HEADER TOXIN 09-OCT-22 8H3Y TITLE BACTEROIDE FRAGILIS TOXIN IN COMPLEX WITH NANOBODY 327 COMPND MOL_ID: 1; COMPND 2 MOLECULE: FRAGILYSIN; COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: ENTEROTOXIN; COMPND 5 EC: 3.4.24.74; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: NANOBODY 327; COMPND 9 CHAIN: D, E, F; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES FRAGILIS; SOURCE 3 ORGANISM_TAXID: 817; SOURCE 4 GENE: BTFP; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 9 ORGANISM_TAXID: 30538; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS BACTEROIDE FRAGILIS TOXIN, NANOBODY, TOXIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.WEN,Y.GUO REVDAT 1 08-FEB-23 8H3Y 0 JRNL AUTH Y.GUO,Z.OUYANG,W.HE,J.ZHANG,Q.QIN,M.JIAO,S.MUYLDERMANS, JRNL AUTH 2 F.FANG ZHENG,Y.WEN JRNL TITL SCREENING AND EPITOPE CHARACTERIZATION OF DIAGNOSTIC JRNL TITL 2 NANOBODY AGAINST TOTAL AND ACTIVATED BACTEROIDE FRAGILIS JRNL TITL 3 TOXIN. JRNL REF FRONT IMMUNOL V. 14 2023 JRNL REFN ESSN 1664-3224 JRNL DOI 10.3389/FIMMU.2023.1065274 REMARK 2 REMARK 2 RESOLUTION. 2.25 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19_4092 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) : 2.25 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.39 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.560 REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 3 NUMBER OF REFLECTIONS : 152840 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.205 REMARK 3 R VALUE (WORKING SET) : 0.204 REMARK 3 FREE R VALUE : 0.244 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.510 REMARK 3 FREE R VALUE TEST SET COUNT : 3843 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 41.3900 - 6.7300 0.95 5470 142 0.1440 0.1236 REMARK 3 2 6.7300 - 5.3400 0.97 5607 145 0.1483 0.1806 REMARK 3 3 5.3400 - 4.6700 0.94 5382 139 0.1328 0.1737 REMARK 3 4 4.6700 - 4.2400 0.97 5580 146 0.1272 0.1749 REMARK 3 5 4.2400 - 3.9400 0.97 5601 145 0.1496 0.1880 REMARK 3 6 3.9400 - 3.7100 0.98 5639 149 0.1762 0.1907 REMARK 3 7 3.7100 - 3.5200 0.93 5371 135 0.1874 0.2483 REMARK 3 8 3.5200 - 3.3700 0.97 5576 146 0.1898 0.2883 REMARK 3 9 3.3700 - 3.2400 0.97 5589 145 0.2120 0.2498 REMARK 3 10 3.2400 - 3.1300 0.97 5608 148 0.2322 0.2978 REMARK 3 11 3.1300 - 3.0300 0.98 5624 146 0.2341 0.2818 REMARK 3 12 3.0300 - 2.9400 0.98 5617 143 0.2416 0.3108 REMARK 3 13 2.9400 - 2.8600 0.98 5635 141 0.2453 0.2795 REMARK 3 14 2.8600 - 2.7900 0.97 5527 142 0.2451 0.2914 REMARK 3 15 2.7900 - 2.7300 0.92 5371 136 0.2660 0.3516 REMARK 3 16 2.7300 - 2.6700 0.95 5395 138 0.2773 0.3383 REMARK 3 17 2.6700 - 2.6200 0.96 5584 143 0.2805 0.3061 REMARK 3 18 2.6200 - 2.5700 0.96 5573 141 0.2809 0.3353 REMARK 3 19 2.5700 - 2.5200 0.97 5475 145 0.2860 0.3397 REMARK 3 20 2.5200 - 2.4800 0.97 5627 147 0.2928 0.2963 REMARK 3 21 2.4800 - 2.4400 0.97 5533 141 0.2984 0.3499 REMARK 3 22 2.4400 - 2.4000 0.97 5574 141 0.3082 0.3371 REMARK 3 23 2.4000 - 2.3700 0.97 5549 143 0.3157 0.3663 REMARK 3 24 2.3700 - 2.3400 0.97 5534 141 0.3297 0.3752 REMARK 3 25 2.3400 - 2.3000 0.97 5615 150 0.3314 0.3462 REMARK 3 26 2.3000 - 2.2700 0.92 5348 132 0.3408 0.3657 REMARK 3 27 2.2700 - 2.2500 0.87 4993 133 0.3442 0.3708 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.040 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 41.43 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 : 0.008 11340 REMARK 3 ANGLE : 0.965 15375 REMARK 3 CHIRALITY : 0.055 1670 REMARK 3 PLANARITY : 0.007 1995 REMARK 3 DIHEDRAL : 6.491 1556 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): -41.4861 -17.1380 50.8314 REMARK 3 T TENSOR REMARK 3 T11: 0.3446 T22: 0.3145 REMARK 3 T33: 0.3449 T12: -0.0014 REMARK 3 T13: 0.0016 T23: 0.0031 REMARK 3 L TENSOR REMARK 3 L11: 0.0528 L22: -0.0348 REMARK 3 L33: 0.1535 L12: 0.0035 REMARK 3 L13: 0.0285 L23: 0.0021 REMARK 3 S TENSOR REMARK 3 S11: 0.0210 S12: 0.0102 S13: -0.0086 REMARK 3 S21: 0.0138 S22: 0.0029 S23: -0.0232 REMARK 3 S31: -0.0139 S32: -0.0127 S33: 0.0000 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 8H3Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 12-OCT-22. REMARK 100 THE DEPOSITION ID IS D_1300032757. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-NOV-20 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 : SSRF REMARK 200 BEAMLINE : BL18U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.98 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 152840 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250 REMARK 200 RESOLUTION RANGE LOW (A) : 41.390 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33 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 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: MOLREP REMARK 200 STARTING MODEL: 3P24 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 49.77 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM TARTRATE DIBASIC, 20% REMARK 280 W/V POLYETHYLENE GLYCOL 3350, PH 6.6, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 78.45050 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.49200 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 78.45050 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 41.49200 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, 3 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 APPLY THE FOLLOWING TO CHAINS: A, F 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, C 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH B 592 LIES ON A SPECIAL POSITION. 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 A 1 REMARK 465 LYS A 2 REMARK 465 ASN A 3 REMARK 465 VAL A 4 REMARK 465 LYS A 5 REMARK 465 LEU A 6 REMARK 465 LEU A 7 REMARK 465 LEU A 8 REMARK 465 MET A 9 REMARK 465 LEU A 10 REMARK 465 GLY A 11 REMARK 465 THR A 12 REMARK 465 ALA A 13 REMARK 465 ALA A 14 REMARK 465 LEU A 15 REMARK 465 LEU A 16 REMARK 465 ALA A 17 REMARK 465 ALA A 18 REMARK 465 CYS A 19 REMARK 465 SER A 20 REMARK 465 ASN A 21 REMARK 465 GLU A 22 REMARK 465 ALA A 23 REMARK 465 ASP A 24 REMARK 465 SER A 25 REMARK 465 LEU A 26 REMARK 465 THR A 27 REMARK 465 THR A 28 REMARK 465 SER A 29 REMARK 465 ILE A 30 REMARK 465 ASP A 31 REMARK 465 ALA A 32 REMARK 465 PRO A 33 REMARK 465 ARG A 162 REMARK 465 THR A 163 REMARK 465 ARG A 164 REMARK 465 SER A 165 REMARK 465 GLN A 200 REMARK 465 VAL A 201 REMARK 465 PRO A 202 REMARK 465 HIS A 203 REMARK 465 GLY A 204 REMARK 465 ILE A 205 REMARK 465 THR A 206 REMARK 465 GLU A 207 REMARK 465 SER A 208 REMARK 465 GLN A 209 REMARK 465 THR A 210 REMARK 465 ARG A 211 REMARK 465 MET B 1 REMARK 465 LYS B 2 REMARK 465 ASN B 3 REMARK 465 VAL B 4 REMARK 465 LYS B 5 REMARK 465 LEU B 6 REMARK 465 LEU B 7 REMARK 465 LEU B 8 REMARK 465 MET B 9 REMARK 465 LEU B 10 REMARK 465 GLY B 11 REMARK 465 THR B 12 REMARK 465 ALA B 13 REMARK 465 ALA B 14 REMARK 465 LEU B 15 REMARK 465 LEU B 16 REMARK 465 ALA B 17 REMARK 465 ALA B 18 REMARK 465 CYS B 19 REMARK 465 SER B 20 REMARK 465 ASN B 21 REMARK 465 GLU B 22 REMARK 465 ALA B 23 REMARK 465 ASP B 24 REMARK 465 SER B 25 REMARK 465 LEU B 26 REMARK 465 THR B 27 REMARK 465 THR B 28 REMARK 465 SER B 29 REMARK 465 ILE B 30 REMARK 465 ASP B 31 REMARK 465 ALA B 32 REMARK 465 PRO B 33 REMARK 465 VAL B 201 REMARK 465 PRO B 202 REMARK 465 HIS B 203 REMARK 465 GLY B 204 REMARK 465 ILE B 205 REMARK 465 THR B 206 REMARK 465 GLU B 207 REMARK 465 SER B 208 REMARK 465 GLN B 209 REMARK 465 THR B 210 REMARK 465 ARG B 211 REMARK 465 HIS D 122 REMARK 465 HIS D 123 REMARK 465 HIS D 124 REMARK 465 HIS D 125 REMARK 465 HIS D 126 REMARK 465 HIS D 127 REMARK 465 HIS E 122 REMARK 465 HIS E 123 REMARK 465 HIS E 124 REMARK 465 HIS E 125 REMARK 465 HIS E 126 REMARK 465 HIS E 127 REMARK 465 GLN F 1 REMARK 465 HIS F 122 REMARK 465 HIS F 123 REMARK 465 HIS F 124 REMARK 465 HIS F 125 REMARK 465 HIS F 126 REMARK 465 HIS F 127 REMARK 465 MET C 1 REMARK 465 LYS C 2 REMARK 465 ASN C 3 REMARK 465 VAL C 4 REMARK 465 LYS C 5 REMARK 465 LEU C 6 REMARK 465 LEU C 7 REMARK 465 LEU C 8 REMARK 465 MET C 9 REMARK 465 LEU C 10 REMARK 465 GLY C 11 REMARK 465 THR C 12 REMARK 465 ALA C 13 REMARK 465 ALA C 14 REMARK 465 LEU C 15 REMARK 465 LEU C 16 REMARK 465 ALA C 17 REMARK 465 ALA C 18 REMARK 465 CYS C 19 REMARK 465 SER C 20 REMARK 465 ASN C 21 REMARK 465 GLU C 22 REMARK 465 ALA C 23 REMARK 465 ASP C 24 REMARK 465 SER C 25 REMARK 465 LEU C 26 REMARK 465 THR C 27 REMARK 465 THR C 28 REMARK 465 SER C 29 REMARK 465 ILE C 30 REMARK 465 ASP C 31 REMARK 465 ALA C 32 REMARK 465 PRO C 33 REMARK 465 ARG C 162 REMARK 465 THR C 163 REMARK 465 ARG C 164 REMARK 465 SER C 165 REMARK 465 ALA C 166 REMARK 465 GLY C 167 REMARK 465 LYS C 168 REMARK 465 VAL C 201 REMARK 465 PRO C 202 REMARK 465 HIS C 203 REMARK 465 GLY C 204 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 A 147 CG CD NE CZ NH1 NH2 REMARK 470 ILE A 149 CG1 CG2 CD1 REMARK 470 LYS A 168 CG CD CE NZ REMARK 470 LEU A 186 CG CD1 CD2 REMARK 470 LYS B 144 CG CD CE NZ REMARK 470 LYS B 145 CG CD CE NZ REMARK 470 ARG B 147 CG CD NE CZ NH1 NH2 REMARK 470 ILE B 149 CG1 CG2 CD1 REMARK 470 ASN B 150 CG OD1 ND2 REMARK 470 LYS B 152 CG CD CE NZ REMARK 470 ARG B 162 CG CD NE CZ NH1 NH2 REMARK 470 ARG B 164 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 182 CG CD CE NZ REMARK 470 GLN B 200 CG CD OE1 NE2 REMARK 470 GLU B 294 CG CD OE1 OE2 REMARK 470 LYS B 312 CG CD CE NZ REMARK 470 GLU B 392 CG CD OE1 OE2 REMARK 470 GLN D 1 CG CD OE1 NE2 REMARK 470 GLN F 113 CG CD OE1 NE2 REMARK 470 ARG C 147 CG CD NE CZ NH1 NH2 REMARK 470 ILE C 149 CG1 CG2 CD1 REMARK 470 ASN C 150 CG OD1 ND2 REMARK 470 LYS C 152 CG CD CE NZ REMARK 470 GLU C 188 CG CD OE1 OE2 REMARK 470 LYS C 292 CG CD CE NZ REMARK 470 LYS C 312 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O ILE F 70 O HOH F 201 2.09 REMARK 500 O LEU C 186 O HOH C 501 2.13 REMARK 500 OG SER C 76 O HOH C 502 2.18 REMARK 500 O HOH A 665 O HOH A 666 2.19 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 SER A 42 25.71 -149.88 REMARK 500 ASP A 66 -160.92 -116.62 REMARK 500 ASN A 70 76.22 -158.63 REMARK 500 ILE A 192 102.34 -51.68 REMARK 500 ASN A 193 77.95 77.30 REMARK 500 SER B 42 14.35 -151.26 REMARK 500 LYS B 145 -74.03 -60.23 REMARK 500 THR B 146 76.08 -55.72 REMARK 500 ASN B 150 39.83 -79.14 REMARK 500 ASN B 228 109.86 -52.57 REMARK 500 LEU D 18 136.18 -170.14 REMARK 500 ALA D 92 169.64 176.84 REMARK 500 LYS D 109 -50.20 -129.27 REMARK 500 SER E 25 66.39 -105.19 REMARK 500 VAL E 48 -60.11 -103.61 REMARK 500 ALA E 92 168.78 173.09 REMARK 500 ASN F 52 159.50 -46.63 REMARK 500 LYS F 109 -50.41 -127.38 REMARK 500 ASP C 66 -152.75 -129.76 REMARK 500 ILE C 149 -31.18 73.30 REMARK 500 ASN C 185 76.92 38.82 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 665 DISTANCE = 5.92 ANGSTROMS REMARK 525 HOH A 666 DISTANCE = 5.93 ANGSTROMS REMARK 525 HOH B 625 DISTANCE = 7.48 ANGSTROMS REMARK 525 HOH B 626 DISTANCE = 7.96 ANGSTROMS REMARK 525 HOH C 654 DISTANCE = 6.67 ANGSTROMS REMARK 525 HOH C 655 DISTANCE = 6.91 ANGSTROMS 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 ZN A 401 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 194 OD1 REMARK 620 2 ASP A 194 OD2 56.8 REMARK 620 3 HIS A 348 NE2 142.9 86.6 REMARK 620 4 HIS A 352 NE2 88.8 112.8 102.0 REMARK 620 5 HIS A 358 NE2 99.2 137.9 113.6 99.1 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN B 401 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 194 OD1 REMARK 620 2 ASP B 194 OD2 56.1 REMARK 620 3 HIS B 348 NE2 159.7 103.7 REMARK 620 4 HIS B 352 NE2 89.6 109.2 100.4 REMARK 620 5 HIS B 358 NE2 108.1 145.3 87.5 100.6 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN C 401 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP C 194 OD1 REMARK 620 2 ASP C 194 OD2 59.2 REMARK 620 3 HIS C 348 NE2 155.2 97.5 REMARK 620 4 HIS C 352 NE2 103.7 112.5 92.8 REMARK 620 5 HIS C 358 NE2 102.7 143.1 91.4 102.7 REMARK 620 N 1 2 3 4 DBREF 8H3Y A 1 397 UNP P54355 ENTM_BACFG 9 405 DBREF 8H3Y B 1 397 UNP P54355 ENTM_BACFG 9 405 DBREF 8H3Y D 1 127 PDB 8H3Y 8H3Y 1 127 DBREF 8H3Y E 1 127 PDB 8H3Y 8H3Y 1 127 DBREF 8H3Y F 1 127 PDB 8H3Y 8H3Y 1 127 DBREF 8H3Y C 1 397 UNP P54355 ENTM_BACFG 9 405 SEQRES 1 A 397 MET LYS ASN VAL LYS LEU LEU LEU MET LEU GLY THR ALA SEQRES 2 A 397 ALA LEU LEU ALA ALA CYS SER ASN GLU ALA ASP SER LEU SEQRES 3 A 397 THR THR SER ILE ASP ALA PRO VAL THR ALA SER ILE ASP SEQRES 4 A 397 LEU GLN SER VAL SER TYR THR ASP LEU ALA THR GLN LEU SEQRES 5 A 397 ASN ASP VAL SER ASP PHE GLY LYS MET ILE ILE LEU LYS SEQRES 6 A 397 ASP ASN GLY PHE ASN ARG GLN VAL HIS VAL SER MET ASP SEQRES 7 A 397 LYS ARG THR LYS ILE GLN LEU ASP ASN GLU ASN VAL ARG SEQRES 8 A 397 LEU PHE ASN GLY ARG ASP LYS ASP SER THR SER PHE ILE SEQRES 9 A 397 LEU GLY ASP GLU PHE ALA VAL LEU ARG PHE TYR ARG ASN SEQRES 10 A 397 GLY GLU SER ILE SER TYR ILE ALA TYR LYS GLU ALA GLN SEQRES 11 A 397 MET MET ASN GLU ILE ALA GLU PHE TYR ALA ALA PRO PHE SEQRES 12 A 397 LYS LYS THR ARG ALA ILE ASN GLU LYS GLU ALA PHE GLU SEQRES 13 A 397 CYS ILE TYR ASP SER ARG THR ARG SER ALA GLY LYS ASP SEQRES 14 A 397 ILE VAL SER VAL LYS ILE ASN ILE ASP LYS ALA LYS LYS SEQRES 15 A 397 ILE LEU ASN LEU PRO GLU CYS ASP TYR ILE ASN ASP TYR SEQRES 16 A 397 ILE LYS THR PRO GLN VAL PRO HIS GLY ILE THR GLU SER SEQRES 17 A 397 GLN THR ARG ALA VAL PRO SER GLU PRO LYS THR VAL TYR SEQRES 18 A 397 VAL ILE CYS LEU ARG GLU ASN GLY SER THR ILE TYR PRO SEQRES 19 A 397 ASN GLU VAL SER ALA GLN MET GLN ASP ALA ALA ASN SER SEQRES 20 A 397 VAL TYR ALA VAL HIS GLY LEU LYS ARG TYR VAL ASN PHE SEQRES 21 A 397 HIS PHE VAL LEU TYR THR THR GLU TYR SER CYS PRO SER SEQRES 22 A 397 GLY ASP ALA LYS GLU GLY LEU GLU GLY PHE THR ALA SER SEQRES 23 A 397 LEU LYS SER ASN PRO LYS ALA GLU GLY TYR ASP ASP GLN SEQRES 24 A 397 ILE TYR PHE LEU ILE ARG TRP GLY THR TRP ASP ASN LYS SEQRES 25 A 397 ILE LEU GLY MET SER TRP PHE ASN SER TYR ASN VAL ASN SEQRES 26 A 397 THR ALA SER ASP PHE GLU ALA SER GLY MET SER THR THR SEQRES 27 A 397 GLN LEU MET TYR PRO GLY VAL MET ALA HIS GLU LEU GLY SEQRES 28 A 397 HIS ILE LEU GLY ALA GLU HIS THR ASP ASN SER LYS ASP SEQRES 29 A 397 LEU MET TYR ALA THR PHE THR GLY TYR LEU SER HIS LEU SEQRES 30 A 397 SER GLU LYS ASN MET ASP ILE ILE ALA LYS ASN LEU GLY SEQRES 31 A 397 TRP GLU ALA ALA ASP GLY ASP SEQRES 1 B 397 MET LYS ASN VAL LYS LEU LEU LEU MET LEU GLY THR ALA SEQRES 2 B 397 ALA LEU LEU ALA ALA CYS SER ASN GLU ALA ASP SER LEU SEQRES 3 B 397 THR THR SER ILE ASP ALA PRO VAL THR ALA SER ILE ASP SEQRES 4 B 397 LEU GLN SER VAL SER TYR THR ASP LEU ALA THR GLN LEU SEQRES 5 B 397 ASN ASP VAL SER ASP PHE GLY LYS MET ILE ILE LEU LYS SEQRES 6 B 397 ASP ASN GLY PHE ASN ARG GLN VAL HIS VAL SER MET ASP SEQRES 7 B 397 LYS ARG THR LYS ILE GLN LEU ASP ASN GLU ASN VAL ARG SEQRES 8 B 397 LEU PHE ASN GLY ARG ASP LYS ASP SER THR SER PHE ILE SEQRES 9 B 397 LEU GLY ASP GLU PHE ALA VAL LEU ARG PHE TYR ARG ASN SEQRES 10 B 397 GLY GLU SER ILE SER TYR ILE ALA TYR LYS GLU ALA GLN SEQRES 11 B 397 MET MET ASN GLU ILE ALA GLU PHE TYR ALA ALA PRO PHE SEQRES 12 B 397 LYS LYS THR ARG ALA ILE ASN GLU LYS GLU ALA PHE GLU SEQRES 13 B 397 CYS ILE TYR ASP SER ARG THR ARG SER ALA GLY LYS ASP SEQRES 14 B 397 ILE VAL SER VAL LYS ILE ASN ILE ASP LYS ALA LYS LYS SEQRES 15 B 397 ILE LEU ASN LEU PRO GLU CYS ASP TYR ILE ASN ASP TYR SEQRES 16 B 397 ILE LYS THR PRO GLN VAL PRO HIS GLY ILE THR GLU SER SEQRES 17 B 397 GLN THR ARG ALA VAL PRO SER GLU PRO LYS THR VAL TYR SEQRES 18 B 397 VAL ILE CYS LEU ARG GLU ASN GLY SER THR ILE TYR PRO SEQRES 19 B 397 ASN GLU VAL SER ALA GLN MET GLN ASP ALA ALA ASN SER SEQRES 20 B 397 VAL TYR ALA VAL HIS GLY LEU LYS ARG TYR VAL ASN PHE SEQRES 21 B 397 HIS PHE VAL LEU TYR THR THR GLU TYR SER CYS PRO SER SEQRES 22 B 397 GLY ASP ALA LYS GLU GLY LEU GLU GLY PHE THR ALA SER SEQRES 23 B 397 LEU LYS SER ASN PRO LYS ALA GLU GLY TYR ASP ASP GLN SEQRES 24 B 397 ILE TYR PHE LEU ILE ARG TRP GLY THR TRP ASP ASN LYS SEQRES 25 B 397 ILE LEU GLY MET SER TRP PHE ASN SER TYR ASN VAL ASN SEQRES 26 B 397 THR ALA SER ASP PHE GLU ALA SER GLY MET SER THR THR SEQRES 27 B 397 GLN LEU MET TYR PRO GLY VAL MET ALA HIS GLU LEU GLY SEQRES 28 B 397 HIS ILE LEU GLY ALA GLU HIS THR ASP ASN SER LYS ASP SEQRES 29 B 397 LEU MET TYR ALA THR PHE THR GLY TYR LEU SER HIS LEU SEQRES 30 B 397 SER GLU LYS ASN MET ASP ILE ILE ALA LYS ASN LEU GLY SEQRES 31 B 397 TRP GLU ALA ALA ASP GLY ASP SEQRES 1 D 127 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 127 ALA GLY GLY SER LEU ARG LEU SER CYS THR TYR SER GLY SEQRES 3 D 127 GLN THR PHE SER ALA TRP ALA MET GLY TRP PHE ARG GLN SEQRES 4 D 127 ALA PRO GLY LYS GLU ARG GLU THR VAL ALA THR ILE ASN SEQRES 5 D 127 TRP ASN GLY GLU ARG THR GLN TYR ALA ASP ALA VAL LYS SEQRES 6 D 127 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASP THR SEQRES 7 D 127 VAL TYR LEU GLU MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 D 127 ALA VAL TYR TYR CYS ALA SER MET MET GLY THR TYR TYR SEQRES 9 D 127 SER GLY SER PRO LYS ASN TRP GLY GLN GLY THR GLN VAL SEQRES 10 D 127 THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 E 127 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 E 127 ALA GLY GLY SER LEU ARG LEU SER CYS THR TYR SER GLY SEQRES 3 E 127 GLN THR PHE SER ALA TRP ALA MET GLY TRP PHE ARG GLN SEQRES 4 E 127 ALA PRO GLY LYS GLU ARG GLU THR VAL ALA THR ILE ASN SEQRES 5 E 127 TRP ASN GLY GLU ARG THR GLN TYR ALA ASP ALA VAL LYS SEQRES 6 E 127 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASP THR SEQRES 7 E 127 VAL TYR LEU GLU MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 E 127 ALA VAL TYR TYR CYS ALA SER MET MET GLY THR TYR TYR SEQRES 9 E 127 SER GLY SER PRO LYS ASN TRP GLY GLN GLY THR GLN VAL SEQRES 10 E 127 THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 F 127 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 127 ALA GLY GLY SER LEU ARG LEU SER CYS THR TYR SER GLY SEQRES 3 F 127 GLN THR PHE SER ALA TRP ALA MET GLY TRP PHE ARG GLN SEQRES 4 F 127 ALA PRO GLY LYS GLU ARG GLU THR VAL ALA THR ILE ASN SEQRES 5 F 127 TRP ASN GLY GLU ARG THR GLN TYR ALA ASP ALA VAL LYS SEQRES 6 F 127 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASP THR SEQRES 7 F 127 VAL TYR LEU GLU MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 F 127 ALA VAL TYR TYR CYS ALA SER MET MET GLY THR TYR TYR SEQRES 9 F 127 SER GLY SER PRO LYS ASN TRP GLY GLN GLY THR GLN VAL SEQRES 10 F 127 THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 C 397 MET LYS ASN VAL LYS LEU LEU LEU MET LEU GLY THR ALA SEQRES 2 C 397 ALA LEU LEU ALA ALA CYS SER ASN GLU ALA ASP SER LEU SEQRES 3 C 397 THR THR SER ILE ASP ALA PRO VAL THR ALA SER ILE ASP SEQRES 4 C 397 LEU GLN SER VAL SER TYR THR ASP LEU ALA THR GLN LEU SEQRES 5 C 397 ASN ASP VAL SER ASP PHE GLY LYS MET ILE ILE LEU LYS SEQRES 6 C 397 ASP ASN GLY PHE ASN ARG GLN VAL HIS VAL SER MET ASP SEQRES 7 C 397 LYS ARG THR LYS ILE GLN LEU ASP ASN GLU ASN VAL ARG SEQRES 8 C 397 LEU PHE ASN GLY ARG ASP LYS ASP SER THR SER PHE ILE SEQRES 9 C 397 LEU GLY ASP GLU PHE ALA VAL LEU ARG PHE TYR ARG ASN SEQRES 10 C 397 GLY GLU SER ILE SER TYR ILE ALA TYR LYS GLU ALA GLN SEQRES 11 C 397 MET MET ASN GLU ILE ALA GLU PHE TYR ALA ALA PRO PHE SEQRES 12 C 397 LYS LYS THR ARG ALA ILE ASN GLU LYS GLU ALA PHE GLU SEQRES 13 C 397 CYS ILE TYR ASP SER ARG THR ARG SER ALA GLY LYS ASP SEQRES 14 C 397 ILE VAL SER VAL LYS ILE ASN ILE ASP LYS ALA LYS LYS SEQRES 15 C 397 ILE LEU ASN LEU PRO GLU CYS ASP TYR ILE ASN ASP TYR SEQRES 16 C 397 ILE LYS THR PRO GLN VAL PRO HIS GLY ILE THR GLU SER SEQRES 17 C 397 GLN THR ARG ALA VAL PRO SER GLU PRO LYS THR VAL TYR SEQRES 18 C 397 VAL ILE CYS LEU ARG GLU ASN GLY SER THR ILE TYR PRO SEQRES 19 C 397 ASN GLU VAL SER ALA GLN MET GLN ASP ALA ALA ASN SER SEQRES 20 C 397 VAL TYR ALA VAL HIS GLY LEU LYS ARG TYR VAL ASN PHE SEQRES 21 C 397 HIS PHE VAL LEU TYR THR THR GLU TYR SER CYS PRO SER SEQRES 22 C 397 GLY ASP ALA LYS GLU GLY LEU GLU GLY PHE THR ALA SER SEQRES 23 C 397 LEU LYS SER ASN PRO LYS ALA GLU GLY TYR ASP ASP GLN SEQRES 24 C 397 ILE TYR PHE LEU ILE ARG TRP GLY THR TRP ASP ASN LYS SEQRES 25 C 397 ILE LEU GLY MET SER TRP PHE ASN SER TYR ASN VAL ASN SEQRES 26 C 397 THR ALA SER ASP PHE GLU ALA SER GLY MET SER THR THR SEQRES 27 C 397 GLN LEU MET TYR PRO GLY VAL MET ALA HIS GLU LEU GLY SEQRES 28 C 397 HIS ILE LEU GLY ALA GLU HIS THR ASP ASN SER LYS ASP SEQRES 29 C 397 LEU MET TYR ALA THR PHE THR GLY TYR LEU SER HIS LEU SEQRES 30 C 397 SER GLU LYS ASN MET ASP ILE ILE ALA LYS ASN LEU GLY SEQRES 31 C 397 TRP GLU ALA ALA ASP GLY ASP HET ZN A 401 1 HET ZN B 401 1 HET ZN C 401 1 HETNAM ZN ZINC ION FORMUL 7 ZN 3(ZN 2+) FORMUL 10 HOH *608(H2 O) HELIX 1 AA1 SER A 44 ASP A 54 1 11 HELIX 2 AA2 ARG A 96 ASP A 99 5 4 HELIX 3 AA3 GLU A 128 ALA A 141 1 14 HELIX 4 AA4 PRO A 142 LYS A 144 5 3 HELIX 5 AA5 ARG A 147 ALA A 154 1 8 HELIX 6 AA6 ILE A 177 ASN A 185 1 9 HELIX 7 AA7 TYR A 233 ALA A 250 1 18 HELIX 8 AA8 GLY A 253 ARG A 256 5 4 HELIX 9 AA9 ASP A 275 ASN A 290 1 16 HELIX 10 AB1 PRO A 291 GLU A 294 5 4 HELIX 11 AB2 TRP A 309 ILE A 313 5 5 HELIX 12 AB3 GLY A 344 LEU A 354 1 11 HELIX 13 AB4 SER A 378 LEU A 389 1 12 HELIX 14 AB5 GLU A 392 GLY A 396 5 5 HELIX 15 AB6 SER B 44 ASP B 54 1 11 HELIX 16 AB7 ARG B 96 ASP B 99 5 4 HELIX 17 AB8 GLU B 128 ALA B 141 1 14 HELIX 18 AB9 PRO B 142 LYS B 144 5 3 HELIX 19 AC1 ASN B 150 GLU B 153 5 4 HELIX 20 AC2 ILE B 177 ASN B 185 1 9 HELIX 21 AC3 TYR B 233 ALA B 250 1 18 HELIX 22 AC4 GLY B 253 ARG B 256 5 4 HELIX 23 AC5 ASP B 275 ASN B 290 1 16 HELIX 24 AC6 PRO B 291 GLU B 294 5 4 HELIX 25 AC7 GLY B 344 LEU B 354 1 11 HELIX 26 AC8 SER B 378 LEU B 389 1 12 HELIX 27 AC9 GLU B 392 GLY B 396 5 5 HELIX 28 AD1 THR D 28 TRP D 32 5 5 HELIX 29 AD2 LYS D 87 THR D 91 5 5 HELIX 30 AD3 THR E 28 TRP E 32 5 5 HELIX 31 AD4 ASP E 62 LYS E 65 5 4 HELIX 32 AD5 LYS E 87 THR E 91 5 5 HELIX 33 AD6 THR F 28 TRP F 32 5 5 HELIX 34 AD7 ASP F 62 LYS F 65 5 4 HELIX 35 AD8 LYS F 87 THR F 91 5 5 HELIX 36 AD9 SER C 44 ASP C 54 1 11 HELIX 37 AE1 ARG C 96 ASP C 99 5 4 HELIX 38 AE2 GLU C 128 ALA C 141 1 14 HELIX 39 AE3 PRO C 142 LYS C 144 5 3 HELIX 40 AE4 ASN C 150 ALA C 154 1 5 HELIX 41 AE5 ILE C 177 ASN C 185 1 9 HELIX 42 AE6 TYR C 233 ALA C 250 1 18 HELIX 43 AE7 GLY C 253 ARG C 256 5 4 HELIX 44 AE8 ASP C 275 SER C 289 1 15 HELIX 45 AE9 ASN C 290 GLU C 294 5 5 HELIX 46 AF1 GLY C 344 LEU C 354 1 11 HELIX 47 AF2 SER C 378 LEU C 389 1 12 HELIX 48 AF3 GLU C 392 GLY C 396 5 5 SHEET 1 AA1 9 ALA A 36 ASP A 39 0 SHEET 2 AA1 9 LYS A 60 LYS A 65 1 O ILE A 63 N ILE A 38 SHEET 3 AA1 9 ASN A 70 MET A 77 -1 O ARG A 71 N LEU A 64 SHEET 4 AA1 9 ARG A 91 ASN A 94 -1 O ASN A 94 N SER A 76 SHEET 5 AA1 9 THR A 101 LEU A 105 -1 O LEU A 105 N ARG A 91 SHEET 6 AA1 9 PHE A 109 ARG A 116 -1 O ARG A 113 N SER A 102 SHEET 7 AA1 9 GLU A 119 TYR A 126 -1 O TYR A 123 N LEU A 112 SHEET 8 AA1 9 ILE A 170 ASN A 176 -1 O ILE A 175 N SER A 122 SHEET 9 AA1 9 PHE A 155 TYR A 159 -1 N ILE A 158 O SER A 172 SHEET 1 AA2 8 GLU A 88 ASN A 89 0 SHEET 2 AA2 8 LYS A 82 LEU A 85 -1 N LEU A 85 O GLU A 88 SHEET 3 AA2 8 VAL A 258 THR A 266 1 O PHE A 262 N LYS A 82 SHEET 4 AA2 8 LYS A 218 ARG A 226 1 N CYS A 224 O VAL A 263 SHEET 5 AA2 8 ILE A 300 ARG A 305 1 O ILE A 300 N ILE A 223 SHEET 6 AA2 8 SER A 333 THR A 337 1 O GLY A 334 N LEU A 303 SHEET 7 AA2 8 GLY A 315 PHE A 319 -1 N MET A 316 O MET A 335 SHEET 8 AA2 8 TYR A 195 LYS A 197 1 N ILE A 196 O PHE A 319 SHEET 1 AA3 9 ALA B 36 ASP B 39 0 SHEET 2 AA3 9 LYS B 60 ASP B 66 1 O ILE B 63 N ILE B 38 SHEET 3 AA3 9 PHE B 69 MET B 77 -1 O VAL B 73 N ILE B 62 SHEET 4 AA3 9 GLU B 88 ASN B 94 -1 O ASN B 94 N SER B 76 SHEET 5 AA3 9 THR B 101 GLY B 106 -1 O LEU B 105 N ARG B 91 SHEET 6 AA3 9 PHE B 109 ARG B 116 -1 O PHE B 109 N GLY B 106 SHEET 7 AA3 9 GLU B 119 TYR B 126 -1 O ILE B 121 N PHE B 114 SHEET 8 AA3 9 ILE B 170 ASN B 176 -1 O ILE B 175 N SER B 122 SHEET 9 AA3 9 PHE B 155 TYR B 159 -1 N ILE B 158 O SER B 172 SHEET 1 AA411 ALA B 36 ASP B 39 0 SHEET 2 AA411 LYS B 60 ASP B 66 1 O ILE B 63 N ILE B 38 SHEET 3 AA411 PHE B 69 MET B 77 -1 O VAL B 73 N ILE B 62 SHEET 4 AA411 GLU B 88 ASN B 94 -1 O ASN B 94 N SER B 76 SHEET 5 AA411 LYS B 82 LEU B 85 -1 N LEU B 85 O GLU B 88 SHEET 6 AA411 VAL B 258 THR B 266 1 O PHE B 262 N LYS B 82 SHEET 7 AA411 LYS B 218 ARG B 226 1 N ARG B 226 O TYR B 265 SHEET 8 AA411 ILE B 300 ARG B 305 1 O PHE B 302 N LEU B 225 SHEET 9 AA411 SER B 333 THR B 337 1 O SER B 336 N LEU B 303 SHEET 10 AA411 GLY B 315 TRP B 318 -1 N MET B 316 O MET B 335 SHEET 11 AA411 TYR B 195 ILE B 196 1 N ILE B 196 O SER B 317 SHEET 1 AA5 4 LEU D 4 SER D 7 0 SHEET 2 AA5 4 LEU D 18 TYR D 24 -1 O SER D 21 N SER D 7 SHEET 3 AA5 4 THR D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 4 AA5 4 PHE D 68 ASP D 73 -1 N SER D 71 O TYR D 80 SHEET 1 AA6 6 LEU D 11 GLN D 13 0 SHEET 2 AA6 6 THR D 115 SER D 120 1 O THR D 118 N VAL D 12 SHEET 3 AA6 6 ALA D 92 MET D 100 -1 N TYR D 94 O THR D 115 SHEET 4 AA6 6 ALA D 33 GLN D 39 -1 N PHE D 37 O TYR D 95 SHEET 5 AA6 6 GLU D 46 ILE D 51 -1 O ALA D 49 N TRP D 36 SHEET 6 AA6 6 THR D 58 TYR D 60 -1 O GLN D 59 N THR D 50 SHEET 1 AA7 4 LEU D 11 GLN D 13 0 SHEET 2 AA7 4 THR D 115 SER D 120 1 O THR D 118 N VAL D 12 SHEET 3 AA7 4 ALA D 92 MET D 100 -1 N TYR D 94 O THR D 115 SHEET 4 AA7 4 SER D 107 TRP D 111 -1 O LYS D 109 N SER D 98 SHEET 1 AA8 4 GLN E 3 SER E 7 0 SHEET 2 AA8 4 LEU E 18 SER E 25 -1 O SER E 25 N GLN E 3 SHEET 3 AA8 4 THR E 78 MET E 83 -1 O MET E 83 N LEU E 18 SHEET 4 AA8 4 PHE E 68 ASP E 73 -1 N THR E 69 O GLU E 82 SHEET 1 AA9 6 GLY E 10 GLN E 13 0 SHEET 2 AA9 6 THR E 115 SER E 120 1 O THR E 118 N GLY E 10 SHEET 3 AA9 6 ALA E 92 MET E 100 -1 N TYR E 94 O THR E 115 SHEET 4 AA9 6 ALA E 33 GLN E 39 -1 N PHE E 37 O TYR E 95 SHEET 5 AA9 6 GLU E 46 ILE E 51 -1 O ALA E 49 N TRP E 36 SHEET 6 AA9 6 THR E 58 TYR E 60 -1 O GLN E 59 N THR E 50 SHEET 1 AB1 4 GLY E 10 GLN E 13 0 SHEET 2 AB1 4 THR E 115 SER E 120 1 O THR E 118 N GLY E 10 SHEET 3 AB1 4 ALA E 92 MET E 100 -1 N TYR E 94 O THR E 115 SHEET 4 AB1 4 SER E 107 TRP E 111 -1 O LYS E 109 N SER E 98 SHEET 1 AB2 4 GLN F 3 SER F 7 0 SHEET 2 AB2 4 LEU F 18 SER F 25 -1 O SER F 25 N GLN F 3 SHEET 3 AB2 4 THR F 78 MET F 83 -1 O MET F 83 N LEU F 18 SHEET 4 AB2 4 PHE F 68 ASP F 73 -1 N SER F 71 O TYR F 80 SHEET 1 AB3 6 GLY F 10 GLN F 13 0 SHEET 2 AB3 6 THR F 115 SER F 120 1 O THR F 118 N VAL F 12 SHEET 3 AB3 6 ALA F 92 MET F 100 -1 N TYR F 94 O THR F 115 SHEET 4 AB3 6 ALA F 33 GLN F 39 -1 N PHE F 37 O TYR F 95 SHEET 5 AB3 6 GLU F 46 ILE F 51 -1 O VAL F 48 N TRP F 36 SHEET 6 AB3 6 THR F 58 TYR F 60 -1 O GLN F 59 N THR F 50 SHEET 1 AB4 4 GLY F 10 GLN F 13 0 SHEET 2 AB4 4 THR F 115 SER F 120 1 O THR F 118 N VAL F 12 SHEET 3 AB4 4 ALA F 92 MET F 100 -1 N TYR F 94 O THR F 115 SHEET 4 AB4 4 SER F 107 TRP F 111 -1 O LYS F 109 N SER F 98 SHEET 1 AB5 9 ALA C 36 ASP C 39 0 SHEET 2 AB5 9 LYS C 60 LYS C 65 1 O LYS C 65 N ILE C 38 SHEET 3 AB5 9 ASN C 70 MET C 77 -1 O ARG C 71 N LEU C 64 SHEET 4 AB5 9 GLU C 88 ASN C 94 -1 O ASN C 94 N SER C 76 SHEET 5 AB5 9 THR C 101 LEU C 105 -1 O PHE C 103 N PHE C 93 SHEET 6 AB5 9 PHE C 109 ARG C 116 -1 O ARG C 113 N SER C 102 SHEET 7 AB5 9 GLU C 119 TYR C 126 -1 O TYR C 123 N LEU C 112 SHEET 8 AB5 9 ILE C 170 ASN C 176 -1 O ILE C 175 N SER C 122 SHEET 9 AB5 9 PHE C 155 TYR C 159 -1 N ILE C 158 O SER C 172 SHEET 1 AB611 ALA C 36 ASP C 39 0 SHEET 2 AB611 LYS C 60 LYS C 65 1 O LYS C 65 N ILE C 38 SHEET 3 AB611 ASN C 70 MET C 77 -1 O ARG C 71 N LEU C 64 SHEET 4 AB611 GLU C 88 ASN C 94 -1 O ASN C 94 N SER C 76 SHEET 5 AB611 LYS C 82 LEU C 85 -1 N ILE C 83 O VAL C 90 SHEET 6 AB611 VAL C 258 THR C 266 1 O PHE C 262 N LYS C 82 SHEET 7 AB611 LYS C 218 ARG C 226 1 N CYS C 224 O VAL C 263 SHEET 8 AB611 ILE C 300 ARG C 305 1 O PHE C 302 N LEU C 225 SHEET 9 AB611 SER C 333 THR C 337 1 O SER C 336 N LEU C 303 SHEET 10 AB611 GLY C 315 TRP C 318 -1 N MET C 316 O MET C 335 SHEET 11 AB611 TYR C 195 ILE C 196 1 N ILE C 196 O SER C 317 SSBOND 1 CYS D 22 CYS D 96 1555 1555 2.01 SSBOND 2 CYS E 22 CYS E 96 1555 1555 2.04 SSBOND 3 CYS F 22 CYS F 96 1555 1555 2.03 LINK OD1 ASP A 194 ZN ZN A 401 1555 1555 2.24 LINK OD2 ASP A 194 ZN ZN A 401 1555 1555 2.24 LINK NE2 HIS A 348 ZN ZN A 401 1555 1555 2.31 LINK NE2 HIS A 352 ZN ZN A 401 1555 1555 2.37 LINK NE2 HIS A 358 ZN ZN A 401 1555 1555 2.31 LINK OD1 ASP B 194 ZN ZN B 401 1555 1555 2.13 LINK OD2 ASP B 194 ZN ZN B 401 1555 1555 2.47 LINK NE2 HIS B 348 ZN ZN B 401 1555 1555 2.30 LINK NE2 HIS B 352 ZN ZN B 401 1555 1555 2.26 LINK NE2 HIS B 358 ZN ZN B 401 1555 1555 2.26 LINK OD1 ASP C 194 ZN ZN C 401 1555 1555 2.10 LINK OD2 ASP C 194 ZN ZN C 401 1555 1555 2.36 LINK NE2 HIS C 348 ZN ZN C 401 1555 1555 2.28 LINK NE2 HIS C 352 ZN ZN C 401 1555 1555 2.23 LINK NE2 HIS C 358 ZN ZN C 401 1555 1555 2.24 CISPEP 1 THR A 198 PRO A 199 0 -1.69 CRYST1 156.901 82.984 139.807 90.00 109.02 90.00 C 1 2 1 12 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.006373 0.000000 0.002196 0.00000 SCALE2 0.000000 0.012051 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007566 0.00000