 O HOH B 818 7124 5793 4443 493 -71 931 O HETATM 3700 O HOH B 819 -5.462 -38.406 24.533 1.00 57.26 O ANISOU 3700 O HOH B 819 7836 7112 6807 301 877 -912 O HETATM 3701 O HOH B 820 6.386 -22.799 6.988 1.00 34.66 O ANISOU 3701 O HOH B 820 3281 3871 6018 1107 1225 639 O HETATM 3702 O HOH B 821 -15.263 13.748 25.511 1.00 36.74 O ANISOU 3702 O HOH B 821 4020 4867 5073 -1972 707 1679 O HETATM 3703 O HOH B 822 -14.894 -18.642 -6.077 1.00 55.13 O ANISOU 3703 O HOH B 822 5205 7826 7916 421 1947 300 O HETATM 3704 O HOH B 823 -14.500 -39.964 8.117 1.00 52.83 O ANISOU 3704 O HOH B 823 9894 4759 5419 -550 4150 -676 O HETATM 3705 O HOH B 824 -9.858 -39.715 12.840 1.00 54.06 O ANISOU 3705 O HOH B 824 8389 6613 5539 4410 1466 453 O HETATM 3706 O HOH B 825 -1.203 -16.548 34.285 1.00 58.44 O ANISOU 3706 O HOH B 825 8084 4953 9167 2671 1710 1456 O HETATM 3707 O HOH B 826 -19.091 -38.289 8.634 1.00 39.34 O ANISOU 3707 O HOH B 826 3594 6298 5055 -1497 -228 -822 O HETATM 3708 O HOH B 827 -0.128 -15.645 29.106 1.00 48.17 O ANISOU 3708 O HOH B 827 5038 8016 5246 518 -462 -206 O HETATM 3709 O HOH B 828 -11.419 -18.883 33.321 1.00 55.77 O ANISOU 3709 O HOH B 828 8721 5184 7285 -2168 -719 663 O HETATM 3710 O HOH B 829 -4.303 -4.299 0.904 1.00 56.29 O ANISOU 3710 O HOH B 829 6042 5266 10079 2934 3434 2121 O HETATM 3711 O HOH B 830 -12.249 -5.080 8.028 1.00 58.11 O ANISOU 3711 O HOH B 830 5674 12433 3971 1393 529 530 O HETATM 3712 O HOH B 831 -5.658 -35.560 29.120 1.00 56.77 O ANISOU 3712 O HOH B 831 5270 8790 7511 617 966 131 O HETATM 3713 O HOH B 832 -30.438 13.007 23.018 1.00 59.60 O ANISOU 3713 O HOH B 832 7806 7688 7152 172 1434 312 O HETATM 3714 O HOH B 833 -17.526 -31.048 -0.068 1.00 51.35 O ANISOU 3714 O HOH B 833 6579 7844 5087 -927 -1925 -91 O HETATM 3715 O HOH B 834 -15.317 -43.227 10.541 1.00 52.61 O ANISOU 3715 O HOH B 834 8506 3193 8289 -708 1010 -920 O HETATM 3716 O HOH M 201 -35.634 -9.656 32.819 1.00 39.96 O ANISOU 3716 O HOH M 201 6607 4008 4570 -782 1944 505 O HETATM 3717 O HOH M 202 -25.935 -23.170 42.315 1.00 27.98 O ANISOU 3717 O HOH M 202 3551 3745 3334 -1084 777 664 O HETATM 3718 O HOH M 203 -30.069 -15.318 39.801 1.00 36.73 O ANISOU 3718 O HOH M 203 5353 3592 5009 -1296 705 -1449 O HETATM 3719 O HOH M 204 -26.023 -15.379 36.978 1.00 29.18 O ANISOU 3719 O HOH M 204 4257 1893 4936 -315 -562 -231 O HETATM 3720 O HOH M 205 -34.202 -23.292 28.578 1.00 22.58 O ANISOU 3720 O HOH M 205 2221 3450 2910 -293 229 1350 O HETATM 3721 O HOH M 206 -13.683 -30.767 41.187 1.00 46.87 O ANISOU 3721 O HOH M 206 4126 6341 7342 1236 -53 1962 O HETATM 3722 O HOH M 207 -17.874 -33.234 45.575 1.00 49.24 O ANISOU 3722 O HOH M 207 8231 6106 4371 -24 -903 1629 O HETATM 3723 O HOH M 208 -25.859 -17.425 39.735 1.00 45.51 O ANISOU 3723 O HOH M 208 7963 3526 5802 -2084 2700 -1107 O HETATM 3724 O HOH M 209 -35.676 -13.916 15.744 1.00 54.68 O ANISOU 3724 O HOH M 209 6331 9877 4568 2982 401 861 O HETATM 3725 O HOH M 210 -22.664 -34.898 43.825 1.00 50.46 O ANISOU 3725 O HOH M 210 6692 6017 6465 2020 -734 847 O HETATM 3726 O HOH M 211 -27.860 -7.052 20.214 1.00 48.93 O ANISOU 3726 O HOH M 211 6014 3194 9382 764 276 1932 O HETATM 3727 O HOH M 212 -38.431 -22.304 21.438 1.00 58.42 O ANISOU 3727 O HOH M 212 6923 6017 9256 3134 -1746 -1074 O HETATM 3728 O HOH M 213 -14.471 -31.165 33.679 1.00 23.80 O ANISOU 3728 O HOH M 213 3771 2059 3214 52 748 305 O HETATM 3729 O HOH M 214 -32.086 -17.880 24.174 1.00 34.56 O ANISOU 3729 O HOH M 214 4422 3832 4879 -803 775 -169 O HETATM 3730 O HOH M 215 -17.316 -26.664 46.189 1.00 38.80 O ANISOU 3730 O HOH M 215 5505 4730 4507 -551 -1004 -959 O HETATM 3731 O HOH M 216 -19.943 -18.401 41.703 1.00 37.19 O ANISOU 3731 O HOH M 216 5226 2519 6386 191 123 -741 O HETATM 3732 O HOH M 217 -19.221 -20.321 44.330 1.00 31.36 O ANISOU 3732 O HOH M 217 5849 2780 3288 -452 -276 -509 O HETATM 3733 O HOH M 218 -15.221 -22.276 43.530 1.00 42.53 O ANISOU 3733 O HOH M 218 6754 4491 4916 -1476 554 -364 O HETATM 3734 O HOH M 219 -38.642 -10.850 32.765 1.00 45.91 O ANISOU 3734 O HOH M 219 5385 3737 8321 -284 -2565 -74 O HETATM 3735 O HOH M 220 -36.907 -14.957 29.594 1.00 56.25 O ANISOU 3735 O HOH M 220 6513 4039 10820 2243 2832 2609 O HETATM 3736 O HOH M 221 -12.808 -32.405 35.657 1.00 54.25 O ANISOU 3736 O HOH M 221 6164 7050 7398 1728 -651 3904 O HETATM 3737 O HOH M 222 -26.092 -10.472 14.475 1.00 47.42 O ANISOU 3737 O HOH M 222 2163 7739 8114 432 -1041 4807 O HETATM 3738 O HOH M 223 -36.134 -20.457 20.204 1.00 54.71 O ANISOU 3738 O HOH M 223 8276 4134 8378 -1716 505 1224 O HETATM 3739 O HOH M 224 -15.361 -24.096 45.574 1.00 44.29 O ANISOU 3739 O HOH M 224 3277 6730 6823 -922 354 -2631 O HETATM 3740 O HOH M 225 -17.465 -17.352 41.381 1.00 55.08 O ANISOU 3740 O HOH M 225 7018 3580 10331 -874 1391 282 O CONECT 3311 3312 CONECT 3312 3311 3313 3316 CONECT 3313 3312 3314 CONECT 3314 3313 3315 3317 CONECT 3315 3314 3316 CONECT 3316 3312 3315 CONECT 3317 3314 3318 3319 3324 CONECT 3318 3317 CONECT 3319 3317 3320 CONECT 3320 3319 3321 3322 CONECT 3321 3320 3336 CONECT 3322 3320 3323 CONECT 3323 3322 3324 3325 CONECT 3324 3317 3323 CONECT 3325 3323 3326 CONECT 3326 3325 3327 CONECT 3327 3326 3328 3329 CONECT 3328 3327 CONECT 3329 3327 3330 CONECT 3330 3329 3331 CONECT 3331 3330 3332 CONECT 3332 3331 3333 CONECT 3333 3332 3334 3335 CONECT 3334 3333 CONECT 3335 3333 3336 CONECT 3336 3321 3335 3337 CONECT 3337 3336 CONECT 3338 3339 3340 3341 3345 CONECT 3339 3338 3369 CONECT 3340 3338 CONECT 3341 3338 CONECT 3342 3343 3344 3345 3349 CONECT 3343 3342 3369 CONECT 3344 3342 CONECT 3345 3338 3342 CONECT 3346 3347 3348 3349 3350 CONECT 3347 3346 CONECT 3348 3346 CONECT 3349 3342 3346 CONECT 3350 3346 3351 CONECT 3351 3350 3352 CONECT 3352 3351 3353 3354 CONECT 3353 3352 3358 CONECT 3354 3352 3355 3356 CONECT 3355 3354 CONECT 3356 3354 3357 3358 CONECT 3357 3356 CONECT 3358 3353 3356 3359 CONECT 3359 3358 3360 3368 CONECT 3360 3359 3361 CONECT 3361 3360 3362 CONECT 3362 3361 3363 3368 CONECT 3363 3362 3364 3365 CONECT 3364 3363 CONECT 3365 3363 3366 CONECT 3366 3365 3367 CONECT 3367 3366 3368 CONECT 3368 3359 3362 3367 CONECT 3369 3339 3343 3433 3455 CONECT 3369 3456 3567 CONECT 3370 3371 3372 CONECT 3371 3370 CONECT 3372 3370 3373 3374 CONECT 3373 3372 CONECT 3374 3372 3375 CONECT 3375 3374 CONECT 3376 3377 3378 CONECT 3377 3376 CONECT 3378 3376 3379 3380 CONECT 3379 3378 CONECT 3380 3378 3381 CONECT 3381 3380 CONECT 3433 3369 CONECT 3455 3369 CONECT 3456 3369 CONECT 3567 3369 MASTER 591 0 5 24 21 0 18 6 3483 2 76 32 END
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Related entries of code: 2v52
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
2kj4
RCSB PDB
PDBbind
32-mer
2roz
RCSB PDB
PDBbind
32-mer
2v51
RCSB PDB
PDBbind
32-mer
Entry Information
PDB ID
2v52
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
G-actin
Ligand Name
32-mer
EC.Number
E.C.-.-.-.-
Resolution
1.45(Å)
Affinity (Kd/Ki/IC50)
Kd=1.9uM
Release Year
2008
Protein/NA Sequence
Check fasta file
Primary Reference
(2008) Embo J. Vol. 27: pp. 3198
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q8K4J6
P68135
Entrez Gene ID
NCBI Entrez Gene ID:
223701
ASD
Information of known allosteric effects of PDB entries
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