HEADER VIRAL PROTEIN/IMMUNE SYSTEM 15-MAY-24 9BTV TITLE CRYO-EM STRUCTURE OF RHESUS ANTIBODY T646-A.01 IN COMPLEX WITH HIV-1 TITLE 2 ENV TRIMER Q23.17 MD39 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 3 CHAIN: A, C, E; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: Q23.MD39 TRANSMEMBRANE PROTEIN GP41; COMPND 8 CHAIN: B, F, G; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: T646-A.01 HEAVY CHAIN; COMPND 12 CHAIN: H; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: T646-A.01 LIGHT CHAIN; COMPND 16 CHAIN: L; COMPND 17 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 10 ORGANISM_TAXID: 11676; SOURCE 11 GENE: ENV; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 17 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 18 ORGANISM_TAXID: 9544; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 24 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 25 ORGANISM_TAXID: 9544; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS NEUTRALIZING ANTIBODY, HIV-1 V2 APEX, SHIV-ELICITED, VIRAL PROTEIN, KEYWDS 2 IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR R.S.ROARK,L.SHAPIRO,P.D.KWONG REVDAT 1 02-JUL-25 9BTV 0 JRNL AUTH R.S.ROARK,L.SHAPIRO,P.D.KWONG JRNL TITL HIV-1 NEUTRALIZING ANTIBODIES IN SHIV-INFECTED MACAQUES JRNL TITL 2 RECAPITULATE STRUCTURALLY DIVERGENT MODES OF HUMAN V2 APEX JRNL TITL 3 RECOGNITION WITH A SINGLE D GENE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.48 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.480 REMARK 3 NUMBER OF PARTICLES : 39411 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9BTV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000284108. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : COMPLEX OF T646-A.01 WITH HIV-1 REMARK 245 Q23.17 ENVELOPE TRIMER REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5800.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, F, G, H, L, D, I, REMARK 350 AND CHAINS: J, K, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e, f, g, h, i, j, k, l, REMARK 350 AND CHAINS: m, n, o, p, q, r, s, t, u, v, REMARK 350 AND CHAINS: w 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 VAL A 31 REMARK 465 GLU A 32 REMARK 465 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 GLU A 62 REMARK 465 THR A 63 REMARK 465 GLU A 64 REMARK 465 VAL A 145 REMARK 465 ASN A 146 REMARK 465 THR A 147 REMARK 465 THR A 148 REMARK 465 GLY A 149 REMARK 465 ASP A 150 REMARK 465 THR A 405A REMARK 465 TRP A 405B REMARK 465 ASN A 405C REMARK 465 ASP A 405D REMARK 465 THR A 405E REMARK 465 ASP A 405F REMARK 465 SER A 405G REMARK 465 THR A 405H REMARK 465 GLN A 405I REMARK 465 GLU A 405J REMARK 465 SER A 405K REMARK 465 VAL A 506 REMARK 465 GLU A 507 REMARK 465 ARG A 508 REMARK 465 ALA B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 VAL B 518 REMARK 465 SER B 519 REMARK 465 SER B 546 REMARK 465 GLY B 547 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 ASN B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 PRO B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 LEU B 568 REMARK 465 GLU B 662 REMARK 465 LEU B 663 REMARK 465 ASP B 664 REMARK 465 VAL C 31 REMARK 465 GLU C 32 REMARK 465 LYS C 59 REMARK 465 ALA C 60 REMARK 465 TYR C 61 REMARK 465 GLU C 62 REMARK 465 THR C 63 REMARK 465 GLU C 64 REMARK 465 SER C 144 REMARK 465 VAL C 145 REMARK 465 ASN C 146 REMARK 465 THR C 147 REMARK 465 THR C 148 REMARK 465 GLY C 149 REMARK 465 ASP C 150 REMARK 465 ASN C 186A REMARK 465 GLN C 186B REMARK 465 GLY C 186C REMARK 465 THR C 405A REMARK 465 TRP C 405B REMARK 465 ASN C 405C REMARK 465 ASP C 405D REMARK 465 THR C 405E REMARK 465 ASP C 405F REMARK 465 SER C 405G REMARK 465 THR C 405H REMARK 465 GLN C 405I REMARK 465 GLU C 405J REMARK 465 SER C 405K REMARK 465 VAL C 506 REMARK 465 GLU C 507 REMARK 465 ARG C 508 REMARK 465 VAL E 31 REMARK 465 GLU E 32 REMARK 465 ALA E 58 REMARK 465 LYS E 59 REMARK 465 ALA E 60 REMARK 465 TYR E 61 REMARK 465 GLU E 62 REMARK 465 THR E 63 REMARK 465 GLU E 64 REMARK 465 SER E 144 REMARK 465 VAL E 145 REMARK 465 ASN E 146 REMARK 465 THR E 147 REMARK 465 THR E 148 REMARK 465 GLY E 149 REMARK 465 ASP E 150 REMARK 465 ARG E 151 REMARK 465 THR E 405A REMARK 465 TRP E 405B REMARK 465 ASN E 405C REMARK 465 ASP E 405D REMARK 465 THR E 405E REMARK 465 ASP E 405F REMARK 465 SER E 405G REMARK 465 THR E 405H REMARK 465 GLN E 405I REMARK 465 GLU E 405J REMARK 465 SER E 405K REMARK 465 VAL E 506 REMARK 465 GLU E 507 REMARK 465 ARG E 508 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 REMARK 465 VAL F 518 REMARK 465 SER F 519 REMARK 465 SER F 546 REMARK 465 GLY F 547 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 ASN F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 PRO F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 GLU F 662 REMARK 465 LEU F 663 REMARK 465 ASP F 664 REMARK 465 ALA G 512 REMARK 465 VAL G 513 REMARK 465 GLY G 514 REMARK 465 ILE G 515 REMARK 465 GLY G 516 REMARK 465 ALA G 517 REMARK 465 VAL G 518 REMARK 465 SER G 519 REMARK 465 SER G 546 REMARK 465 GLY G 547 REMARK 465 ILE G 548 REMARK 465 VAL G 549 REMARK 465 GLN G 550 REMARK 465 GLN G 551 REMARK 465 GLN G 552 REMARK 465 ASN G 553 REMARK 465 ASN G 554 REMARK 465 LEU G 555 REMARK 465 LEU G 556 REMARK 465 ARG G 557 REMARK 465 ALA G 558 REMARK 465 PRO G 559 REMARK 465 GLU G 560 REMARK 465 PRO G 561 REMARK 465 GLN G 562 REMARK 465 GLN G 563 REMARK 465 HIS G 564 REMARK 465 LEU G 565 REMARK 465 LEU G 566 REMARK 465 LYS G 567 REMARK 465 GLU G 662 REMARK 465 LEU G 663 REMARK 465 ASP G 664 REMARK 465 ALA H 114 REMARK 465 SER H 115 REMARK 465 THR H 116 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 ARG H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLU H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 LEU H 138 REMARK 465 GLY H 139 REMARK 465 CYS H 140 REMARK 465 LEU H 141 REMARK 465 VAL H 142 REMARK 465 LYS H 143 REMARK 465 ASP H 144 REMARK 465 TYR H 145 REMARK 465 PHE H 146 REMARK 465 PRO H 147 REMARK 465 GLU H 148 REMARK 465 PRO H 149 REMARK 465 VAL H 150 REMARK 465 THR H 151 REMARK 465 VAL H 152 REMARK 465 SER H 153 REMARK 465 TRP H 154 REMARK 465 ASN H 155 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 SER H 158 REMARK 465 LEU H 159 REMARK 465 THR H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 VAL H 163 REMARK 465 HIS H 164 REMARK 465 THR H 165 REMARK 465 PHE H 166 REMARK 465 PRO H 167 REMARK 465 ALA H 168 REMARK 465 VAL H 169 REMARK 465 LEU H 170 REMARK 465 GLN H 171 REMARK 465 SER H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 LEU H 175 REMARK 465 TYR H 176 REMARK 465 SER H 177 REMARK 465 LEU H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 VAL H 181 REMARK 465 VAL H 182 REMARK 465 THR H 183 REMARK 465 VAL H 184 REMARK 465 PRO H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 GLY H 190 REMARK 465 THR H 191 REMARK 465 GLN H 192 REMARK 465 THR H 193 REMARK 465 TYR H 194 REMARK 465 VAL H 195 REMARK 465 CYS H 196 REMARK 465 ASN H 197 REMARK 465 VAL H 198 REMARK 465 ASN H 199 REMARK 465 HIS H 200 REMARK 465 LYS H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 ASN H 204 REMARK 465 THR H 205 REMARK 465 LYS H 206 REMARK 465 VAL H 207 REMARK 465 ASP H 208 REMARK 465 LYS H 209 REMARK 465 ARG H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 ILE H 213 REMARK 465 LYS H 214 REMARK 465 THR H 215 REMARK 465 CYS H 216 REMARK 465 GLY H 217 REMARK 465 GLY H 218 REMARK 465 GLY H 219 REMARK 465 LEU H 220 REMARK 465 GLU H 221 REMARK 465 VAL H 222 REMARK 465 LEU H 223 REMARK 465 PHE H 224 REMARK 465 GLN H 225 REMARK 465 THR L 105 REMARK 465 VAL L 106 REMARK 465 LEU L 107 REMARK 465 GLY L 108 REMARK 465 GLN L 109 REMARK 465 PRO L 110 REMARK 465 LYS L 111 REMARK 465 ALA L 112 REMARK 465 ALA L 113 REMARK 465 PRO L 114 REMARK 465 SER L 115 REMARK 465 VAL L 116 REMARK 465 THR L 117 REMARK 465 LEU L 118 REMARK 465 PHE L 119 REMARK 465 PRO L 120 REMARK 465 PRO L 121 REMARK 465 SER L 122 REMARK 465 SER L 123 REMARK 465 GLU L 124 REMARK 465 GLU L 125 REMARK 465 LEU L 126 REMARK 465 GLN L 127 REMARK 465 ALA L 128 REMARK 465 ASN L 129 REMARK 465 LYS L 130 REMARK 465 ALA L 131 REMARK 465 THR L 132 REMARK 465 LEU L 133 REMARK 465 VAL L 134 REMARK 465 CYS L 135 REMARK 465 LEU L 136 REMARK 465 ILE L 137 REMARK 465 SER L 138 REMARK 465 ASP L 139 REMARK 465 PHE L 140 REMARK 465 TYR L 141 REMARK 465 PRO L 142 REMARK 465 GLY L 143 REMARK 465 ALA L 144 REMARK 465 VAL L 145 REMARK 465 GLU L 146 REMARK 465 VAL L 147 REMARK 465 ALA L 148 REMARK 465 TRP L 149 REMARK 465 LYS L 150 REMARK 465 ALA L 151 REMARK 465 ASP L 152 REMARK 465 GLY L 153 REMARK 465 SER L 154 REMARK 465 ALA L 155 REMARK 465 VAL L 156 REMARK 465 ASN L 157 REMARK 465 ALA L 158 REMARK 465 GLY L 159 REMARK 465 VAL L 160 REMARK 465 GLU L 161 REMARK 465 THR L 162 REMARK 465 THR L 163 REMARK 465 LYS L 164 REMARK 465 PRO L 165 REMARK 465 SER L 166 REMARK 465 LYS L 167 REMARK 465 GLN L 168 REMARK 465 SER L 169 REMARK 465 ASN L 170 REMARK 465 ASN L 171 REMARK 465 LYS L 172 REMARK 465 TYR L 173 REMARK 465 ALA L 174 REMARK 465 ALA L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 TYR L 178 REMARK 465 LEU L 179 REMARK 465 SER L 180 REMARK 465 LEU L 181 REMARK 465 THR L 182 REMARK 465 SER L 183 REMARK 465 ASP L 184 REMARK 465 GLN L 185 REMARK 465 TRP L 186 REMARK 465 LYS L 187 REMARK 465 SER L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 SER L 191 REMARK 465 TYR L 192 REMARK 465 SER L 193 REMARK 465 CYS L 194 REMARK 465 GLN L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLU L 199 REMARK 465 GLY L 200 REMARK 465 SER L 201 REMARK 465 THR L 202 REMARK 465 VAL L 203 REMARK 465 GLU L 204 REMARK 465 LYS L 205 REMARK 465 THR L 206 REMARK 465 VAL L 207 REMARK 465 ALA L 208 REMARK 465 PRO L 209 REMARK 465 ALA L 210 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 TYR A 191 N - CA - CB ANGL. DEV. = -15.3 DEGREES REMARK 500 CYS C 247 CA - CB - SG ANGL. DEV. = 6.6 DEGREES REMARK 500 CYS E 247 CA - CB - SG ANGL. DEV. = 7.4 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLN A 258 -6.75 73.91 REMARK 500 SER A 364 176.65 59.31 REMARK 500 ASN A 377 12.14 -143.94 REMARK 500 ARG A 500 59.11 -95.23 REMARK 500 ASN B 543 31.03 -92.27 REMARK 500 ALA C 55 116.63 -167.28 REMARK 500 THR C 90 54.18 38.33 REMARK 500 GLN C 258 11.48 59.35 REMARK 500 LYS C 268 11.36 -140.17 REMARK 500 PRO C 313 68.11 -69.20 REMARK 500 ASN C 355 44.70 -89.80 REMARK 500 SER C 364 176.58 60.36 REMARK 500 ASN C 377 32.58 -141.44 REMARK 500 GLU C 492 75.98 -113.38 REMARK 500 LEU E 122 23.79 -79.98 REMARK 500 CYS E 126 57.95 -90.59 REMARK 500 ASN E 186A -50.79 75.43 REMARK 500 SER E 189 -167.34 62.07 REMARK 500 GLN E 258 -6.84 75.49 REMARK 500 SER E 364 -175.78 59.05 REMARK 500 ASP E 457 52.22 -91.82 REMARK 500 ASN F 616 54.46 -92.73 REMARK 500 GLN F 650 -60.94 -103.34 REMARK 500 SER H 15 -5.06 79.17 REMARK 500 SER L 30 -18.71 -140.20 REMARK 500 SER L 32 156.94 -47.86 REMARK 500 GLU L 41 45.59 33.88 REMARK 500 ASN L 50 -117.38 62.50 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44897 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF RHESUS ANTIBODY T646-A.01 IN COMPLEX WITH HIV- REMARK 900 1 ENV Q23.17 MD39 SOSIP DBREF 9BTV A 31 508 UNP O55774 O55774_9HIV1 30 498 DBREF 9BTV B 512 664 UNP O55774 O55774_9HIV1 502 654 DBREF 9BTV C 31 508 UNP O55774 O55774_9HIV1 30 498 DBREF 9BTV E 31 508 UNP O55774 O55774_9HIV1 30 498 DBREF 9BTV F 512 664 UNP O55774 O55774_9HIV1 502 654 DBREF 9BTV G 512 664 UNP O55774 O55774_9HIV1 502 654 DBREF 9BTV H 1 225 PDB 9BTV 9BTV 1 225 DBREF 9BTV L 1 213 PDB 9BTV 9BTV 1 213 SEQADV 9BTV GLU A 106 UNP O55774 THR 105 CONFLICT SEQADV 9BTV ILE A 271 UNP O55774 THR 263 CONFLICT SEQADV 9BTV VAL A 304 UNP O55774 ARG 296 CONFLICT SEQADV 9BTV TYR A 319 UNP O55774 ALA 309 CONFLICT SEQADV 9BTV SER A 473 UNP O55774 GLY 463 CONFLICT SEQADV 9BTV CYS A 501 UNP O55774 ALA 491 CONFLICT SEQADV 9BTV SER B 519 UNP O55774 PHE 509 ENGINEERED MUTATION SEQADV 9BTV ALA B 533 UNP O55774 THR 523 ENGINEERED MUTATION SEQADV 9BTV ASN B 543 UNP O55774 GLN 533 CONFLICT SEQADV 9BTV PRO B 559 UNP O55774 ILE 549 ENGINEERED MUTATION SEQADV 9BTV PRO B 561 UNP O55774 ALA 551 ENGINEERED MUTATION SEQADV 9BTV HIS B 570 UNP O55774 VAL 560 ENGINEERED MUTATION SEQADV 9BTV HIS B 585 UNP O55774 ARG 575 ENGINEERED MUTATION SEQADV 9BTV CYS B 605 UNP O55774 THR 595 ENGINEERED MUTATION SEQADV 9BTV GLU C 106 UNP O55774 THR 105 CONFLICT SEQADV 9BTV ILE C 271 UNP O55774 THR 263 CONFLICT SEQADV 9BTV VAL C 304 UNP O55774 ARG 296 CONFLICT SEQADV 9BTV TYR C 319 UNP O55774 ALA 309 CONFLICT SEQADV 9BTV SER C 473 UNP O55774 GLY 463 CONFLICT SEQADV 9BTV CYS C 501 UNP O55774 ALA 491 CONFLICT SEQADV 9BTV GLU E 106 UNP O55774 THR 105 CONFLICT SEQADV 9BTV ILE E 271 UNP O55774 THR 263 CONFLICT SEQADV 9BTV VAL E 304 UNP O55774 ARG 296 CONFLICT SEQADV 9BTV TYR E 319 UNP O55774 ALA 309 CONFLICT SEQADV 9BTV SER E 473 UNP O55774 GLY 463 CONFLICT SEQADV 9BTV CYS E 501 UNP O55774 ALA 491 CONFLICT SEQADV 9BTV SER F 519 UNP O55774 PHE 509 ENGINEERED MUTATION SEQADV 9BTV ALA F 533 UNP O55774 THR 523 ENGINEERED MUTATION SEQADV 9BTV ASN F 543 UNP O55774 GLN 533 CONFLICT SEQADV 9BTV PRO F 559 UNP O55774 ILE 549 ENGINEERED MUTATION SEQADV 9BTV PRO F 561 UNP O55774 ALA 551 ENGINEERED MUTATION SEQADV 9BTV HIS F 570 UNP O55774 VAL 560 ENGINEERED MUTATION SEQADV 9BTV HIS F 585 UNP O55774 ARG 575 ENGINEERED MUTATION SEQADV 9BTV CYS F 605 UNP O55774 THR 595 ENGINEERED MUTATION SEQADV 9BTV SER G 519 UNP O55774 PHE 509 ENGINEERED MUTATION SEQADV 9BTV ALA G 533 UNP O55774 THR 523 ENGINEERED MUTATION SEQADV 9BTV ASN G 543 UNP O55774 GLN 533 CONFLICT SEQADV 9BTV PRO G 559 UNP O55774 ILE 549 ENGINEERED MUTATION SEQADV 9BTV PRO G 561 UNP O55774 ALA 551 ENGINEERED MUTATION SEQADV 9BTV HIS G 570 UNP O55774 VAL 560 ENGINEERED MUTATION SEQADV 9BTV HIS G 585 UNP O55774 ARG 575 ENGINEERED MUTATION SEQADV 9BTV CYS G 605 UNP O55774 THR 595 ENGINEERED MUTATION SEQRES 1 A 469 VAL GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 469 VAL TRP ARG ASP ALA ASP THR THR LEU PHE CYS ALA SER SEQRES 3 A 469 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 A 469 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 469 GLU ILE HIS LEU ASP ASN VAL THR GLU LYS PHE ASN MET SEQRES 6 A 469 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 A 469 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 469 LEU THR PRO LEU CYS VAL THR LEU HIS CYS THR ASN VAL SEQRES 9 A 469 THR SER VAL ASN THR THR GLY ASP ARG GLU GLY LEU LYS SEQRES 10 A 469 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 A 469 ARG GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE SEQRES 12 A 469 VAL PRO ILE ASN GLU ASN GLN GLY SER GLU TYR ARG LEU SEQRES 13 A 469 ILE ASN CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO SEQRES 14 A 469 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS THR SEQRES 15 A 469 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP GLU GLY SEQRES 16 A 469 PHE ASN GLY THR GLY LEU CYS LYS ASN VAL SER THR VAL SEQRES 17 A 469 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 18 A 469 LEU LEU LEU ASN GLY SER LEU ALA GLU LYS ASN ILE ILE SEQRES 19 A 469 ILE ARG SER GLU ASN ILE THR ASN ASN ALA LYS ILE ILE SEQRES 20 A 469 ILE VAL GLN LEU VAL GLN PRO VAL THR ILE LYS CYS ILE SEQRES 21 A 469 ARG PRO ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY SEQRES 22 A 469 PRO GLY GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY SEQRES 23 A 469 ASP ILE ARG GLN ALA HIS CYS ASN VAL THR ARG SER ARG SEQRES 24 A 469 TRP ASN LYS THR LEU GLN GLU VAL ALA GLU LYS LEU ARG SEQRES 25 A 469 THR TYR PHE GLY ASN LYS THR ILE ILE PHE ALA ASN SER SEQRES 26 A 469 SER GLY GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN SEQRES 27 A 469 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 28 A 469 PHE ASN SER THR TRP TYR VAL ASN SER THR TRP ASN ASP SEQRES 29 A 469 THR ASP SER THR GLN GLU SER ASN ASP THR ILE THR LEU SEQRES 30 A 469 PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG SEQRES 31 A 469 ALA GLY GLN ALA MET TYR ALA PRO PRO ILE PRO GLY VAL SEQRES 32 A 469 ILE LYS CYS GLU SER ASN ILE THR GLY LEU LEU LEU THR SEQRES 33 A 469 ARG ASP GLY GLY LYS ASP ASN ASN VAL ASN GLU THR PHE SEQRES 34 A 469 ARG PRO GLY GLY SER ASP MET ARG ASP ASN TRP ARG SER SEQRES 35 A 469 GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE GLU PRO LEU SEQRES 36 A 469 GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLU SEQRES 37 A 469 ARG SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ILE THR LEU SEQRES 3 B 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 153 GLN GLN ASN ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 B 153 HIS LEU LEU LYS LEU THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 B 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 153 ASN LYS SER LEU ASP GLU ILE TRP ASN ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE ASN ASN TYR THR GLN LEU SEQRES 11 B 153 ILE TYR ARG LEU ILE GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU LYS GLU LEU LEU GLU LEU ASP SEQRES 1 C 469 VAL GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 469 VAL TRP ARG ASP ALA ASP THR THR LEU PHE CYS ALA SER SEQRES 3 C 469 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 C 469 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 469 GLU ILE HIS LEU ASP ASN VAL THR GLU LYS PHE ASN MET SEQRES 6 C 469 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 C 469 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 469 LEU THR PRO LEU CYS VAL THR LEU HIS CYS THR ASN VAL SEQRES 9 C 469 THR SER VAL ASN THR THR GLY ASP ARG GLU GLY LEU LYS SEQRES 10 C 469 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 C 469 ARG GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE SEQRES 12 C 469 VAL PRO ILE ASN GLU ASN GLN GLY SER GLU TYR ARG LEU SEQRES 13 C 469 ILE ASN CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO SEQRES 14 C 469 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS THR SEQRES 15 C 469 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP GLU GLY SEQRES 16 C 469 PHE ASN GLY THR GLY LEU CYS LYS ASN VAL SER THR VAL SEQRES 17 C 469 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 18 C 469 LEU LEU LEU ASN GLY SER LEU ALA GLU LYS ASN ILE ILE SEQRES 19 C 469 ILE ARG SER GLU ASN ILE THR ASN ASN ALA LYS ILE ILE SEQRES 20 C 469 ILE VAL GLN LEU VAL GLN PRO VAL THR ILE LYS CYS ILE SEQRES 21 C 469 ARG PRO ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY SEQRES 22 C 469 PRO GLY GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY SEQRES 23 C 469 ASP ILE ARG GLN ALA HIS CYS ASN VAL THR ARG SER ARG SEQRES 24 C 469 TRP ASN LYS THR LEU GLN GLU VAL ALA GLU LYS LEU ARG SEQRES 25 C 469 THR TYR PHE GLY ASN LYS THR ILE ILE PHE ALA ASN SER SEQRES 26 C 469 SER GLY GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN SEQRES 27 C 469 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 28 C 469 PHE ASN SER THR TRP TYR VAL ASN SER THR TRP ASN ASP SEQRES 29 C 469 THR ASP SER THR GLN GLU SER ASN ASP THR ILE THR LEU SEQRES 30 C 469 PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG SEQRES 31 C 469 ALA GLY GLN ALA MET TYR ALA PRO PRO ILE PRO GLY VAL SEQRES 32 C 469 ILE LYS CYS GLU SER ASN ILE THR GLY LEU LEU LEU THR SEQRES 33 C 469 ARG ASP GLY GLY LYS ASP ASN ASN VAL ASN GLU THR PHE SEQRES 34 C 469 ARG PRO GLY GLY SER ASP MET ARG ASP ASN TRP ARG SER SEQRES 35 C 469 GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE GLU PRO LEU SEQRES 36 C 469 GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLU SEQRES 37 C 469 ARG SEQRES 1 E 469 VAL GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 E 469 VAL TRP ARG ASP ALA ASP THR THR LEU PHE CYS ALA SER SEQRES 3 E 469 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 E 469 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 E 469 GLU ILE HIS LEU ASP ASN VAL THR GLU LYS PHE ASN MET SEQRES 6 E 469 TRP LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE SEQRES 7 E 469 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 E 469 LEU THR PRO LEU CYS VAL THR LEU HIS CYS THR ASN VAL SEQRES 9 E 469 THR SER VAL ASN THR THR GLY ASP ARG GLU GLY LEU LYS SEQRES 10 E 469 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 E 469 ARG GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE SEQRES 12 E 469 VAL PRO ILE ASN GLU ASN GLN GLY SER GLU TYR ARG LEU SEQRES 13 E 469 ILE ASN CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO SEQRES 14 E 469 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS THR SEQRES 15 E 469 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP GLU GLY SEQRES 16 E 469 PHE ASN GLY THR GLY LEU CYS LYS ASN VAL SER THR VAL SEQRES 17 E 469 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 18 E 469 LEU LEU LEU ASN GLY SER LEU ALA GLU LYS ASN ILE ILE SEQRES 19 E 469 ILE ARG SER GLU ASN ILE THR ASN ASN ALA LYS ILE ILE SEQRES 20 E 469 ILE VAL GLN LEU VAL GLN PRO VAL THR ILE LYS CYS ILE SEQRES 21 E 469 ARG PRO ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY SEQRES 22 E 469 PRO GLY GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY SEQRES 23 E 469 ASP ILE ARG GLN ALA HIS CYS ASN VAL THR ARG SER ARG SEQRES 24 E 469 TRP ASN LYS THR LEU GLN GLU VAL ALA GLU LYS LEU ARG SEQRES 25 E 469 THR TYR PHE GLY ASN LYS THR ILE ILE PHE ALA ASN SER SEQRES 26 E 469 SER GLY GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN SEQRES 27 E 469 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 28 E 469 PHE ASN SER THR TRP TYR VAL ASN SER THR TRP ASN ASP SEQRES 29 E 469 THR ASP SER THR GLN GLU SER ASN ASP THR ILE THR LEU SEQRES 30 E 469 PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG SEQRES 31 E 469 ALA GLY GLN ALA MET TYR ALA PRO PRO ILE PRO GLY VAL SEQRES 32 E 469 ILE LYS CYS GLU SER ASN ILE THR GLY LEU LEU LEU THR SEQRES 33 E 469 ARG ASP GLY GLY LYS ASP ASN ASN VAL ASN GLU THR PHE SEQRES 34 E 469 ARG PRO GLY GLY SER ASP MET ARG ASP ASN TRP ARG SER SEQRES 35 E 469 GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE GLU PRO LEU SEQRES 36 E 469 GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLU SEQRES 37 E 469 ARG SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ILE THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN ASN ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 F 153 HIS LEU LEU LYS LEU THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 F 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 153 ASN LYS SER LEU ASP GLU ILE TRP ASN ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP LYS GLU ILE ASN ASN TYR THR GLN LEU SEQRES 11 F 153 ILE TYR ARG LEU ILE GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU LYS GLU LEU LEU GLU LEU ASP SEQRES 1 G 153 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 G 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ILE THR LEU SEQRES 3 G 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 G 153 GLN GLN ASN ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 G 153 HIS LEU LEU LYS LEU THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 G 153 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 G 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 G 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 G 153 ASN LYS SER LEU ASP GLU ILE TRP ASN ASN MET THR TRP SEQRES 10 G 153 LEU GLN TRP ASP LYS GLU ILE ASN ASN TYR THR GLN LEU SEQRES 11 G 153 ILE TYR ARG LEU ILE GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 G 153 LYS ASN GLU LYS GLU LEU LEU GLU LEU ASP SEQRES 1 H 245 GLN VAL GLN LEU ARG GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 245 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY SEQRES 3 H 245 ALA SER ILE SER ASP GLU TYR TYR TRP THR TRP ILE ARG SEQRES 4 H 245 GLN PRO PRO GLY ARG GLY LEU GLU TRP ILE GLY TYR PHE SEQRES 5 H 245 SER GLY ARG ASP GLY TYR PRO HIS TYR ASN ARG PHE LEU SEQRES 6 H 245 GLU SER ARG VAL THR ILE SER VAL ASP THR SER LYS LYS SEQRES 7 H 245 GLN ILE SER LEU ARG LEU THR SER VAL THR ALA ALA ASP SEQRES 8 H 245 THR ALA VAL TYR PHE CYS ALA LYS ALA PRO ARG SER PHE SEQRES 9 H 245 LEU TYR GLY ASP ASP TYS GLY ASP PHE TYR THR GLU SER SEQRES 10 H 245 ASP TYR PHE ASP SER TRP GLY GLN GLY VAL LEU VAL THR SEQRES 11 H 245 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 12 H 245 LEU ALA PRO SER SER ARG SER THR SER GLU SER THR ALA SEQRES 13 H 245 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 14 H 245 VAL THR VAL SER TRP ASN SER GLY SER LEU THR SER GLY SEQRES 15 H 245 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 16 H 245 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 17 H 245 LEU GLY THR GLN THR TYR VAL CYS ASN VAL ASN HIS LYS SEQRES 18 H 245 PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU ILE LYS SEQRES 19 H 245 THR CYS GLY GLY GLY LEU GLU VAL LEU PHE GLN SEQRES 1 L 216 GLN SER VAL LEU THR GLN PRO PRO SER ALA SER GLU ALA SEQRES 2 L 216 ALA ARG LYS SER VAL THR ILE SER CYS SER GLY SER SER SEQRES 3 L 216 SER ASN ILE GLY SER ASN SER VAL SER TRP TYR GLN GLN SEQRES 4 L 216 LEU PRO GLU THR ALA PRO LYS LEU LEU ILE TYR ASN ASN SEQRES 5 L 216 ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY SEQRES 6 L 216 SER LYS SER GLY THR SER ALA SER LEU ALA ILE SER GLY SEQRES 7 L 216 LEU GLN THR GLU ASP GLU ALA ASP TYR TYR CYS GLY ALA SEQRES 8 L 216 TRP ASP GLY SER LEU ARG GLY ASN VAL PHE GLY SER GLY SEQRES 9 L 216 THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 L 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 L 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 L 216 TYR PRO GLY ALA VAL GLU VAL ALA TRP LYS ALA ASP GLY SEQRES 13 L 216 SER ALA VAL ASN ALA GLY VAL GLU THR THR LYS PRO SER SEQRES 14 L 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 L 216 SER LEU THR SER ASP GLN TRP LYS SER HIS LYS SER TYR SEQRES 16 L 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 L 216 THR VAL ALA PRO ALA GLU CYS SER HET TYS H 100E 16 HET NAG D 1 14 HET NAG D 2 14 HET BMA D 3 11 HET MAN D 4 11 HET MAN D 5 11 HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET MAN I 4 11 HET NAG J 1 14 HET NAG J 2 14 HET BMA J 3 11 HET NAG K 1 14 HET NAG K 2 14 HET BMA K 3 11 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET NAG O 1 14 HET NAG O 2 14 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET BMA Q 3 11 HET NAG R 1 14 HET NAG R 2 14 HET NAG S 1 14 HET NAG S 2 14 HET NAG T 1 14 HET NAG T 2 14 HET BMA T 3 11 HET NAG U 1 14 HET NAG U 2 14 HET NAG V 1 14 HET NAG V 2 14 HET NAG W 1 14 HET NAG W 2 14 HET NAG X 1 14 HET NAG X 2 14 HET BMA X 3 11 HET NAG Y 1 14 HET NAG Y 2 14 HET BMA Y 3 11 HET NAG Z 1 14 HET NAG Z 2 14 HET NAG a 1 14 HET NAG a 2 14 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 HET NAG d 1 14 HET NAG d 2 14 HET BMA d 3 11 HET NAG e 1 14 HET NAG e 2 14 HET NAG f 1 14 HET NAG f 2 14 HET NAG g 1 14 HET NAG g 2 14 HET BMA g 3 11 HET NAG h 1 14 HET NAG h 2 14 HET NAG i 1 14 HET NAG i 2 14 HET BMA i 3 11 HET MAN i 4 11 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET MAN j 4 11 HET MAN j 5 11 HET MAN j 6 11 HET NAG k 1 14 HET NAG k 2 14 HET BMA k 3 11 HET MAN k 4 11 HET NAG l 1 14 HET NAG l 2 14 HET NAG m 1 14 HET NAG m 2 14 HET BMA m 3 11 HET NAG n 1 14 HET NAG n 2 14 HET BMA n 3 11 HET NAG o 1 14 HET NAG o 2 14 HET NAG p 1 14 HET NAG p 2 14 HET NAG q 1 14 HET NAG q 2 14 HET NAG r 1 14 HET NAG r 2 14 HET BMA r 3 11 HET NAG s 1 14 HET NAG s 2 14 HET NAG t 1 14 HET NAG t 2 14 HET NAG u 1 14 HET NAG u 2 14 HET BMA u 3 11 HET NAG v 1 14 HET NAG v 2 14 HET NAG w 1 14 HET NAG w 2 14 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG E 604 14 HET NAG F 701 14 HET NAG F 702 14 HET NAG G 701 14 HET NAG G 702 14 HET NAG G 703 14 HETNAM TYS O-SULFO-L-TYROSINE HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 7 TYS C9 H11 N O6 S FORMUL 9 NAG 101(C8 H15 N O6) FORMUL 9 BMA 17(C6 H12 O6) FORMUL 9 MAN 8(C6 H12 O6) HELIX 1 AA1 TRP A 96 ASN A 98 5 3 HELIX 2 AA2 ASN A 99 LYS A 117 1 19 HELIX 3 AA3 LEU A 122 CYS A 126 5 5 HELIX 4 AA4 ARG A 335 PHE A 353 1 19 HELIX 5 AA5 ASP A 368 THR A 373 1 6 HELIX 6 AA6 ASN A 377 GLU A 381 5 5 HELIX 7 AA7 THR A 387 LEU A 390 5 4 HELIX 8 AA8 MET A 475 TYR A 484 1 10 HELIX 9 AA9 LEU B 523 GLY B 527 5 5 HELIX 10 AB1 THR B 529 SER B 534 1 6 HELIX 11 AB2 THR B 536 ASN B 543 1 8 HELIX 12 AB3 HIS B 570 TRP B 596 1 27 HELIX 13 AB4 SER B 618 TRP B 623 1 6 HELIX 14 AB5 THR B 627 ASN B 636 1 10 HELIX 15 AB6 TYR B 638 LEU B 661 1 24 HELIX 16 AB7 ASN C 99 LYS C 117 1 19 HELIX 17 AB8 LEU C 122 CYS C 126 5 5 HELIX 18 AB9 ARG C 335 PHE C 353 1 19 HELIX 19 AC1 ASP C 368 THR C 373 1 6 HELIX 20 AC2 ASN C 377 GLU C 381 5 5 HELIX 21 AC3 ASN C 386 LEU C 390 5 5 HELIX 22 AC4 MET C 475 SER C 481 1 7 HELIX 23 AC5 ALA E 70 CYS E 74 5 5 HELIX 24 AC6 ASN E 99 LYS E 117 1 19 HELIX 25 AC7 LEU E 122 CYS E 126 5 5 HELIX 26 AC8 THR E 334 PHE E 353 1 20 HELIX 27 AC9 ASP E 368 THR E 373 1 6 HELIX 28 AD1 THR E 387 LEU E 390 5 4 HELIX 29 AD2 MET E 475 SER E 481 1 7 HELIX 30 AD3 GLU E 482 TYR E 484 5 3 HELIX 31 AD4 THR F 529 SER F 534 1 6 HELIX 32 AD5 LEU F 537 LEU F 544 1 8 HELIX 33 AD6 THR F 569 GLY F 597 1 29 HELIX 34 AD7 ASN F 611 SER F 615 5 5 HELIX 35 AD8 SER F 618 ASN F 625 1 8 HELIX 36 AD9 THR F 627 GLU F 634 1 8 HELIX 37 AE1 TYR F 638 GLU F 648 1 11 HELIX 38 AE2 GLN F 650 GLU F 659 1 10 HELIX 39 AE3 THR G 529 SER G 534 1 6 HELIX 40 AE4 THR G 536 ASN G 543 1 8 HELIX 41 AE5 THR G 569 TRP G 596 1 28 HELIX 42 AE6 SER G 618 ASN G 625 1 8 HELIX 43 AE7 THR G 627 ILE G 635 1 9 HELIX 44 AE8 TYR G 638 LEU G 661 1 24 HELIX 45 AE9 THR H 83 THR H 87 5 5 HELIX 46 AF1 ASN L 27B ASN L 31 5 5 HELIX 47 AF2 GLN L 79 GLU L 83 5 5 SHEET 1 AA1 3 GLY A 495 THR A 499 0 SHEET 2 AA1 3 TRP A 35 TYR A 39 -1 N TRP A 35 O THR A 499 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O CYS B 604 N VAL A 38 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 TYR A 486 ILE A 491 -1 O GLU A 490 N ARG A 46 SHEET 3 AA2 5 PHE A 223 CYS A 228 -1 N ALA A 224 O VAL A 489 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 GLU A 83 HIS A 85 -1 N ILE A 84 O THR A 244 SHEET 1 AA3 2 GLU A 91 ASN A 94 0 SHEET 2 AA3 2 THR A 236 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AA4 3 HIS A 130 ASN A 133 0 SHEET 2 AA4 3 LEU A 154 THR A 162 -1 O ASN A 156 N THR A 132 SHEET 3 AA4 3 ARG A 169 TYR A 177 -1 O GLN A 170 N MET A 161 SHEET 1 AA5 2 ILE A 181 PRO A 183 0 SHEET 2 AA5 2 TYR A 191 LEU A 193 -1 O ARG A 192 N VAL A 182 SHEET 1 AA6 3 ILE A 201 GLN A 203 0 SHEET 2 AA6 3 ALA A 433 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA6 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA7 7 LEU A 259 LEU A 261 0 SHEET 2 AA7 7 LYS A 444 ARG A 456 -1 O GLY A 451 N LEU A 260 SHEET 3 AA7 7 ILE A 284 ILE A 297 -1 N CYS A 296 O CYS A 445 SHEET 4 AA7 7 ALA A 329 THR A 334 -1 O ASN A 332 N LYS A 295 SHEET 5 AA7 7 THR A 413 ILE A 420 -1 O ILE A 414 N VAL A 333 SHEET 6 AA7 7 PHE A 383 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 7 AA7 7 HIS A 374 SER A 375 -1 N HIS A 374 O CYS A 385 SHEET 1 AA8 6 ILE A 271 ARG A 273 0 SHEET 2 AA8 6 ILE A 284 ILE A 297 -1 O GLN A 287 N ILE A 271 SHEET 3 AA8 6 LYS A 444 ARG A 456 -1 O CYS A 445 N CYS A 296 SHEET 4 AA8 6 ASN A 465 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 5 AA8 6 THR A 358 PHE A 361 1 N ILE A 360 O PHE A 468 SHEET 6 AA8 6 THR A 394 TRP A 395 -1 O TRP A 395 N ILE A 359 SHEET 1 AA9 2 ASN A 301 ILE A 309 0 SHEET 2 AA9 2 GLN A 315 ILE A 323A-1 O GLN A 315 N ILE A 309 SHEET 1 AB1 2 TRP C 35 TYR C 39 0 SHEET 2 AB1 2 GLY C 495 THR C 499 -1 O THR C 499 N TRP C 35 SHEET 1 AB2 4 ARG C 46 ASP C 47 0 SHEET 2 AB2 4 TYR C 486 GLU C 490 -1 O GLU C 490 N ARG C 46 SHEET 3 AB2 4 PHE C 223 LYS C 227 -1 N LEU C 226 O LYS C 487 SHEET 4 AB2 4 SER C 243 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 1 AB3 2 PHE C 53 SER C 56 0 SHEET 2 AB3 2 ILE C 215 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AB4 2 LYS C 92 PHE C 93 0 SHEET 2 AB4 2 GLY C 237 LEU C 238 -1 O GLY C 237 N PHE C 93 SHEET 1 AB5 5 ARG C 169 TYR C 177 0 SHEET 2 AB5 5 LEU C 154 THR C 162 -1 N MET C 161 O GLN C 170 SHEET 3 AB5 5 LEU C 129 ASN C 133 -1 N HIS C 130 O SER C 158 SHEET 4 AB5 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AB5 5 ILE C 181 PRO C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AB6 3 ILE C 201 GLN C 203 0 SHEET 2 AB6 3 ALA C 433 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AB6 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AB7 5 LEU C 259 LEU C 261 0 SHEET 2 AB7 5 SER C 447 ARG C 456 -1 O GLY C 451 N LEU C 260 SHEET 3 AB7 5 ILE C 284 ILE C 297 -1 N ILE C 284 O LEU C 454 SHEET 4 AB7 5 GLU C 466 PRO C 470 0 SHEET 5 AB7 5 ILE C 359 PHE C 361 1 N ILE C 360 O PHE C 468 SHEET 1 AB8 5 ILE C 271 ARG C 273 0 SHEET 2 AB8 5 ILE C 284 ILE C 297 -1 O GLN C 287 N ILE C 271 SHEET 3 AB8 5 SER C 447 ARG C 456 -1 O LEU C 454 N ILE C 284 SHEET 4 AB8 5 HIS C 330 THR C 334 0 SHEET 5 AB8 5 THR C 413 PRO C 417 -1 O ILE C 414 N VAL C 333 SHEET 1 AB9 2 ASN C 302 ILE C 309 0 SHEET 2 AB9 2 GLN C 315 ILE C 323 -1 O GLN C 315 N ILE C 309 SHEET 1 AC1 3 LEU E 494 THR E 499 0 SHEET 2 AC1 3 TRP E 35 TYR E 40 -1 N TYR E 39 O GLY E 495 SHEET 3 AC1 3 ILE G 603 PRO G 609 -1 O CYS G 604 N VAL E 38 SHEET 1 AC2 5 TRP E 45 ASP E 47 0 SHEET 2 AC2 5 TYR E 486 ILE E 491 -1 O GLU E 490 N ARG E 46 SHEET 3 AC2 5 PHE E 223 CYS E 228 -1 N ALA E 224 O VAL E 489 SHEET 4 AC2 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AC2 5 GLU E 83 HIS E 85 -1 N ILE E 84 O THR E 244 SHEET 1 AC3 3 VAL E 75 PRO E 76 0 SHEET 2 AC3 3 PHE E 53 SER E 56 1 N CYS E 54 O VAL E 75 SHEET 3 AC3 3 HIS E 216 CYS E 218 -1 O HIS E 216 N ALA E 55 SHEET 1 AC4 2 LYS E 92 ASN E 94 0 SHEET 2 AC4 2 THR E 236 LEU E 238 -1 O GLY E 237 N PHE E 93 SHEET 1 AC5 3 HIS E 130 ASN E 133 0 SHEET 2 AC5 3 LEU E 154 THR E 162 -1 O ASN E 156 N THR E 132 SHEET 3 AC5 3 ARG E 169 TYR E 177 -1 O GLN E 170 N MET E 161 SHEET 1 AC6 2 ILE E 181 PRO E 183 0 SHEET 2 AC6 2 TYR E 191 LEU E 193 -1 O ARG E 192 N VAL E 182 SHEET 1 AC7 3 ILE E 201 GLN E 203 0 SHEET 2 AC7 3 ALA E 433 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AC7 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AC8 8 SER E 256 THR E 257 0 SHEET 2 AC8 8 HIS E 374 CYS E 378 -1 O SER E 375 N THR E 257 SHEET 3 AC8 8 GLU E 381 CYS E 385 -1 O CYS E 385 N HIS E 374 SHEET 4 AC8 8 LEU E 416 LYS E 421 -1 O ARG E 419 N TYR E 384 SHEET 5 AC8 8 ALA E 329 VAL E 333 -1 N ALA E 329 O CYS E 418 SHEET 6 AC8 8 ILE E 284 ARG E 298 -1 N LYS E 295 O ASN E 332 SHEET 7 AC8 8 ILE E 443 ARG E 456 -1 O LEU E 454 N ILE E 284 SHEET 8 AC8 8 ILE E 271 ARG E 273 0 SHEET 1 AC9 6 LEU E 260 LEU E 261 0 SHEET 2 AC9 6 ILE E 443 ARG E 456 -1 O GLY E 451 N LEU E 260 SHEET 3 AC9 6 ILE E 284 ARG E 298 -1 N ILE E 284 O LEU E 454 SHEET 4 AC9 6 ASN E 465 PRO E 470 0 SHEET 5 AC9 6 THR E 358 PHE E 361 1 N ILE E 360 O PHE E 468 SHEET 6 AC9 6 THR E 394 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 1 AD1 2 THR E 303 ARG E 308 0 SHEET 2 AD1 2 ALA E 316 ASP E 322 -1 O PHE E 317 N ILE E 307 SHEET 1 AD2 4 GLN H 3 SER H 7 0 SHEET 2 AD2 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AD2 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 AD2 4 VAL H 67 ASP H 72 -1 N SER H 70 O SER H 79 SHEET 1 AD3 6 LEU H 11 VAL H 12 0 SHEET 2 AD3 6 VAL H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AD3 6 ALA H 88 PRO H 95A-1 N TYR H 90 O VAL H 107 SHEET 4 AD3 6 TYR H 33 GLN H 39 -1 N ILE H 37 O PHE H 91 SHEET 5 AD3 6 GLU H 46 SER H 52 -1 O GLY H 49 N TRP H 36 SHEET 6 AD3 6 PRO H 57 TYR H 59 -1 O HIS H 58 N TYR H 50 SHEET 1 AD4 2 PHE H 95D TYR H 100A 0 SHEET 2 AD4 2 PHE H 100H TYR H 100I-1 O PHE H 100H N LEU H 100 SHEET 1 AD5 3 THR L 20 SER L 24 0 SHEET 2 AD5 3 SER L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 3 AD5 3 PHE L 62 SER L 67 -1 N SER L 63 O ALA L 74 SHEET 1 AD6 4 PRO L 44 ILE L 48 0 SHEET 2 AD6 4 TRP L 35 GLN L 38 -1 N GLN L 37 O LYS L 45 SHEET 3 AD6 4 ASP L 85 ASP L 92 -1 O ASP L 85 N GLN L 38 SHEET 4 AD6 4 GLY L 95B PHE L 98 -1 O VAL L 97 N ALA L 90 SHEET 1 AD7 4 PRO L 44 ILE L 48 0 SHEET 2 AD7 4 TRP L 35 GLN L 38 -1 N GLN L 37 O LYS L 45 SHEET 3 AD7 4 ASP L 85 ASP L 92 -1 O ASP L 85 N GLN L 38 SHEET 4 AD7 4 THR L 102 LYS L 103 -1 O THR L 102 N TYR L 86 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.04 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.04 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 10 CYS A 501 CYS B 605 1555 1555 2.03 SSBOND 11 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 12 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 13 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 14 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 15 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 16 CYS C 218 CYS C 247 1555 1555 2.04 SSBOND 17 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 18 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 19 CYS C 378 CYS C 445 1555 1555 2.02 SSBOND 20 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 21 CYS C 501 CYS F 605 1555 1555 2.03 SSBOND 22 CYS E 54 CYS E 74 1555 1555 2.01 SSBOND 23 CYS E 119 CYS E 205 1555 1555 2.09 SSBOND 24 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 25 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 26 CYS E 218 CYS E 247 1555 1555 2.04 SSBOND 27 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 28 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 29 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 30 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 31 CYS E 501 CYS G 605 1555 1555 2.03 SSBOND 32 CYS F 598 CYS F 604 1555 1555 2.01 SSBOND 33 CYS G 598 CYS G 604 1555 1555 2.03 SSBOND 34 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 35 CYS L 23 CYS L 88 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 133 C1 NAG S 1 1555 1555 1.45 LINK ND2 ASN A 156 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN A 241 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 339 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 465 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN B 611 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN B 625 C1 NAG B 702 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 701 1555 1555 1.52 LINK ND2 ASN C 88 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 133 C1 NAG f 1 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG i 1 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG h 1 1555 1555 1.45 LINK ND2 ASN C 234 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN C 241 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN C 301 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN C 339 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG c 1 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG C 602 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 465 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG l 1 1555 1555 1.46 LINK ND2 ASN E 133 C1 NAG t 1 1555 1555 1.44 LINK ND2 ASN E 156 C1 NAG k 1 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG j 1 1555 1555 1.43 LINK ND2 ASN E 197 C1 NAG v 1 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG n 1 1555 1555 1.45 LINK ND2 ASN E 241 C1 NAG m 1 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG u 1 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG o 1 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG s 1 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG r 1 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG q 1 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 392 C1 NAG p 1 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 465 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN F 611 C1 NAG w 1 1555 1555 1.44 LINK ND2 ASN F 625 C1 NAG F 702 1555 1555 1.45 LINK ND2 ASN F 637 C1 NAG F 701 1555 1555 1.45 LINK ND2 ASN G 611 C1 NAG G 702 1555 1555 1.44 LINK ND2 ASN G 625 C1 NAG G 701 1555 1555 1.44 LINK ND2 ASN G 637 C1 NAG G 703 1555 1555 1.44 LINK C ASP H 100D N TYS H 100E 1555 1555 1.33 LINK C TYS H 100E N GLY H 100F 1555 1555 1.33 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.47 LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.45 LINK O6 BMA D 3 C1 MAN D 5 1555 1555 1.45 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.47 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45 LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.46 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.45 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.46 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.45 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.44 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.47 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.45 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.45 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.46 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.44 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.45 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.45 LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.45 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.45 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.45 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.44 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.47 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.45 LINK O4 NAG g 2 C1 BMA g 3 1555 1555 1.44 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.45 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.44 LINK O4 NAG i 2 C1 BMA i 3 1555 1555 1.45 LINK O6 BMA i 3 C1 MAN i 4 1555 1555 1.45 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.39 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.39 LINK O6 BMA j 3 C1 MAN j 4 1555 1555 1.40 LINK O3 BMA j 3 C1 MAN j 6 1555 1555 1.39 LINK O6 MAN j 4 C1 MAN j 5 1555 1555 1.40 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.45 LINK O4 NAG k 2 C1 BMA k 3 1555 1555 1.45 LINK O6 BMA k 3 C1 MAN k 4 1555 1555 1.45 LINK O4 NAG l 1 C1 NAG l 2 1555 1555 1.47 LINK O4 NAG m 1 C1 NAG m 2 1555 1555 1.45 LINK O4 NAG m 2 C1 BMA m 3 1555 1555 1.45 LINK O4 NAG n 1 C1 NAG n 2 1555 1555 1.45 LINK O4 NAG n 2 C1 BMA n 3 1555 1555 1.45 LINK O4 NAG o 1 C1 NAG o 2 1555 1555 1.45 LINK O4 NAG p 1 C1 NAG p 2 1555 1555 1.46 LINK O4 NAG q 1 C1 NAG q 2 1555 1555 1.46 LINK O4 NAG r 1 C1 NAG r 2 1555 1555 1.44 LINK O4 NAG r 2 C1 BMA r 3 1555 1555 1.45 LINK O4 NAG s 1 C1 NAG s 2 1555 1555 1.44 LINK O4 NAG t 1 C1 NAG t 2 1555 1555 1.46 LINK O4 NAG u 1 C1 NAG u 2 1555 1555 1.45 LINK O4 NAG u 2 C1 BMA u 3 1555 1555 1.45 LINK O4 NAG v 1 C1 NAG v 2 1555 1555 1.45 LINK O4 NAG w 1 C1 NAG w 2 1555 1555 1.45 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000