HEADER IMMUNE SYSTEM 10-JAN-25 9MSP TITLE CRYSTAL STRUCTURE OF MPXV A35R IN COMPLEX WITH NEUTRALIZING ANTIBODY TITLE 2 EV35-7 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN OPG161; COMPND 3 CHAIN: E, F, A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: EV35-7 HEAVY CHAIN; COMPND 7 CHAIN: H, C; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: EV35-7 LIGHT CHAIN; COMPND 11 CHAIN: L, D; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MONKEYPOX VIRUS; SOURCE 3 ORGANISM_TAXID: 10244; SOURCE 4 GENE: OPG161, MPXVGP145; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_TAXID: 9606; SOURCE 10 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS ANTIBODY, MPOX, MONKEYPOX, A35, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR M.YUAN,I.A.WILSON REVDAT 1 10-SEP-25 9MSP 0 JRNL AUTH R.F.FANTIN,M.YUAN,S.C.PARK,B.BOZARTH,H.COHN,M.IGNACIO, JRNL AUTH 2 P.EARL,A.CIVLJAK,G.LAGHLALI,D.ZHANG,X.ZHU,J.CRANDELL, JRNL AUTH 3 V.MONTEIRO,J.J.CLARK,C.COTTER,M.BURKHARDT,G.SINGH,P.WARANG, JRNL AUTH 4 J.GARCIA-BERNALT DIEGO,K.SRIVASTAVA,L.A.LUGO,L.PISCHEL, JRNL AUTH 5 I.YILDIRIM,S.B.OMER,D.DA SILVA,F.KRAMMER,G.BAJIC,V.SIMON, JRNL AUTH 6 M.SCHOTSAERT,C.LUCAS,I.A.WILSON,B.MOSS,C.H.COELHO JRNL TITL HUMAN MONOCLONAL ANTIBODIES TARGETING A35 PROTECT FROM DEATH JRNL TITL 2 CAUSED BY MPOX. JRNL REF CELL 2025 JRNL REFN ISSN 1097-4172 JRNL PMID 40865529 JRNL DOI 10.1016/J.CELL.2025.08.004 REMARK 2 REMARK 2 RESOLUTION. 2.19 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21.2_5419: ???) 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) : 2.19 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.74 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 3 NUMBER OF REFLECTIONS : 73826 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.213 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.250 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960 REMARK 3 FREE R VALUE TEST SET COUNT : 3661 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 44.7400 - 6.4800 0.99 3017 142 0.1943 0.2312 REMARK 3 2 6.4800 - 5.1500 1.00 2908 135 0.1864 0.2245 REMARK 3 3 5.1500 - 4.5000 0.93 2699 117 0.1519 0.1640 REMARK 3 4 4.5000 - 4.0900 0.99 2841 137 0.1600 0.1583 REMARK 3 5 4.0900 - 3.7900 1.00 2852 147 0.1784 0.2310 REMARK 3 6 3.7900 - 3.5700 0.99 2767 179 0.1917 0.2178 REMARK 3 7 3.5700 - 3.3900 0.99 2802 150 0.1997 0.2201 REMARK 3 8 3.3900 - 3.2400 0.99 2799 169 0.2072 0.2111 REMARK 3 9 3.2400 - 3.1200 0.99 2802 154 0.2156 0.2910 REMARK 3 10 3.1200 - 3.0100 1.00 2835 145 0.2245 0.2372 REMARK 3 11 3.0100 - 2.9200 1.00 2795 153 0.2399 0.3078 REMARK 3 12 2.9200 - 2.8300 1.00 2806 148 0.2497 0.2995 REMARK 3 13 2.8300 - 2.7600 1.00 2763 157 0.2472 0.2809 REMARK 3 14 2.7600 - 2.6900 1.00 2816 148 0.2421 0.2986 REMARK 3 15 2.6900 - 2.6300 1.00 2808 144 0.2456 0.3167 REMARK 3 16 2.6300 - 2.5700 1.00 2772 143 0.2513 0.3293 REMARK 3 17 2.5700 - 2.5200 0.98 2813 119 0.2489 0.2624 REMARK 3 18 2.5200 - 2.4800 0.94 2632 131 0.2494 0.3003 REMARK 3 19 2.4800 - 2.4300 0.95 2661 146 0.2572 0.3039 REMARK 3 20 2.4300 - 2.3900 0.94 2601 144 0.2725 0.3742 REMARK 3 21 2.3900 - 2.3500 0.94 2621 138 0.2636 0.3533 REMARK 3 22 2.3500 - 2.3200 0.93 2613 134 0.2605 0.3067 REMARK 3 23 2.3200 - 2.2800 0.91 2533 130 0.2671 0.3317 REMARK 3 24 2.2800 - 2.2500 0.89 2485 125 0.2667 0.3195 REMARK 3 25 2.2500 - 2.2200 0.85 2378 131 0.2681 0.3266 REMARK 3 26 2.2200 - 2.1900 0.63 1746 95 0.2631 0.3239 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) : 0.290 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.430 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 : 0.003 NULL REMARK 3 ANGLE : 0.626 NULL REMARK 3 CHIRALITY : 0.045 1386 REMARK 3 PLANARITY : 0.004 1579 REMARK 3 DIHEDRAL : 16.382 3257 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 9MSP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291741. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-DEC-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL12-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 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 : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75918 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 200 DATA REDUNDANCY : 10.00 REMARK 200 R MERGE (I) : 0.11800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9 REMARK 200 DATA REDUNDANCY IN SHELL : 7.90 REMARK 200 R MERGE FOR SHELL (I) : 1.66300 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.90 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 4000, 0.2 M AMMONIUM SULFATE, REMARK 280 AND 0.1 M ACETATE PH 4.6, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 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 134.21150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 134.21150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 51.66950 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.94300 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 51.66950 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.94300 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 134.21150 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 51.66950 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.94300 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 134.21150 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 51.66950 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.94300 REMARK 290 SMTRY3 8 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, H, L 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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 90 REMARK 465 THR E 91 REMARK 465 THR E 92 REMARK 465 GLN E 93 REMARK 465 TYR E 94 REMARK 465 ASP E 95 REMARK 465 HIS E 96 REMARK 465 LYS E 97 REMARK 465 GLU E 98 REMARK 465 ASP E 165 REMARK 465 TYR E 166 REMARK 465 GLN E 167 REMARK 465 ASP E 168 REMARK 465 SER E 169 REMARK 465 ASP E 170 REMARK 465 VAL E 171 REMARK 465 HIS E 184 REMARK 465 HIS E 185 REMARK 465 HIS E 186 REMARK 465 HIS E 187 REMARK 465 HIS E 188 REMARK 465 HIS E 189 REMARK 465 SER F 90 REMARK 465 THR F 91 REMARK 465 THR F 92 REMARK 465 GLN F 93 REMARK 465 TYR F 94 REMARK 465 ASP F 95 REMARK 465 HIS F 96 REMARK 465 LYS F 97 REMARK 465 GLU F 98 REMARK 465 SER F 164 REMARK 465 ASP F 165 REMARK 465 TYR F 166 REMARK 465 GLN F 167 REMARK 465 ASP F 168 REMARK 465 SER F 183 REMARK 465 HIS F 184 REMARK 465 HIS F 185 REMARK 465 HIS F 186 REMARK 465 HIS F 187 REMARK 465 HIS F 188 REMARK 465 HIS F 189 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP L 1 REMARK 465 SER L 52 REMARK 465 SER L 53 REMARK 465 LEU L 54 REMARK 465 GLU L 55 REMARK 465 SER L 56 REMARK 465 GLY L 57 REMARK 465 VAL L 58 REMARK 465 GLY L 210 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER A 90 REMARK 465 THR A 91 REMARK 465 THR A 92 REMARK 465 GLN A 93 REMARK 465 TYR A 94 REMARK 465 ASP A 95 REMARK 465 HIS A 96 REMARK 465 LYS A 97 REMARK 465 GLU A 98 REMARK 465 SER A 164 REMARK 465 ASP A 165 REMARK 465 TYR A 166 REMARK 465 GLN A 167 REMARK 465 ASP A 168 REMARK 465 SER A 169 REMARK 465 ASP A 170 REMARK 465 VAL A 171 REMARK 465 HIS A 184 REMARK 465 HIS A 185 REMARK 465 HIS A 186 REMARK 465 HIS A 187 REMARK 465 HIS A 188 REMARK 465 HIS A 189 REMARK 465 SER B 90 REMARK 465 THR B 91 REMARK 465 THR B 92 REMARK 465 GLN B 93 REMARK 465 TYR B 94 REMARK 465 ASP B 95 REMARK 465 HIS B 96 REMARK 465 LYS B 97 REMARK 465 GLU B 98 REMARK 465 GLY B 182 REMARK 465 SER B 183 REMARK 465 HIS B 184 REMARK 465 HIS B 185 REMARK 465 HIS B 186 REMARK 465 HIS B 187 REMARK 465 HIS B 188 REMARK 465 HIS B 189 REMARK 465 SER C 215 REMARK 465 CYS C 216 REMARK 465 LYS D 50 REMARK 465 ALA D 51 REMARK 465 SER D 52 REMARK 465 SER D 53 REMARK 465 LEU D 54 REMARK 465 GLU D 55 REMARK 465 SER D 56 REMARK 465 GLY D 57 REMARK 465 VAL D 58 REMARK 465 CYS D 212 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 GLN F 106 -102.58 56.41 REMARK 500 ASP H 144 63.05 62.40 REMARK 500 SER L 30 -63.67 63.61 REMARK 500 ALA L 84 -169.46 -166.72 REMARK 500 ASN L 92 118.94 -160.09 REMARK 500 GLN B 106 -92.75 57.34 REMARK 500 THR B 162 132.68 -34.86 REMARK 500 ASP B 165 31.75 -84.67 REMARK 500 TYR B 166 -149.44 45.17 REMARK 500 SER C 128 -9.44 72.49 REMARK 500 ASP C 144 65.80 62.17 REMARK 500 SER D 60 151.33 67.55 REMARK 500 ALA D 84 -169.55 -167.20 REMARK 500 ASN D 92 118.94 -161.10 REMARK 500 LYS D 169 -61.90 -90.53 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG L 61 0.26 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF1 9MSP E 90 181 UNP PG161_MONPV DBREF2 9MSP E A0A7H0DND2 90 181 DBREF1 9MSP F 90 181 UNP PG161_MONPV DBREF2 9MSP F A0A7H0DND2 90 181 DBREF 9MSP H 1 216 PDB 9MSP 9MSP 1 216 DBREF 9MSP L 1 212 PDB 9MSP 9MSP 1 212 DBREF1 9MSP A 90 181 UNP PG161_MONPV DBREF2 9MSP A A0A7H0DND2 90 181 DBREF1 9MSP B 90 181 UNP PG161_MONPV DBREF2 9MSP B A0A7H0DND2 90 181 DBREF 9MSP C 1 216 PDB 9MSP 9MSP 1 216 DBREF 9MSP D 1 212 PDB 9MSP 9MSP 1 212 SEQADV 9MSP GLY E 182 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP SER E 183 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS E 184 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS E 185 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS E 186 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS E 187 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS E 188 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS E 189 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP GLY F 182 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP SER F 183 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS F 184 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS F 185 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS F 186 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS F 187 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS F 188 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS F 189 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP GLY A 182 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP SER A 183 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS A 184 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS A 185 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS A 186 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS A 187 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS A 188 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS A 189 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP GLY B 182 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP SER B 183 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS B 184 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS B 185 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS B 186 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS B 187 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS B 188 UNP A0A7H0DND EXPRESSION TAG SEQADV 9MSP HIS B 189 UNP A0A7H0DND EXPRESSION TAG SEQRES 1 E 100 SER THR THR GLN TYR ASP HIS LYS GLU SER CYS ASN GLY SEQRES 2 E 100 LEU TYR TYR GLN GLY SER CYS TYR ILE LEU HIS SER ASP SEQRES 3 E 100 TYR LYS SER PHE GLU ASP ALA LYS ALA ASN CYS ALA ALA SEQRES 4 E 100 GLU SER SER THR LEU PRO ASN LYS SER ASP VAL LEU THR SEQRES 5 E 100 THR TRP LEU ILE ASP TYR VAL GLU ASP THR TRP GLY SER SEQRES 6 E 100 ASP GLY ASN PRO ILE THR LYS THR THR SER ASP TYR GLN SEQRES 7 E 100 ASP SER ASP VAL SER GLN GLU VAL ARG LYS TYR PHE CYS SEQRES 8 E 100 THR GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 F 100 SER THR THR GLN TYR ASP HIS LYS GLU SER CYS ASN GLY SEQRES 2 F 100 LEU TYR TYR GLN GLY SER CYS TYR ILE LEU HIS SER ASP SEQRES 3 F 100 TYR LYS SER PHE GLU ASP ALA LYS ALA ASN CYS ALA ALA SEQRES 4 F 100 GLU SER SER THR LEU PRO ASN LYS SER ASP VAL LEU THR SEQRES 5 F 100 THR TRP LEU ILE ASP TYR VAL GLU ASP THR TRP GLY SER SEQRES 6 F 100 ASP GLY ASN PRO ILE THR LYS THR THR SER ASP TYR GLN SEQRES 7 F 100 ASP SER ASP VAL SER GLN GLU VAL ARG LYS TYR PHE CYS SEQRES 8 F 100 THR GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 H 225 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 H 225 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 225 PHE THR PHE SER ARG HIS GLY MET HIS TRP VAL ARG GLN SEQRES 4 H 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL THR VAL ILE SER SEQRES 5 H 225 TYR ASP GLY ILE LYS LYS TYR TYR THR ASP SER VAL LYS SEQRES 6 H 225 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 225 LEU TYR LEU GLN MET ASN SER LEU ARG PRO ASP ASP THR SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG GLN ASP CYS GLY GLY ASP SEQRES 9 H 225 CYS PHE SER ARG PHE ASP SER TRP GLY GLN GLY THR LEU SEQRES 10 H 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 H 225 PRO LYS SER CYS SEQRES 1 L 212 ASP ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 L 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 212 GLN SER ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 212 PRO GLY LYS ALA PRO LYS LEU LEU MET TYR LYS ALA SER SEQRES 5 L 212 SER LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 212 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 212 GLN PRO ASP ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 L 212 ASN SER TYR SER LEU THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 L 212 ASP LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 212 VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE ASN SEQRES 17 L 212 ARG GLY GLU CYS SEQRES 1 A 100 SER THR THR GLN TYR ASP HIS LYS GLU SER CYS ASN GLY SEQRES 2 A 100 LEU TYR TYR GLN GLY SER CYS TYR ILE LEU HIS SER ASP SEQRES 3 A 100 TYR LYS SER PHE GLU ASP ALA LYS ALA ASN CYS ALA ALA SEQRES 4 A 100 GLU SER SER THR LEU PRO ASN LYS SER ASP VAL LEU THR SEQRES 5 A 100 THR TRP LEU ILE ASP TYR VAL GLU ASP THR TRP GLY SER SEQRES 6 A 100 ASP GLY ASN PRO ILE THR LYS THR THR SER ASP TYR GLN SEQRES 7 A 100 ASP SER ASP VAL SER GLN GLU VAL ARG LYS TYR PHE CYS SEQRES 8 A 100 THR GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 B 100 SER THR THR GLN TYR ASP HIS LYS GLU SER CYS ASN GLY SEQRES 2 B 100 LEU TYR TYR GLN GLY SER CYS TYR ILE LEU HIS SER ASP SEQRES 3 B 100 TYR LYS SER PHE GLU ASP ALA LYS ALA ASN CYS ALA ALA SEQRES 4 B 100 GLU SER SER THR LEU PRO ASN LYS SER ASP VAL LEU THR SEQRES 5 B 100 THR TRP LEU ILE ASP TYR VAL GLU ASP THR TRP GLY SER SEQRES 6 B 100 ASP GLY ASN PRO ILE THR LYS THR THR SER ASP TYR GLN SEQRES 7 B 100 ASP SER ASP VAL SER GLN GLU VAL ARG LYS TYR PHE CYS SEQRES 8 B 100 THR GLY SER HIS HIS HIS HIS HIS HIS SEQRES 1 C 225 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY VAL VAL GLN SEQRES 2 C 225 PRO GLY ARG SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 225 PHE THR PHE SER ARG HIS GLY MET HIS TRP VAL ARG GLN SEQRES 4 C 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL THR VAL ILE SER SEQRES 5 C 225 TYR ASP GLY ILE LYS LYS TYR TYR THR ASP SER VAL LYS SEQRES 6 C 225 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 C 225 LEU TYR LEU GLN MET ASN SER LEU ARG PRO ASP ASP THR SEQRES 8 C 225 ALA VAL TYR TYR CYS ALA ARG GLN ASP CYS GLY GLY ASP SEQRES 9 C 225 CYS PHE SER ARG PHE ASP SER TRP GLY GLN GLY THR LEU SEQRES 10 C 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 C 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 C 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 C 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 C 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 C 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 C 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 C 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 C 225 PRO LYS SER CYS SEQRES 1 D 212 ASP ILE GLN MET THR GLN SER PRO SER THR LEU SER ALA SEQRES 2 D 212 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 D 212 GLN SER ILE SER SER TRP LEU ALA TRP TYR GLN GLN LYS SEQRES 4 D 212 PRO GLY LYS ALA PRO LYS LEU LEU MET TYR LYS ALA SER SEQRES 5 D 212 SER LEU GLU SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 D 212 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 D 212 GLN PRO ASP ASP PHE ALA THR TYR TYR CYS GLN GLN TYR SEQRES 8 D 212 ASN SER TYR SER LEU THR PHE GLY PRO GLY THR LYS VAL SEQRES 9 D 212 ASP LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 D 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 D 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 D 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 D 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 D 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 D 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 D 212 VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE ASN SEQRES 17 D 212 ARG GLY GLU CYS HET ACT E 201 4 HET EDO F 201 4 HET SO4 L 301 5 HET EDO A 201 4 HET SO4 C 301 5 HET SO4 D 301 5 HETNAM ACT ACETATE ION HETNAM EDO 1,2-ETHANEDIOL HETNAM SO4 SULFATE ION HETSYN EDO ETHYLENE GLYCOL FORMUL 9 ACT C2 H3 O2 1- FORMUL 10 EDO 2(C2 H6 O2) FORMUL 11 SO4 3(O4 S 2-) FORMUL 15 HOH *457(H2 O) HELIX 1 AA1 SER E 118 ALA E 128 1 11 HELIX 2 AA2 ASN E 135 VAL E 139 5 5 HELIX 3 AA3 LEU E 144 GLU E 149 1 6 HELIX 4 AA4 SER F 118 ALA F 128 1 11 HELIX 5 AA5 ASN F 135 VAL F 139 5 5 HELIX 6 AA6 LEU F 144 GLU F 149 1 6 HELIX 7 AA7 THR H 28 HIS H 32 5 5 HELIX 8 AA8 ASP H 61 LYS H 64 5 4 HELIX 9 AA9 ARG H 83 THR H 87 5 5 HELIX 10 AB1 SER H 156 ALA H 158 5 3 HELIX 11 AB2 SER H 187 GLY H 190 5 4 HELIX 12 AB3 LYS H 201 ASN H 204 5 4 HELIX 13 AB4 GLN L 79 PHE L 83 5 5 HELIX 14 AB5 SER L 121 LYS L 126 1 6 HELIX 15 AB6 LYS L 183 LYS L 188 1 6 HELIX 16 AB7 SER A 118 ALA A 128 1 11 HELIX 17 AB8 ASN A 135 VAL A 139 5 5 HELIX 18 AB9 LEU A 144 GLU A 149 1 6 HELIX 19 AC1 PHE B 119 ALA B 128 1 10 HELIX 20 AC2 ASN B 135 VAL B 139 5 5 HELIX 21 AC3 LEU B 144 GLU B 149 1 6 HELIX 22 AC4 THR C 28 HIS C 32 5 5 HELIX 23 AC5 ASP C 61 LYS C 64 5 4 HELIX 24 AC6 ARG C 83 THR C 87 5 5 HELIX 25 AC7 SER C 156 ALA C 158 5 3 HELIX 26 AC8 SER C 187 GLN C 192 1 6 HELIX 27 AC9 LYS C 201 ASN C 204 5 4 HELIX 28 AD1 GLN D 79 PHE D 83 5 5 HELIX 29 AD2 SER D 121 LYS D 126 1 6 HELIX 30 AD3 LYS D 183 LYS D 188 1 6 SHEET 1 AA1 3 LEU E 103 TYR E 105 0 SHEET 2 AA1 3 SER E 108 LYS E 117 -1 O TYR E 110 N LEU E 103 SHEET 3 AA1 3 ARG E 176 THR E 181 -1 O TYR E 178 N HIS E 113 SHEET 1 AA2 3 LEU F 103 TYR F 105 0 SHEET 2 AA2 3 SER F 108 LYS F 117 -1 O SER F 108 N TYR F 105 SHEET 3 AA2 3 ARG F 176 THR F 181 -1 O ARG F 176 N LYS F 117 SHEET 1 AA3 4 GLN H 3 SER H 7 0 SHEET 2 AA3 4 LEU H 18 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AA3 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA3 4 PHE H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AA4 6 GLY H 10 VAL H 12 0 SHEET 2 AA4 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA4 6 ALA H 88 GLN H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA4 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA4 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA4 6 LYS H 57 TYR H 59 -1 O TYR H 58 N VAL H 50 SHEET 1 AA5 4 GLY H 10 VAL H 12 0 SHEET 2 AA5 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA5 4 ALA H 88 GLN H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA5 4 PHE H 100E TRP H 103 -1 O SER H 102 N ARG H 94 SHEET 1 AA6 4 SER H 120 LEU H 124 0 SHEET 2 AA6 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA6 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA6 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA7 4 SER H 120 LEU H 124 0 SHEET 2 AA7 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA7 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA7 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA8 3 THR H 151 TRP H 154 0 SHEET 2 AA8 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA8 3 THR H 205 VAL H 211 -1 O VAL H 207 N VAL H 198 SHEET 1 AA9 4 MET L 4 SER L 7 0 SHEET 2 AA9 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA9 4 GLU L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AA9 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB1 5 THR L 10 ALA L 13 0 SHEET 2 AB1 5 THR L 102 LEU L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AB1 5 THR L 85 TYR L 91 -1 N TYR L 86 O THR L 102 SHEET 4 AB1 5 SER L 31 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AB1 5 LYS L 45 LEU L 46 -1 O LYS L 45 N GLN L 37 SHEET 1 AB2 4 THR L 10 ALA L 13 0 SHEET 2 AB2 4 THR L 102 LEU L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AB2 4 THR L 85 TYR L 91 -1 N TYR L 86 O THR L 102 SHEET 4 AB2 4 LEU L 96 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB3 4 SER L 114 PHE L 118 0 SHEET 2 AB3 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AB3 4 TYR L 173 SER L 182 -1 O LEU L 175 N LEU L 136 SHEET 4 AB3 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB4 4 ALA L 153 LEU L 154 0 SHEET 2 AB4 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB4 4 VAL L 191 GLN L 198 -1 O GLU L 195 N GLN L 147 SHEET 4 AB4 4 THR L 201 ASN L 208 -1 O LYS L 205 N CYS L 194 SHEET 1 AB5 3 LEU A 103 TYR A 105 0 SHEET 2 AB5 3 SER A 108 LYS A 117 -1 O TYR A 110 N LEU A 103 SHEET 3 AB5 3 ARG A 176 THR A 181 -1 O CYS A 180 N ILE A 111 SHEET 1 AB6 3 LEU B 103 TYR B 105 0 SHEET 2 AB6 3 SER B 108 SER B 118 -1 O SER B 108 N TYR B 105 SHEET 3 AB6 3 VAL B 175 CYS B 180 -1 O ARG B 176 N LYS B 117 SHEET 1 AB7 4 GLN C 3 SER C 7 0 SHEET 2 AB7 4 LEU C 18 SER C 25 -1 O ALA C 23 N VAL C 5 SHEET 3 AB7 4 THR C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AB7 4 PHE C 67 ASP C 72 -1 N SER C 70 O TYR C 79 SHEET 1 AB8 6 GLY C 10 VAL C 12 0 SHEET 2 AB8 6 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12 SHEET 3 AB8 6 ALA C 88 GLN C 95 -1 N TYR C 90 O THR C 107 SHEET 4 AB8 6 MET C 34 GLN C 39 -1 N VAL C 37 O TYR C 91 SHEET 5 AB8 6 LEU C 45 ILE C 51 -1 O GLU C 46 N ARG C 38 SHEET 6 AB8 6 LYS C 57 TYR C 59 -1 O TYR C 58 N VAL C 50 SHEET 1 AB9 4 GLY C 10 VAL C 12 0 SHEET 2 AB9 4 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12 SHEET 3 AB9 4 ALA C 88 GLN C 95 -1 N TYR C 90 O THR C 107 SHEET 4 AB9 4 PHE C 100E TRP C 103 -1 O SER C 102 N ARG C 94 SHEET 1 AC1 4 SER C 120 LEU C 124 0 SHEET 2 AC1 4 THR C 135 TYR C 145 -1 O LEU C 141 N PHE C 122 SHEET 3 AC1 4 TYR C 176 PRO C 185 -1 O VAL C 184 N ALA C 136 SHEET 4 AC1 4 VAL C 163 THR C 165 -1 N HIS C 164 O VAL C 181 SHEET 1 AC2 4 SER C 120 LEU C 124 0 SHEET 2 AC2 4 THR C 135 TYR C 145 -1 O LEU C 141 N PHE C 122 SHEET 3 AC2 4 TYR C 176 PRO C 185 -1 O VAL C 184 N ALA C 136 SHEET 4 AC2 4 VAL C 169 LEU C 170 -1 N VAL C 169 O SER C 177 SHEET 1 AC3 3 THR C 151 TRP C 154 0 SHEET 2 AC3 3 ILE C 195 HIS C 200 -1 O ASN C 197 N SER C 153 SHEET 3 AC3 3 THR C 205 LYS C 210 -1 O THR C 205 N HIS C 200 SHEET 1 AC4 4 MET D 4 SER D 7 0 SHEET 2 AC4 4 VAL D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AC4 4 GLU D 70 ILE D 75 -1 O LEU D 73 N ILE D 21 SHEET 4 AC4 4 PHE D 62 GLY D 66 -1 N SER D 63 O THR D 74 SHEET 1 AC5 5 THR D 10 ALA D 13 0 SHEET 2 AC5 5 THR D 102 LEU D 106 1 O LYS D 103 N LEU D 11 SHEET 3 AC5 5 THR D 85 TYR D 91 -1 N TYR D 86 O THR D 102 SHEET 4 AC5 5 SER D 31 GLN D 38 -1 N SER D 31 O TYR D 91 SHEET 5 AC5 5 LYS D 45 LEU D 46 -1 O LYS D 45 N GLN D 37 SHEET 1 AC6 4 THR D 10 ALA D 13 0 SHEET 2 AC6 4 THR D 102 LEU D 106 1 O LYS D 103 N LEU D 11 SHEET 3 AC6 4 THR D 85 TYR D 91 -1 N TYR D 86 O THR D 102 SHEET 4 AC6 4 LEU D 96 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AC7 4 SER D 114 PHE D 118 0 SHEET 2 AC7 4 THR D 129 PHE D 139 -1 O VAL D 133 N PHE D 118 SHEET 3 AC7 4 TYR D 173 SER D 182 -1 O LEU D 179 N VAL D 132 SHEET 4 AC7 4 SER D 159 VAL D 163 -1 N SER D 162 O SER D 176 SHEET 1 AC8 4 ALA D 153 LEU D 154 0 SHEET 2 AC8 4 LYS D 145 VAL D 150 -1 N VAL D 150 O ALA D 153 SHEET 3 AC8 4 VAL D 191 GLN D 198 -1 O GLU D 195 N GLN D 147 SHEET 4 AC8 4 THR D 201 ASN D 208 -1 O LYS D 205 N CYS D 194 SSBOND 1 CYS E 100 CYS E 109 1555 1555 2.04 SSBOND 2 CYS E 126 CYS E 180 1555 1555 2.04 SSBOND 3 CYS F 100 CYS F 109 1555 1555 2.04 SSBOND 4 CYS F 126 CYS F 180 1555 1555 2.04 SSBOND 5 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 6 CYS H 97 CYS H 100A 1555 1555 2.04 SSBOND 7 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 8 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 9 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 10 CYS A 100 CYS A 109 1555 1555 2.04 SSBOND 11 CYS A 126 CYS A 180 1555 1555 2.04 SSBOND 12 CYS B 100 CYS B 109 1555 1555 2.03 SSBOND 13 CYS B 126 CYS B 180 1555 1555 2.04 SSBOND 14 CYS C 22 CYS C 92 1555 1555 2.04 SSBOND 15 CYS C 97 CYS C 100A 1555 1555 2.03 SSBOND 16 CYS C 140 CYS C 196 1555 1555 2.04 SSBOND 17 CYS D 23 CYS D 88 1555 1555 2.04 SSBOND 18 CYS D 134 CYS D 194 1555 1555 2.04 CISPEP 1 PHE H 146 PRO H 147 0 -6.59 CISPEP 2 GLU H 148 PRO H 149 0 0.44 CISPEP 3 SER L 7 PRO L 8 0 -2.69 CISPEP 4 TYR L 140 PRO L 141 0 3.32 CISPEP 5 PHE C 146 PRO C 147 0 -6.24 CISPEP 6 GLU C 148 PRO C 149 0 1.54 CISPEP 7 SER D 7 PRO D 8 0 -2.25 CISPEP 8 TYR D 140 PRO D 141 0 3.91 CRYST1 103.339 107.886 268.423 90.00 90.00 90.00 C 2 2 21 32 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 0.009677 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009269 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003725 0.00000