HEADER VIRAL PROTEIN 20-DEC-22 8FK5 TITLE CRYO-EM STRUCTURE OF PG9RSH DU011 FAB IN COMPLEX WITH BG505 DS- TITLE 2 SOSIP.664 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 3 CHAIN: A, B, F; COMPND 4 FRAGMENT: UNP RESIDUES 509-661; COMPND 5 SYNONYM: ENV POLYPROTEIN; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 9 CHAIN: C, G, I; COMPND 10 FRAGMENT: UNP RESIDUES 30-510; COMPND 11 SYNONYM: ENV POLYPROTEIN; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: IMMUNOBLOBULIN G1 FAB HEAVY CHAIN VARIABLE REGION COMPND 15 (FRAGMENT); COMPND 16 CHAIN: H; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: IMMUNOGLOBULIN LAMBDA-1 LIGHT CHAIN-LIKE; COMPND 20 CHAIN: L; COMPND 21 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_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 9 ORGANISM_TAXID: 11676; SOURCE 10 STRAIN: BG505; SOURCE 11 GENE: ENV; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 GENE: VHCH1; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 21 MOL_ID: 4; SOURCE 22 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 23 ORGANISM_COMMON: HUMAN; SOURCE 24 ORGANISM_TAXID: 9606; SOURCE 25 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS CD4, HIV-1, SOSIP, VACCINE, IMMUNE SYSTEM, LLAMA, V2 APEX, KEYWDS 2 THERAPEUTIC, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.GORMAN,P.D.KWONG JRNL AUTH G.T.HOLT,J.GORMAN,S.WANG,A.U.LOWEGARD,B.ZHANG,T.LIU,B.C.LIN, JRNL AUTH 2 M.K.LOUDER,M.S.FRENKEL,K.MCKEE,S.O'DELL,R.RAWI,C.-H.SHEN, JRNL AUTH 3 N.A.DORIA-ROSE,P.D.KWONG,B.R.DONALD JRNL TITL IMPROVED HIV-1 NEUTRALIZATION BREADTH AND POTENCY OF V2-APEX JRNL TITL 2 ANTIBODIES BY IN SILICO DESIGN JRNL REF CELL REP JRNL REFN ESSN 2211-1247 REMARK 2 REMARK 2 RESOLUTION. 3.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LEGINON, CRYOSPARC, PHENIX, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6NNF REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT 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) : 3.400 REMARK 3 NUMBER OF PARTICLES : 230180 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8FK5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000270857. 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 : CRYO-EM STRUCTURE OF PG9RSH REMARK 245 DU011 FAB IN COMPLEX WITH BG505 REMARK 245 DS-SOSIP.664 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 2.00 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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) : 63.75 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, F, G, I, H, L, D, E, 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 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 ALA A 512 REMARK 465 VAL A 513 REMARK 465 GLY A 514 REMARK 465 ILE A 515 REMARK 465 GLY A 516 REMARK 465 ALA A 517 REMARK 465 GLY A 547 REMARK 465 ILE A 548 REMARK 465 VAL A 549 REMARK 465 GLN A 550 REMARK 465 GLN A 551 REMARK 465 GLN A 552 REMARK 465 SER A 553 REMARK 465 ASN A 554 REMARK 465 LEU A 555 REMARK 465 LEU A 556 REMARK 465 ARG A 557 REMARK 465 ALA A 558 REMARK 465 PRO A 559 REMARK 465 GLU A 560 REMARK 465 ALA A 561 REMARK 465 GLN A 562 REMARK 465 GLN A 563 REMARK 465 HIS A 564 REMARK 465 LEU A 565 REMARK 465 LEU A 566 REMARK 465 LYS A 567 REMARK 465 LEU A 568 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 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 SER 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 ALA 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 ALA C 31 REMARK 465 GLU C 32 REMARK 465 GLU C 185A REMARK 465 ASN C 185B REMARK 465 GLN C 185C REMARK 465 GLY C 185D REMARK 465 ASN C 185E REMARK 465 ARG C 185F REMARK 465 SER C 185G REMARK 465 ASN C 185H REMARK 465 ASN C 185I REMARK 465 SER C 185J REMARK 465 ASN C 185K REMARK 465 THR C 400 REMARK 465 SER C 401 REMARK 465 VAL C 402 REMARK 465 GLN C 403 REMARK 465 GLY C 404 REMARK 465 SER C 405 REMARK 465 ASN C 406 REMARK 465 SER C 407 REMARK 465 THR C 408 REMARK 465 GLY C 409 REMARK 465 VAL C 506 REMARK 465 GLY C 507 REMARK 465 ARG C 508 REMARK 465 ARG C 509 REMARK 465 ARG C 510 REMARK 465 ARG C 511 REMARK 465 ARG C 512 REMARK 465 ARG C 513 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 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 SER 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 ALA 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 LEU F 568 REMARK 465 ALA G 31 REMARK 465 GLU G 32 REMARK 465 GLU G 185A REMARK 465 ASN G 185B REMARK 465 GLN G 185C REMARK 465 GLY G 185D REMARK 465 ASN G 185E REMARK 465 ARG G 185F REMARK 465 SER G 185G REMARK 465 ASN G 185H REMARK 465 ASN G 185I REMARK 465 SER G 185J REMARK 465 ASN G 185K REMARK 465 THR G 400 REMARK 465 SER G 401 REMARK 465 VAL G 402 REMARK 465 GLN G 403 REMARK 465 GLY G 404 REMARK 465 SER G 405 REMARK 465 ASN G 406 REMARK 465 SER G 407 REMARK 465 THR G 408 REMARK 465 GLY G 409 REMARK 465 VAL G 506 REMARK 465 GLY G 507 REMARK 465 ARG G 508 REMARK 465 ARG G 509 REMARK 465 ARG G 510 REMARK 465 ARG G 511 REMARK 465 ARG G 512 REMARK 465 ARG G 513 REMARK 465 ALA I 31 REMARK 465 GLU I 32 REMARK 465 GLU I 185A REMARK 465 ASN I 185B REMARK 465 GLN I 185C REMARK 465 GLY I 185D REMARK 465 ASN I 185E REMARK 465 ARG I 185F REMARK 465 SER I 185G REMARK 465 ASN I 185H REMARK 465 ASN I 185I REMARK 465 SER I 185J REMARK 465 ASN I 185K REMARK 465 THR I 400 REMARK 465 SER I 401 REMARK 465 VAL I 402 REMARK 465 GLN I 403 REMARK 465 GLY I 404 REMARK 465 SER I 405 REMARK 465 ASN I 406 REMARK 465 SER I 407 REMARK 465 THR I 408 REMARK 465 GLY I 409 REMARK 465 VAL I 506 REMARK 465 GLY I 507 REMARK 465 ARG I 508 REMARK 465 ARG I 509 REMARK 465 ARG I 510 REMARK 465 ARG I 511 REMARK 465 ARG I 512 REMARK 465 ARG I 513 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 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY 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 ALA 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 ILE 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 LYS H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 PRO H 213 REMARK 465 LYS H 214 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS 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 GLN L 1 REMARK 465 GLY L 107 REMARK 465 GLN L 108 REMARK 465 PRO L 109 REMARK 465 LYS L 110 REMARK 465 ALA L 111 REMARK 465 ALA L 112 REMARK 465 PRO L 113 REMARK 465 SER L 114 REMARK 465 VAL L 115 REMARK 465 THR L 116 REMARK 465 LEU L 117 REMARK 465 PHE L 118 REMARK 465 PRO L 119 REMARK 465 PRO L 120 REMARK 465 SER L 121 REMARK 465 SER L 122 REMARK 465 GLU L 123 REMARK 465 GLU L 124 REMARK 465 LEU L 125 REMARK 465 GLN L 126 REMARK 465 ALA L 127 REMARK 465 ASN L 128 REMARK 465 LYS L 129 REMARK 465 ALA L 130 REMARK 465 THR L 131 REMARK 465 LEU L 132 REMARK 465 VAL L 133 REMARK 465 CYS L 134 REMARK 465 LEU L 135 REMARK 465 ILE L 136 REMARK 465 SER L 137 REMARK 465 ASP L 138 REMARK 465 PHE L 139 REMARK 465 TYR L 140 REMARK 465 PRO L 141 REMARK 465 GLY L 142 REMARK 465 ALA L 143 REMARK 465 VAL L 144 REMARK 465 THR L 145 REMARK 465 VAL L 146 REMARK 465 ALA L 147 REMARK 465 TRP L 148 REMARK 465 LYS L 149 REMARK 465 ALA L 150 REMARK 465 ASP L 151 REMARK 465 SER L 152 REMARK 465 SER L 153 REMARK 465 PRO L 154 REMARK 465 VAL L 155 REMARK 465 LYS L 156 REMARK 465 ALA L 157 REMARK 465 GLY L 158 REMARK 465 VAL L 159 REMARK 465 GLU L 160 REMARK 465 THR L 161 REMARK 465 THR L 162 REMARK 465 THR L 163 REMARK 465 PRO L 164 REMARK 465 SER L 165 REMARK 465 LYS L 166 REMARK 465 GLN L 167 REMARK 465 SER L 168 REMARK 465 ASN L 169 REMARK 465 ASN L 170 REMARK 465 LYS L 171 REMARK 465 TYR L 172 REMARK 465 ALA L 173 REMARK 465 ALA L 174 REMARK 465 SER L 175 REMARK 465 SER L 176 REMARK 465 TYR L 177 REMARK 465 LEU L 178 REMARK 465 SER L 179 REMARK 465 LEU L 180 REMARK 465 THR L 181 REMARK 465 PRO L 182 REMARK 465 GLU L 183 REMARK 465 GLN L 184 REMARK 465 TRP L 185 REMARK 465 LYS L 186 REMARK 465 SER L 187 REMARK 465 HIS L 188 REMARK 465 LYS L 189 REMARK 465 SER L 190 REMARK 465 TYR L 191 REMARK 465 SER L 192 REMARK 465 CYS L 193 REMARK 465 GLN L 194 REMARK 465 VAL L 195 REMARK 465 THR L 196 REMARK 465 HIS L 197 REMARK 465 GLU L 198 REMARK 465 GLY L 199 REMARK 465 SER L 200 REMARK 465 THR L 201 REMARK 465 VAL L 202 REMARK 465 GLU L 203 REMARK 465 LYS L 204 REMARK 465 THR L 205 REMARK 465 VAL L 206 REMARK 465 ALA L 207 REMARK 465 PRO L 208 REMARK 465 THR L 209 REMARK 465 GLU L 210 REMARK 465 CYS L 211 REMARK 465 SER L 212 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 TYR C 61 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR G 61 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR I 61 CG CD1 CD2 CE1 CE2 CZ OH 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 ASP A 632 OG SER A 636 2.05 REMARK 500 OD1 ASP C 457 OG1 THR C 467 2.09 REMARK 500 NH2 ARG G 350 O ASN G 398 2.17 REMARK 500 OG1 THR B 627 OE1 GLN B 630 2.17 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 LEU A 523 17.36 59.18 REMARK 500 GLN C 258 -6.79 73.57 REMARK 500 GLU C 268 -8.01 74.58 REMARK 500 ASN C 363 -178.20 -69.37 REMARK 500 SER C 397 -2.73 68.16 REMARK 500 ILE F 622 -55.99 -124.50 REMARK 500 ALA G 73 -6.07 74.03 REMARK 500 ASN G 80 64.10 32.50 REMARK 500 LEU G 122 33.12 -98.47 REMARK 500 ASN G 137 43.17 -141.57 REMARK 500 GLN G 258 -7.04 73.71 REMARK 500 GLU G 268 -9.29 74.68 REMARK 500 MET G 426 -8.40 71.03 REMARK 500 LYS I 65 50.86 -92.40 REMARK 500 LEU I 122 55.44 -91.53 REMARK 500 MET I 150 58.37 -94.09 REMARK 500 GLN I 258 -8.56 73.29 REMARK 500 PHE I 376 -173.00 -170.86 REMARK 500 ASN I 462 0.62 -61.85 REMARK 500 VAL H 48 -63.14 -103.43 REMARK 500 ASP H 100I -162.37 -65.51 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-29248 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF PG9RSH DU011 FAB IN COMPLEX WITH BG505 DS- REMARK 900 SOSIP.664 DBREF 8FK5 A 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8FK5 B 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8FK5 C 31 513 UNP Q2N0S6 Q2N0S6_9HIV1 30 510 DBREF 8FK5 F 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8FK5 G 31 513 UNP Q2N0S6 Q2N0S6_9HIV1 30 510 DBREF 8FK5 I 31 513 UNP Q2N0S6 Q2N0S6_9HIV1 30 510 DBREF 8FK5 H 4 218 UNP A4F255 A4F255_HUMAN 1 232 DBREF 8FK5 L 1 212 UNP Q6PJG0 Q6PJG0_HUMAN 20 235 SEQADV 8FK5 PRO A 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8FK5 CYS A 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 8FK5 PRO B 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8FK5 CYS B 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 8FK5 CYS C 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 8FK5 ASN C 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8FK5 CYS C 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 8FK5 CYS C 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8FK5 ARG C 509 UNP Q2N0S6 GLU 506 CONFLICT SEQADV 8FK5 ARG C 510 UNP Q2N0S6 LYS 507 CONFLICT SEQADV 8FK5 ARG C 512 UNP Q2N0S6 ALA 509 CONFLICT SEQADV 8FK5 ARG C 513 UNP Q2N0S6 VAL 510 CONFLICT SEQADV 8FK5 PRO F 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8FK5 CYS F 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 8FK5 CYS G 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 8FK5 ASN G 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8FK5 CYS G 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 8FK5 CYS G 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8FK5 ARG G 509 UNP Q2N0S6 GLU 506 CONFLICT SEQADV 8FK5 ARG G 510 UNP Q2N0S6 LYS 507 CONFLICT SEQADV 8FK5 ARG G 512 UNP Q2N0S6 ALA 509 CONFLICT SEQADV 8FK5 ARG G 513 UNP Q2N0S6 VAL 510 CONFLICT SEQADV 8FK5 CYS I 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 8FK5 ASN I 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 8FK5 CYS I 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 8FK5 CYS I 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8FK5 ARG I 509 UNP Q2N0S6 GLU 506 CONFLICT SEQADV 8FK5 ARG I 510 UNP Q2N0S6 LYS 507 CONFLICT SEQADV 8FK5 ARG I 512 UNP Q2N0S6 ALA 509 CONFLICT SEQADV 8FK5 ARG I 513 UNP Q2N0S6 VAL 510 CONFLICT SEQADV 8FK5 GLU H 2 UNP A4F255 EXPRESSION TAG SEQADV 8FK5 ARG H 3 UNP A4F255 EXPRESSION TAG SEQADV 8FK5 VAL H 5 UNP A4F255 GLU 2 CONFLICT SEQADV 8FK5 SER H 16 UNP A4F255 LYS 13 CONFLICT SEQADV 8FK5 ALA H 23 UNP A4F255 THR 20 CONFLICT SEQADV 8FK5 ASP H 28 UNP A4F255 ILE 25 CONFLICT SEQADV 8FK5 ARG H 31 UNP A4F255 ASP 28 CONFLICT SEQADV 8FK5 GLN H 32 UNP A4F255 PHE 29 CONFLICT SEQADV 8FK5 GLN H 43 UNP A4F255 LYS 40 CONFLICT SEQADV 8FK5 TRP H 47 UNP A4F255 SER 44 CONFLICT SEQADV 8FK5 PHE H 50 UNP A4F255 THR 47 CONFLICT SEQADV 8FK5 LYS H 52 UNP A4F255 TRP 49 CONFLICT SEQADV 8FK5 TYR H 52A UNP A4F255 SER 50 CONFLICT SEQADV 8FK5 GLU H 56 UNP A4F255 ASN 54 CONFLICT SEQADV 8FK5 LYS H 57 UNP A4F255 GLU 55 CONFLICT SEQADV 8FK5 TYR H 58 UNP A4F255 LYS 56 CONFLICT SEQADV 8FK5 HIS H 59 UNP A4F255 TYR 57 CONFLICT SEQADV 8FK5 TRP H 64 UNP A4F255 THR 62 CONFLICT SEQADV 8FK5 LEU H 67 UNP A4F255 PHE 65 CONFLICT SEQADV 8FK5 SER H 68 UNP A4F255 ALA 66 CONFLICT SEQADV 8FK5 ASP H 76 UNP A4F255 ASN 74 CONFLICT SEQADV 8FK5 THR H 77 UNP A4F255 MET 75 CONFLICT SEQADV 8FK5 GLN H 81 UNP A4F255 HIS 79 CONFLICT SEQADV 8FK5 ASN H 82A UNP A4F255 ASP 81 CONFLICT SEQADV 8FK5 SER H 82B UNP A4F255 ASN 82 CONFLICT SEQADV 8FK5 VAL H 84 UNP A4F255 ALA 85 CONFLICT SEQADV 8FK5 THR H 89 UNP A4F255 VAL 90 CONFLICT SEQADV 8FK5 PHE H 91 UNP A4F255 TYR 92 CONFLICT SEQADV 8FK5 VAL H 93 UNP A4F255 ALA 94 CONFLICT SEQADV 8FK5 GLU H 95 UNP A4F255 ASP 96 CONFLICT SEQADV 8FK5 GLY H 97 UNP A4F255 INSERTION SEQADV 8FK5 GLY H 98 UNP A4F255 INSERTION SEQADV 8FK5 PRO H 99 UNP A4F255 INSERTION SEQADV 8FK5 TYR H 100A UNP A4F255 MET 99 CONFLICT SEQADV 8FK5 ARG H 100B UNP A4F255 ILE 100 CONFLICT SEQADV 8FK5 ASN H 100C UNP A4F255 THR 101 CONFLICT SEQADV 8FK5 GLY H 100D UNP A4F255 PHE 102 CONFLICT SEQADV 8FK5 TYR H 100E UNP A4F255 ALA 103 CONFLICT SEQADV 8FK5 TYR H 100F UNP A4F255 ARG 104 CONFLICT SEQADV 8FK5 TYS H 100G UNP A4F255 ILE 105 CONFLICT SEQADV 8FK5 TYS H 100H UNP A4F255 LEU 106 CONFLICT SEQADV 8FK5 H UNP A4F255 PRO 108 DELETION SEQADV 8FK5 H UNP A4F255 PRO 109 DELETION SEQADV 8FK5 TYR H 100K UNP A4F255 HIS 111 CONFLICT SEQADV 8FK5 ASP H 100L UNP A4F255 LYS 112 CONFLICT SEQADV 8FK5 TYR H 100N UNP A4F255 INSERTION SEQADV 8FK5 TYR H 100O UNP A4F255 INSERTION SEQADV 8FK5 ASN H 100P UNP A4F255 INSERTION SEQADV 8FK5 TYR H 100Q UNP A4F255 INSERTION SEQADV 8FK5 HIS H 100R UNP A4F255 INSERTION SEQADV 8FK5 TYR H 100S UNP A4F255 INSERTION SEQADV 8FK5 LYS H 105 UNP A4F255 GLN 119 CONFLICT SEQADV 8FK5 THR H 110 UNP A4F255 ILE 124 CONFLICT SEQADV 8FK5 GLY H 219 UNP A4F255 EXPRESSION TAG SEQADV 8FK5 LEU H 220 UNP A4F255 EXPRESSION TAG SEQADV 8FK5 GLU H 221 UNP A4F255 EXPRESSION TAG SEQADV 8FK5 VAL H 222 UNP A4F255 EXPRESSION TAG SEQADV 8FK5 LEU H 223 UNP A4F255 EXPRESSION TAG SEQADV 8FK5 PHE H 224 UNP A4F255 EXPRESSION TAG SEQADV 8FK5 GLN H 225 UNP A4F255 EXPRESSION TAG SEQADV 8FK5 GLN L 24 UNP Q6PJG0 THR 42 CONFLICT SEQADV 8FK5 ASN L 27A UNP Q6PJG0 THR 46 CONFLICT SEQADV 8FK5 GLY L 29 UNP Q6PJG0 SER 50 CONFLICT SEQADV 8FK5 TYR L 30 UNP Q6PJG0 HIS 51 CONFLICT SEQADV 8FK5 GLU L 31 UNP Q6PJG0 SER 52 CONFLICT SEQADV 8FK5 SER L 32 UNP Q6PJG0 LEU 53 CONFLICT SEQADV 8FK5 VAL L 46 UNP Q6PJG0 PHE 67 CONFLICT SEQADV 8FK5 VAL L 47 UNP Q6PJG0 LEU 68 CONFLICT SEQADV 8FK5 TYR L 49 UNP Q6PJG0 PHE 70 CONFLICT SEQADV 8FK5 ASP L 50 UNP Q6PJG0 GLU 71 CONFLICT SEQADV 8FK5 VAL L 51 UNP Q6PJG0 GLY 72 CONFLICT SEQADV 8FK5 GLY L 84 UNP Q6PJG0 ALA 105 CONFLICT SEQADV 8FK5 LYS L 89 UNP Q6PJG0 CYS 110 CONFLICT SEQADV 8FK5 LEU L 91 UNP Q6PJG0 TYR 112 CONFLICT SEQADV 8FK5 THR L 92 UNP Q6PJG0 VAL 113 CONFLICT SEQADV 8FK5 SER L 93 UNP Q6PJG0 GLY 114 CONFLICT SEQADV 8FK5 ARG L 94 UNP Q6PJG0 SER 115 CONFLICT SEQADV 8FK5 SER L 95 UNP Q6PJG0 GLY 116 CONFLICT SEQADV 8FK5 HIS L 95A UNP Q6PJG0 THR 117 CONFLICT SEQADV 8FK5 ARG L 96 UNP Q6PJG0 VAL 118 CONFLICT SEQADV 8FK5 THR L 100 UNP Q6PJG0 GLY 122 CONFLICT SEQADV 8FK5 LYS L 189 UNP Q6PJG0 ARG 212 CONFLICT SEQRES 1 A 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 A 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 A 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 A 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 A 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 A 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 A 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 A 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 A 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 A 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 A 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 A 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 B 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 B 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET 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 SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 B 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 B 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG 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 ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 C 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 C 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 C 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 C 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 C 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 C 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 C 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 C 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 C 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 C 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 C 481 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 C 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 C 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 C 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 C 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 C 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 C 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 C 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 C 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 C 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 C 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 C 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 C 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 C 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 C 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 C 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 C 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 C 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 C 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 C 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 C 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 C 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 C 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 C 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET 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 SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 F 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG 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 ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 G 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 G 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 G 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 G 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 G 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 G 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 G 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 G 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 G 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 G 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 G 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 G 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 G 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 G 481 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 G 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 G 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 G 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 G 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 G 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 G 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 G 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 G 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 G 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 G 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 G 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 G 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 G 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 G 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 G 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 G 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 G 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 G 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 G 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 G 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 G 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 G 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 G 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 I 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 I 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 I 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 I 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 I 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 I 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 I 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 I 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 I 481 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 I 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 I 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 I 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 I 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 I 481 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 I 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 I 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 I 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 I 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 I 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 I 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 I 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 I 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 I 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 I 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 I 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 I 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 I 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 I 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 I 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 I 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 I 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 I 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 I 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 I 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 I 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 I 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 I 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 H 248 GLU ARG LEU VAL GLU SER GLY GLY GLY VAL VAL GLN PRO SEQRES 2 H 248 GLY SER SER LEU ARG LEU SER CYS ALA ALA SER GLY PHE SEQRES 3 H 248 ASP PHE SER ARG GLN GLY MET HIS TRP VAL ARG GLN ALA SEQRES 4 H 248 PRO GLY GLN GLY LEU GLU TRP VAL ALA PHE ILE LYS TYR SEQRES 5 H 248 ASP GLY SER GLU LYS TYR HIS ALA ASP SER VAL TRP GLY SEQRES 6 H 248 ARG LEU SER ILE SER ARG ASP ASN SER LYS ASP THR LEU SEQRES 7 H 248 TYR LEU GLN MET ASN SER LEU ARG VAL GLU ASP THR ALA SEQRES 8 H 248 THR TYR PHE CYS VAL ARG GLU ALA GLY GLY PRO ASP TYR SEQRES 9 H 248 ARG ASN GLY TYR TYR TYS TYS ASP PHE TYR ASP GLY TYR SEQRES 10 H 248 TYR ASN TYR HIS TYR MET ASP VAL TRP GLY LYS GLY THR SEQRES 11 H 248 THR VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 12 H 248 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 13 H 248 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 14 H 248 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 15 H 248 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 16 H 248 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 17 H 248 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 18 H 248 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 19 H 248 GLU PRO LYS SER CYS ASP LYS GLY LEU GLU VAL LEU PHE SEQRES 20 H 248 GLN SEQRES 1 L 216 GLN SER ALA LEU THR GLN PRO ALA SER VAL SER GLY SER SEQRES 2 L 216 PRO GLY GLN SER ILE THR ILE SER CYS GLN GLY THR SER SEQRES 3 L 216 ASN ASP VAL GLY GLY TYR GLU SER VAL SER TRP TYR GLN SEQRES 4 L 216 GLN HIS PRO GLY LYS ALA PRO LYS VAL VAL ILE TYR ASP SEQRES 5 L 216 VAL SER LYS ARG PRO SER GLY VAL SER ASN ARG PHE SER SEQRES 6 L 216 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER SEQRES 7 L 216 GLY LEU GLN ALA GLU ASP GLU GLY ASP TYR TYR CYS LYS SEQRES 8 L 216 SER LEU THR SER ARG SER HIS ARG VAL PHE GLY THR 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 THR VAL ALA TRP LYS ALA ASP SER SEQRES 13 L 216 SER PRO VAL LYS ALA GLY VAL GLU THR THR THR 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 PRO GLU 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 THR GLU CYS SER HET TYS H 100G 16 HET TYS H 100H 16 HET NAG A 701 14 HET NAG A 702 14 HET NAG A 703 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 C 605 14 HET NAG C 606 14 HET NAG C 607 14 HET NAG C 608 14 HET NAG C 609 14 HET NAG C 610 14 HET NAG C 611 14 HET NAG F 701 14 HET NAG F 702 14 HET NAG G 601 14 HET NAG G 602 14 HET NAG G 603 14 HET NAG G 604 14 HET NAG G 605 14 HET NAG G 606 14 HET NAG G 607 14 HET NAG G 608 14 HET NAG G 609 14 HET NAG G 610 14 HET NAG G 611 14 HET NAG I 601 14 HET NAG I 602 14 HET NAG I 603 14 HET NAG I 604 14 HET NAG I 605 14 HET NAG I 606 14 HET NAG I 607 14 HET NAG I 608 14 HET NAG I 609 14 HET NAG D 1 14 HET NAG D 2 14 HET NAG E 1 14 HET NAG E 2 14 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 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 MAN Q 4 11 HET MAN Q 5 11 HET MAN Q 6 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 NAG U 1 14 HET NAG U 2 14 HET NAG V 1 14 HET NAG V 2 14 HET BMA V 3 11 HET MAN V 4 11 HET MAN V 5 11 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 MAN X 4 11 HET MAN X 5 11 HET MAN X 6 11 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 HET NAG a 1 14 HET NAG a 2 14 HET BMA a 3 11 HET MAN a 4 11 HET MAN a 5 11 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 MAN d 4 11 HET MAN d 5 11 HET NAG e 1 14 HET NAG e 2 14 HET BMA e 3 11 HET MAN e 4 11 HET MAN e 5 11 HET MAN e 6 11 HET MAN e 7 11 HET MAN e 8 11 HET MAN e 9 11 HETNAM TYS O-SULFO-L-TYROSINE HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 7 TYS 2(C9 H11 N O6 S) FORMUL 9 NAG 84(C8 H15 N O6) FORMUL 49 BMA 7(C6 H12 O6) FORMUL 49 MAN 21(C6 H12 O6) HELIX 1 AA1 LEU A 523 SER A 528 5 6 HELIX 2 AA2 THR A 529 MET A 535 1 7 HELIX 3 AA3 THR A 536 ARG A 542 1 7 HELIX 4 AA4 VAL A 570 TRP A 596 1 27 HELIX 5 AA5 ASN A 618 ASN A 625 1 8 HELIX 6 AA6 THR A 627 SER A 636 1 10 HELIX 7 AA7 TYR A 638 ASP A 664 1 27 HELIX 8 AA8 LEU B 523 GLY B 527 5 5 HELIX 9 AA9 GLY B 531 MET B 535 5 5 HELIX 10 AB1 THR B 536 ASN B 543 1 8 HELIX 11 AB2 TRP B 571 TRP B 596 1 26 HELIX 12 AB3 LEU B 619 ASP B 624 1 6 HELIX 13 AB4 THR B 627 ILE B 635 1 9 HELIX 14 AB5 TYR B 638 ASP B 664 1 27 HELIX 15 AB6 ASP C 57 GLU C 64 1 8 HELIX 16 AB7 ASN C 99 SER C 115 1 17 HELIX 17 AB8 THR C 139 ARG C 151 5 5 HELIX 18 AB9 ASN C 195 THR C 198 5 4 HELIX 19 AC1 SER C 334 PHE C 353 1 20 HELIX 20 AC2 ASP C 368 THR C 373 1 6 HELIX 21 AC3 THR C 387 LEU C 390 5 4 HELIX 22 AC4 ARG C 476 TYR C 484 1 9 HELIX 23 AC5 THR F 529 SER F 534 1 6 HELIX 24 AC6 THR F 536 ASN F 543 1 8 HELIX 25 AC7 GLY F 572 ILE F 595 1 24 HELIX 26 AC8 ASN F 618 ILE F 622 5 5 HELIX 27 AC9 THR F 627 SER F 636 1 10 HELIX 28 AD1 TYR F 638 ALA F 662 1 25 HELIX 29 AD2 ASP G 57 GLU G 62 1 6 HELIX 30 AD3 ASN G 98 SER G 115 1 18 HELIX 31 AD4 LEU G 122 CYS G 126 5 5 HELIX 32 AD5 THR G 139 ARG G 151 5 5 HELIX 33 AD6 ASN G 195 THR G 198 5 4 HELIX 34 AD7 LYS G 335 ARG G 350 1 16 HELIX 35 AD8 LYS G 351 PHE G 353 5 3 HELIX 36 AD9 ASP G 368 THR G 373 1 6 HELIX 37 AE1 THR G 387 LEU G 390 5 4 HELIX 38 AE2 ASP G 474 TYR G 484 1 11 HELIX 39 AE3 ASP I 57 THR I 63 1 7 HELIX 40 AE4 ASN I 98 SER I 115 1 18 HELIX 41 AE5 ASN I 195 THR I 198 5 4 HELIX 42 AE6 SER I 334 GLY I 354 1 21 HELIX 43 AE7 ASP I 368 THR I 373 1 6 HELIX 44 AE8 MET I 475 SER I 481 1 7 HELIX 45 AE9 ASP H 61 TRP H 64 5 4 HELIX 46 AF1 ARG H 83 THR H 87 5 5 HELIX 47 AF2 GLN L 79 GLU L 83 5 5 SHEET 1 AA1 3 ILE A 603 PRO A 609 0 SHEET 2 AA1 3 TRP C 35 TYR C 40 -1 O VAL C 36 N THR A 606 SHEET 3 AA1 3 LEU C 494 THR C 499 -1 O GLY C 495 N TYR C 39 SHEET 1 AA2 3 ILE B 603 PRO B 609 0 SHEET 2 AA2 3 TRP G 35 TYR G 40 -1 O VAL G 38 N CYS B 604 SHEET 3 AA2 3 LEU G 494 THR G 499 -1 O GLY G 495 N TYR G 39 SHEET 1 AA3 5 TRP C 45 ASP C 47 0 SHEET 2 AA3 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AA3 5 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AA3 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AA3 5 ILE C 84 LEU C 86 -1 N ILE C 84 O THR C 244 SHEET 1 AA4 3 VAL C 75 PRO C 76 0 SHEET 2 AA4 3 PHE C 53 SER C 56 1 N SER C 56 O VAL C 75 SHEET 3 AA4 3 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AA5 2 GLU C 91 ASN C 94 0 SHEET 2 AA5 2 THR C 236 CYS C 239 -1 O CYS C 239 N GLU C 91 SHEET 1 AA6 2 LYS C 121 LEU C 122 0 SHEET 2 AA6 2 CYS C 201 THR C 202 -1 O CYS C 201 N LEU C 122 SHEET 1 AA7 5 LYS C 169 TYR C 177 0 SHEET 2 AA7 5 LEU C 154 THR C 162 -1 N LYS C 155 O PHE C 176 SHEET 3 AA7 5 LEU C 129 ASN C 133 -1 N GLN C 130 O SER C 158 SHEET 4 AA7 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AA7 5 VAL C 181 GLN C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AA812 LEU C 260 LEU C 261 0 SHEET 2 AA812 MET C 271 ARG C 273 0 SHEET 3 AA812 ILE C 284 ILE C 309 -1 O LEU C 285 N ARG C 273 SHEET 4 AA812 GLN C 315 ILE C 323 -1 O ILE C 323 N ASN C 301 SHEET 5 AA812 ALA C 329 VAL C 333 -1 O ASN C 332 N ASN C 295 SHEET 6 AA812 ILE C 358 PHE C 361 0 SHEET 7 AA812 HIS C 374 CYS C 378 0 SHEET 8 AA812 GLU C 381 CYS C 385 -1 O PHE C 383 N PHE C 376 SHEET 9 AA812 SER C 393 TRP C 395 -1 O TRP C 395 N ILE C 359 SHEET 10 AA812 ILE C 414 ILE C 420 -1 O ARG C 419 N TYR C 384 SHEET 11 AA812 GLY C 441 ARG C 456 -1 O SER C 447 N ILE C 294 SHEET 12 AA812 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 1 AA9 3 ILE F 603 PRO F 609 0 SHEET 2 AA9 3 TRP I 35 TYR I 40 -1 O VAL I 38 N CYS F 604 SHEET 3 AA9 3 LEU I 494 THR I 499 -1 O GLY I 495 N TYR I 39 SHEET 1 AB1 5 TRP G 45 ASP G 47 0 SHEET 2 AB1 5 TYR G 486 ILE G 491 -1 O LYS G 490 N LYS G 46 SHEET 3 AB1 5 PHE G 223 CYS G 228 -1 N LEU G 226 O LYS G 487 SHEET 4 AB1 5 VAL G 242 VAL G 245 -1 O SER G 243 N LYS G 227 SHEET 5 AB1 5 GLU G 83 LEU G 86 -1 N ILE G 84 O THR G 244 SHEET 1 AB2 3 VAL G 75 PRO G 76 0 SHEET 2 AB2 3 PHE G 53 SER G 56 1 N SER G 56 O VAL G 75 SHEET 3 AB2 3 HIS G 216 CYS G 218 -1 O CYS G 218 N PHE G 53 SHEET 1 AB3 2 GLU G 91 ASN G 94 0 SHEET 2 AB3 2 THR G 236 CYS G 239 -1 O CYS G 239 N GLU G 91 SHEET 1 AB4 5 LYS G 169 TYR G 177 0 SHEET 2 AB4 5 LEU G 154 THR G 162 -1 N MET G 161 O GLN G 170 SHEET 3 AB4 5 LEU G 129 ASN G 133 -1 N THR G 132 O ASN G 156 SHEET 4 AB4 5 GLU G 190 LEU G 193 -1 O TYR G 191 N LEU G 129 SHEET 5 AB4 5 VAL G 181 GLN G 183 -1 N VAL G 182 O ARG G 192 SHEET 1 AB5 3 THR G 202 GLN G 203 0 SHEET 2 AB5 3 MET G 434 TYR G 435 1 O TYR G 435 N THR G 202 SHEET 3 AB5 3 ILE G 423 ILE G 424 -1 N ILE G 424 O MET G 434 SHEET 1 AB6 7 LEU G 259 LEU G 260 0 SHEET 2 AB6 7 MET G 271 ARG G 273 0 SHEET 3 AB6 7 ILE G 284 GLN G 287 -1 O LEU G 285 N ARG G 273 SHEET 4 AB6 7 ILE G 358 PHE G 361 0 SHEET 5 AB6 7 SER G 393 TRP G 395 -1 O TRP G 395 N ILE G 359 SHEET 6 AB6 7 GLY G 451 ASP G 457 -1 O LEU G 454 N ILE G 284 SHEET 7 AB6 7 THR G 465 PRO G 470 -1 O ARG G 469 N THR G 455 SHEET 1 AB7 6 HIS G 374 CYS G 378 0 SHEET 2 AB7 6 GLU G 381 CYS G 385 -1 O PHE G 383 N PHE G 376 SHEET 3 AB7 6 SER G 413 ILE G 420 -1 O ARG G 419 N TYR G 384 SHEET 4 AB7 6 ALA G 329 SER G 334 -1 N VAL G 333 O ILE G 414 SHEET 5 AB7 6 ILE G 294 ARG G 298 -1 N ASN G 295 O ASN G 332 SHEET 6 AB7 6 ILE G 443 SER G 447 -1 O SER G 447 N ILE G 294 SHEET 1 AB8 2 ARG G 304 GLY G 312 0 SHEET 2 AB8 2 GLN G 315 THR G 320 -1 O PHE G 317 N ILE G 307 SHEET 1 AB9 5 TRP I 45 ASP I 47 0 SHEET 2 AB9 5 TYR I 486 ILE I 491 -1 O LYS I 490 N LYS I 46 SHEET 3 AB9 5 PHE I 223 CYS I 228 -1 N LEU I 226 O LYS I 487 SHEET 4 AB9 5 VAL I 242 VAL I 245 -1 O SER I 243 N LYS I 227 SHEET 5 AB9 5 ILE I 84 LEU I 86 -1 N ILE I 84 O THR I 244 SHEET 1 AC1 3 VAL I 75 PRO I 76 0 SHEET 2 AC1 3 PHE I 53 SER I 56 1 N SER I 56 O VAL I 75 SHEET 3 AC1 3 HIS I 216 CYS I 218 -1 O CYS I 218 N PHE I 53 SHEET 1 AC2 2 GLU I 91 ASN I 94 0 SHEET 2 AC2 2 THR I 236 CYS I 239 -1 O CYS I 239 N GLU I 91 SHEET 1 AC3 5 GLN I 130 ASN I 133 0 SHEET 2 AC3 5 LEU I 154 THR I 162 -1 O ASN I 156 N THR I 132 SHEET 3 AC3 5 LYS I 168 TYR I 177 -1 O VAL I 172 N PHE I 159 SHEET 4 AC3 5 TYR H 100E PHE H 100J 1 O TYR H 100F N LYS I 169 SHEET 5 AC3 5 ASP H 100 ARG H 100B-1 N ARG H 100B O TYR H 100E SHEET 1 AC4 2 VAL I 181 GLN I 183 0 SHEET 2 AC4 2 TYR I 191 LEU I 193 -1 O ARG I 192 N VAL I 182 SHEET 1 AC5 3 THR I 202 GLN I 203 0 SHEET 2 AC5 3 MET I 434 TYR I 435 1 O TYR I 435 N THR I 202 SHEET 3 AC5 3 ILE I 423 ILE I 424 -1 N ILE I 424 O MET I 434 SHEET 1 AC6 7 LEU I 259 LEU I 261 0 SHEET 2 AC6 7 MET I 271 ARG I 273 0 SHEET 3 AC6 7 ILE I 284 VAL I 292 -1 O LEU I 285 N ARG I 273 SHEET 4 AC6 7 ILE I 359 PHE I 361 0 SHEET 5 AC6 7 SER I 393 TRP I 395 -1 O TRP I 395 N ILE I 359 SHEET 6 AC6 7 ILE I 449 ARG I 456 -1 O LEU I 454 N ILE I 284 SHEET 7 AC6 7 GLU I 466 PRO I 470 -1 O ARG I 469 N THR I 455 SHEET 1 AC7 6 HIS I 374 CYS I 378 0 SHEET 2 AC7 6 GLU I 381 CYS I 385 -1 O PHE I 383 N PHE I 376 SHEET 3 AC7 6 ILE I 414 LYS I 421 -1 O ARG I 419 N TYR I 384 SHEET 4 AC7 6 ALA I 329 VAL I 333 -1 N VAL I 333 O ILE I 414 SHEET 5 AC7 6 ILE I 294 ARG I 298 -1 N ASN I 295 O ASN I 332 SHEET 6 AC7 6 ILE I 443 VAL I 446 -1 O ILE I 443 N ARG I 298 SHEET 1 AC8 2 ASN I 301 GLY I 312 0 SHEET 2 AC8 2 GLN I 315 ILE I 323 -1 O ILE I 323 N ASN I 301 SHEET 1 AC9 4 ARG H 3 SER H 7 0 SHEET 2 AC9 4 SER H 17 SER H 25 -1 O ALA H 23 N VAL H 5 SHEET 3 AC9 4 THR H 77 ASN H 82A-1 O MET H 82 N LEU H 18 SHEET 4 AC9 4 LEU H 67 ASP H 72 -1 N SER H 70 O TYR H 79 SHEET 1 AD1 7 GLY H 10 VAL H 12 0 SHEET 2 AD1 7 MET H 34 GLN H 39 0 SHEET 3 AD1 7 GLU H 46 ILE H 51 -1 O VAL H 48 N TRP H 36 SHEET 4 AD1 7 LYS H 57 HIS H 59 -1 O TYR H 58 N PHE H 50 SHEET 5 AD1 7 ALA H 88 GLY H 98 -1 O PHE H 91 N VAL H 37 SHEET 6 AD1 7 TYR H 100O TRP H 103 -1 O TYR H 100Q N ALA H 96 SHEET 7 AD1 7 THR H 107 VAL H 111 -1 O THR H 107 N TYR H 90 SHEET 1 AD2 6 SER L 9 GLY L 13 0 SHEET 2 AD2 6 VAL L 33 GLN L 38 0 SHEET 3 AD2 6 LYS L 45 ILE L 48 -1 O LYS L 45 N GLN L 37 SHEET 4 AD2 6 GLY L 84 LEU L 91 -1 O LYS L 89 N SER L 34 SHEET 5 AD2 6 ARG L 96 PHE L 98 -1 O VAL L 97 N SER L 90 SHEET 6 AD2 6 THR L 102 VAL L 106 -1 O LEU L 104 N GLY L 84 SHEET 1 AD3 3 ILE L 19 GLN L 24 0 SHEET 2 AD3 3 THR L 70 ILE L 75 -1 O ALA L 71 N CYS L 23 SHEET 3 AD3 3 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SSBOND 1 CYS A 598 CYS A 604 1555 1555 2.03 SSBOND 2 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 3 CYS B 605 CYS G 501 1555 1555 2.04 SSBOND 4 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 5 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 6 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 7 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 8 CYS C 201 CYS C 433 1555 1555 2.03 SSBOND 9 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 10 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 11 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 12 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 13 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 14 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 15 CYS F 605 CYS I 501 1555 1555 2.03 SSBOND 16 CYS G 54 CYS G 74 1555 1555 2.03 SSBOND 17 CYS G 119 CYS G 205 1555 1555 2.03 SSBOND 18 CYS G 126 CYS G 196 1555 1555 2.03 SSBOND 19 CYS G 131 CYS G 157 1555 1555 2.03 SSBOND 20 CYS G 201 CYS G 433 1555 1555 2.03 SSBOND 21 CYS G 218 CYS G 247 1555 1555 2.04 SSBOND 22 CYS G 228 CYS G 239 1555 1555 2.03 SSBOND 23 CYS G 296 CYS G 331 1555 1555 2.03 SSBOND 24 CYS G 378 CYS G 445 1555 1555 2.03 SSBOND 25 CYS G 385 CYS G 418 1555 1555 2.03 SSBOND 26 CYS I 54 CYS I 74 1555 1555 2.03 SSBOND 27 CYS I 119 CYS I 205 1555 1555 2.03 SSBOND 28 CYS I 126 CYS I 196 1555 1555 2.03 SSBOND 29 CYS I 131 CYS I 157 1555 1555 2.03 SSBOND 30 CYS I 201 CYS I 433 1555 1555 2.03 SSBOND 31 CYS I 218 CYS I 247 1555 1555 2.04 SSBOND 32 CYS I 228 CYS I 239 1555 1555 2.03 SSBOND 33 CYS I 296 CYS I 331 1555 1555 2.03 SSBOND 34 CYS I 378 CYS I 445 1555 1555 2.03 SSBOND 35 CYS I 385 CYS I 418 1555 1555 2.03 SSBOND 36 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 37 CYS L 23 CYS L 88 1555 1555 2.03 LINK ND2 ASN A 611 C1 NAG A 701 1555 1555 1.44 LINK ND2 ASN A 618 C1 NAG A 703 1555 1555 1.44 LINK ND2 ASN A 637 C1 NAG A 702 1555 1555 1.44 LINK ND2 ASN B 611 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 702 1555 1555 1.44 LINK ND2 ASN C 88 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 133 C1 NAG C 602 1555 1555 1.44 LINK ND2 ASN C 137 C1 NAG C 611 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN C 295 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN C 301 C1 NAG C 605 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG C 606 1555 1555 1.44 LINK ND2 ASN C 339 C1 NAG C 607 1555 1555 1.44 LINK ND2 ASN C 355 C1 NAG C 608 1555 1555 1.45 LINK ND2 ASN C 363 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG C 609 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG C 610 1555 1555 1.44 LINK ND2 ASN F 611 C1 NAG F 701 1555 1555 1.44 LINK ND2 ASN F 637 C1 NAG F 702 1555 1555 1.44 LINK ND2 ASN G 88 C1 NAG G 601 1555 1555 1.44 LINK ND2 ASN G 133 C1 NAG G 602 1555 1555 1.44 LINK ND2 ASN G 137 C1 NAG G 610 1555 1555 1.44 LINK ND2 ASN G 156 C1 NAG G 603 1555 1555 1.44 LINK ND2 ASN G 160 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN G 197 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN G 234 C1 NAG G 604 1555 1555 1.44 LINK ND2 ASN G 262 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN G 276 C1 NAG G 611 1555 1555 1.44 LINK ND2 ASN G 295 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN G 301 C1 NAG G 605 1555 1555 1.44 LINK ND2 ASN G 332 C1 NAG G 606 1555 1555 1.44 LINK ND2 ASN G 339 C1 NAG G 607 1555 1555 1.44 LINK ND2 ASN G 355 C1 NAG G 608 1555 1555 1.45 LINK ND2 ASN G 363 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN G 386 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN G 392 C1 NAG G 609 1555 1555 1.44 LINK ND2 ASN G 448 C1 NAG U 1 1555 1555 1.45 LINK ND2 ASN I 88 C1 NAG I 601 1555 1555 1.44 LINK ND2 ASN I 133 C1 NAG I 602 1555 1555 1.44 LINK ND2 ASN I 137 C1 NAG I 609 1555 1555 1.44 LINK ND2 ASN I 156 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN I 160 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN I 197 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN I 234 C1 NAG I 603 1555 1555 1.44 LINK ND2 ASN I 262 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN I 276 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN I 295 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN I 301 C1 NAG I 604 1555 1555 1.44 LINK ND2 ASN I 332 C1 NAG I 605 1555 1555 1.44 LINK ND2 ASN I 339 C1 NAG I 606 1555 1555 1.44 LINK ND2 ASN I 355 C1 NAG I 607 1555 1555 1.44 LINK ND2 ASN I 363 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN I 386 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN I 392 C1 NAG I 608 1555 1555 1.44 LINK ND2 ASN I 448 C1 NAG c 1 1555 1555 1.44 LINK C TYR H 100F N TYS H 100G 1555 1555 1.34 LINK C TYS H 100G N TYS H 100H 1555 1555 1.33 LINK C TYS H 100H N ASP H 100I 1555 1555 1.33 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.45 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.44 LINK O3 BMA J 3 C1 MAN J 4 1555 1555 1.45 LINK O6 BMA J 3 C1 MAN J 6 1555 1555 1.45 LINK O2 MAN J 4 C1 MAN J 5 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.44 LINK O3 BMA Q 3 C1 MAN Q 4 1555 1555 1.45 LINK O6 BMA Q 3 C1 MAN Q 6 1555 1555 1.45 LINK O2 MAN Q 4 C1 MAN Q 5 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 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.44 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.44 LINK O3 BMA V 3 C1 MAN V 4 1555 1555 1.45 LINK O6 BMA V 3 C1 MAN V 5 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.45 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.44 LINK O3 BMA X 3 C1 MAN X 4 1555 1555 1.45 LINK O6 BMA X 3 C1 MAN X 6 1555 1555 1.44 LINK O2 MAN X 4 C1 MAN X 5 1555 1555 1.44 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.45 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 LINK O4 NAG a 2 C1 BMA a 3 1555 1555 1.44 LINK O3 BMA a 3 C1 MAN a 4 1555 1555 1.45 LINK O6 BMA a 3 C1 MAN a 5 1555 1555 1.45 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.45 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.45 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 e 1 C1 NAG e 2 1555 1555 1.45 LINK O4 NAG e 2 C1 BMA e 3 1555 1555 1.44 LINK O6 BMA e 3 C1 MAN e 4 1555 1555 1.45 LINK O3 BMA e 3 C1 MAN e 8 1555 1555 1.45 LINK O6 MAN e 4 C1 MAN e 5 1555 1555 1.44 LINK O3 MAN e 4 C1 MAN e 7 1555 1555 1.45 LINK O2 MAN e 5 C1 MAN e 6 1555 1555 1.44 LINK O2 MAN e 8 C1 MAN e 9 1555 1555 1.50 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