| HEADER VIRAL PROTEIN/IMMUNE SYSTEM 19-JUL-24 9CQA |
| TITLE STRUCTURE OF ANTIBODY 1G1 BOUND TO THE CENTRAL CONSERVED REGION OF RSV |
| TITLE 2 G |
| COMPND 9 MOL_ID: 3; |
| COMPND 10 MOLECULE: MATURE SECRETED GLYCOPROTEIN G; |
| COMPND 11 CHAIN: A; |
| COMPND 12 SYNONYM: MATURE SG; |
| COMPND 13 ENGINEERED: YES |
| SOURCE MOL_ID: 1; |
| SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; |
| SOURCE 3 ORGANISM_COMMON: HUMAN; |
| SOURCE 4 ORGANISM_TAXID: 9606; |
| SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; |
| SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; |
| SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; |
| SOURCE 8 MOL_ID: 2; |
| SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; |
| SOURCE 10 ORGANISM_COMMON: HUMAN; |
| SOURCE 11 ORGANISM_TAXID: 9606; |
| SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; |
| SOURCE 13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; |
| SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; |
| SOURCE 15 MOL_ID: 3; |
| SOURCE 16 ORGANISM_SCIENTIFIC: RESPIRATORY SYNCYTIAL VIRUS A2; |
| SOURCE 17 ORGANISM_TAXID: 1972429; |
| SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI; |
| SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562 |
| KEYWDS ANTIBODY, RESPIRATORY SYNCYTIAL VIRUS, G GLYCOPROTEIN, VIRAL PROTEIN, |
| KEYWDS 2 VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX |
| EXPDTA X-RAY DIFFRACTION |
| AUTHOR M.G.JUAREZ,R.M.DUBOIS |
| REVDAT 2 02-APR-25 9CQA 1 JRNL |
| REVDAT 1 19-FEB-25 9CQA 0 |
| JRNL AUTH M.G.JUAREZ,S.M.O'ROURKE,J.V.DZIMIANSKI,D.GAGNON,G.PENUNURI, |
| JRNL AUTH 2 V.H.B.SERRAO,R.B.CORBETT-DETIG,L.M.KAUVAR,R.M.DUBOIS |
| JRNL TITL STRUCTURES OF RESPIRATORY SYNCYTIAL VIRUS G BOUND TO BROADLY |
| JRNL TITL 2 REACTIVE ANTIBODIES PROVIDE INSIGHTS INTO VACCINE DESIGN. |
| JRNL REF SCI REP V. 15 8666 2025 |
| JRNL REFN ESSN 2045-2322 |
| JRNL PMID 40082629 |
| JRNL DOI 10.1038/S41598-025-92886-W |
| REMARK 2 |
| REMARK 2 RESOLUTION. 1.74 ANGSTROMS. |
| REMARK 3 |
| REMARK 3 REFINEMENT. |
| REMARK 3 PROGRAM : PHENIX (1.20.1_4487: 000) |
| 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) : 1.74 |
| REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.32 |
| REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 |
| REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1 |
| REMARK 3 NUMBER OF REFLECTIONS : 110700 |
| REMARK 3 |
| REMARK 3 FIT TO DATA USED IN REFINEMENT. |
| REMARK 3 R VALUE (WORKING + TEST SET) : 0.211 |
| REMARK 3 R VALUE (WORKING SET) : 0.211 |
| REMARK 3 FREE R VALUE : 0.225 |
| REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.810 |
| REMARK 3 FREE R VALUE TEST SET COUNT : 2004 |
| 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 47.3200 - 4.1900 0.99 8179 152 0.1886 0.1944 |
| REMARK 3 2 4.1900 - 3.3300 1.00 7945 144 0.1879 0.2115 |
| REMARK 3 3 3.3300 - 2.9100 0.99 7858 143 0.2091 0.2074 |
| REMARK 3 4 2.9100 - 2.6400 0.99 7785 159 0.2173 0.2293 |
| REMARK 3 5 2.6400 - 2.4500 1.00 7839 131 0.2194 0.2263 |
| REMARK 3 6 2.4500 - 2.3100 1.00 7790 154 0.2171 0.2488 |
| REMARK 3 7 2.3100 - 2.1900 1.00 7770 134 0.2207 0.2568 |
| REMARK 3 8 2.1900 - 2.1000 0.99 7737 144 0.2144 0.2314 |
| REMARK 3 9 2.1000 - 2.0200 1.00 7715 147 0.2262 0.2563 |
| REMARK 3 10 2.0200 - 1.9500 0.99 7766 148 0.2433 0.2944 |
| REMARK 3 11 1.9500 - 1.8900 1.00 7709 130 0.2496 0.2683 |
| REMARK 3 12 1.8900 - 1.8300 1.00 7782 147 0.2669 0.2631 |
| REMARK 3 13 1.8300 - 1.7800 0.99 7673 142 0.3035 0.3059 |
| REMARK 3 14 1.7800 - 1.7400 0.93 7148 129 0.3448 0.3247 |
| REMARK 3 |
| REMARK 3 BULK SOLVENT MODELLING. |
| REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL |
| REMARK 3 SOLVENT RADIUS : 1.10 |
| REMARK 3 SHRINKAGE RADIUS : 0.90 |
| REMARK 3 K_SOL : NULL |
| REMARK 3 B_SOL : NULL |
| REMARK 3 |
| REMARK 3 ERROR ESTIMATES. |
| REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210 |
| REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.660 |
| REMARK 3 |
| REMARK 3 B VALUES. |
| REMARK 3 FROM WILSON PLOT (A**2) : NULL |
| REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL |
| REMARK 3 OVERALL ANISOTROPIC B VALUE. |
| REMARK 3 B11 (A**2) : NULL |
| REMARK 3 B22 (A**2) : NULL |
| REMARK 3 B33 (A**2) : NULL |
| REMARK 3 B12 (A**2) : NULL |
| REMARK 3 B13 (A**2) : NULL |
| REMARK 3 B23 (A**2) : NULL |
| REMARK 3 |
| REMARK 3 TWINNING INFORMATION. |
| REMARK 3 FRACTION: NULL |
| REMARK 3 OPERATOR: NULL |
| REMARK 3 |
| REMARK 3 DEVIATIONS FROM IDEAL VALUES. |
| REMARK 3 RMSD COUNT |
| REMARK 3 BOND : 0.007 7236 |
| REMARK 3 ANGLE : 0.969 9874 |
| REMARK 3 CHIRALITY : 0.063 1108 |
| REMARK 3 PLANARITY : 0.011 1258 |
| REMARK 3 DIHEDRAL : 14.023 2542 |
| 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 9CQA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 |
| REMARK 100 |
| REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-24. |
| REMARK 100 THE DEPOSITION ID IS D_1000285967. |
| REMARK 200 |
| REMARK 200 EXPERIMENTAL DETAILS |
| REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION |
| REMARK 200 DATE OF DATA COLLECTION : 22-APR-22 |
| 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 : APS |
| REMARK 200 BEAMLINE : 23-ID-B |
| REMARK 200 X-RAY GENERATOR MODEL : NULL |
| REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M |
| REMARK 200 WAVELENGTH OR RANGE (A) : 1.033167 |
| REMARK 200 MONOCHROMATOR : NULL |
| REMARK 200 OPTICS : NULL |
| REMARK 200 |
| REMARK 200 DETECTOR TYPE : PIXEL |
| REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M |
| REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS |
| REMARK 200 DATA SCALING SOFTWARE : AIMLESS |
| REMARK 200 |
| REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 110905 |
| REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740 |
| REMARK 200 RESOLUTION RANGE LOW (A) : 47.320 |
| REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL |
| REMARK 200 |
| REMARK 200 OVERALL. |
| REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 |
| REMARK 200 DATA REDUNDANCY : 13.20 |
| REMARK 200 R MERGE (I) : NULL |
| REMARK 200 R SYM (I) : NULL |
| REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.6000 |
| REMARK 200 |
| REMARK 200 IN THE HIGHEST RESOLUTION SHELL. |
| REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74 |
| REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77 |
| REMARK 200 COMPLETENESS FOR SHELL (%) : NULL |
| REMARK 200 DATA REDUNDANCY IN SHELL : NULL |
| REMARK 200 R MERGE FOR SHELL (I) : NULL |
| REMARK 200 R SYM FOR SHELL (I) : NULL |
| REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL |
| REMARK 200 |
| REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH |
| REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT |
| REMARK 200 SOFTWARE USED: PHASER |
| REMARK 200 STARTING MODEL: NULL |
| REMARK 200 |
| REMARK 200 REMARK: NULL |
| REMARK 280 |
| REMARK 280 CRYSTAL |
| REMARK 280 SOLVENT CONTENT, VS (%): 47.79 |
| REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36 |
| REMARK 280 |
| REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS (PH 6.5), 0.2M AMMONIUM |
| REMARK 280 SULFATE, AND 24.5% PEG 3350, VAPOR DIFFUSION, HANGING DROP, |
| REMARK 280 TEMPERATURE 295.15K |
| 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 38.20900 |
| REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 |
| REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 87.59050 |
| REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 |
| REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.37650 |
| REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 87.59050 |
| REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.20900 |
| REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.37650 |
| REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 |
| REMARK 290 |
| REMARK 290 REMARK: NULL |
| REMARK 300 |
| REMARK 300 BIOMOLECULE: 1, 2 |
| 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: TRIMERIC |
| REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC |
| REMARK 350 SOFTWARE USED: PISA |
| REMARK 350 TOTAL BURIED SURFACE AREA: 5690 ANGSTROM**2 |
| REMARK 350 SURFACE AREA OF THE COMPLEX: 21410 ANGSTROM**2 |
| REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL |
| REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, A |
| REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 |
| REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 |
| REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 |
| REMARK 350 |
| REMARK 350 BIOMOLECULE: 2 |
| REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC |
| REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC |
| REMARK 350 SOFTWARE USED: PISA |
| REMARK 350 TOTAL BURIED SURFACE AREA: 5290 ANGSTROM**2 |
| REMARK 350 SURFACE AREA OF THE COMPLEX: 21310 ANGSTROM**2 |
| REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL |
| REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G, B |
| REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 |
| REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 |
| REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 |
| REMARK 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 SER E 138 |
| REMARK 465 SER E 139 |
| REMARK 465 LYS E 140 |
| REMARK 465 SER E 141 |
| REMARK 465 THR E 142 |
| REMARK 465 SER E 143 |
| REMARK 465 GLY E 144 |
| REMARK 465 LYS E 225 |
| REMARK 465 SER E 226 |
| REMARK 465 CYS E 227 |
| REMARK 465 ALA E 228 |
| REMARK 465 SER E 229 |
| REMARK 465 LEU E 230 |
| REMARK 465 VAL E 231 |
| REMARK 465 PRO E 232 |
| REMARK 465 ARG E 233 |
| REMARK 465 GLY E 234 |
| REMARK 465 SER E 235 |
| REMARK 465 GLY E 236 |
| REMARK 465 TRP E 237 |
| REMARK 465 SER E 238 |
| REMARK 465 HIS E 239 |
| REMARK 465 PRO E 240 |
| REMARK 465 GLN E 241 |
| REMARK 465 PHE E 242 |
| REMARK 465 GLU E 243 |
| REMARK 465 LYS E 244 |
| REMARK 465 GLY E 245 |
| REMARK 465 GLY E 246 |
| REMARK 465 GLY E 247 |
| REMARK 465 SER E 248 |
| REMARK 465 GLY E 249 |
| REMARK 465 GLY E 250 |
| REMARK 465 GLY E 251 |
| REMARK 465 SER E 252 |
| REMARK 465 GLY E 253 |
| REMARK 465 GLY E 254 |
| REMARK 465 GLY E 255 |
| REMARK 465 SER E 256 |
| REMARK 465 TRP E 257 |
| REMARK 465 SER E 258 |
| REMARK 465 HIS E 259 |
| REMARK 465 PRO E 260 |
| REMARK 465 GLN E 261 |
| REMARK 465 PHE E 262 |
| REMARK 465 GLU E 263 |
| REMARK 465 LYS E 264 |
| REMARK 465 GLU F 214 |
| REMARK 465 CYS F 215 |
| REMARK 465 SER D 138 |
| REMARK 465 SER D 139 |
| REMARK 465 LYS D 140 |
| REMARK 465 SER D 141 |
| REMARK 465 THR D 142 |
| REMARK 465 SER D 143 |
| REMARK 465 GLY D 144 |
| REMARK 465 LYS D 225 |
| REMARK 465 SER D 226 |
| REMARK 465 CYS D 227 |
| REMARK 465 ALA D 228 |
| REMARK 465 SER D 229 |
| REMARK 465 LEU D 230 |
| REMARK 465 VAL D 231 |
| REMARK 465 PRO D 232 |
| REMARK 465 ARG D 233 |
| REMARK 465 GLY D 234 |
| REMARK 465 SER D 235 |
| REMARK 465 GLY D 236 |
| REMARK 465 TRP D 237 |
| REMARK 465 SER D 238 |
| REMARK 465 HIS D 239 |
| REMARK 465 PRO D 240 |
| REMARK 465 GLN D 241 |
| REMARK 465 PHE D 242 |
| REMARK 465 GLU D 243 |
| REMARK 465 LYS D 244 |
| REMARK 465 GLY D 245 |
| REMARK 465 GLY D 246 |
| REMARK 465 GLY D 247 |
| REMARK 465 SER D 248 |
| REMARK 465 GLY D 249 |
| REMARK 465 GLY D 250 |
| REMARK 465 GLY D 251 |
| REMARK 465 SER D 252 |
| REMARK 465 GLY D 253 |
| REMARK 465 GLY D 254 |
| REMARK 465 GLY D 255 |
| REMARK 465 SER D 256 |
| REMARK 465 TRP D 257 |
| REMARK 465 SER D 258 |
| REMARK 465 HIS D 259 |
| REMARK 465 PRO D 260 |
| REMARK 465 GLN D 261 |
| REMARK 465 PHE D 262 |
| REMARK 465 GLU D 263 |
| REMARK 465 LYS D 264 |
| REMARK 465 GLU G 214 |
| REMARK 465 CYS G 215 |
| REMARK 465 MET A 155 |
| REMARK 465 GLY A 156 |
| REMARK 465 SER A 157 |
| REMARK 465 LYS A 158 |
| REMARK 465 PRO A 159 |
| REMARK 465 ASN A 160 |
| REMARK 465 ILE A 189 |
| REMARK 465 PRO A 190 |
| REMARK 465 ASN A 191 |
| REMARK 465 LYS A 192 |
| REMARK 465 LYS A 193 |
| REMARK 465 PRO A 194 |
| REMARK 465 GLY A 195 |
| REMARK 465 LYS A 196 |
| REMARK 465 LYS A 197 |
| REMARK 465 HIS A 198 |
| REMARK 465 HIS A 199 |
| REMARK 465 HIS A 200 |
| REMARK 465 HIS A 201 |
| REMARK 465 HIS A 202 |
| REMARK 465 HIS A 203 |
| REMARK 465 MET B 155 |
| REMARK 465 GLY B 156 |
| REMARK 465 SER B 157 |
| REMARK 465 LYS B 158 |
| REMARK 465 PRO B 159 |
| REMARK 465 ASN B 160 |
| REMARK 465 ILE B 189 |
| REMARK 465 PRO B 190 |
| REMARK 465 ASN B 191 |
| REMARK 465 LYS B 192 |
| REMARK 465 LYS B 193 |
| REMARK 465 PRO B 194 |
| REMARK 465 GLY B 195 |
| REMARK 465 LYS B 196 |
| REMARK 465 LYS B 197 |
| REMARK 465 HIS B 198 |
| REMARK 465 HIS B 199 |
| REMARK 465 HIS B 200 |
| REMARK 465 HIS B 201 |
| REMARK 465 HIS B 202 |
| REMARK 465 HIS B 203 |
| 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 ASP E 155 68.18 62.52 |
| REMARK 500 THR F 50 -41.54 68.76 |
| REMARK 500 SER F 66 94.12 -167.03 |
| REMARK 500 ALA F 83 170.96 179.91 |
| REMARK 500 ASP D 155 62.44 62.80 |
| REMARK 500 THR G 50 -43.55 70.85 |
| REMARK 500 SER A 177 -119.58 53.15 |
| REMARK 500 SER B 177 -120.01 53.81 |
| REMARK 500 |
| REMARK 500 REMARK: NULL |
| DBREF 9CQA E 1 264 PDB 9CQA 9CQA 1 264 |
| DBREF 9CQA F 1 215 PDB 9CQA 9CQA 1 215 |
| DBREF 9CQA D 1 264 PDB 9CQA 9CQA 1 264 |
| DBREF 9CQA G 1 215 PDB 9CQA 9CQA 1 215 |
| DBREF 9CQA A 157 197 UNP P03423 GLYC_HRSVA 157 197 |
| DBREF 9CQA B 157 197 UNP P03423 GLYC_HRSVA 157 197 |
| SEQADV 9CQA MET A 155 UNP P03423 INITIATING METHIONINE |
| SEQADV 9CQA GLY A 156 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA HIS A 198 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA HIS A 199 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA HIS A 200 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA HIS A 201 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA HIS A 202 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA HIS A 203 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA MET B 155 UNP P03423 INITIATING METHIONINE |
| SEQADV 9CQA GLY B 156 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA HIS B 198 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA HIS B 199 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA HIS B 200 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA HIS B 201 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA HIS B 202 UNP P03423 EXPRESSION TAG |
| SEQADV 9CQA HIS B 203 UNP P03423 EXPRESSION TAG |
| SEQRES 1 E 264 GLN VAL HIS LEU VAL GLN SER GLY VAL GLU VAL LYS LYS |
| SEQRES 2 E 264 PRO GLY ALA SER VAL ARG VAL SER CYS LYS ALA SER GLY |
| SEQRES 3 E 264 TYR THR PHE ALA THR TYR GLY ILE THR TRP VAL ARG GLN |
| SEQRES 4 E 264 ALA PRO GLY ARG GLY LEU GLU TRP VAL GLY TRP ILE THR |
| SEQRES 5 E 264 PRO TYR ASN ASP ARG THR SER TYR ALA GLN ILE PHE HIS |
| SEQRES 6 E 264 GLY ARG VAL THR MET THR THR ASP THR SER THR ASN THR |
| SEQRES 7 E 264 ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP THR |
| SEQRES 8 E 264 ALA MET TYR TYR CYS ALA ARG ASN HIS CYS ASN PHE TYR |
| SEQRES 9 E 264 HIS ASP PHE TRP SER GLY LEU ASP TYR TRP GLY GLN GLY |
| SEQRES 10 E 264 THR LEU VAL SER VAL SER SER ALA SER THR LYS GLY PRO |
| SEQRES 11 E 264 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER |
| SEQRES 12 E 264 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR |
| SEQRES 13 E 264 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA |
| SEQRES 14 E 264 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN |
| SEQRES 15 E 264 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL |
| SEQRES 16 E 264 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN |
| SEQRES 17 E 264 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS |
| SEQRES 18 E 264 VAL GLU PRO LYS SER CYS ALA SER LEU VAL PRO ARG GLY |
| SEQRES 19 E 264 SER GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY |
| SEQRES 20 E 264 SER GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS PRO |
| SEQRES 21 E 264 GLN PHE GLU LYS |
| SEQRES 1 F 215 SER PHE GLU LEU THR GLN PRO PRO SER VAL SER VAL SER |
| SEQRES 2 F 215 PRO GLY GLN THR ALA ARG ILE THR CYS SER GLY ASP ALA |
| SEQRES 3 F 215 LEU PRO LYS GLN TYR VAL TYR TRP TYR GLN GLN LYS PRO |
| SEQRES 4 F 215 GLY GLN ALA PRO VAL LEU VAL ILE TYR LYS THR THR GLU |
| SEQRES 5 F 215 ARG PRO SER GLY ILE PRO GLU ARG PHE SER ASP SER SER |
| SEQRES 6 F 215 SER GLY THR THR VAL THR LEU THR ILE SER ALA ALA GLN |
| SEQRES 7 F 215 ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SER VAL ASP |
| SEQRES 8 F 215 SER SER GLY THR TYR VAL PHE GLY ILE GLY THR LYS VAL |
| SEQRES 9 F 215 THR VAL LEU GLY ARG THR VAL ALA ALA PRO SER VAL PHE |
| SEQRES 10 F 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR |
| SEQRES 11 F 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG |
| SEQRES 12 F 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN |
| SEQRES 13 F 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER |
| SEQRES 14 F 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU |
| SEQRES 15 F 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS |
| SEQRES 16 F 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS |
| SEQRES 17 F 215 SER PHE ASN ARG GLY GLU CYS |
| SEQRES 1 D 264 GLN VAL HIS LEU VAL GLN SER GLY VAL GLU VAL LYS LYS |
| SEQRES 2 D 264 PRO GLY ALA SER VAL ARG VAL SER CYS LYS ALA SER GLY |
| SEQRES 3 D 264 TYR THR PHE ALA THR TYR GLY ILE THR TRP VAL ARG GLN |
| SEQRES 4 D 264 ALA PRO GLY ARG GLY LEU GLU TRP VAL GLY TRP ILE THR |
| SEQRES 5 D 264 PRO TYR ASN ASP ARG THR SER TYR ALA GLN ILE PHE HIS |
| SEQRES 6 D 264 GLY ARG VAL THR MET THR THR ASP THR SER THR ASN THR |
| SEQRES 7 D 264 ALA TYR MET GLU LEU ARG SER LEU ARG SER ASP ASP THR |
| SEQRES 8 D 264 ALA MET TYR TYR CYS ALA ARG ASN HIS CYS ASN PHE TYR |
| SEQRES 9 D 264 HIS ASP PHE TRP SER GLY LEU ASP TYR TRP GLY GLN GLY |
| SEQRES 10 D 264 THR LEU VAL SER VAL SER SER ALA SER THR LYS GLY PRO |
| SEQRES 11 D 264 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER |
| SEQRES 12 D 264 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR |
| SEQRES 13 D 264 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA |
| SEQRES 14 D 264 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN |
| SEQRES 15 D 264 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL |
| SEQRES 16 D 264 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN |
| SEQRES 17 D 264 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS |
| SEQRES 18 D 264 VAL GLU PRO LYS SER CYS ALA SER LEU VAL PRO ARG GLY |
| SEQRES 19 D 264 SER GLY TRP SER HIS PRO GLN PHE GLU LYS GLY GLY GLY |
| SEQRES 20 D 264 SER GLY GLY GLY SER GLY GLY GLY SER TRP SER HIS PRO |
| SEQRES 21 D 264 GLN PHE GLU LYS |
| SEQRES 1 G 215 SER PHE GLU LEU THR GLN PRO PRO SER VAL SER VAL SER |
| SEQRES 2 G 215 PRO GLY GLN THR ALA ARG ILE THR CYS SER GLY ASP ALA |
| SEQRES 3 G 215 LEU PRO LYS GLN TYR VAL TYR TRP TYR GLN GLN LYS PRO |
| SEQRES 4 G 215 GLY GLN ALA PRO VAL LEU VAL ILE TYR LYS THR THR GLU |
| SEQRES 5 G 215 ARG PRO SER GLY ILE PRO GLU ARG PHE SER ASP SER SER |
| SEQRES 6 G 215 SER GLY THR THR VAL THR LEU THR ILE SER ALA ALA GLN |
| SEQRES 7 G 215 ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SER VAL ASP |
| SEQRES 8 G 215 SER SER GLY THR TYR VAL PHE GLY ILE GLY THR LYS VAL |
| SEQRES 9 G 215 THR VAL LEU GLY ARG THR VAL ALA ALA PRO SER VAL PHE |
| SEQRES 10 G 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR |
| SEQRES 11 G 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG |
| SEQRES 12 G 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN |
| SEQRES 13 G 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER |
| SEQRES 14 G 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU |
| SEQRES 15 G 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS |
| SEQRES 16 G 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS |
| SEQRES 17 G 215 SER PHE ASN ARG GLY GLU CYS |
| SEQRES 1 A 49 MET GLY SER LYS PRO ASN ASN ASP PHE HIS PHE GLU VAL |
| SEQRES 2 A 49 PHE ASN PHE VAL PRO CYS SER ILE CYS SER ASN ASN PRO |
| SEQRES 3 A 49 THR CYS TRP ALA ILE CYS LYS ARG ILE PRO ASN LYS LYS |
| SEQRES 4 A 49 PRO GLY LYS LYS HIS HIS HIS HIS HIS HIS |
| SEQRES 1 B 49 MET GLY SER LYS PRO ASN ASN ASP PHE HIS PHE GLU VAL |
| SEQRES 2 B 49 PHE ASN PHE VAL PRO CYS SER ILE CYS SER ASN ASN PRO |
| SEQRES 3 B 49 THR CYS TRP ALA ILE CYS LYS ARG ILE PRO ASN LYS LYS |
| SEQRES 4 B 49 PRO GLY LYS LYS HIS HIS HIS HIS HIS HIS |
| HET SO4 E 301 5 |
| HET SO4 G 301 5 |
| HET SO4 A 301 5 |
| HET SO4 B 301 5 |
| HETNAM SO4 SULFATE ION |
| FORMUL 7 SO4 4(O4 S 2-) |
| FORMUL 11 HOH *393(H2 O) |
| HELIX 1 AA1 THR E 28 TYR E 32 5 5 |
| HELIX 2 AA2 GLN E 62 HIS E 65 5 4 |
| HELIX 3 AA3 ARG E 87 THR E 91 5 5 |
| HELIX 4 AA4 SER E 167 ALA E 169 5 3 |
| HELIX 5 AA5 SER E 198 GLY E 201 5 4 |
| HELIX 6 AA6 LYS E 212 ASN E 215 5 4 |
| HELIX 7 AA7 GLN F 78 GLU F 82 5 5 |
| HELIX 8 AA8 SER F 122 SER F 128 1 7 |
| HELIX 9 AA9 LYS F 184 LYS F 189 1 6 |
| HELIX 10 AB1 THR D 28 TYR D 32 5 5 |
| HELIX 11 AB2 GLN D 62 HIS D 65 5 4 |
| HELIX 12 AB3 ARG D 87 THR D 91 5 5 |
| HELIX 13 AB4 SER D 167 ALA D 169 5 3 |
| HELIX 14 AB5 SER D 198 LEU D 200 5 3 |
| HELIX 15 AB6 LYS D 212 ASN D 215 5 4 |
| HELIX 16 AB7 GLN G 78 GLU G 82 5 5 |
| HELIX 17 AB8 SER G 122 SER G 128 1 7 |
| HELIX 18 AB9 LYS G 184 GLU G 188 1 5 |
| HELIX 19 AC1 PRO A 172 CYS A 176 5 5 |
| HELIX 20 AC2 ASN A 179 CYS A 186 1 8 |
| HELIX 21 AC3 PRO B 172 CYS B 176 5 5 |
| HELIX 22 AC4 ASN B 179 CYS B 186 1 8 |
| SHEET 1 AA1 4 HIS E 3 GLN E 6 0 |
| SHEET 2 AA1 4 VAL E 18 SER E 25 -1 O LYS E 23 N VAL E 5 |
| SHEET 3 AA1 4 THR E 78 LEU E 83 -1 O ALA E 79 N CYS E 22 |
| SHEET 4 AA1 4 VAL E 68 ASP E 73 -1 N ASP E 73 O THR E 78 |
| SHEET 1 AA2 6 GLU E 10 LYS E 12 0 |
| SHEET 2 AA2 6 THR E 118 VAL E 122 1 O SER E 121 N LYS E 12 |
| SHEET 3 AA2 6 ALA E 92 ASN E 99 -1 N TYR E 94 O THR E 118 |
| SHEET 4 AA2 6 GLY E 33 GLN E 39 -1 N VAL E 37 O TYR E 95 |
| SHEET 5 AA2 6 GLU E 46 THR E 52 -1 O GLU E 46 N ARG E 38 |
| SHEET 6 AA2 6 ARG E 57 TYR E 60 -1 O ARG E 57 N THR E 52 |
| SHEET 1 AA3 2 CYS E 101 ASN E 102 0 |
| SHEET 2 AA3 2 PHE E 107 TRP E 108 -1 O PHE E 107 N ASN E 102 |
| SHEET 1 AA4 4 SER E 131 LEU E 135 0 |
| SHEET 2 AA4 4 THR E 146 TYR E 156 -1 O GLY E 150 N LEU E 135 |
| SHEET 3 AA4 4 TYR E 187 PRO E 196 -1 O VAL E 195 N ALA E 147 |
| SHEET 4 AA4 4 VAL E 174 THR E 176 -1 N HIS E 175 O VAL E 192 |
| SHEET 1 AA5 4 SER E 131 LEU E 135 0 |
| SHEET 2 AA5 4 THR E 146 TYR E 156 -1 O GLY E 150 N LEU E 135 |
| SHEET 3 AA5 4 TYR E 187 PRO E 196 -1 O VAL E 195 N ALA E 147 |
| SHEET 4 AA5 4 VAL E 180 LEU E 181 -1 N VAL E 180 O SER E 188 |
| SHEET 1 AA6 3 THR E 162 TRP E 165 0 |
| SHEET 2 AA6 3 ILE E 206 HIS E 211 -1 O ASN E 208 N SER E 164 |
| SHEET 3 AA6 3 THR E 216 LYS E 221 -1 O VAL E 218 N VAL E 209 |
| SHEET 1 AA7 5 SER F 9 VAL F 12 0 |
| SHEET 2 AA7 5 THR F 102 VAL F 106 1 O THR F 105 N VAL F 12 |
| SHEET 3 AA7 5 ALA F 83 VAL F 90 -1 N ALA F 83 O VAL F 104 |
| SHEET 4 AA7 5 TYR F 33 GLN F 37 -1 N GLN F 37 O ASP F 84 |
| SHEET 5 AA7 5 VAL F 44 ILE F 47 -1 O VAL F 46 N TRP F 34 |
| SHEET 1 AA8 4 SER F 9 VAL F 12 0 |
| SHEET 2 AA8 4 THR F 102 VAL F 106 1 O THR F 105 N VAL F 12 |
| SHEET 3 AA8 4 ALA F 83 VAL F 90 -1 N ALA F 83 O VAL F 104 |
| SHEET 4 AA8 4 TYR F 96 PHE F 98 -1 O VAL F 97 N SER F 89 |
| SHEET 1 AA9 3 ALA F 18 SER F 23 0 |
| SHEET 2 AA9 3 THR F 69 ILE F 74 -1 O LEU F 72 N ILE F 20 |
| SHEET 3 AA9 3 PHE F 61 SER F 66 -1 N SER F 62 O THR F 73 |
| SHEET 1 AB1 4 SER F 115 PHE F 119 0 |
| SHEET 2 AB1 4 THR F 130 PHE F 140 -1 O LEU F 136 N PHE F 117 |
| SHEET 3 AB1 4 TYR F 174 SER F 183 -1 O LEU F 182 N ALA F 131 |
| SHEET 4 AB1 4 SER F 160 VAL F 164 -1 N SER F 163 O SER F 177 |
| SHEET 1 AB2 4 ALA F 154 LEU F 155 0 |
| SHEET 2 AB2 4 LYS F 146 VAL F 151 -1 N VAL F 151 O ALA F 154 |
| SHEET 3 AB2 4 VAL F 192 THR F 198 -1 O GLU F 196 N GLN F 148 |
| SHEET 4 AB2 4 VAL F 206 ASN F 211 -1 O VAL F 206 N VAL F 197 |
| SHEET 1 AB3 4 HIS D 3 GLN D 6 0 |
| SHEET 2 AB3 4 VAL D 18 SER D 25 -1 O LYS D 23 N VAL D 5 |
| SHEET 3 AB3 4 THR D 78 LEU D 83 -1 O MET D 81 N VAL D 20 |
| SHEET 4 AB3 4 VAL D 68 ASP D 73 -1 N ASP D 73 O THR D 78 |
| SHEET 1 AB4 6 GLU D 10 LYS D 12 0 |
| SHEET 2 AB4 6 THR D 118 VAL D 122 1 O SER D 121 N LYS D 12 |
| SHEET 3 AB4 6 ALA D 92 ASN D 99 -1 N TYR D 94 O THR D 118 |
| SHEET 4 AB4 6 GLY D 33 GLN D 39 -1 N VAL D 37 O TYR D 95 |
| SHEET 5 AB4 6 GLU D 46 THR D 52 -1 O GLU D 46 N ARG D 38 |
| SHEET 6 AB4 6 ARG D 57 TYR D 60 -1 O ARG D 57 N THR D 52 |
| SHEET 1 AB5 2 CYS D 101 ASN D 102 0 |
| SHEET 2 AB5 2 PHE D 107 TRP D 108 -1 O PHE D 107 N ASN D 102 |
| SHEET 1 AB6 4 SER D 131 LEU D 135 0 |
| SHEET 2 AB6 4 THR D 146 TYR D 156 -1 O LEU D 152 N PHE D 133 |
| SHEET 3 AB6 4 TYR D 187 PRO D 196 -1 O VAL D 195 N ALA D 147 |
| SHEET 4 AB6 4 VAL D 174 THR D 176 -1 N HIS D 175 O VAL D 192 |
| SHEET 1 AB7 4 SER D 131 LEU D 135 0 |
| SHEET 2 AB7 4 THR D 146 TYR D 156 -1 O LEU D 152 N PHE D 133 |
| SHEET 3 AB7 4 TYR D 187 PRO D 196 -1 O VAL D 195 N ALA D 147 |
| SHEET 4 AB7 4 VAL D 180 LEU D 181 -1 N VAL D 180 O SER D 188 |
| SHEET 1 AB8 3 THR D 162 TRP D 165 0 |
| SHEET 2 AB8 3 ILE D 206 HIS D 211 -1 O ASN D 208 N SER D 164 |
| SHEET 3 AB8 3 THR D 216 LYS D 221 -1 O VAL D 218 N VAL D 209 |
| SHEET 1 AB9 5 SER G 9 VAL G 12 0 |
| SHEET 2 AB9 5 THR G 102 VAL G 106 1 O THR G 105 N VAL G 12 |
| SHEET 3 AB9 5 ALA G 83 VAL G 90 -1 N ALA G 83 O VAL G 104 |
| SHEET 4 AB9 5 TYR G 33 GLN G 37 -1 N GLN G 37 O ASP G 84 |
| SHEET 5 AB9 5 VAL G 44 ILE G 47 -1 O VAL G 46 N TRP G 34 |
| SHEET 1 AC1 4 SER G 9 VAL G 12 0 |
| SHEET 2 AC1 4 THR G 102 VAL G 106 1 O THR G 105 N VAL G 12 |
| SHEET 3 AC1 4 ALA G 83 VAL G 90 -1 N ALA G 83 O VAL G 104 |
| SHEET 4 AC1 4 TYR G 96 PHE G 98 -1 O VAL G 97 N SER G 89 |
| SHEET 1 AC2 3 ALA G 18 SER G 23 0 |
| SHEET 2 AC2 3 THR G 69 ILE G 74 -1 O LEU G 72 N ILE G 20 |
| SHEET 3 AC2 3 PHE G 61 SER G 66 -1 N SER G 62 O THR G 73 |
| SHEET 1 AC3 4 SER G 115 PHE G 119 0 |
| SHEET 2 AC3 4 THR G 130 PHE G 140 -1 O LEU G 136 N PHE G 117 |
| SHEET 3 AC3 4 TYR G 174 SER G 183 -1 O LEU G 180 N VAL G 133 |
| SHEET 4 AC3 4 SER G 160 VAL G 164 -1 N SER G 163 O SER G 177 |
| SHEET 1 AC4 3 ALA G 145 VAL G 151 0 |
| SHEET 2 AC4 3 VAL G 192 HIS G 199 -1 O GLU G 196 N GLN G 148 |
| SHEET 3 AC4 3 VAL G 206 ASN G 211 -1 O VAL G 206 N VAL G 197 |
| SSBOND 1 CYS E 22 CYS E 96 1555 1555 2.08 |
| SSBOND 2 CYS E 151 CYS E 207 1555 1555 2.04 |
| SSBOND 3 CYS F 22 CYS F 87 1555 1555 2.09 |
| SSBOND 4 CYS F 135 CYS F 195 1555 1555 2.07 |
| SSBOND 5 CYS D 22 CYS D 96 1555 1555 2.08 |
| SSBOND 6 CYS D 151 CYS D 207 1555 1555 2.03 |
| SSBOND 7 CYS G 22 CYS G 87 1555 1555 2.09 |
| SSBOND 8 CYS G 135 CYS G 195 1555 1555 2.06 |
| SSBOND 9 CYS A 173 CYS A 186 1555 1555 2.04 |
| SSBOND 10 CYS A 176 CYS A 182 1555 1555 2.06 |
| SSBOND 11 CYS B 173 CYS B 186 1555 1555 2.04 |
| SSBOND 12 CYS B 176 CYS B 182 1555 1555 2.06 |
| CISPEP 1 PHE E 157 PRO E 158 0 -5.10 |
| CISPEP 2 GLU E 159 PRO E 160 0 -2.29 |
| CISPEP 3 TYR F 141 PRO F 142 0 0.68 |
| CISPEP 4 PHE D 157 PRO D 158 0 -8.15 |
| CISPEP 5 GLU D 159 PRO D 160 0 -0.47 |
| CISPEP 6 TYR G 141 PRO G 142 0 4.76 |
| CRYST1 76.418 80.753 175.181 90.00 90.00 90.00 P 21 21 21 8 |
| 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 0.013086 0.000000 0.000000 0.00000 |
| SCALE2 0.000000 0.012383 0.000000 0.00000 |
| SCALE3 0.000000 0.000000 0.005708 0.00000 |
| TER 1666 PRO E 224 |
| TER 3292 GLY F 213 |
| TER 4958 PRO D 224 |
| TER 6584 GLY G 213 |
| ATOM 6585 N ASN A 161 31.445 -17.034 -63.157 1.00 49.81 N |
| ATOM 6586 CA ASN A 161 31.915 -15.741 -62.679 1.00 46.20 C |
| ATOM 6587 C ASN A 161 31.443 -15.464 -61.253 1.00 40.87 C |
| ATOM 6588 O ASN A 161 30.879 -14.393 -60.976 1.00 38.08 O |
| ATOM 6589 CB ASN A 161 31.445 -14.628 -63.610 1.00 50.34 C |
| ATOM 6590 CG ASN A 161 32.094 -14.707 -64.976 1.00 57.67 C |
| ATOM 6591 OD1 ASN A 161 31.409 -14.757 -66.002 1.00 60.21 O |
| ATOM 6592 ND2 ASN A 161 33.427 -14.755 -64.996 1.00 60.68 N |
| ATOM 6593 N ASP A 162 31.677 -16.428 -60.358 1.00 34.16 N |
| ATOM 6594 CA ASP A 162 31.370 -16.290 -58.941 1.00 32.00 C |
| ATOM 6595 C ASP A 162 32.653 -16.299 -58.124 1.00 32.05 C |
| ATOM 6596 O ASP A 162 33.581 -17.067 -58.414 1.00 29.15 O |
| ATOM 6597 CB ASP A 162 30.454 -17.397 -58.429 1.00 32.40 C |
| ATOM 6598 CG ASP A 162 29.949 -17.108 -57.027 1.00 31.20 C |
| ATOM 6599 OD1 ASP A 162 29.055 -16.240 -56.873 1.00 31.50 O |
| ATOM 6600 OD2 ASP A 162 30.493 -17.717 -56.078 1.00 28.20 O |
| ATOM 6601 N PHE A 163 32.683 -15.467 -57.079 1.00 27.37 N |
| ATOM 6602 CA PHE A 163 33.905 -15.240 -56.325 1.00 26.78 C |
| ATOM 6603 C PHE A 163 33.792 -15.637 -54.860 1.00 27.97 C |
| ATOM 6604 O PHE A 163 34.721 -15.369 -54.088 1.00 26.53 O |
| ATOM 6605 CB PHE A 163 34.317 -13.772 -56.494 1.00 28.47 C |
| ATOM 6606 CG PHE A 163 34.538 -13.414 -57.931 1.00 27.97 C |
| ATOM 6607 CD1 PHE A 163 35.740 -13.723 -58.546 1.00 32.79 C |
| ATOM 6608 CD2 PHE A 163 33.514 -12.851 -58.689 1.00 32.45 C |
| ATOM 6609 CE1 PHE A 163 35.943 -13.437 -59.879 1.00 37.12 C |
| ATOM 6610 CE2 PHE A 163 33.708 -12.557 -60.033 1.00 34.02 C |
| ATOM 6611 CZ PHE A 163 34.929 -12.850 -60.625 1.00 37.67 C |
| ATOM 6612 N HIS A 164 32.732 -16.344 -54.512 1.00 23.29 N |
| ATOM 6613 CA HIS A 164 32.700 -16.923 -53.157 1.00 25.96 C |
| ATOM 6614 C HIS A 164 33.837 -17.946 -53.078 1.00 25.35 C |
| ATOM 6615 O HIS A 164 34.015 -18.706 -54.037 1.00 25.46 O |
| ATOM 6616 CB HIS A 164 31.378 -17.629 -52.882 1.00 24.44 C |
| ATOM 6617 CG HIS A 164 30.195 -16.750 -52.679 1.00 23.95 C |
| ATOM 6618 ND1 HIS A 164 29.352 -16.381 -53.702 1.00 26.02 N |
| ATOM 6619 CD2 HIS A 164 29.697 -16.200 -51.573 1.00 21.65 C |
| ATOM 6620 CE1 HIS A 164 28.391 -15.619 -53.217 1.00 22.60 C |
| ATOM 6621 NE2 HIS A 164 28.581 -15.499 -51.927 1.00 26.64 N |
| ATOM 6622 N PHE A 165 34.562 -17.957 -51.976 1.00 23.84 N |
| ATOM 6623 CA PHE A 165 35.668 -18.878 -51.710 1.00 26.80 C |
| ATOM 6624 C PHE A 165 36.827 -18.731 -52.700 1.00 26.88 C |
| ATOM 6625 O PHE A 165 37.670 -19.625 -52.801 1.00 31.35 O |
| ATOM 6626 CB PHE A 165 35.176 -20.333 -51.666 1.00 25.99 C |
| ATOM 6627 CG PHE A 165 34.067 -20.555 -50.673 1.00 23.32 C |
| ATOM 6628 CD1 PHE A 165 34.346 -20.645 -49.314 1.00 26.22 C |
| ATOM 6629 CD2 PHE A 165 32.749 -20.680 -51.093 1.00 24.61 C |
| ATOM 6630 CE1 PHE A 165 33.326 -20.843 -48.387 1.00 25.58 C |
| ATOM 6631 CE2 PHE A 165 31.735 -20.882 -50.174 1.00 25.28 C |
| ATOM 6632 CZ PHE A 165 32.022 -20.953 -48.820 1.00 26.50 C |
| ATOM 6633 N GLU A 166 36.896 -17.631 -53.436 1.00 25.79 N |
| ATOM 6634 CA GLU A 166 38.015 -17.394 -54.334 1.00 28.96 C |
| ATOM 6635 C GLU A 166 38.978 -16.398 -53.689 1.00 26.88 C |
| ATOM 6636 O GLU A 166 38.752 -15.896 -52.584 1.00 27.14 O |
| ATOM 6637 CB GLU A 166 37.519 -16.910 -55.700 1.00 27.88 C |
| ATOM 6638 CG GLU A 166 36.542 -17.865 -56.409 1.00 29.91 C |
| ATOM 6639 CD GLU A 166 37.230 -19.070 -57.016 1.00 38.65 C |
| ATOM 6640 OE1 GLU A 166 38.478 -19.117 -56.994 1.00 38.42 O |
| ATOM 6641 OE2 GLU A 166 36.523 -19.977 -57.501 1.00 39.90 O |
| ATOM 6642 N VAL A 167 40.069 -16.090 -54.391 1.00 26.79 N |
| ATOM 6643 CA VAL A 167 41.117 -15.247 -53.822 1.00 29.40 C |
| ATOM 6644 C VAL A 167 41.165 -13.850 -54.425 1.00 26.89 C |
| ATOM 6645 O VAL A 167 41.867 -12.986 -53.872 1.00 27.42 O |
| ATOM 6646 CB VAL A 167 42.508 -15.902 -53.946 1.00 29.47 C |
| ATOM 6647 CG1 VAL A 167 42.553 -17.216 -53.181 1.00 31.79 C |
| ATOM 6648 CG2 VAL A 167 42.883 -16.058 -55.403 1.00 30.31 C |
| ATOM 6649 N PHE A 168 40.454 -13.596 -55.524 1.00 25.70 N |
| ATOM 6650 CA PHE A 168 40.536 -12.320 -56.229 1.00 28.14 C |
| ATOM 6651 C PHE A 168 39.176 -12.006 -56.843 1.00 30.33 C |
| ATOM 6652 O PHE A 168 38.708 -12.755 -57.703 1.00 30.17 O |
| ATOM 6653 CB PHE A 168 41.610 -12.383 -57.325 1.00 27.92 C |
| ATOM 6654 CG PHE A 168 41.867 -11.061 -57.995 1.00 26.35 C |
| ATOM 6655 CD1 PHE A 168 41.095 -10.653 -59.076 1.00 31.67 C |
| ATOM 6656 CD2 PHE A 168 42.874 -10.233 -57.549 1.00 27.65 C |
| ATOM 6657 CE1 PHE A 168 41.327 -9.430 -59.686 1.00 32.30 C |
| ATOM 6658 CE2 PHE A 168 43.110 -9.003 -58.164 1.00 30.45 C |
| ATOM 6659 CZ PHE A 168 42.339 -8.616 -59.231 1.00 30.83 C |
| ATOM 6660 N ASN A 169 38.553 -10.905 -56.427 1.00 29.19 N |
| ATOM 6661 CA ASN A 169 37.273 -10.488 -56.983 1.00 25.56 C |
| ATOM 6662 C ASN A 169 37.480 -9.420 -58.054 1.00 27.89 C |
| ATOM 6663 O ASN A 169 38.363 -8.577 -57.938 1.00 29.00 O |
| ATOM 6664 CB ASN A 169 36.358 -9.949 -55.886 1.00 26.23 C |
| ATOM 6665 CG ASN A 169 35.007 -9.482 -56.427 1.00 26.29 C |
| ATOM 6666 OD1 ASN A 169 34.380 -10.170 -57.223 1.00 28.79 O |
| ATOM 6667 ND2 ASN A 169 34.555 -8.321 -55.970 1.00 25.72 N |
| ATOM 6668 N PHE A 170 36.664 -9.459 -59.098 1.00 29.07 N |
| ATOM 6669 CA PHE A 170 36.844 -8.547 -60.218 1.00 30.11 C |
| ATOM 6670 C PHE A 170 36.153 -7.221 -59.925 1.00 31.92 C |
| ATOM 6671 O PHE A 170 34.931 -7.173 -59.743 1.00 31.30 O |
| ATOM 6672 CB PHE A 170 36.319 -9.184 -61.503 1.00 36.49 C |
| ATOM 6673 CG PHE A 170 37.303 -10.140 -62.136 1.00 44.13 C |
| ATOM 6674 CD1 PHE A 170 37.813 -11.209 -61.410 1.00 41.37 C |
| ATOM 6675 CD2 PHE A 170 37.711 -9.983 -63.454 1.00 49.62 C |
| ATOM 6676 CE1 PHE A 170 38.726 -12.093 -61.972 1.00 44.26 C |
| ATOM 6677 CE2 PHE A 170 38.619 -10.876 -64.023 1.00 50.40 C |
| ATOM 6678 CZ PHE A 170 39.122 -11.930 -63.276 1.00 45.88 C |
| ATOM 6679 N VAL A 171 36.942 -6.160 -59.844 1.00 29.14 N |
| ATOM 6680 CA VAL A 171 36.465 -4.801 -59.602 1.00 30.85 C |
| ATOM 6681 C VAL A 171 36.700 -3.996 -60.874 1.00 33.34 C |
| ATOM 6682 O VAL A 171 37.854 -3.866 -61.308 1.00 32.30 O |
| ATOM 6683 CB VAL A 171 37.180 -4.154 -58.406 1.00 30.47 C |
| ATOM 6684 CG1 VAL A 171 36.637 -2.741 -58.144 1.00 31.03 C |
| ATOM 6685 CG2 VAL A 171 37.053 -5.025 -57.165 1.00 27.37 C |
| ATOM 6686 N PRO A 172 35.659 -3.451 -61.506 1.00 33.38 N |
| ATOM 6687 CA PRO A 172 35.854 -2.759 -62.789 1.00 35.34 C |
| ATOM 6688 C PRO A 172 36.531 -1.413 -62.607 1.00 34.95 C |
| ATOM 6689 O PRO A 172 36.240 -0.665 -61.668 1.00 36.17 O |
| ATOM 6690 CB PRO A 172 34.428 -2.591 -63.322 1.00 40.17 C |
| ATOM 6691 CG PRO A 172 33.574 -2.563 -62.083 1.00 35.93 C |
| ATOM 6692 CD PRO A 172 34.237 -3.504 -61.116 1.00 33.85 C |
| ATOM 6693 N CYS A 173 37.431 -1.095 -63.540 1.00 38.95 N |
| ATOM 6694 CA CYS A 173 38.166 0.160 -63.443 1.00 36.69 C |
| ATOM 6695 C CYS A 173 37.247 1.365 -63.619 1.00 37.53 C |
| ATOM 6696 O CYS A 173 37.609 2.469 -63.205 1.00 37.74 O |
| ATOM 6697 CB CYS A 173 39.294 0.182 -64.475 1.00 38.82 C |
| ATOM 6698 SG CYS A 173 40.677 -0.992 -64.113 1.00 41.73 S |
| ATOM 6699 N SER A 174 36.057 1.177 -64.195 1.00 39.42 N |
| ATOM 6700 CA SER A 174 35.158 2.308 -64.414 1.00 39.78 C |
| ATOM 6701 C SER A 174 34.708 2.970 -63.114 1.00 42.11 C |
| ATOM 6702 O SER A 174 34.278 4.130 -63.145 1.00 41.25 O |
| ATOM 6703 CB SER A 174 33.937 1.865 -65.213 1.00 43.79 C |
| ATOM 6704 OG SER A 174 33.164 0.945 -64.470 1.00 47.29 O |
| ATOM 6705 N ILE A 175 34.802 2.277 -61.972 1.00 38.75 N |
| ATOM 6706 CA ILE A 175 34.364 2.833 -60.690 1.00 37.39 C |
| ATOM 6707 C ILE A 175 35.494 3.442 -59.881 1.00 40.63 C |
| ATOM 6708 O ILE A 175 35.250 3.905 -58.757 1.00 40.64 O |
| ATOM 6709 CB ILE A 175 33.642 1.778 -59.822 1.00 38.96 C |
| ATOM 6710 CG1 ILE A 175 34.661 0.786 -59.226 1.00 35.13 C |
| ATOM 6711 CG2 ILE A 175 32.501 1.114 -60.595 1.00 37.88 C |
| ATOM 6712 CD1 ILE A 175 34.134 -0.020 -58.068 1.00 35.77 C |
| ATOM 6713 N CYS A 176 36.716 3.477 -60.409 1.00 37.97 N |
| ATOM 6714 CA CYS A 176 37.858 3.776 -59.554 1.00 39.13 C |
| ATOM 6715 C CYS A 176 38.046 5.259 -59.279 1.00 43.83 C |
| ATOM 6716 O CYS A 176 38.685 5.598 -58.277 1.00 45.36 O |
| ATOM 6717 CB CYS A 176 39.126 3.200 -60.179 1.00 37.34 C |
| ATOM 6718 SG CYS A 176 39.216 1.412 -59.924 1.00 38.39 S |
| ATOM 6719 N SER A 177 37.514 6.142 -60.135 1.00 42.34 N |
| ATOM 6720 CA SER A 177 37.596 7.577 -59.881 1.00 45.93 C |
| ATOM 6721 C SER A 177 39.042 7.993 -59.630 1.00 44.30 C |
| ATOM 6722 O SER A 177 39.907 7.784 -60.487 1.00 43.34 O |
| ATOM 6723 CB SER A 177 36.693 7.951 -58.700 1.00 49.24 C |
| ATOM 6724 OG SER A 177 37.232 9.017 -57.947 1.00 52.91 O |
| ATOM 6725 N ASN A 178 39.342 8.543 -58.457 1.00 43.18 N |
| ATOM 6726 CA ASN A 178 40.728 8.858 -58.152 1.00 47.46 C |
| ATOM 6727 C ASN A 178 41.211 8.107 -56.913 1.00 45.93 C |
| ATOM 6728 O ASN A 178 42.146 8.544 -56.236 1.00 47.13 O |
| ATOM 6729 CB ASN A 178 40.944 10.366 -58.006 1.00 48.70 C |
| ATOM 6730 CG ASN A 178 40.289 10.951 -56.770 1.00 55.71 C |
| ATOM 6731 OD1 ASN A 178 39.416 10.338 -56.144 1.00 57.42 O |
| ATOM 6732 ND2 ASN A 178 40.733 12.151 -56.397 1.00 57.42 N |
| ATOM 6733 N ASN A 179 40.606 6.953 -56.632 1.00 43.59 N |
| ATOM 6734 CA ASN A 179 41.018 6.095 -55.529 1.00 38.56 C |
| ATOM 6735 C ASN A 179 42.209 5.237 -55.953 1.00 37.60 C |
| ATOM 6736 O ASN A 179 42.060 4.370 -56.826 1.00 37.14 O |
| ATOM 6737 CB ASN A 179 39.848 5.212 -55.092 1.00 42.41 C |
| ATOM 6738 CG ASN A 179 40.114 4.494 -53.796 1.00 40.81 C |
| ATOM 6739 OD1 ASN A 179 40.999 3.644 -53.719 1.00 40.16 O |
| ATOM 6740 ND2 ASN A 179 39.334 4.812 -52.772 1.00 42.80 N |
| ATOM 6741 N PRO A 180 43.393 5.438 -55.367 1.00 37.21 N |
| ATOM 6742 CA PRO A 180 44.573 4.688 -55.832 1.00 37.15 C |
| ATOM 6743 C PRO A 180 44.509 3.209 -55.517 1.00 36.55 C |
| ATOM 6744 O PRO A 180 45.095 2.409 -56.258 1.00 37.31 O |
| ATOM 6745 CB PRO A 180 45.755 5.363 -55.114 1.00 41.86 C |
| ATOM 6746 CG PRO A 180 45.187 6.331 -54.153 1.00 45.42 C |
| ATOM 6747 CD PRO A 180 43.698 6.389 -54.283 1.00 41.98 C |
| ATOM 6748 N THR A 181 43.826 2.820 -54.441 1.00 34.84 N |
| ATOM 6749 CA THR A 181 43.672 1.398 -54.142 1.00 32.04 C |
| ATOM 6750 C THR A 181 42.888 0.711 -55.250 1.00 34.11 C |
| ATOM 6751 O THR A 181 43.266 -0.363 -55.745 1.00 31.90 O |
| ATOM 6752 CB THR A 181 42.955 1.233 -52.806 1.00 36.36 C |
| ATOM 6753 OG1 THR A 181 43.831 1.655 -51.759 1.00 36.75 O |
| ATOM 6754 CG2 THR A 181 42.592 -0.232 -52.575 1.00 35.01 C |
| ATOM 6755 N CYS A 182 41.787 1.336 -55.662 1.00 33.51 N |
| ATOM 6756 CA CYS A 182 40.973 0.799 -56.739 1.00 31.14 C |
| ATOM 6757 C CYS A 182 41.798 0.591 -58.008 1.00 31.28 C |
| ATOM 6758 O CYS A 182 41.773 -0.489 -58.612 1.00 30.81 O |
| ATOM 6759 CB CYS A 182 39.799 1.748 -56.988 1.00 32.22 C |
| ATOM 6760 SG CYS A 182 38.513 1.050 -58.022 1.00 37.18 S |
| ATOM 6761 N TRP A 183 42.538 1.624 -58.430 1.00 30.57 N |
| ATOM 6762 CA TRP A 183 43.335 1.507 -59.645 1.00 30.96 C |
| ATOM 6763 C TRP A 183 44.384 0.413 -59.527 1.00 32.72 C |
| ATOM 6764 O TRP A 183 44.760 -0.196 -60.534 1.00 34.23 O |
| ATOM 6765 CB TRP A 183 44.009 2.842 -59.982 1.00 35.06 C |
| ATOM 6766 CG TRP A 183 43.061 3.820 -60.621 1.00 34.92 C |
| ATOM 6767 CD1 TRP A 183 42.520 4.939 -60.054 1.00 36.81 C |
| ATOM 6768 CD2 TRP A 183 42.471 3.702 -61.920 1.00 33.31 C |
| ATOM 6769 NE1 TRP A 183 41.662 5.554 -60.944 1.00 37.80 N |
| ATOM 6770 CE2 TRP A 183 41.612 4.808 -62.094 1.00 34.98 C |
| ATOM 6771 CE3 TRP A 183 42.602 2.778 -62.962 1.00 33.37 C |
| ATOM 6772 CZ2 TRP A 183 40.894 5.018 -63.266 1.00 35.65 C |
| ATOM 6773 CZ3 TRP A 183 41.891 2.982 -64.123 1.00 35.31 C |
| ATOM 6774 CH2 TRP A 183 41.047 4.097 -64.270 1.00 36.74 C |
| ATOM 6775 N ALA A 184 44.859 0.145 -58.311 1.00 32.95 N |
| ATOM 6776 CA ALA A 184 45.893 -0.871 -58.130 1.00 31.38 C |
| ATOM 6777 C ALA A 184 45.377 -2.277 -58.428 1.00 31.52 C |
| ATOM 6778 O ALA A 184 46.145 -3.128 -58.892 1.00 31.43 O |
| ATOM 6779 CB ALA A 184 46.458 -0.782 -56.704 1.00 31.33 C |
| ATOM 6780 N ILE A 185 44.089 -2.540 -58.205 1.00 27.97 N |
| ATOM 6781 CA ILE A 185 43.551 -3.895 -58.291 1.00 31.08 C |
| ATOM 6782 C ILE A 185 42.479 -4.064 -59.360 1.00 32.04 C |
| ATOM 6783 O ILE A 185 42.026 -5.201 -59.579 1.00 30.80 O |
| ATOM 6784 CB ILE A 185 42.985 -4.363 -56.934 1.00 31.28 C |
| ATOM 6785 CG1 ILE A 185 42.036 -3.284 -56.393 1.00 31.15 C |
| ATOM 6786 CG2 ILE A 185 44.137 -4.665 -55.967 1.00 29.72 C |
| ATOM 6787 CD1 ILE A 185 40.542 -3.528 -56.641 1.00 31.30 C |
| ATOM 6788 N CYS A 186 42.027 -2.993 -60.012 1.00 30.23 N |
| ATOM 6789 CA CYS A 186 40.861 -3.097 -60.879 1.00 30.68 C |
| ATOM 6790 C CYS A 186 41.206 -3.785 -62.200 1.00 37.70 C |
| ATOM 6791 O CYS A 186 42.369 -3.876 -62.604 1.00 35.56 O |
| ATOM 6792 CB CYS A 186 40.256 -1.713 -61.158 1.00 32.93 C |
| ATOM 6793 SG CYS A 186 41.307 -0.608 -62.210 1.00 33.34 S |
| ATOM 6794 N LYS A 187 40.161 -4.272 -62.868 1.00 36.25 N |
| ATOM 6795 CA LYS A 187 40.238 -4.920 -64.171 1.00 38.58 C |
| ATOM 6796 C LYS A 187 39.355 -4.173 -65.164 1.00 44.13 C |
| ATOM 6797 O LYS A 187 38.295 -3.657 -64.800 1.00 42.52 O |
| ATOM 6798 CB LYS A 187 39.775 -6.383 -64.107 1.00 44.11 C |
| ATOM 6799 CG LYS A 187 40.438 -7.214 -63.024 1.00 44.22 C |
| ATOM 6800 CD LYS A 187 41.687 -7.883 -63.541 1.00 46.66 C |
| ATOM 6801 CE LYS A 187 41.356 -8.835 -64.672 1.00 50.14 C |
| ATOM 6802 NZ LYS A 187 42.614 -9.359 -65.286 1.00 56.56 N |
| ATOM 6803 N ARG A 188 39.824 -4.090 -66.407 1.00 49.59 N |
| ATOM 6804 CA ARG A 188 39.035 -3.437 -67.479 1.00 53.62 C |
| ATOM 6805 C ARG A 188 37.981 -4.434 -67.960 1.00 58.30 C |
| ATOM 6806 O ARG A 188 36.907 -3.953 -68.352 1.00 58.24 O |
| ATOM 6807 CB ARG A 188 39.937 -3.029 -68.648 1.00 56.61 C |
| ATOM 6808 CG ARG A 188 41.214 -2.301 -68.262 1.00 57.14 C |
| ATOM 6809 CD ARG A 188 42.124 -2.201 -69.472 1.00 59.82 C |
| ATOM 6810 NE ARG A 188 43.388 -1.531 -69.208 1.00 63.24 N |
| ATOM 6811 CZ ARG A 188 44.577 -2.113 -69.302 1.00 61.96 C |
| ATOM 6812 NH1 ARG A 188 44.660 -3.427 -69.383 1.00 59.29 N |
| ATOM 6813 NH2 ARG A 188 45.675 -1.378 -69.312 1.00 60.58 N |
| TER 6814 ARG A 188 |
| TER 7044 ARG B 188 |
| HETATM 7055 S SO4 A 301 42.861 -5.799 -67.149 1.00 30.00 S |
| HETATM 7056 O1 SO4 A 301 43.383 -5.474 -68.444 1.00 30.00 O |
| HETATM 7057 O2 SO4 A 301 41.487 -6.193 -67.274 1.00 30.00 O |
| HETATM 7058 O3 SO4 A 301 43.618 -6.877 -66.590 1.00 30.00 O |
| HETATM 7059 O4 SO4 A 301 42.958 -4.655 -66.294 1.00 30.00 O |
| HETATM 7446 O HOH A 401 32.300 -19.614 -56.177 1.00 40.00 O |
| HETATM 7447 O HOH A 402 39.377 -15.164 -58.619 1.00 41.78 O |
| HETATM 7448 O HOH A 403 33.065 -9.042 -59.320 1.00 28.80 O |
| HETATM 7449 O HOH A 404 39.600 -6.580 -59.594 1.00 32.81 O |
| HETATM 7450 O HOH A 405 30.364 -13.852 -56.597 1.00 27.63 O |
| HETATM 7451 O HOH A 406 34.177 -17.591 -63.549 1.00 57.74 O |
| CONECT 160 758 |
| CONECT 758 160 |
| CONECT 1116 1530 |
| CONECT 1530 1116 |
| CONECT 1826 2332 |
| CONECT 2332 1826 |
| CONECT 2676 3155 |
| CONECT 3155 2676 |
| CONECT 3452 4050 |
| CONECT 4050 3452 |
| CONECT 4408 4822 |
| CONECT 4822 4408 |
| CONECT 5118 5624 |
| CONECT 5624 5118 |
| CONECT 5968 6447 |
| CONECT 6447 5968 |
| CONECT 6698 6793 |
| CONECT 6718 6760 |
| CONECT 6760 6718 |
| CONECT 6793 6698 |
| CONECT 6928 7023 |
| CONECT 6948 6990 |
| CONECT 6990 6948 |
| CONECT 7023 6928 |
| CONECT 7045 7046 7047 7048 7049 |
| CONECT 7046 7045 |
| CONECT 7047 7045 |
| CONECT 7048 7045 |
| CONECT 7049 7045 |
| CONECT 7050 7051 7052 7053 7054 |
| CONECT 7051 7050 |
| CONECT 7052 7050 |
| CONECT 7053 7050 |
| CONECT 7054 7050 |
| CONECT 7055 7056 7057 7058 7059 |
| CONECT 7056 7055 |
| CONECT 7057 7055 |
| CONECT 7058 7055 |
| CONECT 7059 7055 |
| CONECT 7060 7061 7062 7063 7064 |
| CONECT 7061 7060 |
| CONECT 7062 7060 |
| CONECT 7063 7060 |
| CONECT 7064 7060 |
| MASTER 390 0 4 22 85 0 0 6 7451 6 44 84 |
| END |
|
|
