HEADER VIRAL PROTEIN/IMMUNE SYSTEM 21-MAR-25 9NVX TITLE CRYO-EM STRUCTURE OF RHESUS ANTIBODY CI91-APEX1.01 IN COMPLEX WITH HIV TITLE 2 ENV TRIMER Q23-APEX-GT2 CAVEAT 9NVX COMPND MOL_ID: 1; COMPND 2 MOLECULE: CI91-APEX1.01 HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: CI91-APEX1.01 LAMBDA CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HIV ENVELOPE GP120; COMPND 11 CHAIN: b, d, f; COMPND 12 SYNONYM: ENV POLYPROTEIN; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: HIV ENVELOPE GP41 ECTODOMAIN; COMPND 16 CHAIN: c, e, g; COMPND 17 SYNONYM: ENV POLYPROTEIN; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_TAXID: 9544; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 8 ORGANISM_TAXID: 9544; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 13 ORGANISM_TAXID: 11676; SOURCE 14 GENE: ENV; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 4; SOURCE 18 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 19 ORGANISM_TAXID: 11676; SOURCE 20 GENE: ENV; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS IMMUNE COMPLEX, NEUTRALIZATION, V2 APEX, GERMLINE-TARGETING, VIRAL KEYWDS 2 PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR R.S.ROARK,L.S.SHAPIRO,P.D.KWONG REVDAT 1 01-APR-26 9NVX 0 JRNL AUTH N.MISHRA,R.S.ROARK,P.D.KWONG,G.M.SHAW,R.ANDRABI JRNL TITL GERMLINE-TARGETING HIV IMMUNOGEN INDUCES CROSS-NEUTRALIZING JRNL TITL 2 ANTIBODIES IN OUTBRED MACAQUES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC 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) : 3.000 REMARK 3 NUMBER OF PARTICLES : 88000 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 9NVX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1000294244. 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 : CI91-APEX1.01 FAB IN COMPLEX REMARK 245 WITH HIV 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 : 7.50 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 BIOQUANTUM (6K X REMARK 245 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 : OTHER 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, b, c, d, e, f, g, A, B, REMARK 350 AND CHAINS: C, D, E, F, G, I, J, K, M, REMARK 350 AND CHAINS: N, O, P, Q, R, S, T, U, V, W, REMARK 350 AND CHAINS: X, Y, Z, a, h, i, j, k, l, REMARK 350 AND CHAINS: m, n, o, p, q, r, s, t 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 H 139 REMARK 465 SER H 140 REMARK 465 THR H 141 REMARK 465 LYS H 142 REMARK 465 GLY H 143 REMARK 465 PRO H 144 REMARK 465 SER H 145 REMARK 465 VAL H 146 REMARK 465 PHE H 147 REMARK 465 PRO H 148 REMARK 465 LEU H 149 REMARK 465 ALA H 150 REMARK 465 PRO H 151 REMARK 465 SER H 152 REMARK 465 SER H 153 REMARK 465 ARG H 154 REMARK 465 SER H 155 REMARK 465 THR H 156 REMARK 465 SER H 157 REMARK 465 GLU H 158 REMARK 465 SER H 159 REMARK 465 THR H 160 REMARK 465 ALA H 161 REMARK 465 ALA H 162 REMARK 465 LEU H 163 REMARK 465 GLY H 164 REMARK 465 CYS H 165 REMARK 465 LEU H 166 REMARK 465 VAL H 167 REMARK 465 LYS H 168 REMARK 465 ASP H 169 REMARK 465 TYR H 170 REMARK 465 PHE H 171 REMARK 465 PRO H 172 REMARK 465 GLU H 173 REMARK 465 PRO H 174 REMARK 465 VAL H 175 REMARK 465 THR H 176 REMARK 465 VAL H 177 REMARK 465 SER H 178 REMARK 465 TRP H 179 REMARK 465 ASN H 180 REMARK 465 SER H 181 REMARK 465 GLY H 182 REMARK 465 SER H 183 REMARK 465 LEU H 184 REMARK 465 THR H 185 REMARK 465 SER H 186 REMARK 465 GLY H 187 REMARK 465 VAL H 188 REMARK 465 HIS H 189 REMARK 465 THR H 190 REMARK 465 PHE H 191 REMARK 465 PRO H 192 REMARK 465 ALA H 193 REMARK 465 VAL H 194 REMARK 465 LEU H 195 REMARK 465 GLN H 196 REMARK 465 SER H 197 REMARK 465 SER H 198 REMARK 465 GLY H 199 REMARK 465 LEU H 200 REMARK 465 TYR H 201 REMARK 465 SER H 202 REMARK 465 LEU H 203 REMARK 465 SER H 204 REMARK 465 SER H 205 REMARK 465 VAL H 206 REMARK 465 VAL H 207 REMARK 465 THR H 208 REMARK 465 VAL H 209 REMARK 465 PRO H 210 REMARK 465 SER H 211 REMARK 465 SER H 212 REMARK 465 SER H 213 REMARK 465 LEU H 214 REMARK 465 GLY H 215 REMARK 465 THR H 216 REMARK 465 GLN H 217 REMARK 465 THR H 218 REMARK 465 TYR H 219 REMARK 465 VAL H 220 REMARK 465 CYS H 221 REMARK 465 ASN H 222 REMARK 465 VAL H 223 REMARK 465 ASN H 224 REMARK 465 HIS H 225 REMARK 465 LYS H 226 REMARK 465 PRO H 227 REMARK 465 SER H 228 REMARK 465 ASN H 229 REMARK 465 THR H 230 REMARK 465 LYS H 231 REMARK 465 VAL H 232 REMARK 465 ASP H 233 REMARK 465 LYS H 234 REMARK 465 ARG H 235 REMARK 465 VAL H 236 REMARK 465 GLU H 237 REMARK 465 ILE H 238 REMARK 465 LYS H 239 REMARK 465 THR H 240 REMARK 465 CYS H 241 REMARK 465 GLY H 242 REMARK 465 GLY H 243 REMARK 465 GLY H 244 REMARK 465 LEU H 245 REMARK 465 GLU H 246 REMARK 465 VAL H 247 REMARK 465 LEU H 248 REMARK 465 PHE H 249 REMARK 465 GLN H 250 REMARK 465 THR L 128 REMARK 465 VAL L 129 REMARK 465 LEU L 130 REMARK 465 GLY L 131 REMARK 465 GLN L 132 REMARK 465 PRO L 133 REMARK 465 LYS L 134 REMARK 465 ALA L 135 REMARK 465 ALA L 136 REMARK 465 PRO L 137 REMARK 465 SER L 138 REMARK 465 VAL L 139 REMARK 465 THR L 140 REMARK 465 LEU L 141 REMARK 465 PHE L 142 REMARK 465 PRO L 143 REMARK 465 PRO L 144 REMARK 465 SER L 145 REMARK 465 SER L 146 REMARK 465 GLU L 147 REMARK 465 GLU L 148 REMARK 465 LEU L 149 REMARK 465 GLN L 150 REMARK 465 ALA L 151 REMARK 465 ASN L 152 REMARK 465 LYS L 153 REMARK 465 ALA L 154 REMARK 465 THR L 155 REMARK 465 LEU L 156 REMARK 465 VAL L 157 REMARK 465 CYS L 158 REMARK 465 LEU L 159 REMARK 465 ILE L 160 REMARK 465 SER L 161 REMARK 465 ASP L 162 REMARK 465 PHE L 163 REMARK 465 TYR L 164 REMARK 465 PRO L 165 REMARK 465 GLY L 166 REMARK 465 ALA L 167 REMARK 465 VAL L 168 REMARK 465 GLU L 169 REMARK 465 VAL L 170 REMARK 465 ALA L 171 REMARK 465 TRP L 172 REMARK 465 LYS L 173 REMARK 465 ALA L 174 REMARK 465 ASP L 175 REMARK 465 GLY L 176 REMARK 465 SER L 177 REMARK 465 ALA L 178 REMARK 465 VAL L 179 REMARK 465 ASN L 180 REMARK 465 ALA L 181 REMARK 465 GLY L 182 REMARK 465 VAL L 183 REMARK 465 GLU L 184 REMARK 465 THR L 185 REMARK 465 THR L 186 REMARK 465 LYS L 187 REMARK 465 PRO L 188 REMARK 465 SER L 189 REMARK 465 LYS L 190 REMARK 465 GLN L 191 REMARK 465 SER L 192 REMARK 465 ASN L 193 REMARK 465 ASN L 194 REMARK 465 LYS L 195 REMARK 465 TYR L 196 REMARK 465 ALA L 197 REMARK 465 ALA L 198 REMARK 465 SER L 199 REMARK 465 SER L 200 REMARK 465 TYR L 201 REMARK 465 LEU L 202 REMARK 465 SER L 203 REMARK 465 LEU L 204 REMARK 465 THR L 205 REMARK 465 SER L 206 REMARK 465 ASP L 207 REMARK 465 GLN L 208 REMARK 465 TRP L 209 REMARK 465 LYS L 210 REMARK 465 SER L 211 REMARK 465 HIS L 212 REMARK 465 LYS L 213 REMARK 465 SER L 214 REMARK 465 TYR L 215 REMARK 465 SER L 216 REMARK 465 CYS L 217 REMARK 465 GLN L 218 REMARK 465 VAL L 219 REMARK 465 THR L 220 REMARK 465 HIS L 221 REMARK 465 GLU L 222 REMARK 465 GLY L 223 REMARK 465 SER L 224 REMARK 465 THR L 225 REMARK 465 VAL L 226 REMARK 465 GLU L 227 REMARK 465 LYS L 228 REMARK 465 THR L 229 REMARK 465 VAL L 230 REMARK 465 ALA L 231 REMARK 465 PRO L 232 REMARK 465 ALA L 233 REMARK 465 GLU L 234 REMARK 465 CYS L 235 REMARK 465 SER L 236 REMARK 465 ALA b 31 REMARK 465 GLU b 32 REMARK 465 ALA b 60 REMARK 465 TYR b 61 REMARK 465 GLU b 62 REMARK 465 THR b 63 REMARK 465 SER b 144 REMARK 465 VAL b 145 REMARK 465 ASN b 146 REMARK 465 THR b 147 REMARK 465 THR b 148 REMARK 465 GLY b 149 REMARK 465 ASP b 403 REMARK 465 THR b 404 REMARK 465 ASP b 405 REMARK 465 SER b 406 REMARK 465 THR b 407 REMARK 465 GLN b 408 REMARK 465 GLU b 409 REMARK 465 ARG b 504 REMARK 465 VAL b 505 REMARK 465 VAL b 506 REMARK 465 GLU b 507 REMARK 465 GLY b 508 REMARK 465 GLY b 509 REMARK 465 GLY b 510 REMARK 465 GLY b 511 REMARK 465 SER b 512 REMARK 465 GLY b 513 REMARK 465 GLY b 514 REMARK 465 GLY b 515 REMARK 465 GLY b 516 REMARK 465 SER b 517 REMARK 465 ALA c 512 REMARK 465 VAL c 513 REMARK 465 GLY c 514 REMARK 465 ILE c 515 REMARK 465 GLY c 516 REMARK 465 ALA c 517 REMARK 465 VAL c 518 REMARK 465 GLY c 547 REMARK 465 ILE c 548 REMARK 465 VAL c 549 REMARK 465 GLN c 550 REMARK 465 PRO c 551 REMARK 465 GLN c 552 REMARK 465 ASN c 553 REMARK 465 ASN c 554 REMARK 465 LEU c 555 REMARK 465 LEU c 556 REMARK 465 ARG c 557 REMARK 465 ALA c 558 REMARK 465 PRO c 559 REMARK 465 GLU c 560 REMARK 465 ALA c 561 REMARK 465 GLN c 562 REMARK 465 ALA c 662 REMARK 465 LEU c 663 REMARK 465 ASP c 664 REMARK 465 ALA d 31 REMARK 465 GLU d 32 REMARK 465 ALA d 60 REMARK 465 TYR d 61 REMARK 465 GLU d 62 REMARK 465 THR d 63 REMARK 465 SER d 144 REMARK 465 VAL d 145 REMARK 465 ASN d 146 REMARK 465 THR d 147 REMARK 465 THR d 148 REMARK 465 GLY d 149 REMARK 465 ASP d 403 REMARK 465 THR d 404 REMARK 465 ASP d 405 REMARK 465 SER d 406 REMARK 465 THR d 407 REMARK 465 GLN d 408 REMARK 465 GLU d 409 REMARK 465 ARG d 504 REMARK 465 VAL d 505 REMARK 465 VAL d 506 REMARK 465 GLU d 507 REMARK 465 GLY d 508 REMARK 465 GLY d 509 REMARK 465 GLY d 510 REMARK 465 GLY d 511 REMARK 465 SER d 512 REMARK 465 GLY d 513 REMARK 465 GLY d 514 REMARK 465 GLY d 515 REMARK 465 GLY d 516 REMARK 465 SER d 517 REMARK 465 ALA e 512 REMARK 465 VAL e 513 REMARK 465 GLY e 514 REMARK 465 ILE e 515 REMARK 465 GLY e 516 REMARK 465 ALA e 517 REMARK 465 VAL e 518 REMARK 465 GLY e 547 REMARK 465 ILE e 548 REMARK 465 VAL e 549 REMARK 465 GLN e 550 REMARK 465 PRO e 551 REMARK 465 GLN e 552 REMARK 465 ASN e 553 REMARK 465 ASN e 554 REMARK 465 LEU e 555 REMARK 465 LEU e 556 REMARK 465 ARG e 557 REMARK 465 ALA e 558 REMARK 465 PRO e 559 REMARK 465 GLU e 560 REMARK 465 ALA e 561 REMARK 465 GLN e 562 REMARK 465 ALA e 662 REMARK 465 LEU e 663 REMARK 465 ASP e 664 REMARK 465 ALA f 31 REMARK 465 GLU f 32 REMARK 465 ALA f 60 REMARK 465 TYR f 61 REMARK 465 GLU f 62 REMARK 465 THR f 63 REMARK 465 SER f 144 REMARK 465 VAL f 145 REMARK 465 ASN f 146 REMARK 465 THR f 147 REMARK 465 THR f 148 REMARK 465 GLY f 149 REMARK 465 ASP f 403 REMARK 465 THR f 404 REMARK 465 ASP f 405 REMARK 465 SER f 406 REMARK 465 THR f 407 REMARK 465 GLN f 408 REMARK 465 GLU f 409 REMARK 465 ARG f 504 REMARK 465 VAL f 505 REMARK 465 VAL f 506 REMARK 465 GLU f 507 REMARK 465 GLY f 508 REMARK 465 GLY f 509 REMARK 465 GLY f 510 REMARK 465 GLY f 511 REMARK 465 SER f 512 REMARK 465 GLY f 513 REMARK 465 GLY f 514 REMARK 465 GLY f 515 REMARK 465 GLY f 516 REMARK 465 SER f 517 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 GLY g 547 REMARK 465 ILE g 548 REMARK 465 VAL g 549 REMARK 465 GLN g 550 REMARK 465 PRO 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 ALA g 561 REMARK 465 GLN g 562 REMARK 465 ALA g 662 REMARK 465 LEU g 663 REMARK 465 ASP g 664 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 ND2 ASN b 386 O5 NAG O 1 2.18 REMARK 500 REMARK 500 REMARK: NULL 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 GLN L 48 CB - CA - C ANGL. DEV. = -13.0 DEGREES REMARK 500 TYR f 217 CB - CA - C ANGL. DEV. = -14.4 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 ASP H 36 51.81 -99.93 REMARK 500 ASP H 114 -65.07 -105.82 REMARK 500 ALA L 49 70.30 56.05 REMARK 500 ASP L 57 -17.77 70.58 REMARK 500 ARG L 65 -17.39 -147.89 REMARK 500 GLN b 258 -11.19 72.97 REMARK 500 ASN b 411 -66.19 -91.44 REMARK 500 ASN b 425 75.58 -102.14 REMARK 500 GLN b 432 58.92 39.36 REMARK 500 ASP b 461 -10.14 76.07 REMARK 500 GLU d 186 -11.78 79.79 REMARK 500 ASN d 187 -32.23 -137.75 REMARK 500 SER d 189 -150.75 50.03 REMARK 500 GLN d 258 -10.97 71.90 REMARK 500 SER d 274 139.32 -172.14 REMARK 500 TRP d 338 -72.45 -80.12 REMARK 500 CYS d 378 51.89 -91.47 REMARK 500 THR d 387 2.70 -68.17 REMARK 500 LYS d 502 6.65 -62.46 REMARK 500 ALA f 55 115.53 -163.07 REMARK 500 LEU f 122 32.99 -91.15 REMARK 500 SER f 199 149.77 -173.86 REMARK 500 GLN f 258 -11.40 73.21 REMARK 500 SER f 274 140.68 -170.78 REMARK 500 CYS f 378 54.03 -92.79 REMARK 500 THR f 387 -24.53 78.30 REMARK 500 THR f 400 118.94 -160.86 REMARK 500 ASN f 425 75.18 -119.67 REMARK 500 ASP f 461 -4.25 72.33 REMARK 500 LYS f 502 38.54 73.85 REMARK 500 ARG g 520 -150.95 52.68 REMARK 500 ASN g 625 30.49 -141.29 REMARK 500 GLU g 659 63.58 66.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-49867 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF RHESUS ANTIBODY CI91-APEX1.01 IN COMPLEX WITH REMARK 900 HIV ENV TRIMER Q23-APEX-GT2 DBREF 9NVX H 1 250 PDB 9NVX 9NVX 1 250 DBREF 9NVX L 1 236 PDB 9NVX 9NVX 1 236 DBREF 9NVX b 31 517 UNP O55774 O55774_HV1 30 507 DBREF 9NVX c 512 664 UNP O55774 O55774_HV1 502 654 DBREF 9NVX d 31 517 UNP O55774 O55774_HV1 30 507 DBREF 9NVX e 512 664 UNP O55774 O55774_HV1 502 654 DBREF 9NVX f 31 517 UNP O55774 O55774_HV1 30 507 DBREF 9NVX g 512 664 UNP O55774 O55774_HV1 502 654 SEQADV 9NVX ALA b 31 UNP O55774 VAL 30 CONFLICT SEQADV 9NVX GLU b 49 UNP O55774 ASP 48 CONFLICT SEQADV 9NVX ARG b 132 UNP O55774 THR 131 CONFLICT SEQADV 9NVX GLU b 153 UNP O55774 GLY 144 CONFLICT SEQADV 9NVX THR b 158 UNP O55774 SER 149 CONFLICT SEQADV 9NVX CYS b 201 UNP O55774 ILE 193 CONFLICT SEQADV 9NVX ALA b 219 UNP O55774 THR 211 CONFLICT SEQADV 9NVX TYR b 302 UNP O55774 ASN 294 CONFLICT SEQADV 9NVX MET b 320 UNP O55774 THR 310 CONFLICT SEQADV 9NVX SER b 334 UNP O55774 THR 325 CONFLICT SEQADV 9NVX CYS b 433 UNP O55774 ALA 423 CONFLICT SEQADV 9NVX CYS b 501 UNP O55774 ALA 491 CONFLICT SEQADV 9NVX GLY b 508 UNP O55774 ARG 498 CONFLICT SEQADV 9NVX GLY b 509 UNP O55774 GLU 499 CONFLICT SEQADV 9NVX GLY b 510 UNP O55774 LYS 500 CONFLICT SEQADV 9NVX GLY b 511 UNP O55774 ARG 501 CONFLICT SEQADV 9NVX SER b 512 UNP O55774 ALA 502 CONFLICT SEQADV 9NVX GLY b 513 UNP O55774 VAL 503 CONFLICT SEQADV 9NVX GLY b 515 UNP O55774 ILE 505 CONFLICT SEQADV 9NVX SER b 517 UNP O55774 ALA 507 CONFLICT SEQADV 9NVX ARG c 519 UNP O55774 PHE 509 CONFLICT SEQADV 9NVX ARG c 520 UNP O55774 LEU 510 CONFLICT SEQADV 9NVX ALA c 533 UNP O55774 THR 523 CONFLICT SEQADV 9NVX PRO c 551 UNP O55774 GLN 541 CONFLICT SEQADV 9NVX PRO c 559 UNP O55774 ILE 549 CONFLICT SEQADV 9NVX GLY c 569 UNP O55774 THR 559 CONFLICT SEQADV 9NVX CYS c 605 UNP O55774 THR 595 CONFLICT SEQADV 9NVX GLY c 636 UNP O55774 ASN 626 CONFLICT SEQADV 9NVX ALA c 662 UNP O55774 GLU 652 CONFLICT SEQADV 9NVX ALA d 31 UNP O55774 VAL 30 CONFLICT SEQADV 9NVX GLU d 49 UNP O55774 ASP 48 CONFLICT SEQADV 9NVX ARG d 132 UNP O55774 THR 131 CONFLICT SEQADV 9NVX GLU d 153 UNP O55774 GLY 144 CONFLICT SEQADV 9NVX THR d 158 UNP O55774 SER 149 CONFLICT SEQADV 9NVX CYS d 201 UNP O55774 ILE 193 CONFLICT SEQADV 9NVX ALA d 219 UNP O55774 THR 211 CONFLICT SEQADV 9NVX TYR d 302 UNP O55774 ASN 294 CONFLICT SEQADV 9NVX MET d 320 UNP O55774 THR 310 CONFLICT SEQADV 9NVX SER d 334 UNP O55774 THR 325 CONFLICT SEQADV 9NVX CYS d 433 UNP O55774 ALA 423 CONFLICT SEQADV 9NVX CYS d 501 UNP O55774 ALA 491 CONFLICT SEQADV 9NVX GLY d 508 UNP O55774 ARG 498 CONFLICT SEQADV 9NVX GLY d 509 UNP O55774 GLU 499 CONFLICT SEQADV 9NVX GLY d 510 UNP O55774 LYS 500 CONFLICT SEQADV 9NVX GLY d 511 UNP O55774 ARG 501 CONFLICT SEQADV 9NVX SER d 512 UNP O55774 ALA 502 CONFLICT SEQADV 9NVX GLY d 513 UNP O55774 VAL 503 CONFLICT SEQADV 9NVX GLY d 515 UNP O55774 ILE 505 CONFLICT SEQADV 9NVX SER d 517 UNP O55774 ALA 507 CONFLICT SEQADV 9NVX ARG e 519 UNP O55774 PHE 509 CONFLICT SEQADV 9NVX ARG e 520 UNP O55774 LEU 510 CONFLICT SEQADV 9NVX ALA e 533 UNP O55774 THR 523 CONFLICT SEQADV 9NVX PRO e 551 UNP O55774 GLN 541 CONFLICT SEQADV 9NVX PRO e 559 UNP O55774 ILE 549 CONFLICT SEQADV 9NVX GLY e 569 UNP O55774 THR 559 CONFLICT SEQADV 9NVX CYS e 605 UNP O55774 THR 595 CONFLICT SEQADV 9NVX GLY e 636 UNP O55774 ASN 626 CONFLICT SEQADV 9NVX ALA e 662 UNP O55774 GLU 652 CONFLICT SEQADV 9NVX ALA f 31 UNP O55774 VAL 30 CONFLICT SEQADV 9NVX GLU f 49 UNP O55774 ASP 48 CONFLICT SEQADV 9NVX ARG f 132 UNP O55774 THR 131 CONFLICT SEQADV 9NVX GLU f 153 UNP O55774 GLY 144 CONFLICT SEQADV 9NVX THR f 158 UNP O55774 SER 149 CONFLICT SEQADV 9NVX CYS f 201 UNP O55774 ILE 193 CONFLICT SEQADV 9NVX ALA f 219 UNP O55774 THR 211 CONFLICT SEQADV 9NVX TYR f 302 UNP O55774 ASN 294 CONFLICT SEQADV 9NVX MET f 320 UNP O55774 THR 310 CONFLICT SEQADV 9NVX SER f 334 UNP O55774 THR 325 CONFLICT SEQADV 9NVX CYS f 433 UNP O55774 ALA 423 CONFLICT SEQADV 9NVX CYS f 501 UNP O55774 ALA 491 CONFLICT SEQADV 9NVX GLY f 508 UNP O55774 ARG 498 CONFLICT SEQADV 9NVX GLY f 509 UNP O55774 GLU 499 CONFLICT SEQADV 9NVX GLY f 510 UNP O55774 LYS 500 CONFLICT SEQADV 9NVX GLY f 511 UNP O55774 ARG 501 CONFLICT SEQADV 9NVX SER f 512 UNP O55774 ALA 502 CONFLICT SEQADV 9NVX GLY f 513 UNP O55774 VAL 503 CONFLICT SEQADV 9NVX GLY f 515 UNP O55774 ILE 505 CONFLICT SEQADV 9NVX SER f 517 UNP O55774 ALA 507 CONFLICT SEQADV 9NVX ARG g 519 UNP O55774 PHE 509 CONFLICT SEQADV 9NVX ARG g 520 UNP O55774 LEU 510 CONFLICT SEQADV 9NVX ALA g 533 UNP O55774 THR 523 CONFLICT SEQADV 9NVX PRO g 551 UNP O55774 GLN 541 CONFLICT SEQADV 9NVX PRO g 559 UNP O55774 ILE 549 CONFLICT SEQADV 9NVX GLY g 569 UNP O55774 THR 559 CONFLICT SEQADV 9NVX CYS g 605 UNP O55774 THR 595 CONFLICT SEQADV 9NVX GLY g 636 UNP O55774 ASN 626 CONFLICT SEQADV 9NVX ALA g 662 UNP O55774 GLU 652 CONFLICT SEQRES 1 H 244 GLU VAL GLN LEU MET GLU SER GLY GLY ASP LEU VAL GLN SEQRES 2 H 244 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 244 PHE PHE PHE SER ASP TYR TYR MET GLN TRP VAL ARG GLN SEQRES 4 H 244 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY LEU ILE ARG SEQRES 5 H 244 ASN LYS ALA ASP SER GLU THR THR GLU TYR ALA LEU SER SEQRES 6 H 244 VAL LYS GLY ARG VAL THR LEU SER ARG ASP ASP SER ASN SEQRES 7 H 244 SER ILE THR TYR LEU GLN MET ASN ASN LEU LYS THR GLU SEQRES 8 H 244 ASP THR ALA VAL TYR TYR CYS ALA ARG THR TYR PHE THR SEQRES 9 H 244 TYR TYR TYS ASP GLY GLY ASP TYS THR GLU GLU ARG THR SEQRES 10 H 244 TYR PHE ASP SER TRP GLY GLN GLY VAL LEU VAL THR VAL SEQRES 11 H 244 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 12 H 244 ALA PRO SER SER ARG SER THR SER GLU SER THR ALA ALA SEQRES 13 H 244 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 14 H 244 THR VAL SER TRP ASN SER GLY SER LEU THR SER GLY VAL SEQRES 15 H 244 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 16 H 244 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 17 H 244 GLY THR GLN THR TYR VAL CYS ASN VAL ASN HIS LYS PRO SEQRES 18 H 244 SER ASN THR LYS VAL ASP LYS ARG VAL GLU ILE LYS THR SEQRES 19 H 244 CYS GLY GLY GLY LEU GLU VAL LEU PHE GLN SEQRES 1 L 218 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL SER SEQRES 2 L 218 PRO GLY GLN THR ALA ARG ILE THR CYS GLY GLY ASP ASN SEQRES 3 L 218 ILE GLY SER THR ILE VAL HIS TRP TYR GLN GLN LYS PRO SEQRES 4 L 218 PRO GLN ALA PRO VAL VAL VAL ILE TYR ASP ASP ARG GLU SEQRES 5 L 218 ARG PRO SER GLY ILE PRO GLN ARG PHE SER GLY SER LYS SEQRES 6 L 218 SER GLY THR THR ALA THR LEU THR ILE SER GLY VAL GLU SEQRES 7 L 218 ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN VAL TRP ASP SEQRES 8 L 218 GLY SER SER ASP HIS PRO VAL PHE PHE GLY GLY GLY THR SEQRES 9 L 218 ARG LEU THR VAL LEU THR VAL LEU GLY GLN PRO LYS ALA SEQRES 10 L 218 ALA PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU SEQRES 11 L 218 LEU GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER SEQRES 12 L 218 ASP PHE TYR PRO GLY ALA VAL GLU VAL ALA TRP LYS ALA SEQRES 13 L 218 ASP GLY SER ALA VAL ASN ALA GLY VAL GLU THR THR LYS SEQRES 14 L 218 PRO SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER SEQRES 15 L 218 TYR LEU SER LEU THR SER ASP GLN TRP LYS SER HIS LYS SEQRES 16 L 218 SER TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL SEQRES 17 L 218 GLU LYS THR VAL ALA PRO ALA GLU CYS SER SEQRES 1 b 478 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 b 478 VAL TRP ARG ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 b 478 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 b 478 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 b 478 GLU ILE HIS LEU ASP ASN VAL THR GLU LYS PHE ASN MET SEQRES 6 b 478 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 b 478 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 b 478 LEU THR PRO LEU CYS VAL THR LEU HIS CYS ARG ASN VAL SEQRES 9 b 478 THR SER VAL ASN THR THR GLY ASP ARG GLU GLU LEU LYS SEQRES 10 b 478 ASN CYS THR PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 b 478 ARG GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE SEQRES 12 b 478 VAL PRO ILE ASN GLU ASN GLN GLY SER GLU TYR ARG LEU SEQRES 13 b 478 ILE ASN CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO SEQRES 14 b 478 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA SEQRES 15 b 478 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP GLU GLY SEQRES 16 b 478 PHE ASN GLY THR GLY LEU CYS LYS ASN VAL SER THR VAL SEQRES 17 b 478 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 18 b 478 LEU LEU LEU ASN GLY SER LEU ALA GLU LYS ASN ILE THR SEQRES 19 b 478 ILE ARG SER GLU ASN ILE THR ASN ASN ALA LYS ILE ILE SEQRES 20 b 478 ILE VAL GLN LEU VAL GLN PRO VAL THR ILE LYS CYS ILE SEQRES 21 b 478 ARG PRO ASN ASN TYR THR ARG LYS SER ILE ARG ILE GLY SEQRES 22 b 478 PRO GLY GLN ALA PHE TYR ALA MET GLY ASP ILE ILE GLY SEQRES 23 b 478 ASP ILE ARG GLN ALA HIS CYS ASN VAL SER ARG SER ARG SEQRES 24 b 478 TRP ASN LYS THR LEU GLN GLU VAL ALA GLU LYS LEU ARG SEQRES 25 b 478 THR TYR PHE GLY ASN LYS THR ILE ILE PHE ALA ASN SER SEQRES 26 b 478 SER GLY GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN SEQRES 27 b 478 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 28 b 478 PHE ASN SER THR TRP TYR VAL ASN SER THR TRP ASN ASP SEQRES 29 b 478 THR ASP SER THR GLN GLU SER ASN ASP THR ILE THR LEU SEQRES 30 b 478 PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG SEQRES 31 b 478 ALA GLY GLN CYS MET TYR ALA PRO PRO ILE PRO GLY VAL SEQRES 32 b 478 ILE LYS CYS GLU SER ASN ILE THR GLY LEU LEU LEU THR SEQRES 33 b 478 ARG ASP GLY GLY LYS ASP ASN ASN VAL ASN GLU THR PHE SEQRES 34 b 478 ARG PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER SEQRES 35 b 478 GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE GLU PRO LEU SEQRES 36 b 478 GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLU SEQRES 37 b 478 GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 1 c 153 ALA VAL GLY ILE GLY ALA VAL ARG ARG GLY PHE LEU GLY SEQRES 2 c 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ILE THR LEU SEQRES 3 c 153 THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL GLN SEQRES 4 c 153 PRO GLN ASN ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 c 153 HIS LEU LEU LYS LEU GLY VAL TRP GLY ILE LYS GLN LEU SEQRES 6 c 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 c 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 c 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 c 153 ASN LYS SER LEU ASP GLU ILE TRP ASN ASN MET THR TRP SEQRES 10 c 153 LEU GLN TRP ASP LYS GLU ILE GLY ASN TYR THR GLN LEU SEQRES 11 c 153 ILE TYR ARG LEU ILE GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 c 153 LYS ASN GLU LYS GLU LEU LEU ALA LEU ASP SEQRES 1 d 478 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 d 478 VAL TRP ARG ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 d 478 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 d 478 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 d 478 GLU ILE HIS LEU ASP ASN VAL THR GLU LYS PHE ASN MET SEQRES 6 d 478 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 d 478 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 d 478 LEU THR PRO LEU CYS VAL THR LEU HIS CYS ARG ASN VAL SEQRES 9 d 478 THR SER VAL ASN THR THR GLY ASP ARG GLU GLU LEU LYS SEQRES 10 d 478 ASN CYS THR PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 d 478 ARG GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE SEQRES 12 d 478 VAL PRO ILE ASN GLU ASN GLN GLY SER GLU TYR ARG LEU SEQRES 13 d 478 ILE ASN CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO SEQRES 14 d 478 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA SEQRES 15 d 478 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP GLU GLY SEQRES 16 d 478 PHE ASN GLY THR GLY LEU CYS LYS ASN VAL SER THR VAL SEQRES 17 d 478 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 18 d 478 LEU LEU LEU ASN GLY SER LEU ALA GLU LYS ASN ILE THR SEQRES 19 d 478 ILE ARG SER GLU ASN ILE THR ASN ASN ALA LYS ILE ILE SEQRES 20 d 478 ILE VAL GLN LEU VAL GLN PRO VAL THR ILE LYS CYS ILE SEQRES 21 d 478 ARG PRO ASN ASN TYR THR ARG LYS SER ILE ARG ILE GLY SEQRES 22 d 478 PRO GLY GLN ALA PHE TYR ALA MET GLY ASP ILE ILE GLY SEQRES 23 d 478 ASP ILE ARG GLN ALA HIS CYS ASN VAL SER ARG SER ARG SEQRES 24 d 478 TRP ASN LYS THR LEU GLN GLU VAL ALA GLU LYS LEU ARG SEQRES 25 d 478 THR TYR PHE GLY ASN LYS THR ILE ILE PHE ALA ASN SER SEQRES 26 d 478 SER GLY GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN SEQRES 27 d 478 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 28 d 478 PHE ASN SER THR TRP TYR VAL ASN SER THR TRP ASN ASP SEQRES 29 d 478 THR ASP SER THR GLN GLU SER ASN ASP THR ILE THR LEU SEQRES 30 d 478 PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG SEQRES 31 d 478 ALA GLY GLN CYS MET TYR ALA PRO PRO ILE PRO GLY VAL SEQRES 32 d 478 ILE LYS CYS GLU SER ASN ILE THR GLY LEU LEU LEU THR SEQRES 33 d 478 ARG ASP GLY GLY LYS ASP ASN ASN VAL ASN GLU THR PHE SEQRES 34 d 478 ARG PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER SEQRES 35 d 478 GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE GLU PRO LEU SEQRES 36 d 478 GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLU SEQRES 37 d 478 GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 1 e 153 ALA VAL GLY ILE GLY ALA VAL ARG ARG GLY PHE LEU GLY SEQRES 2 e 153 ALA ALA GLY SER THR MET GLY ALA ALA SER ILE THR LEU SEQRES 3 e 153 THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL GLN SEQRES 4 e 153 PRO GLN ASN ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 e 153 HIS LEU LEU LYS LEU GLY VAL TRP GLY ILE LYS GLN LEU SEQRES 6 e 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 e 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 e 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 e 153 ASN LYS SER LEU ASP GLU ILE TRP ASN ASN MET THR TRP SEQRES 10 e 153 LEU GLN TRP ASP LYS GLU ILE GLY ASN TYR THR GLN LEU SEQRES 11 e 153 ILE TYR ARG LEU ILE GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 e 153 LYS ASN GLU LYS GLU LEU LEU ALA LEU ASP SEQRES 1 f 478 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 f 478 VAL TRP ARG ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 f 478 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 f 478 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 f 478 GLU ILE HIS LEU ASP ASN VAL THR GLU LYS PHE ASN MET SEQRES 6 f 478 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 f 478 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 f 478 LEU THR PRO LEU CYS VAL THR LEU HIS CYS ARG ASN VAL SEQRES 9 f 478 THR SER VAL ASN THR THR GLY ASP ARG GLU GLU LEU LYS SEQRES 10 f 478 ASN CYS THR PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 f 478 ARG GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE SEQRES 12 f 478 VAL PRO ILE ASN GLU ASN GLN GLY SER GLU TYR ARG LEU SEQRES 13 f 478 ILE ASN CYS ASN THR SER ALA CYS THR GLN ALA CYS PRO SEQRES 14 f 478 LYS VAL SER PHE GLU PRO ILE PRO ILE HIS TYR CYS ALA SEQRES 15 f 478 PRO ALA GLY PHE ALA ILE LEU LYS CYS LYS ASP GLU GLY SEQRES 16 f 478 PHE ASN GLY THR GLY LEU CYS LYS ASN VAL SER THR VAL SEQRES 17 f 478 GLN CYS THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN SEQRES 18 f 478 LEU LEU LEU ASN GLY SER LEU ALA GLU LYS ASN ILE THR SEQRES 19 f 478 ILE ARG SER GLU ASN ILE THR ASN ASN ALA LYS ILE ILE SEQRES 20 f 478 ILE VAL GLN LEU VAL GLN PRO VAL THR ILE LYS CYS ILE SEQRES 21 f 478 ARG PRO ASN ASN TYR THR ARG LYS SER ILE ARG ILE GLY SEQRES 22 f 478 PRO GLY GLN ALA PHE TYR ALA MET GLY ASP ILE ILE GLY SEQRES 23 f 478 ASP ILE ARG GLN ALA HIS CYS ASN VAL SER ARG SER ARG SEQRES 24 f 478 TRP ASN LYS THR LEU GLN GLU VAL ALA GLU LYS LEU ARG SEQRES 25 f 478 THR TYR PHE GLY ASN LYS THR ILE ILE PHE ALA ASN SER SEQRES 26 f 478 SER GLY GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN SEQRES 27 f 478 CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU SEQRES 28 f 478 PHE ASN SER THR TRP TYR VAL ASN SER THR TRP ASN ASP SEQRES 29 f 478 THR ASP SER THR GLN GLU SER ASN ASP THR ILE THR LEU SEQRES 30 f 478 PRO CYS ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG SEQRES 31 f 478 ALA GLY GLN CYS MET TYR ALA PRO PRO ILE PRO GLY VAL SEQRES 32 f 478 ILE LYS CYS GLU SER ASN ILE THR GLY LEU LEU LEU THR SEQRES 33 f 478 ARG ASP GLY GLY LYS ASP ASN ASN VAL ASN GLU THR PHE SEQRES 34 f 478 ARG PRO GLY GLY GLY ASP MET ARG ASP ASN TRP ARG SER SEQRES 35 f 478 GLU LEU TYR LYS TYR LYS VAL VAL GLU ILE GLU PRO LEU SEQRES 36 f 478 GLY VAL ALA PRO THR ARG CYS LYS ARG ARG VAL VAL GLU SEQRES 37 f 478 GLY GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 1 g 153 ALA VAL GLY ILE GLY ALA VAL ARG ARG 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 GLN LEU LEU SER GLY ILE VAL GLN SEQRES 4 g 153 PRO GLN ASN ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 g 153 HIS LEU LEU LYS LEU GLY VAL TRP GLY ILE LYS GLN LEU SEQRES 6 g 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG 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 GLY 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 ALA LEU ASP HET TYS H 113 16 HET TYS H 118 16 HET NAG A 1 14 HET NAG A 2 14 HET NAG B 1 14 HET NAG B 2 14 HET BMA B 3 11 HET NAG C 1 14 HET NAG C 2 14 HET BMA C 3 11 HET MAN C 4 11 HET NAG D 1 14 HET NAG D 2 14 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 NAG I 1 14 HET NAG I 2 14 HET NAG J 1 14 HET NAG J 2 14 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 NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET MAN R 4 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 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 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 NAG h 1 14 HET NAG h 2 14 HET NAG i 1 14 HET NAG i 2 14 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET MAN j 4 11 HET NAG k 1 14 HET NAG k 2 14 HET NAG l 1 14 HET NAG l 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 NAG r 1 14 HET NAG r 2 14 HET NAG s 1 14 HET NAG s 2 14 HET BMA s 3 11 HET NAG t 1 14 HET NAG t 2 14 HET NAG b 601 14 HET NAG b 602 14 HET NAG b 603 14 HET NAG b 604 14 HET NAG b 605 14 HET NAG b 606 14 HET NAG b 607 14 HET NAG c 701 14 HET NAG c 702 14 HET NAG c 703 14 HET NAG d 601 14 HET NAG d 602 14 HET NAG d 603 14 HET NAG d 604 14 HET NAG d 605 14 HET NAG d 606 14 HET NAG d 607 14 HET NAG d 608 14 HET NAG e 701 14 HET NAG e 702 14 HET NAG e 703 14 HET NAG f 601 14 HET NAG f 602 14 HET NAG f 603 14 HET NAG f 604 14 HET NAG f 605 14 HET NAG f 606 14 HET NAG f 607 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 1 TYS 2(C9 H11 N O6 S) FORMUL 9 NAG 107(C8 H15 N O6) FORMUL 10 BMA 7(C6 H12 O6) FORMUL 11 MAN 3(C6 H12 O6) HELIX 1 AA1 PHE H 29 TYR H 37 5 5 HELIX 2 AA2 ASN H 58 SER H 62 5 5 HELIX 3 AA3 ASP H 82 ASN H 84 5 3 HELIX 4 AA4 LYS H 95 THR H 99 5 5 HELIX 5 AA5 ASN L 27 THR L 37 5 5 HELIX 6 AA6 GLU L 95 GLU L 99 5 5 HELIX 7 AA7 ALA b 70 CYS b 74 5 5 HELIX 8 AA8 ASN b 98 LYS b 117 1 20 HELIX 9 AA9 LEU b 122 CYS b 126 5 5 HELIX 10 AB1 ASN b 185 GLY b 188A 5 5 HELIX 11 AB2 SER b 334 THR b 351 1 18 HELIX 12 AB3 ASP b 368 THR b 373 1 6 HELIX 13 AB4 MET b 475 TYR b 484 1 10 HELIX 14 AB5 THR c 529 SER c 534 1 6 HELIX 15 AB6 LEU c 537 ARG c 542 1 6 HELIX 16 AB7 GLN c 543 LEU c 545 5 3 HELIX 17 AB8 GLY c 569 TRP c 596 1 28 HELIX 18 AB9 ASP c 620 ASN c 625 1 6 HELIX 19 AC1 TRP c 628 TYR c 643 1 16 HELIX 20 AC2 ARG c 644 LYS c 658 1 15 HELIX 21 AC3 ALA d 70 CYS d 74 5 5 HELIX 22 AC4 ASN d 98 LYS d 117 1 20 HELIX 23 AC5 LEU d 122 CYS d 126 5 5 HELIX 24 AC6 SER d 334 THR d 351 1 18 HELIX 25 AC7 ASP d 368 THR d 373 1 6 HELIX 26 AC8 THR d 387 LEU d 390 5 4 HELIX 27 AC9 MET d 475 TYR d 484 1 10 HELIX 28 AD1 THR e 529 SER e 534 1 6 HELIX 29 AD2 THR e 536 GLN e 543 1 8 HELIX 30 AD3 GLY e 569 TRP e 596 1 28 HELIX 31 AD4 SER e 618 ASN e 625 1 8 HELIX 32 AD5 THR e 627 ILE e 635 1 9 HELIX 33 AD6 ILE e 635 LYS e 658 1 24 HELIX 34 AD7 ALA f 70 CYS f 74 5 5 HELIX 35 AD8 ASN f 98 LEU f 116 1 19 HELIX 36 AD9 LEU f 122 CYS f 126 5 5 HELIX 37 AE1 SER f 334 THR f 351 1 18 HELIX 38 AE2 ASP f 368 THR f 373 1 6 HELIX 39 AE3 MET f 475 TYR f 484 1 10 HELIX 40 AE4 THR g 529 SER g 534 1 6 HELIX 41 AE5 THR g 536 GLN g 543 1 8 HELIX 42 AE6 GLY g 569 TRP g 596 1 28 HELIX 43 AE7 SER g 618 TRP g 623 1 6 HELIX 44 AE8 THR g 627 GLY g 636 1 10 HELIX 45 AE9 TYR g 638 LYS g 658 1 21 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 SER H 18 SER H 26 -1 O ALA H 24 N MET H 5 SHEET 3 AA1 4 ILE H 86 ASN H 92 -1 O LEU H 89 N LEU H 21 SHEET 4 AA1 4 VAL H 76 ASP H 81 -1 N THR H 77 O GLN H 90 SHEET 1 AA2 6 LEU H 12 VAL H 13 0 SHEET 2 AA2 6 VAL H 132 VAL H 136 1 O THR H 135 N VAL H 13 SHEET 3 AA2 6 ALA H 100 ARG H 106 -1 N TYR H 102 O VAL H 132 SHEET 4 AA2 6 MET H 39 GLN H 44 -1 N GLN H 40 O ALA H 105 SHEET 5 AA2 6 LEU H 50 ILE H 56 -1 O GLU H 51 N ARG H 43 SHEET 6 AA2 6 THR H 65 TYR H 67 -1 O GLU H 66 N LEU H 55 SHEET 1 AA3 4 LEU H 12 VAL H 13 0 SHEET 2 AA3 4 VAL H 132 VAL H 136 1 O THR H 135 N VAL H 13 SHEET 3 AA3 4 ALA H 100 ARG H 106 -1 N TYR H 102 O VAL H 132 SHEET 4 AA3 4 SER H 127 TRP H 128 -1 N SER H 127 O ARG H 106 SHEET 1 AA4 2 TYR H 111 TYS H 113 0 SHEET 2 AA4 2 ASP H 117 THR H 119 -1 O TYS H 118 N TYR H 112 SHEET 1 AA5 5 SER L 9 VAL L 13 0 SHEET 2 AA5 5 THR L 122 VAL L 126 1 O ARG L 123 N VAL L 11 SHEET 3 AA5 5 ASP L 101 TRP L 107 -1 N TYR L 102 O THR L 122 SHEET 4 AA5 5 ILE L 38 GLN L 44 -1 N HIS L 40 O GLN L 105 SHEET 5 AA5 5 PRO L 50 ILE L 54 -1 O VAL L 51 N GLN L 43 SHEET 1 AA6 4 SER L 9 VAL L 13 0 SHEET 2 AA6 4 THR L 122 VAL L 126 1 O ARG L 123 N VAL L 11 SHEET 3 AA6 4 ASP L 101 TRP L 107 -1 N TYR L 102 O THR L 122 SHEET 4 AA6 4 VAL L 116 PHE L 118 -1 O PHE L 117 N VAL L 106 SHEET 1 AA7 3 ALA L 19 GLY L 24 0 SHEET 2 AA7 3 THR L 86 ILE L 91 -1 O ALA L 87 N CYS L 23 SHEET 3 AA7 3 PHE L 76 SER L 83 -1 N SER L 77 O THR L 90 SHEET 1 AA8 3 GLY b 495 THR b 499 0 SHEET 2 AA8 3 TRP b 35 TYR b 39 -1 N TYR b 39 O GLY b 495 SHEET 3 AA8 3 ILE c 603 PRO c 609 -1 O VAL c 608 N VAL b 36 SHEET 1 AA9 5 TRP b 45 ASP b 47 0 SHEET 2 AA9 5 TYR b 486 ILE b 491 -1 O GLU b 490 N ARG b 46 SHEET 3 AA9 5 PHE b 223 CYS b 228 -1 N LEU b 226 O LYS b 487 SHEET 4 AA9 5 VAL b 242 VAL b 245 -1 O SER b 243 N LYS b 227 SHEET 5 AA9 5 GLU b 83 HIS b 85 -1 N ILE b 84 O THR b 244 SHEET 1 AB1 3 VAL b 75 PRO b 76 0 SHEET 2 AB1 3 PHE b 53 SER b 56 1 N SER b 56 O VAL b 75 SHEET 3 AB1 3 HIS b 216 CYS b 218 -1 O HIS b 216 N ALA b 55 SHEET 1 AB2 2 GLU b 91 ASN b 94 0 SHEET 2 AB2 2 THR b 236 CYS b 239 -1 O CYS b 239 N GLU b 91 SHEET 1 AB3 5 ARG b 169 TYR b 177 0 SHEET 2 AB3 5 LEU b 154 THR b 162 -1 N MET b 161 O GLN b 170 SHEET 3 AB3 5 LEU b 129 ASN b 133 -1 N ARG b 132 O ASN b 156 SHEET 4 AB3 5 GLU b 190 LEU b 193 -1 O TYR b 191 N LEU b 129 SHEET 5 AB3 5 ILE b 181 PRO b 183 -1 N VAL b 182 O ARG b 192 SHEET 1 AB4 3 THR b 202 GLN b 203 0 SHEET 2 AB4 3 MET b 434 TYR b 435 1 O TYR b 435 N THR b 202 SHEET 3 AB4 3 ILE b 423 ILE b 424 -1 N ILE b 424 O MET b 434 SHEET 1 AB5 7 LEU b 259 LEU b 261 0 SHEET 2 AB5 7 ILE b 443 ARG b 456 -1 O GLY b 451 N LEU b 260 SHEET 3 AB5 7 ILE b 284 ARG b 298 -1 N ILE b 284 O LEU b 454 SHEET 4 AB5 7 ALA b 329 VAL b 333 -1 O ASN b 332 N LYS b 295 SHEET 5 AB5 7 LEU b 416 LYS b 421 -1 O CYS b 418 N ALA b 329 SHEET 6 AB5 7 GLU b 381 CYS b 385 -1 N TYR b 384 O ARG b 419 SHEET 7 AB5 7 HIS b 374 CYS b 378 -1 N HIS b 374 O CYS b 385 SHEET 1 AB6 6 THR b 271 ARG b 273 0 SHEET 2 AB6 6 ILE b 284 ARG b 298 -1 O ILE b 285 N ARG b 273 SHEET 3 AB6 6 ILE b 443 ARG b 456 -1 O LEU b 454 N ILE b 284 SHEET 4 AB6 6 ASN b 465 PRO b 470 -1 O ARG b 469 N THR b 455 SHEET 5 AB6 6 THR b 357 PHE b 361 1 N ILE b 359 O GLU b 466 SHEET 6 AB6 6 SER b 393 TRP b 395 -1 O TRP b 395 N ILE b 358 SHEET 1 AB7 2 ASN b 301 GLY b 312 0 SHEET 2 AB7 2 GLN b 315 ILE b 323A-1 O PHE b 317 N ILE b 307 SHEET 1 AB8 3 LEU d 494 THR d 499 0 SHEET 2 AB8 3 TRP d 35 TYR d 40 -1 N TYR d 39 O GLY d 495 SHEET 3 AB8 3 ILE e 603 PRO e 609 -1 O VAL e 608 N VAL d 36 SHEET 1 AB9 5 TRP d 45 ASP d 47 0 SHEET 2 AB9 5 TYR d 486 ILE d 491 -1 O GLU d 490 N ARG d 46 SHEET 3 AB9 5 PHE d 223 CYS d 228 -1 N LEU d 226 O LYS d 487 SHEET 4 AB9 5 VAL d 242 VAL d 245 -1 O SER d 243 N LYS d 227 SHEET 5 AB9 5 GLU d 83 HIS d 85 -1 N ILE d 84 O THR d 244 SHEET 1 AC1 2 GLU d 91 ASN d 94 0 SHEET 2 AC1 2 THR d 236 CYS d 239 -1 O CYS d 239 N GLU d 91 SHEET 1 AC2 3 HIS d 130 ARG d 132 0 SHEET 2 AC2 3 LEU d 154 THR d 162 -1 O ASN d 156 N ARG d 132 SHEET 3 AC2 3 ARG d 169 TYR d 177 -1 O GLN d 170 N MET d 161 SHEET 1 AC3 2 ILE d 181 PRO d 183 0 SHEET 2 AC3 2 TYR d 191 LEU d 193 -1 O ARG d 192 N VAL d 182 SHEET 1 AC4 3 THR d 202 GLN d 203 0 SHEET 2 AC4 3 MET d 434 TYR d 435 1 O TYR d 435 N THR d 202 SHEET 3 AC4 3 ILE d 423 ILE d 424 -1 N ILE d 424 O MET d 434 SHEET 1 AC5 7 LEU d 259 LEU d 261 0 SHEET 2 AC5 7 ILE d 443 ARG d 456 -1 O THR d 450 N LEU d 260 SHEET 3 AC5 7 ILE d 284 ARG d 298 -1 N ILE d 284 O LEU d 454 SHEET 4 AC5 7 ALA d 329 VAL d 333 -1 O ASN d 332 N LYS d 295 SHEET 5 AC5 7 LEU d 416 LYS d 421 -1 O LEU d 416 N CYS d 331 SHEET 6 AC5 7 PHE d 382 CYS d 385 -1 N TYR d 384 O ARG d 419 SHEET 7 AC5 7 HIS d 374 ASN d 377 -1 N HIS d 374 O CYS d 385 SHEET 1 AC6 6 THR d 271 ARG d 273 0 SHEET 2 AC6 6 ILE d 284 ARG d 298 -1 O ILE d 285 N ARG d 273 SHEET 3 AC6 6 ILE d 443 ARG d 456 -1 O LEU d 454 N ILE d 284 SHEET 4 AC6 6 ASN d 465 ARG d 469 -1 O ARG d 469 N THR d 455 SHEET 5 AC6 6 THR d 357 PHE d 361 1 N ILE d 359 O GLU d 466 SHEET 6 AC6 6 SER d 393 TRP d 395 -1 O SER d 393 N PHE d 361 SHEET 1 AC7 2 TYR d 302 GLY d 312 0 SHEET 2 AC7 2 GLN d 315 ILE d 323 -1 O PHE d 317 N ILE d 307 SHEET 1 AC8 3 GLY f 495 THR f 499 0 SHEET 2 AC8 3 TRP f 35 TYR f 39 -1 N THR f 37 O ALA f 497 SHEET 3 AC8 3 ILE g 603 PRO g 609 -1 O VAL g 608 N VAL f 36 SHEET 1 AC9 5 TRP f 45 ASP f 47 0 SHEET 2 AC9 5 TYR f 486 ILE f 491 -1 O GLU f 490 N ARG f 46 SHEET 3 AC9 5 PHE f 223 CYS f 228 -1 N ALA f 224 O VAL f 489 SHEET 4 AC9 5 VAL f 242 VAL f 245 -1 O SER f 243 N LYS f 227 SHEET 5 AC9 5 GLU f 83 LEU f 86 -1 N ILE f 84 O THR f 244 SHEET 1 AD1 3 VAL f 75 PRO f 76 0 SHEET 2 AD1 3 PHE f 53 SER f 56 1 N SER f 56 O VAL f 75 SHEET 3 AD1 3 HIS f 216 CYS f 218 -1 O CYS f 218 N PHE f 53 SHEET 1 AD2 2 LYS f 92 ASN f 94 0 SHEET 2 AD2 2 THR f 236 LEU f 238 -1 O GLY f 237 N PHE f 93 SHEET 1 AD3 5 ARG f 169 TYR f 177 0 SHEET 2 AD3 5 LEU f 154 THR f 162 -1 N MET f 161 O GLN f 170 SHEET 3 AD3 5 LEU f 129 ARG f 132 -1 N HIS f 130 O THR f 158 SHEET 4 AD3 5 GLU f 190 LEU f 193 -1 O TYR f 191 N LEU f 129 SHEET 5 AD3 5 ILE f 181 PRO f 183 -1 N VAL f 182 O ARG f 192 SHEET 1 AD4 3 THR f 202 GLN f 203 0 SHEET 2 AD4 3 MET f 434 TYR f 435 1 O TYR f 435 N THR f 202 SHEET 3 AD4 3 ILE f 423 ILE f 424 -1 N ILE f 424 O MET f 434 SHEET 1 AD5 7 LEU f 259 LEU f 261 0 SHEET 2 AD5 7 ILE f 443 ARG f 456 -1 O GLY f 451 N LEU f 260 SHEET 3 AD5 7 ILE f 284 ARG f 298 -1 N ILE f 284 O LEU f 454 SHEET 4 AD5 7 ALA f 329 VAL f 333 -1 O ASN f 332 N LYS f 295 SHEET 5 AD5 7 ILE f 414 LYS f 421 -1 O ILE f 414 N VAL f 333 SHEET 6 AD5 7 PHE f 382 CYS f 385 -1 N TYR f 384 O ARG f 419 SHEET 7 AD5 7 HIS f 374 ASN f 377 -1 N PHE f 376 O PHE f 383 SHEET 1 AD6 6 THR f 271 ARG f 273 0 SHEET 2 AD6 6 ILE f 284 ARG f 298 -1 O ILE f 285 N ARG f 273 SHEET 3 AD6 6 ILE f 443 ARG f 456 -1 O LEU f 454 N ILE f 284 SHEET 4 AD6 6 ASN f 465 PRO f 470 -1 O ARG f 469 N THR f 455 SHEET 5 AD6 6 THR f 357 PHE f 361 1 N ILE f 359 O PHE f 468 SHEET 6 AD6 6 SER f 393 TRP f 395 -1 O TRP f 395 N ILE f 358 SHEET 1 AD7 2 TYR f 302 GLY f 312 0 SHEET 2 AD7 2 GLN f 315 ILE f 323 -1 O PHE f 317 N ILE f 307 SSBOND 1 CYS H 23 CYS H 104 1555 1555 2.04 SSBOND 2 CYS L 23 CYS L 104 1555 1555 2.03 SSBOND 3 CYS b 54 CYS b 74 1555 1555 2.04 SSBOND 4 CYS b 119 CYS b 205 1555 1555 2.03 SSBOND 5 CYS b 126 CYS b 196 1555 1555 2.02 SSBOND 6 CYS b 131 CYS b 157 1555 1555 2.03 SSBOND 7 CYS b 201 CYS b 433 1555 1555 2.03 SSBOND 8 CYS b 218 CYS b 247 1555 1555 2.03 SSBOND 9 CYS b 228 CYS b 239 1555 1555 2.03 SSBOND 10 CYS b 296 CYS b 331 1555 1555 2.03 SSBOND 11 CYS b 378 CYS b 445 1555 1555 2.01 SSBOND 12 CYS b 385 CYS b 418 1555 1555 2.00 SSBOND 13 CYS b 501 CYS c 605 1555 1555 2.03 SSBOND 14 CYS c 598 CYS c 604 1555 1555 2.03 SSBOND 15 CYS d 54 CYS d 74 1555 1555 2.03 SSBOND 16 CYS d 119 CYS d 205 1555 1555 2.03 SSBOND 17 CYS d 126 CYS d 196 1555 1555 2.03 SSBOND 18 CYS d 131 CYS d 157 1555 1555 2.03 SSBOND 19 CYS d 201 CYS d 433 1555 1555 2.03 SSBOND 20 CYS d 218 CYS d 247 1555 1555 2.03 SSBOND 21 CYS d 228 CYS d 239 1555 1555 2.03 SSBOND 22 CYS d 296 CYS d 331 1555 1555 2.03 SSBOND 23 CYS d 378 CYS d 445 1555 1555 2.04 SSBOND 24 CYS d 385 CYS d 418 1555 1555 2.03 SSBOND 25 CYS d 501 CYS e 605 1555 1555 2.00 SSBOND 26 CYS e 598 CYS e 604 1555 1555 2.01 SSBOND 27 CYS f 54 CYS f 74 1555 1555 2.04 SSBOND 28 CYS f 119 CYS f 205 1555 1555 2.03 SSBOND 29 CYS f 126 CYS f 196 1555 1555 2.03 SSBOND 30 CYS f 131 CYS f 157 1555 1555 2.03 SSBOND 31 CYS f 201 CYS f 433 1555 1555 2.03 SSBOND 32 CYS f 218 CYS f 247 1555 1555 2.04 SSBOND 33 CYS f 228 CYS f 239 1555 1555 2.03 SSBOND 34 CYS f 296 CYS f 331 1555 1555 2.03 SSBOND 35 CYS f 378 CYS f 445 1555 1555 2.04 SSBOND 36 CYS f 385 CYS f 418 1555 1555 2.03 SSBOND 37 CYS f 501 CYS g 605 1555 1555 2.03 SSBOND 38 CYS g 598 CYS g 604 1555 1555 2.03 LINK C TYR H 112 N TYS H 113 1555 1555 1.33 LINK C TYS H 113 N ASP H 114 1555 1555 1.33 LINK C ASP H 117 N TYS H 118 1555 1555 1.33 LINK C TYS H 118 N THR H 119 1555 1555 1.33 LINK ND2 ASN b 88 C1 NAG b 601 1555 1555 1.50 LINK ND2 ASN b 133 C1 NAG b 602 1555 1555 1.44 LINK ND2 ASN b 156 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN b 160 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN b 197 C1 NAG F 1 1555 1555 1.43 LINK ND2 ASN b 234 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN b 241 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN b 262 C1 NAG C 1 1555 1555 1.44 LINK ND2 ASN b 269 C1 NAG b 604 1555 1555 1.44 LINK ND2 ASN b 276 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN b 301 C1 NAG K 1 1555 1555 1.45 LINK ND2 ASN b 332 C1 NAG B 1 1555 1555 1.44 LINK ND2 ASN b 339 C1 NAG b 607 1555 1555 1.43 LINK ND2 ASN b 355 C1 NAG b 603 1555 1555 1.44 LINK ND2 ASN b 363 C1 NAG b 606 1555 1555 1.43 LINK ND2 ASN b 386 C1 NAG O 1 1555 1555 1.43 LINK ND2 ASN b 392 C1 NAG A 1 1555 1555 1.44 LINK ND2 ASN b 398 C1 NAG b 605 1555 1555 1.45 LINK ND2 ASN b 448 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN b 465 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN c 611 C1 NAG c 701 1555 1555 1.44 LINK ND2 ASN c 625 C1 NAG c 703 1555 1555 1.44 LINK ND2 ASN c 637 C1 NAG c 702 1555 1555 1.44 LINK ND2 ASN d 88 C1 NAG d 604 1555 1555 1.44 LINK ND2 ASN d 133 C1 NAG d 601 1555 1555 1.44 LINK ND2 ASN d 156 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN d 160 C1 NAG a 1 1555 1555 1.43 LINK ND2 ASN d 197 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN d 234 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN d 241 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN d 262 C1 NAG R 1 1555 1555 1.43 LINK ND2 ASN d 269 C1 NAG d 603 1555 1555 1.44 LINK ND2 ASN d 276 C1 NAG W 1 1555 1555 1.45 LINK ND2 ASN d 301 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN d 332 C1 NAG Q 1 1555 1555 1.40 LINK ND2 ASN d 339 C1 NAG d 608 1555 1555 1.43 LINK ND2 ASN d 355 C1 NAG d 602 1555 1555 1.46 LINK ND2 ASN d 363 C1 NAG d 606 1555 1555 1.43 LINK ND2 ASN d 386 C1 NAG d 607 1555 1555 1.42 LINK ND2 ASN d 392 C1 NAG P 1 1555 1555 1.45 LINK ND2 ASN d 398 C1 NAG d 605 1555 1555 1.46 LINK ND2 ASN d 448 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN d 465 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN e 611 C1 NAG e 701 1555 1555 1.44 LINK ND2 ASN e 625 C1 NAG e 703 1555 1555 1.44 LINK ND2 ASN e 637 C1 NAG e 702 1555 1555 1.44 LINK ND2 ASN f 88 C1 NAG f 601 1555 1555 1.45 LINK ND2 ASN f 133 C1 NAG f 602 1555 1555 1.44 LINK ND2 ASN f 156 C1 NAG k 1 1555 1555 1.44 LINK ND2 ASN f 160 C1 NAG s 1 1555 1555 1.42 LINK ND2 ASN f 197 C1 NAG l 1 1555 1555 1.44 LINK ND2 ASN f 234 C1 NAG m 1 1555 1555 1.44 LINK ND2 ASN f 241 C1 NAG n 1 1555 1555 1.43 LINK ND2 ASN f 262 C1 NAG j 1 1555 1555 1.43 LINK ND2 ASN f 269 C1 NAG f 605 1555 1555 1.44 LINK ND2 ASN f 276 C1 NAG o 1 1555 1555 1.44 LINK ND2 ASN f 301 C1 NAG p 1 1555 1555 1.44 LINK ND2 ASN f 332 C1 NAG i 1 1555 1555 1.41 LINK ND2 ASN f 339 C1 NAG f 603 1555 1555 1.45 LINK ND2 ASN f 355 C1 NAG f 604 1555 1555 1.44 LINK ND2 ASN f 363 C1 NAG f 607 1555 1555 1.43 LINK ND2 ASN f 386 C1 NAG t 1 1555 1555 1.44 LINK ND2 ASN f 392 C1 NAG h 1 1555 1555 1.44 LINK ND2 ASN f 398 C1 NAG f 606 1555 1555 1.45 LINK ND2 ASN f 448 C1 NAG q 1 1555 1555 1.44 LINK ND2 ASN f 465 C1 NAG r 1 1555 1555 1.44 LINK ND2 ASN g 611 C1 NAG g 701 1555 1555 1.44 LINK ND2 ASN g 625 C1 NAG g 703 1555 1555 1.44 LINK ND2 ASN g 637 C1 NAG g 702 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 B 2 C1 BMA B 3 1555 1555 1.45 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.40 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.39 LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.39 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 F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.45 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.46 LINK O4 NAG K 1 C1 NAG K 2 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 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.39 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.39 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.39 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.39 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.39 LINK O3 BMA R 3 C1 MAN R 4 1555 1555 1.40 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 1.45 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 LINK O4 NAG X 1 C1 NAG X 2 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 1.47 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.40 LINK O4 NAG a 2 C1 BMA a 3 1555 1555 1.39 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.39 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 O3 BMA j 3 C1 MAN j 4 1555 1555 1.40 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.44 LINK O4 NAG l 1 C1 NAG l 2 1555 1555 1.45 LINK O4 NAG m 1 C1 NAG m 2 1555 1555 1.45 LINK O4 NAG n 1 C1 NAG n 2 1555 1555 1.40 LINK O4 NAG o 1 C1 NAG o 2 1555 1555 1.45 LINK O4 NAG p 1 C1 NAG p 2 1555 1555 1.44 LINK O4 NAG q 1 C1 NAG q 2 1555 1555 1.44 LINK O4 NAG r 1 C1 NAG r 2 1555 1555 1.44 LINK O4 NAG s 1 C1 NAG s 2 1555 1555 1.40 LINK O4 NAG s 2 C1 BMA s 3 1555 1555 1.39 LINK O4 NAG t 1 C1 NAG t 2 1555 1555 1.39 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