HEADER VIRAL PROTEIN/IMMUNE SYSTEM 15-MAY-24 9BTL TITLE CRYO-EM STRUCTURE OF RHESUS ANTIBODY 41328-A.01 IN COMPLEX WITH HIV-1 TITLE 2 ENV BG505 DS-SOSIP COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 3 CHAIN: A, E, I; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 8 CHAIN: B, F, J; COMPND 9 SYNONYM: ENV POLYPROTEIN; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: 41328-A.01 HEAVY CHAIN; COMPND 13 CHAIN: H; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: 41328-A.01 LIGHT CHAIN; COMPND 17 CHAIN: L; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 10 ORGANISM_TAXID: 11676; SOURCE 11 GENE: ENV; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 17 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 18 ORGANISM_TAXID: 9544; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 24 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 25 ORGANISM_TAXID: 9544; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS NEUTRALIZING ANTIBODY, HIV-1 V2 APEX, SHIV-ELICITED, VIRAL PROTEIN, KEYWDS 2 IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR R.S.ROARK,L.SHAPIRO,P.D.KWONG REVDAT 1 21-MAY-25 9BTL 0 JRNL AUTH R.S.ROARK,L.SHAPIRO,P.D.KWONG JRNL TITL HIV-1 NEUTRALIZING ANTIBODIES IN SHIV-INFECTED MACAQUES JRNL TITL 2 RECAPITULATE STRUCTURALLY DIVERGENT MODES OF HUMAN V2 APEX JRNL TITL 3 RECOGNITION WITH A SINGLE D GENE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.96 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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) : 2.960 REMARK 3 NUMBER OF PARTICLES : 176070 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 9BTL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000284102. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : COMPLEX OF 41328-A.01 WITH HIV REMARK 245 -1 BG505 ENVELOPE TRIMER REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5800.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, H, I, J, L, C, D, REMARK 350 AND CHAINS: G, K, M, N, O, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e, f, g, h, i, j, k, l, REMARK 350 AND CHAINS: m, n, o, p, q 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 31 REMARK 465 GLU A 32 REMARK 465 ALA A 58 REMARK 465 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 GLU A 62 REMARK 465 THR A 63 REMARK 465 GLU A 64 REMARK 465 LYS A 65 REMARK 465 GLU A 185A REMARK 465 ASN A 185B REMARK 465 GLN A 185C REMARK 465 GLY A 185D REMARK 465 ASN A 185E REMARK 465 ARG A 185F REMARK 465 SER A 185G REMARK 465 ASN A 185H REMARK 465 ASN A 185I REMARK 465 SER A 185J REMARK 465 ASN A 405A REMARK 465 THR A 405B REMARK 465 SER A 405C REMARK 465 VAL A 405D REMARK 465 GLN A 405E REMARK 465 GLY A 405F REMARK 465 SER A 405G REMARK 465 ASN A 405H REMARK 465 SER A 405I REMARK 465 THR A 405J REMARK 465 GLY A 405K REMARK 465 SER A 405L REMARK 465 ASN A 405M REMARK 465 VAL A 506 REMARK 465 GLY A 507 REMARK 465 ARG A 508 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 PHE B 519 REMARK 465 SER B 546 REMARK 465 GLY B 547 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 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 ALA E 31 REMARK 465 GLU E 32 REMARK 465 ALA E 58 REMARK 465 LYS E 59 REMARK 465 ALA E 60 REMARK 465 TYR E 61 REMARK 465 GLU E 62 REMARK 465 THR E 63 REMARK 465 GLU E 64 REMARK 465 LYS E 65 REMARK 465 ASN E 186A REMARK 465 GLN E 186B REMARK 465 GLY E 186C REMARK 465 ASN E 186D REMARK 465 ARG E 186E REMARK 465 SER E 186F REMARK 465 ASN E 186G REMARK 465 ASN E 186H REMARK 465 SER E 186I REMARK 465 ASN E 186J REMARK 465 ASN E 405A REMARK 465 THR E 405B REMARK 465 SER E 405C REMARK 465 VAL E 405D REMARK 465 GLN E 405E REMARK 465 GLY E 405F REMARK 465 SER E 405G REMARK 465 ASN E 405H REMARK 465 SER E 405I REMARK 465 THR E 405J REMARK 465 GLY E 405K REMARK 465 SER E 405L REMARK 465 ASN E 405M REMARK 465 VAL E 506 REMARK 465 GLY E 507 REMARK 465 ARG E 508 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 REMARK 465 VAL F 518 REMARK 465 PHE F 519 REMARK 465 SER F 546 REMARK 465 GLY F 547 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 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 ALA H 114 REMARK 465 SER H 115 REMARK 465 THR H 116 REMARK 465 LYS H 117 REMARK 465 GLY H 118 REMARK 465 PRO H 119 REMARK 465 SER H 120 REMARK 465 VAL H 121 REMARK 465 PHE H 122 REMARK 465 PRO H 123 REMARK 465 LEU H 124 REMARK 465 ALA H 125 REMARK 465 PRO H 126 REMARK 465 SER H 127 REMARK 465 SER H 128 REMARK 465 ARG H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLU H 133 REMARK 465 SER H 134 REMARK 465 THR H 135 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 LEU H 138 REMARK 465 GLY H 139 REMARK 465 CYS H 140 REMARK 465 LEU H 141 REMARK 465 VAL H 142 REMARK 465 LYS H 143 REMARK 465 ASP H 144 REMARK 465 TYR H 145 REMARK 465 PHE H 146 REMARK 465 PRO H 147 REMARK 465 GLU H 148 REMARK 465 PRO H 149 REMARK 465 VAL H 150 REMARK 465 THR H 151 REMARK 465 VAL H 152 REMARK 465 SER H 153 REMARK 465 TRP H 154 REMARK 465 ASN H 155 REMARK 465 SER H 156 REMARK 465 GLY H 157 REMARK 465 SER H 158 REMARK 465 LEU H 159 REMARK 465 THR H 160 REMARK 465 SER H 161 REMARK 465 GLY H 162 REMARK 465 VAL H 163 REMARK 465 HIS H 164 REMARK 465 THR H 165 REMARK 465 PHE H 166 REMARK 465 PRO H 167 REMARK 465 ALA H 168 REMARK 465 VAL H 169 REMARK 465 LEU H 170 REMARK 465 GLN H 171 REMARK 465 SER H 172 REMARK 465 SER H 173 REMARK 465 GLY H 174 REMARK 465 LEU H 175 REMARK 465 TYR H 176 REMARK 465 SER H 177 REMARK 465 LEU H 178 REMARK 465 SER H 179 REMARK 465 SER H 180 REMARK 465 VAL H 181 REMARK 465 VAL H 182 REMARK 465 THR H 183 REMARK 465 VAL H 184 REMARK 465 PRO H 185 REMARK 465 SER H 186 REMARK 465 SER H 187 REMARK 465 SER H 188 REMARK 465 LEU H 189 REMARK 465 GLY H 190 REMARK 465 THR H 191 REMARK 465 GLN H 192 REMARK 465 THR H 193 REMARK 465 TYR H 194 REMARK 465 VAL H 195 REMARK 465 CYS H 196 REMARK 465 ASN H 197 REMARK 465 VAL H 198 REMARK 465 ASN H 199 REMARK 465 HIS H 200 REMARK 465 LYS H 201 REMARK 465 PRO H 202 REMARK 465 SER H 203 REMARK 465 ASN H 204 REMARK 465 THR H 205 REMARK 465 LYS H 206 REMARK 465 VAL H 207 REMARK 465 ASP H 208 REMARK 465 LYS H 209 REMARK 465 ARG H 210 REMARK 465 VAL H 211 REMARK 465 GLU H 212 REMARK 465 ILE H 213 REMARK 465 LYS H 214 REMARK 465 THR H 215 REMARK 465 CYS H 216 REMARK 465 GLY H 217 REMARK 465 GLY H 218 REMARK 465 GLY H 219 REMARK 465 LEU H 220 REMARK 465 GLU H 221 REMARK 465 VAL H 222 REMARK 465 LEU H 223 REMARK 465 PHE H 224 REMARK 465 GLN H 225 REMARK 465 ALA I 31 REMARK 465 GLU I 32 REMARK 465 ALA I 58 REMARK 465 LYS I 59 REMARK 465 ALA I 60 REMARK 465 TYR I 61 REMARK 465 GLU I 62 REMARK 465 THR I 63 REMARK 465 GLU I 64 REMARK 465 LYS I 65 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 397A REMARK 465 THR I 397B REMARK 465 SER I 397C REMARK 465 VAL I 397D REMARK 465 GLN I 397E REMARK 465 GLY I 397F REMARK 465 SER I 397G REMARK 465 ASN I 397H REMARK 465 SER I 397I REMARK 465 THR I 397J REMARK 465 GLY I 397K REMARK 465 SER I 397L REMARK 465 VAL I 506 REMARK 465 GLY I 507 REMARK 465 ARG I 508 REMARK 465 VAL J 513 REMARK 465 GLY J 514 REMARK 465 ILE J 515 REMARK 465 GLY J 516 REMARK 465 ALA J 517 REMARK 465 VAL J 518 REMARK 465 PHE J 519 REMARK 465 SER J 546 REMARK 465 GLY J 547 REMARK 465 ILE J 548 REMARK 465 VAL J 549 REMARK 465 GLN J 550 REMARK 465 GLN J 551 REMARK 465 GLN J 552 REMARK 465 SER J 553 REMARK 465 ASN J 554 REMARK 465 LEU J 555 REMARK 465 LEU J 556 REMARK 465 ARG J 557 REMARK 465 ALA J 558 REMARK 465 PRO J 559 REMARK 465 GLU J 560 REMARK 465 ALA J 561 REMARK 465 GLN J 562 REMARK 465 GLN J 563 REMARK 465 HIS J 564 REMARK 465 LEU J 565 REMARK 465 LEU J 566 REMARK 465 THR L 105 REMARK 465 VAL L 106 REMARK 465 LEU L 107 REMARK 465 GLY L 108 REMARK 465 GLN L 109 REMARK 465 PRO L 110 REMARK 465 LYS L 111 REMARK 465 ALA L 112 REMARK 465 ALA L 113 REMARK 465 PRO L 114 REMARK 465 SER L 115 REMARK 465 VAL L 116 REMARK 465 THR L 117 REMARK 465 LEU L 118 REMARK 465 PHE L 119 REMARK 465 PRO L 120 REMARK 465 PRO L 121 REMARK 465 SER L 122 REMARK 465 SER L 123 REMARK 465 GLU L 124 REMARK 465 GLU L 125 REMARK 465 LEU L 126 REMARK 465 GLN L 127 REMARK 465 ALA L 128 REMARK 465 ASN L 129 REMARK 465 LYS L 130 REMARK 465 ALA L 131 REMARK 465 THR L 132 REMARK 465 LEU L 133 REMARK 465 VAL L 134 REMARK 465 CYS L 135 REMARK 465 LEU L 136 REMARK 465 ILE L 137 REMARK 465 SER L 138 REMARK 465 ASP L 139 REMARK 465 PHE L 140 REMARK 465 TYR L 141 REMARK 465 PRO L 142 REMARK 465 GLY L 143 REMARK 465 ALA L 144 REMARK 465 VAL L 145 REMARK 465 GLU L 146 REMARK 465 VAL L 147 REMARK 465 ALA L 148 REMARK 465 TRP L 149 REMARK 465 LYS L 150 REMARK 465 ALA L 151 REMARK 465 ASP L 152 REMARK 465 GLY L 153 REMARK 465 SER L 154 REMARK 465 ALA L 155 REMARK 465 VAL L 156 REMARK 465 ASN L 157 REMARK 465 ALA L 158 REMARK 465 GLY L 159 REMARK 465 VAL L 160 REMARK 465 GLU L 161 REMARK 465 THR L 162 REMARK 465 THR L 163 REMARK 465 LYS L 164 REMARK 465 PRO L 165 REMARK 465 SER L 166 REMARK 465 LYS L 167 REMARK 465 GLN L 168 REMARK 465 SER L 169 REMARK 465 ASN L 170 REMARK 465 ASN L 171 REMARK 465 LYS L 172 REMARK 465 TYR L 173 REMARK 465 ALA L 174 REMARK 465 ALA L 175 REMARK 465 SER L 176 REMARK 465 SER L 177 REMARK 465 TYR L 178 REMARK 465 LEU L 179 REMARK 465 SER L 180 REMARK 465 LEU L 181 REMARK 465 THR L 182 REMARK 465 SER L 183 REMARK 465 ASP L 184 REMARK 465 GLN L 185 REMARK 465 TRP L 186 REMARK 465 LYS L 187 REMARK 465 SER L 188 REMARK 465 HIS L 189 REMARK 465 LYS L 190 REMARK 465 SER L 191 REMARK 465 TYR L 192 REMARK 465 SER L 193 REMARK 465 CYS L 194 REMARK 465 GLN L 195 REMARK 465 VAL L 196 REMARK 465 THR L 197 REMARK 465 HIS L 198 REMARK 465 GLU L 199 REMARK 465 GLY L 200 REMARK 465 SER L 201 REMARK 465 THR L 202 REMARK 465 VAL L 203 REMARK 465 GLU L 204 REMARK 465 LYS L 205 REMARK 465 THR L 206 REMARK 465 VAL L 207 REMARK 465 ALA L 208 REMARK 465 PRO L 209 REMARK 465 ALA L 210 REMARK 465 GLU L 211 REMARK 465 CYS L 212 REMARK 465 SER L 213 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: 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 SG CYS E 131 SG CYS E 157 1.76 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 LEU A 259 CA - CB - CG ANGL. DEV. = 17.4 DEGREES REMARK 500 CYS A 501 CA - CB - SG ANGL. DEV. = 9.5 DEGREES REMARK 500 CYS B 605 CA - CB - SG ANGL. DEV. = 8.0 DEGREES REMARK 500 GLU B 621 CA - CB - CG ANGL. DEV. = 13.4 DEGREES REMARK 500 CYS E 54 CB - CA - C ANGL. DEV. = -14.4 DEGREES REMARK 500 ASP H 72 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES REMARK 500 CYS I 501 CA - CB - SG ANGL. DEV. = 13.1 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 ALA A 70 71.31 56.26 REMARK 500 LEU A 122 37.39 -98.03 REMARK 500 ASN A 137 24.12 84.97 REMARK 500 MET A 150 46.15 -84.23 REMARK 500 SER A 199 -169.73 -167.16 REMARK 500 GLN A 258 -12.08 73.87 REMARK 500 SER A 460 53.11 -92.70 REMARK 500 ASP B 624 32.16 -99.82 REMARK 500 ASN B 625 -37.22 -132.62 REMARK 500 LEU E 122 58.16 -93.83 REMARK 500 PRO E 124 1.36 -68.19 REMARK 500 ASP E 140 -37.76 68.84 REMARK 500 THR E 163 -166.72 -123.74 REMARK 500 SER E 199 147.77 -172.44 REMARK 500 GLN E 258 -6.47 68.06 REMARK 500 ASN E 356 19.16 52.09 REMARK 500 THR E 387 33.95 -96.81 REMARK 500 THR E 461 18.79 58.18 REMARK 500 ASN E 462 -11.93 70.08 REMARK 500 ASN F 607 53.73 -93.52 REMARK 500 ASN F 625 -18.12 -140.09 REMARK 500 GLU H 16 -168.25 -112.29 REMARK 500 ILE H 48 -61.40 -105.98 REMARK 500 ASN H 65 46.67 33.48 REMARK 500 ALA I 48 -168.32 -161.58 REMARK 500 GLN I 258 -9.95 70.09 REMARK 500 SER I 460 -148.60 55.87 REMARK 500 LEU J 568 70.40 57.90 REMARK 500 THR J 569 79.39 61.44 REMARK 500 ASN J 616 49.03 -93.88 REMARK 500 LEU L 4 66.20 60.01 REMARK 500 ALA L 14 -179.47 -68.47 REMARK 500 ARG L 16 -8.83 67.94 REMARK 500 SER L 26 -169.16 -126.24 REMARK 500 ASN L 51 -11.56 68.26 REMARK 500 ALA L 77 70.47 57.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44893 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF RHESUS ANTIBODY 41328-A.01 IN COMPLEX WITH HIV- REMARK 900 1 ENV BG505 DS-SOSIP DBREF 9BTL A 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 9BTL B 513 664 UNP Q2N0S6 Q2N0S6_9HIV1 510 661 DBREF 9BTL E 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 9BTL F 513 664 UNP Q2N0S6 Q2N0S6_9HIV1 510 661 DBREF 9BTL H 1 225 PDB 9BTL 9BTL 1 225 DBREF 9BTL I 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 9BTL J 513 664 UNP Q2N0S6 Q2N0S6_9HIV1 510 661 DBREF 9BTL L 1 213 PDB 9BTL 9BTL 1 213 SEQADV 9BTL CYS A 201 UNP Q2N0S6 ILE 200 ENGINEERED MUTATION SEQADV 9BTL ASN A 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 9BTL CYS A 433 UNP Q2N0S6 ALA 430 ENGINEERED MUTATION SEQADV 9BTL CYS A 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 9BTL PRO B 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 9BTL CYS B 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 9BTL CYS E 201 UNP Q2N0S6 ILE 200 ENGINEERED MUTATION SEQADV 9BTL ASN E 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 9BTL CYS E 433 UNP Q2N0S6 ALA 430 ENGINEERED MUTATION SEQADV 9BTL CYS E 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 9BTL PRO F 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 9BTL CYS F 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 9BTL CYS I 201 UNP Q2N0S6 ILE 200 ENGINEERED MUTATION SEQADV 9BTL ASN I 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 9BTL CYS I 433 UNP Q2N0S6 ALA 430 ENGINEERED MUTATION SEQADV 9BTL CYS I 501 UNP Q2N0S6 ALA 498 ENGINEERED MUTATION SEQADV 9BTL PRO J 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 9BTL CYS J 605 UNP Q2N0S6 THR 602 CONFLICT SEQRES 1 A 476 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 476 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 A 476 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 A 476 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 476 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 A 476 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 A 476 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 476 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 A 476 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 A 476 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 A 476 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 A 476 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 A 476 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 A 476 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 A 476 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 A 476 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 A 476 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 A 476 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 A 476 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 A 476 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 A 476 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 A 476 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 A 476 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 A 476 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 A 476 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 A 476 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 A 476 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 A 476 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 A 476 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 A 476 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 A 476 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 A 476 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 A 476 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 A 476 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 A 476 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 A 476 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 A 476 CYS LYS ARG ARG VAL VAL GLY ARG SEQRES 1 B 152 VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY ALA SEQRES 2 B 152 ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU THR SEQRES 3 B 152 VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN GLN SEQRES 4 B 152 GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN HIS SEQRES 5 B 152 LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU GLN SEQRES 6 B 152 ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP GLN SEQRES 7 B 152 GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU ILE SEQRES 8 B 152 CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER ASN SEQRES 9 B 152 ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP LEU SEQRES 10 B 152 GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE ILE SEQRES 11 B 152 TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU LYS SEQRES 12 B 152 ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 E 476 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 E 476 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 E 476 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 E 476 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 E 476 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 E 476 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 E 476 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 E 476 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 E 476 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 E 476 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 E 476 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 E 476 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 E 476 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 E 476 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 E 476 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 E 476 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 E 476 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 E 476 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 E 476 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 E 476 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 E 476 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 E 476 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 E 476 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 E 476 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 E 476 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 E 476 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 E 476 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 E 476 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 E 476 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 E 476 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 E 476 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 E 476 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 E 476 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 E 476 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 E 476 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 E 476 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 E 476 CYS LYS ARG ARG VAL VAL GLY ARG SEQRES 1 F 152 VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY ALA SEQRES 2 F 152 ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU THR SEQRES 3 F 152 VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN GLN SEQRES 4 F 152 GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN HIS SEQRES 5 F 152 LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU GLN SEQRES 6 F 152 ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP GLN SEQRES 7 F 152 GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU ILE SEQRES 8 F 152 CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER ASN SEQRES 9 F 152 ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP LEU SEQRES 10 F 152 GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE ILE SEQRES 11 F 152 TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU LYS SEQRES 12 F 152 ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 H 245 GLN VAL GLN LEU GLN GLN TRP GLY GLU GLY LEU VAL LYS SEQRES 2 H 245 PRO SER GLU THR LEU SER LEU SER CYS ALA VAL TYR GLY SEQRES 3 H 245 GLY SER ILE SER GLY HIS TYR TYR TRP SER TRP ILE ARG SEQRES 4 H 245 GLN ALA PRO GLY LYS GLY LEU GLU TRP ILE GLY LYS ILE SEQRES 5 H 245 ASP ALA ASN SER ALA SER THR ASN TYR ASN PRO SER PHE SEQRES 6 H 245 LYS ASN ARG VAL SER ILE SER LYS ASP THR SER LYS LYS SEQRES 7 H 245 GLN PHE TYR LEU ASN LEU HIS SER VAL THR ALA ALA ASP SEQRES 8 H 245 THR ALA VAL TYR TYR CYS ALA ARG GLY SER ILE TYR TYR SEQRES 9 H 245 GLU ASP ASP ASP GLY TYR TYR TYR SER GLU ALA THR TYR SEQRES 10 H 245 LEU HIS LEU HIS LEU TRP GLY GLN GLY VAL VAL VAL THR SEQRES 11 H 245 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 12 H 245 LEU ALA PRO SER SER ARG SER THR SER GLU SER THR ALA SEQRES 13 H 245 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 14 H 245 VAL THR VAL SER TRP ASN SER GLY SER LEU THR SER GLY SEQRES 15 H 245 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 16 H 245 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 17 H 245 LEU GLY THR GLN THR TYR VAL CYS ASN VAL ASN HIS LYS SEQRES 18 H 245 PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU ILE LYS SEQRES 19 H 245 THR CYS GLY GLY GLY LEU GLU VAL LEU PHE GLN SEQRES 1 I 476 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 I 476 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 I 476 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 I 476 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 I 476 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 I 476 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 I 476 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 I 476 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 I 476 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 I 476 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 I 476 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 I 476 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 I 476 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 I 476 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 I 476 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 I 476 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 I 476 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 I 476 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 I 476 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 I 476 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 I 476 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 I 476 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 I 476 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 I 476 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 I 476 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 I 476 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 I 476 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 I 476 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 I 476 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 I 476 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 I 476 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 I 476 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 I 476 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 I 476 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 I 476 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 I 476 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 I 476 CYS LYS ARG ARG VAL VAL GLY ARG SEQRES 1 J 152 VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY ALA SEQRES 2 J 152 ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU THR SEQRES 3 J 152 VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN GLN SEQRES 4 J 152 GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN HIS SEQRES 5 J 152 LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU GLN SEQRES 6 J 152 ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP GLN SEQRES 7 J 152 GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU ILE SEQRES 8 J 152 CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER ASN SEQRES 9 J 152 ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP LEU SEQRES 10 J 152 GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE ILE SEQRES 11 J 152 TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU LYS SEQRES 12 J 152 ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 L 216 GLN SER VAL LEU THR GLN PRO PRO SER ALA SER GLU ALA SEQRES 2 L 216 ALA ARG LYS ARG VAL SER ILE SER CYS SER GLY SER PHE SEQRES 3 L 216 SER ASN ILE GLY THR ASN SER VAL SER TRP TYR GLN HIS SEQRES 4 L 216 LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR HIS ASN SEQRES 5 L 216 GLY GLN ARG ALA SER GLY VAL SER ASP ARG PHE SER GLY SEQRES 6 L 216 SER LYS SER GLY THR SER ALA SER LEU ALA ILE SER ALA SEQRES 7 L 216 LEU GLN THR GLU ASP GLU ALA ASP TYR TYR CYS ALA THR SEQRES 8 L 216 TRP ASP ASP MET LEU ASN GLY TYR PHE PHE GLY ALA GLY SEQRES 9 L 216 THR ARG LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 L 216 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 L 216 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 L 216 TYR PRO GLY ALA VAL GLU VAL ALA TRP LYS ALA ASP GLY SEQRES 13 L 216 SER ALA VAL ASN ALA GLY VAL GLU THR THR LYS PRO SER SEQRES 14 L 216 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 L 216 SER LEU THR SER ASP GLN TRP LYS SER HIS LYS SER TYR SEQRES 16 L 216 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 L 216 THR VAL ALA PRO ALA GLU CYS SER HET NAG C 1 14 HET NAG C 2 14 HET NAG D 1 14 HET NAG D 2 14 HET NAG G 1 14 HET NAG G 2 14 HET NAG K 1 14 HET NAG K 2 14 HET BMA K 3 11 HET MAN K 4 11 HET NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 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 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 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 NAG Y 1 14 HET NAG Y 2 14 HET BMA Y 3 11 HET MAN Y 4 11 HET MAN Y 5 11 HET NAG Z 1 14 HET NAG Z 2 14 HET NAG a 1 14 HET NAG a 2 14 HET NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 HET NAG d 1 14 HET NAG d 2 14 HET 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 h 1 14 HET NAG h 2 14 HET NAG i 1 14 HET NAG i 2 14 HET BMA i 3 11 HET NAG j 1 14 HET NAG j 2 14 HET NAG k 1 14 HET NAG k 2 14 HET BMA k 3 11 HET MAN k 4 11 HET NAG l 1 14 HET NAG l 2 14 HET BMA l 3 11 HET MAN l 4 11 HET NAG m 1 14 HET NAG m 2 14 HET NAG n 1 14 HET NAG n 2 14 HET NAG o 1 14 HET NAG o 2 14 HET NAG p 1 14 HET NAG p 2 14 HET NAG q 1 14 HET NAG q 2 14 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG A 605 14 HET NAG A 606 14 HET NAG A 607 14 HET NAG A 608 14 HET NAG B 701 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG E 604 14 HET NAG E 605 14 HET NAG F 701 14 HET NAG F 702 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 J 701 14 HET NAG J 702 14 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 9 NAG 94(C8 H15 N O6) FORMUL 12 BMA 8(C6 H12 O6) FORMUL 12 MAN 7(C6 H12 O6) HELIX 1 AA1 ALA A 70 CYS A 74 5 5 HELIX 2 AA2 ASN A 99 LYS A 117 1 19 HELIX 3 AA3 LEU A 122 CYS A 126 5 5 HELIX 4 AA4 LYS A 335 GLY A 354 1 20 HELIX 5 AA5 ASP A 368 THR A 373 1 6 HELIX 6 AA6 THR A 387 LEU A 390 5 4 HELIX 7 AA7 MET A 475 SER A 481 1 7 HELIX 8 AA8 THR B 529 SER B 534 1 6 HELIX 9 AA9 THR B 536 ARG B 542 1 7 HELIX 10 AB1 THR B 569 ILE B 595 1 27 HELIX 11 AB2 ASN B 618 ILE B 622 5 5 HELIX 12 AB3 THR B 627 LYS B 633 1 7 HELIX 13 AB4 TYR B 638 ASP B 664 1 27 HELIX 14 AB5 ALA E 70 CYS E 74 5 5 HELIX 15 AB6 ASN E 98 LYS E 117 1 20 HELIX 16 AB7 LEU E 122 CYS E 126 5 5 HELIX 17 AB8 ASN E 195 THR E 198 5 4 HELIX 18 AB9 LYS E 335 GLY E 354 1 20 HELIX 19 AC1 ASP E 368 THR E 373 1 6 HELIX 20 AC2 ASN E 425 ARG E 429 5 5 HELIX 21 AC3 GLY E 459 SER E 463 5 5 HELIX 22 AC4 ASP E 474 SER E 481 1 8 HELIX 23 AC5 GLY F 531 MET F 535 5 5 HELIX 24 AC6 THR F 536 ARG F 542 1 7 HELIX 25 AC7 ASN F 543 LEU F 545 5 3 HELIX 26 AC8 THR F 569 TRP F 596 1 28 HELIX 27 AC9 LEU F 619 ASP F 624 1 6 HELIX 28 AD1 THR F 627 ASP F 664 1 38 HELIX 29 AD2 PRO H 61 LYS H 64 5 4 HELIX 30 AD3 THR H 83 THR H 87 5 5 HELIX 31 AD4 ALA H 100J LEU H 100M 5 4 HELIX 32 AD5 ASN I 99 LEU I 116 1 18 HELIX 33 AD6 LYS I 335 GLY I 354 1 20 HELIX 34 AD7 ASP I 368 THR I 373 1 6 HELIX 35 AD8 MET I 475 SER I 481 1 7 HELIX 36 AD9 THR J 529 SER J 534 1 6 HELIX 37 AE1 THR J 536 LEU J 544 1 9 HELIX 38 AE2 THR J 569 ILE J 595 1 27 HELIX 39 AE3 ASN J 618 MET J 626 1 9 HELIX 40 AE4 THR J 627 ILE J 635 1 9 HELIX 41 AE5 TYR J 638 ASP J 664 1 27 HELIX 42 AE6 GLN L 79 GLU L 83 5 5 SHEET 1 AA1 3 GLY A 495 THR A 499 0 SHEET 2 AA1 3 TRP A 35 TYR A 39 -1 N THR A 37 O ALA A 497 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O CYS B 604 N VAL A 38 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 VAL A 488 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 PHE A 223 CYS A 228 -1 N ALA A 224 O VAL A 489 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 GLU A 83 LEU A 86 -1 N ILE A 84 O THR A 244 SHEET 1 AA3 3 VAL A 75 PRO A 76 0 SHEET 2 AA3 3 PHE A 53 SER A 56 1 N SER A 56 O VAL A 75 SHEET 3 AA3 3 HIS A 216 CYS A 218 -1 O CYS A 218 N PHE A 53 SHEET 1 AA4 2 GLU A 91 ASN A 94 0 SHEET 2 AA4 2 THR A 236 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AA5 3 LEU A 129 GLN A 130 0 SHEET 2 AA5 3 GLU A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 3 AA5 3 VAL A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA6 2 LEU A 154 THR A 162 0 SHEET 2 AA6 2 LYS A 169 TYR A 177 -1 O PHE A 176 N LYS A 155 SHEET 1 AA7 3 THR A 202 GLN A 203 0 SHEET 2 AA7 3 MET A 434 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA7 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA8 6 LEU A 259 LEU A 261 0 SHEET 2 AA8 6 ILE A 443 ARG A 456 -1 O GLY A 451 N LEU A 260 SHEET 3 AA8 6 ILE A 284 ARG A 298 -1 N CYS A 296 O CYS A 445 SHEET 4 AA8 6 THR A 465 PRO A 470 0 SHEET 5 AA8 6 ILE A 358 PHE A 361 1 N ARG A 360 O GLU A 466 SHEET 6 AA8 6 SER A 393 TRP A 395 -1 O SER A 393 N PHE A 361 SHEET 1 AA9 5 MET A 271 ARG A 273 0 SHEET 2 AA9 5 ILE A 284 ARG A 298 -1 O LEU A 285 N ARG A 273 SHEET 3 AA9 5 ILE A 443 ARG A 456 -1 O CYS A 445 N CYS A 296 SHEET 4 AA9 5 HIS A 330 SER A 334 0 SHEET 5 AA9 5 SER A 413 THR A 415 -1 O ILE A 414 N VAL A 333 SHEET 1 AB1 2 ARG A 304 GLY A 312 0 SHEET 2 AB1 2 GLN A 315 THR A 320 -1 O PHE A 317 N ILE A 307 SHEET 1 AB2 3 HIS A 374 SER A 375 0 SHEET 2 AB2 3 PHE A 383 CYS A 385 -1 O CYS A 385 N HIS A 374 SHEET 3 AB2 3 CYS A 418 ILE A 420 -1 O ARG A 419 N TYR A 384 SHEET 1 AB3 3 LEU E 494 THR E 499 0 SHEET 2 AB3 3 TRP E 35 TYR E 40 -1 N TYR E 39 O GLY E 495 SHEET 3 AB3 3 ILE F 603 PRO F 609 -1 O CYS F 604 N VAL E 38 SHEET 1 AB4 5 TRP E 45 ASP E 47 0 SHEET 2 AB4 5 TYR E 486 ILE E 491 -1 O LYS E 490 N LYS E 46 SHEET 3 AB4 5 PHE E 223 CYS E 228 -1 N ALA E 224 O VAL E 489 SHEET 4 AB4 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AB4 5 GLU E 83 LEU E 86 -1 N ILE E 84 O THR E 244 SHEET 1 AB5 2 PHE E 53 ALA E 55 0 SHEET 2 AB5 2 HIS E 216 CYS E 218 -1 O CYS E 218 N PHE E 53 SHEET 1 AB6 2 GLU E 91 ASN E 94 0 SHEET 2 AB6 2 THR E 236 CYS E 239 -1 O GLY E 237 N PHE E 93 SHEET 1 AB7 5 LYS E 169 TYR E 177 0 SHEET 2 AB7 5 LEU E 154 THR E 162 -1 N MET E 161 O GLN E 170 SHEET 3 AB7 5 LEU E 129 ASN E 133 -1 N THR E 132 O ASN E 156 SHEET 4 AB7 5 GLU E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 5 AB7 5 VAL E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AB8 3 THR E 202 GLN E 203 0 SHEET 2 AB8 3 MET E 434 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AB8 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AB9 7 LEU E 259 LEU E 261 0 SHEET 2 AB9 7 GLY E 441 ARG E 456 -1 O GLY E 451 N LEU E 260 SHEET 3 AB9 7 ILE E 284 ASN E 302 -1 N VAL E 292 O ILE E 449 SHEET 4 AB9 7 ALA E 329 SER E 334 -1 O ASN E 332 N ASN E 295 SHEET 5 AB9 7 SER E 413 LYS E 421 -1 O ILE E 414 N VAL E 333 SHEET 6 AB9 7 GLU E 381 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 AB9 7 HIS E 374 CYS E 378 -1 N HIS E 374 O CYS E 385 SHEET 1 AC1 6 MET E 271 SER E 274 0 SHEET 2 AC1 6 ILE E 284 ASN E 302 -1 O LEU E 285 N ARG E 273 SHEET 3 AC1 6 GLY E 441 ARG E 456 -1 O ILE E 449 N VAL E 292 SHEET 4 AC1 6 THR E 465 PRO E 470 -1 O ARG E 469 N THR E 455 SHEET 5 AC1 6 ILE E 358 PHE E 361 1 N ARG E 360 O GLU E 466 SHEET 6 AC1 6 SER E 393 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 1 AC2 2 ARG E 304 GLY E 312 0 SHEET 2 AC2 2 GLN E 315 THR E 320 -1 O PHE E 317 N ILE E 307 SHEET 1 AC3 4 GLN H 3 GLY H 8 0 SHEET 2 AC3 4 LEU H 18 TYR H 25 -1 O ALA H 23 N GLN H 5 SHEET 3 AC3 4 GLN H 77 LEU H 82 -1 O LEU H 82 N LEU H 18 SHEET 4 AC3 4 VAL H 67 ASP H 72 -1 N SER H 68 O ASN H 81 SHEET 1 AC4 2 LEU H 11 VAL H 12 0 SHEET 2 AC4 2 THR H 110 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 1 AC5 5 THR H 57 TYR H 59 0 SHEET 2 AC5 5 LEU H 45 ASP H 52 -1 N LYS H 50 O ASN H 58 SHEET 3 AC5 5 TYR H 33 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 4 AC5 5 VAL H 89 SER H 96 -1 O TYR H 91 N ILE H 37 SHEET 5 AC5 5 HIS H 100N LEU H 100O-1 O HIS H 100N N SER H 96 SHEET 1 AC6 2 TYR H 98 GLU H 100 0 SHEET 2 AC6 2 TYR H 100F SER H 100H-1 O TYR H 100G N TYR H 99 SHEET 1 AC7 3 LEU I 494 THR I 499 0 SHEET 2 AC7 3 TRP I 35 TYR I 40 -1 N THR I 37 O ALA I 497 SHEET 3 AC7 3 ILE J 603 CYS J 604 -1 O CYS J 604 N VAL I 38 SHEET 1 AC8 5 TRP I 45 ASP I 47 0 SHEET 2 AC8 5 VAL I 488 ILE I 491 -1 O LYS I 490 N LYS I 46 SHEET 3 AC8 5 PHE I 223 CYS I 228 -1 N ALA I 224 O VAL I 489 SHEET 4 AC8 5 VAL I 242 VAL I 245 -1 O SER I 243 N LYS I 227 SHEET 5 AC8 5 GLU I 83 LEU I 86 -1 N ILE I 84 O THR I 244 SHEET 1 AC9 3 VAL I 75 PRO I 76 0 SHEET 2 AC9 3 PHE I 53 SER I 56 1 N SER I 56 O VAL I 75 SHEET 3 AC9 3 HIS I 216 CYS I 218 -1 O CYS I 218 N PHE I 53 SHEET 1 AD1 2 GLU I 91 ASN I 94 0 SHEET 2 AD1 2 THR I 236 CYS I 239 -1 O CYS I 239 N GLU I 91 SHEET 1 AD2 2 VAL I 120 LYS I 121 0 SHEET 2 AD2 2 THR I 202 GLN I 203 -1 O GLN I 203 N VAL I 120 SHEET 1 AD3 5 LYS I 169 TYR I 177 0 SHEET 2 AD3 5 LEU I 154 THR I 162 -1 N MET I 161 O GLN I 170 SHEET 3 AD3 5 LEU I 129 ASN I 133 -1 N THR I 132 O ASN I 156 SHEET 4 AD3 5 LYS I 189 LEU I 193 -1 O TYR I 191 N LEU I 129 SHEET 5 AD3 5 VAL I 181 GLN I 183 -1 N VAL I 182 O ARG I 192 SHEET 1 AD4 7 LEU I 259 LEU I 261 0 SHEET 2 AD4 7 ILE I 443 ARG I 456 -1 O GLY I 451 N LEU I 260 SHEET 3 AD4 7 ILE I 284 ARG I 298 -1 N ILE I 284 O LEU I 454 SHEET 4 AD4 7 HIS I 330 SER I 334 -1 O ASN I 332 N ASN I 295 SHEET 5 AD4 7 SER I 413 LYS I 421 -1 O ILE I 414 N VAL I 333 SHEET 6 AD4 7 GLU I 381 CYS I 385 -1 N TYR I 384 O ARG I 419 SHEET 7 AD4 7 HIS I 374 CYS I 378 -1 N HIS I 374 O CYS I 385 SHEET 1 AD5 6 MET I 271 ARG I 273 0 SHEET 2 AD5 6 ILE I 284 ARG I 298 -1 O LEU I 285 N ARG I 273 SHEET 3 AD5 6 ILE I 443 ARG I 456 -1 O LEU I 454 N ILE I 284 SHEET 4 AD5 6 THR I 465 PRO I 470 -1 O ARG I 469 N THR I 455 SHEET 5 AD5 6 ILE I 358 PHE I 361 1 N ARG I 360 O GLU I 466 SHEET 6 AD5 6 SER I 393 TRP I 395 -1 O TRP I 395 N ILE I 359 SHEET 1 AD6 2 ARG I 304 GLY I 312 0 SHEET 2 AD6 2 GLN I 315 THR I 320 -1 O PHE I 317 N ILE I 307 SHEET 1 AD7 2 ILE I 423 ILE I 424 0 SHEET 2 AD7 2 MET I 434 TYR I 435 -1 O MET I 434 N ILE I 424 SHEET 1 AD8 3 VAL L 19 SER L 24 0 SHEET 2 AD8 3 SER L 70 ILE L 75 -1 O ALA L 71 N CYS L 23 SHEET 3 AD8 3 PHE L 62 SER L 67 -1 N SER L 63 O ALA L 74 SHEET 1 AD9 5 GLN L 53 ARG L 54 0 SHEET 2 AD9 5 LYS L 45 TYR L 49 -1 N TYR L 49 O GLN L 53 SHEET 3 AD9 5 SER L 34 HIS L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 AD9 5 ASP L 85 ASP L 92 -1 O ALA L 89 N SER L 34 SHEET 5 AD9 5 GLY L 95B PHE L 98 -1 O GLY L 95B N ASP L 92 SHEET 1 AE1 5 GLN L 53 ARG L 54 0 SHEET 2 AE1 5 LYS L 45 TYR L 49 -1 N TYR L 49 O GLN L 53 SHEET 3 AE1 5 SER L 34 HIS L 38 -1 N TRP L 35 O LEU L 47 SHEET 4 AE1 5 ASP L 85 ASP L 92 -1 O ALA L 89 N SER L 34 SHEET 5 AE1 5 THR L 102 ARG L 103 -1 O THR L 102 N TYR L 86 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.07 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 201 CYS A 433 1555 1555 2.03 SSBOND 6 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 7 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 8 CYS A 296 CYS A 331 1555 1555 2.02 SSBOND 9 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 10 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 11 CYS A 501 CYS B 605 1555 1555 2.13 SSBOND 12 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 13 CYS E 54 CYS E 74 1555 1555 2.02 SSBOND 14 CYS E 119 CYS E 205 1555 1555 2.04 SSBOND 15 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 16 CYS E 201 CYS E 433 1555 1555 2.03 SSBOND 17 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 18 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 19 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 20 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 21 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 22 CYS E 501 CYS F 605 1555 1555 2.03 SSBOND 23 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 24 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 25 CYS I 54 CYS I 74 1555 1555 2.06 SSBOND 26 CYS I 119 CYS I 205 1555 1555 2.03 SSBOND 27 CYS I 126 CYS I 196 1555 1555 2.03 SSBOND 28 CYS I 131 CYS I 157 1555 1555 2.03 SSBOND 29 CYS I 201 CYS I 433 1555 1555 2.03 SSBOND 30 CYS I 218 CYS I 247 1555 1555 2.03 SSBOND 31 CYS I 228 CYS I 239 1555 1555 2.03 SSBOND 32 CYS I 296 CYS I 331 1555 1555 2.22 SSBOND 33 CYS I 378 CYS I 445 1555 1555 2.03 SSBOND 34 CYS I 385 CYS I 418 1555 1555 2.03 SSBOND 35 CYS I 501 CYS J 605 1555 1555 2.03 SSBOND 36 CYS J 598 CYS J 604 1555 1555 2.03 SSBOND 37 CYS L 23 CYS L 88 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 133 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 137 C1 NAG A 608 1555 1555 1.43 LINK ND2 ASN A 156 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG A 606 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG A 607 1555 1555 1.44 LINK ND2 ASN A 295 C1 NAG N 1 1555 1555 1.43 LINK ND2 ASN A 301 C1 NAG A 605 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG R 1 1555 1555 1.45 LINK ND2 ASN A 339 C1 NAG A 604 1555 1555 1.44 LINK ND2 ASN A 355 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG C 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN E 133 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 137 C1 NAG E 605 1555 1555 1.45 LINK ND2 ASN E 156 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN E 234 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 295 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN E 301 C1 NAG c 1 1555 1555 1.45 LINK ND2 ASN E 332 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN E 355 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN E 392 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN F 611 C1 NAG F 701 1555 1555 1.45 LINK ND2 ASN F 637 C1 NAG F 702 1555 1555 1.46 LINK ND2 ASN I 88 C1 NAG I 604 1555 1555 1.44 LINK ND2 ASN I 133 C1 NAG n 1 1555 1555 1.44 LINK ND2 ASN I 145 C1 NAG I 606 1555 1555 1.43 LINK ND2 ASN I 156 C1 NAG l 1 1555 1555 1.43 LINK ND2 ASN I 160 C1 NAG k 1 1555 1555 1.44 LINK ND2 ASN I 197 C1 NAG m 1 1555 1555 1.44 LINK ND2 ASN I 234 C1 NAG q 1 1555 1555 1.45 LINK ND2 ASN I 262 C1 NAG i 1 1555 1555 1.44 LINK ND2 ASN I 276 C1 NAG I 602 1555 1555 1.44 LINK ND2 ASN I 295 C1 NAG j 1 1555 1555 1.44 LINK ND2 ASN I 301 C1 NAG p 1 1555 1555 1.44 LINK ND2 ASN I 332 C1 NAG o 1 1555 1555 1.44 LINK ND2 ASN I 339 C1 NAG I 605 1555 1555 1.44 LINK ND2 ASN I 355 C1 NAG I 603 1555 1555 1.44 LINK ND2 ASN I 363 C1 NAG f 1 1555 1555 1.44 LINK ND2 ASN I 386 C1 NAG h 1 1555 1555 1.44 LINK ND2 ASN I 392 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN I 448 C1 NAG I 601 1555 1555 1.44 LINK ND2 ASN J 618 C1 NAG J 701 1555 1555 1.45 LINK ND2 ASN J 637 C1 NAG J 702 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.44 LINK O3 BMA K 3 C1 MAN K 4 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 1.44 LINK O4 NAG O 2 C1 BMA O 3 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 1.45 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 V 2 C1 BMA V 3 1555 1555 1.45 LINK O3 BMA V 3 C1 MAN V 4 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 1.45 LINK O6 BMA X 3 C1 MAN X 4 1555 1555 1.45 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.44 LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.45 LINK O3 BMA Y 3 C1 MAN Y 4 1555 1555 1.46 LINK O6 BMA Y 3 C1 MAN Y 5 1555 1555 1.45 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 b 1 C1 NAG b 2 1555 1555 1.44 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.44 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.45 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.45 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.45 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.45 LINK O4 NAG i 2 C1 BMA i 3 1555 1555 1.45 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.45 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.44 LINK O4 NAG k 2 C1 BMA k 3 1555 1555 1.45 LINK O3 BMA k 3 C1 MAN k 4 1555 1555 1.45 LINK O4 NAG l 1 C1 NAG l 2 1555 1555 1.44 LINK O4 NAG l 2 C1 BMA l 3 1555 1555 1.44 LINK O3 BMA l 3 C1 MAN l 4 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 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