HEADER VIRAL PROTEIN 21-AUG-23 8KHC TITLE SARS-COV-2 OMICRON SPIKE IN COMPLEX WITH 5817 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE GLYCOPROTEIN; COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEAVY CHAIN OF 5817 FAB; COMPND 8 CHAIN: F, H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: LIGHT CHAIN OF 5817 FAB; COMPND 12 CHAIN: G, J; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_TAXID: 2697049; SOURCE 5 GENE: S, 2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS SARS-COV-2, OMICRON, RBD, FAB, VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR L.CAO,X.WANG REVDAT 1 17-APR-24 8KHC 0 JRNL AUTH Y.WANG,Z.ZHANG,M.YANG,X.XIONG,Q.YAN,L.CAO,P.WEI,Y.ZHANG, JRNL AUTH 2 L.ZHANG,K.LV,J.CHEN,X.LIU,X.ZHAO,J.XIAO,S.ZHANG,A.ZHU,M.GAN, JRNL AUTH 3 J.ZHANG,R.CAI,J.ZHUO,Y.ZHANG,H.RAO,B.QU,Y.ZHANG,L.CHEN, JRNL AUTH 4 J.DAI,L.CHENG,Q.HU,Y.CHEN,H.LV,R.T.Y.SO,M.PEIRIS,J.ZHAO, JRNL AUTH 5 X.LIU,C.K.P.MOK,X.WANG,J.ZHAO JRNL TITL IDENTIFICATION OF A BROAD SARBECOVIRUS NEUTRALIZING ANTIBODY JRNL TITL 2 TARGETING A CONSERVED EPITOPE ON THE RECEPTOR-BINDING JRNL TITL 3 DOMAIN. JRNL REF CELL REP V. 43 13653 2024 JRNL REFN ESSN 2211-1247 JRNL PMID 38175758 JRNL DOI 10.1016/J.CELREP.2023.113653 REMARK 2 REMARK 2 RESOLUTION. 3.00 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) : 3.000 REMARK 3 NUMBER OF PARTICLES : 5129 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8KHC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-AUG-23. REMARK 100 THE DEPOSITION ID IS D_1300038718. 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 : SARS-COV-2 OMICRON SPIKE IN REMARK 245 COMPLEX WITH 5817 FAB 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00 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) : 4500.00 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: HEPTAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, F, G, H, J, D, E REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 HIS A 69 REMARK 465 VAL A 70 REMARK 465 SER A 71 REMARK 465 GLY A 72 REMARK 465 THR A 73 REMARK 465 ASN A 74 REMARK 465 GLY A 75 REMARK 465 THR A 76 REMARK 465 LYS A 77 REMARK 465 ARG A 78 REMARK 465 PHE A 79 REMARK 465 VAL A 143 REMARK 465 TYR A 144 REMARK 465 TYR A 145 REMARK 465 HIS A 146 REMARK 465 LYS A 147 REMARK 465 ASN A 148 REMARK 465 ASN A 149 REMARK 465 LYS A 150 REMARK 465 SER A 151 REMARK 465 TRP A 152 REMARK 465 MET A 153 REMARK 465 GLU A 154 REMARK 465 SER A 155 REMARK 465 ASP A 156 REMARK 465 MET A 177 REMARK 465 ASP A 178 REMARK 465 LEU A 179 REMARK 465 GLU A 180 REMARK 465 GLY A 181 REMARK 465 LYS A 182 REMARK 465 GLN A 183 REMARK 465 GLY A 184 REMARK 465 ASN A 185 REMARK 465 PHE A 186 REMARK 465 ASN A 214 REMARK 465 LEU A 215 REMARK 465 VAL A 216 REMARK 465 ARG A 217 REMARK 465 ASN A 333A REMARK 465 ILE A 333B REMARK 465 THR A 333C REMARK 465 PRO A 624 REMARK 465 VAL A 625 REMARK 465 ALA A 626 REMARK 465 ILE A 627 REMARK 465 HIS A 628 REMARK 465 ALA A 629 REMARK 465 ASP A 630 REMARK 465 GLN A 631 REMARK 465 LEU A 632 REMARK 465 THR A 633 REMARK 465 PRO A 634 REMARK 465 THR A 635 REMARK 465 TRP A 636 REMARK 465 ARG A 637 REMARK 465 VAL A 638 REMARK 465 TYR A 639 REMARK 465 SER A 640 REMARK 465 THR A 641 REMARK 465 GLY A 642 REMARK 465 SER A 643 REMARK 465 GLN A 680 REMARK 465 THR A 681 REMARK 465 ASN A 682 REMARK 465 SER A 683 REMARK 465 PRO A 684 REMARK 465 ARG A 685 REMARK 465 ARG A 686 REMARK 465 ALA A 687 REMARK 465 ARG A 688 REMARK 465 SER A 689 REMARK 465 VAL A 690 REMARK 465 ALA A 691 REMARK 465 SER A 692 REMARK 465 GLN A 693 REMARK 465 ALA A 832 REMARK 465 ASP A 833 REMARK 465 ALA A 834 REMARK 465 GLY A 835 REMARK 465 PHE A 836 REMARK 465 ILE A 837 REMARK 465 LYS A 838 REMARK 465 GLN A 839 REMARK 465 TYR A 840 REMARK 465 GLY A 841 REMARK 465 ASP A 842 REMARK 465 CYS A 843 REMARK 465 LEU A 844 REMARK 465 GLY A 845 REMARK 465 ASP A 846 REMARK 465 ILE A 847 REMARK 465 ALA A 848 REMARK 465 ALA A 849 REMARK 465 ARG A 850 REMARK 465 ASP A 851 REMARK 465 LEU A 852 REMARK 465 ILE A 853 REMARK 465 CYS A 854 REMARK 465 ALA A 855 REMARK 465 GLN A 856 REMARK 465 LYS A 857 REMARK 465 HIS B 69 REMARK 465 VAL B 70 REMARK 465 SER B 71 REMARK 465 GLY B 72 REMARK 465 THR B 73 REMARK 465 ASN B 74 REMARK 465 GLY B 75 REMARK 465 THR B 76 REMARK 465 LYS B 77 REMARK 465 ARG B 78 REMARK 465 PHE B 79 REMARK 465 VAL B 143 REMARK 465 TYR B 144 REMARK 465 TYR B 145 REMARK 465 HIS B 146 REMARK 465 LYS B 147 REMARK 465 ASN B 148 REMARK 465 ASN B 149 REMARK 465 LYS B 150 REMARK 465 SER B 151 REMARK 465 TRP B 152 REMARK 465 MET B 153 REMARK 465 GLU B 154 REMARK 465 SER B 155 REMARK 465 ASP B 156 REMARK 465 MET B 177 REMARK 465 ASP B 178 REMARK 465 LEU B 179 REMARK 465 GLU B 180 REMARK 465 GLY B 181 REMARK 465 LYS B 182 REMARK 465 GLN B 183 REMARK 465 GLY B 184 REMARK 465 ASN B 185 REMARK 465 PHE B 186 REMARK 465 ASN B 214 REMARK 465 LEU B 215 REMARK 465 VAL B 216 REMARK 465 ARG B 217 REMARK 465 ASN B 333A REMARK 465 ILE B 333B REMARK 465 THR B 333C REMARK 465 LYS B 531 REMARK 465 PRO B 624 REMARK 465 VAL B 625 REMARK 465 ALA B 626 REMARK 465 ILE B 627 REMARK 465 HIS B 628 REMARK 465 ALA B 629 REMARK 465 ASP B 630 REMARK 465 GLN B 631 REMARK 465 LEU B 632 REMARK 465 THR B 633 REMARK 465 PRO B 634 REMARK 465 THR B 635 REMARK 465 TRP B 636 REMARK 465 ARG B 637 REMARK 465 VAL B 638 REMARK 465 TYR B 639 REMARK 465 SER B 640 REMARK 465 THR B 641 REMARK 465 GLY B 642 REMARK 465 GLN B 680 REMARK 465 THR B 681 REMARK 465 ASN B 682 REMARK 465 SER B 683 REMARK 465 PRO B 684 REMARK 465 ARG B 685 REMARK 465 ARG B 686 REMARK 465 ALA B 687 REMARK 465 ARG B 688 REMARK 465 SER B 689 REMARK 465 VAL B 690 REMARK 465 ALA B 691 REMARK 465 SER B 692 REMARK 465 ALA B 832 REMARK 465 ASP B 833 REMARK 465 ALA B 834 REMARK 465 GLY B 835 REMARK 465 PHE B 836 REMARK 465 ILE B 837 REMARK 465 LYS B 838 REMARK 465 GLN B 839 REMARK 465 TYR B 840 REMARK 465 GLY B 841 REMARK 465 ASP B 842 REMARK 465 CYS B 843 REMARK 465 LEU B 844 REMARK 465 GLY B 845 REMARK 465 ASP B 846 REMARK 465 ILE B 847 REMARK 465 ALA B 848 REMARK 465 ALA B 849 REMARK 465 ARG B 850 REMARK 465 ASP B 851 REMARK 465 LEU B 852 REMARK 465 ILE B 853 REMARK 465 CYS B 854 REMARK 465 ALA B 855 REMARK 465 GLN B 856 REMARK 465 HIS C 69 REMARK 465 VAL C 70 REMARK 465 SER C 71 REMARK 465 GLY C 72 REMARK 465 THR C 73 REMARK 465 ASN C 74 REMARK 465 GLY C 75 REMARK 465 THR C 76 REMARK 465 LYS C 77 REMARK 465 ARG C 78 REMARK 465 PHE C 79 REMARK 465 ASP C 80 REMARK 465 VAL C 143 REMARK 465 TYR C 144 REMARK 465 TYR C 145 REMARK 465 HIS C 146 REMARK 465 LYS C 147 REMARK 465 ASN C 148 REMARK 465 ASN C 149 REMARK 465 LYS C 150 REMARK 465 SER C 151 REMARK 465 TRP C 152 REMARK 465 MET C 153 REMARK 465 GLU C 154 REMARK 465 SER C 155 REMARK 465 ASP C 156 REMARK 465 PHE C 157 REMARK 465 MET C 177 REMARK 465 ASP C 178 REMARK 465 LEU C 179 REMARK 465 GLU C 180 REMARK 465 GLY C 181 REMARK 465 LYS C 182 REMARK 465 GLN C 183 REMARK 465 GLY C 184 REMARK 465 ASN C 185 REMARK 465 PHE C 186 REMARK 465 ASN C 214 REMARK 465 LEU C 215 REMARK 465 VAL C 216 REMARK 465 ARG C 217 REMARK 465 PRO C 624 REMARK 465 VAL C 625 REMARK 465 ALA C 626 REMARK 465 ILE C 627 REMARK 465 HIS C 628 REMARK 465 ALA C 629 REMARK 465 ASP C 630 REMARK 465 GLN C 631 REMARK 465 LEU C 632 REMARK 465 THR C 633 REMARK 465 PRO C 634 REMARK 465 THR C 635 REMARK 465 TRP C 636 REMARK 465 ARG C 637 REMARK 465 VAL C 638 REMARK 465 TYR C 639 REMARK 465 SER C 640 REMARK 465 GLN C 680 REMARK 465 THR C 681 REMARK 465 ASN C 682 REMARK 465 SER C 683 REMARK 465 PRO C 684 REMARK 465 ARG C 685 REMARK 465 ARG C 686 REMARK 465 ALA C 687 REMARK 465 ARG C 688 REMARK 465 SER C 689 REMARK 465 VAL C 690 REMARK 465 ALA C 691 REMARK 465 SER C 692 REMARK 465 ALA C 832 REMARK 465 ASP C 833 REMARK 465 ALA C 834 REMARK 465 GLY C 835 REMARK 465 PHE C 836 REMARK 465 ILE C 837 REMARK 465 LYS C 838 REMARK 465 GLN C 839 REMARK 465 TYR C 840 REMARK 465 GLY C 841 REMARK 465 ASP C 842 REMARK 465 CYS C 843 REMARK 465 LEU C 844 REMARK 465 GLY C 845 REMARK 465 ASP C 846 REMARK 465 ILE C 847 REMARK 465 ALA C 848 REMARK 465 ALA C 849 REMARK 465 ARG C 850 REMARK 465 ASP C 851 REMARK 465 LEU C 852 REMARK 465 ILE C 853 REMARK 465 CYS C 854 REMARK 465 ALA C 855 REMARK 465 GLN C 856 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ASP A 40 CG OD1 OD2 REMARK 470 SER A 46 OG REMARK 470 GLN A 52 CG CD OE1 NE2 REMARK 470 ASP A 53 CG OD1 OD2 REMARK 470 ASP A 80 CG OD1 OD2 REMARK 470 ASN A 87 CG OD1 ND2 REMARK 470 LYS A 97 CG CD CE NZ REMARK 470 SER A 98 OG REMARK 470 THR A 109 OG1 CG2 REMARK 470 LEU A 110 CG CD1 CD2 REMARK 470 ASP A 111 CG OD1 OD2 REMARK 470 SER A 112 OG REMARK 470 LYS A 113 CG CD CE NZ REMARK 470 GLN A 115 CG CD OE1 NE2 REMARK 470 ASN A 121 CG OD1 ND2 REMARK 470 ASN A 122 CG OD1 ND2 REMARK 470 GLU A 132 CG CD OE1 OE2 REMARK 470 PHE A 133 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN A 134 CG CD OE1 NE2 REMARK 470 ASN A 137 CG OD1 ND2 REMARK 470 PHE A 157 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A 158 CG CD NE CZ NH1 NH2 REMARK 470 TYR A 160 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER A 161 OG REMARK 470 SER A 162 OG REMARK 470 ASN A 164 CG OD1 ND2 REMARK 470 GLN A 173 CG CD OE1 NE2 REMARK 470 LYS A 187 CG CD CE NZ REMARK 470 ILE A 210 CG1 CG2 CD1 REMARK 470 LEU A 247 CG CD1 CD2 REMARK 470 ARG A 249 CG CD NE CZ NH1 NH2 REMARK 470 TYR A 251 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 SER A 257 OG REMARK 470 THR A 262 OG1 CG2 REMARK 470 ARG A 322 CG CD NE CZ NH1 NH2 REMARK 470 THR A 326 OG1 CG2 REMARK 470 LYS A 531 CG CD CE NZ REMARK 470 LYS A 532 CG CD CE NZ REMARK 470 GLU A 557 CG CD OE1 OE2 REMARK 470 ASN A 559 CG OD1 ND2 REMARK 470 LYS A 561 CG CD CE NZ REMARK 470 GLN A 567 CG CD OE1 NE2 REMARK 470 ASP A 571 CG OD1 OD2 REMARK 470 ASP A 574 CG OD1 OD2 REMARK 470 THR A 575 OG1 CG2 REMARK 470 GLN A 583 CG CD OE1 NE2 REMARK 470 THR A 621 OG1 CG2 REMARK 470 ARG A 649 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 664 CG CD OE1 OE2 REMARK 470 SER A 676 OG REMARK 470 GLN A 678 CG CD OE1 NE2 REMARK 470 THR A 679 OG1 CG2 REMARK 470 GLU A 751 CG CD OE1 OE2 REMARK 470 LYS A 789 CG CD CE NZ REMARK 470 LYS A 793 CG CD CE NZ REMARK 470 ILE A 797 CG1 CG2 CD1 REMARK 470 LEU A 831 CG CD1 CD2 REMARK 470 LYS A 924 CG CD CE NZ REMARK 470 LYS A 936 CG CD CE NZ REMARK 470 ASP A 939 CG OD1 OD2 REMARK 470 SER A 943 OG REMARK 470 THR A 944 OG1 CG2 REMARK 470 SER A 946 OG REMARK 470 ASP A 988 CG OD1 OD2 REMARK 470 GLU A 991 CG CD OE1 OE2 REMARK 470 LYS A1041 CG CD CE NZ REMARK 470 LYS A1048 CG CD CE NZ REMARK 470 SER A1054 OG REMARK 470 ARG A1110 CG CD NE CZ NH1 NH2 REMARK 470 GLU A1114 CG CD OE1 OE2 REMARK 470 GLN A1145 CG CD OE1 NE2 REMARK 470 GLU A1147 CG CD OE1 OE2 REMARK 470 LEU A1148 CG CD1 CD2 REMARK 470 ILE B 68 CG1 CG2 CD1 REMARK 470 THR B 108 OG1 CG2 REMARK 470 THR B 109 OG1 CG2 REMARK 470 LEU B 110 CG CD1 CD2 REMARK 470 ASP B 111 CG OD1 OD2 REMARK 470 SER B 112 OG REMARK 470 LYS B 113 CG CD CE NZ REMARK 470 ASN B 121 CG OD1 ND2 REMARK 470 ASN B 122 CG OD1 ND2 REMARK 470 GLU B 132 CG CD OE1 OE2 REMARK 470 PHE B 133 CG CD1 CD2 CE1 CE2 CZ REMARK 470 PHE B 157 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG B 158 CG CD NE CZ NH1 NH2 REMARK 470 TYR B 160 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN B 173 CG CD OE1 NE2 REMARK 470 LEU B 176 CG CD1 CD2 REMARK 470 LYS B 187 CG CD CE NZ REMARK 470 TYR B 200 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN B 221 CG CD OE1 NE2 REMARK 470 GLU B 227 CG CD OE1 OE2 REMARK 470 LEU B 247 CG CD1 CD2 REMARK 470 ARG B 249 CG CD NE CZ NH1 NH2 REMARK 470 TYR B 251 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU B 252 CG CD1 CD2 REMARK 470 THR B 253 OG1 CG2 REMARK 470 THR B 262 OG1 CG2 REMARK 470 LYS B 307 CG CD CE NZ REMARK 470 GLN B 324 CG CD OE1 NE2 REMARK 470 THR B 326 OG1 CG2 REMARK 470 LYS B 532 CG CD CE NZ REMARK 470 LYS B 560 CG CD CE NZ REMARK 470 LYS B 561 CG CD CE NZ REMARK 470 ASP B 571 CG OD1 OD2 REMARK 470 ILE B 572 CG1 CG2 CD1 REMARK 470 GLN B 583 CG CD OE1 NE2 REMARK 470 THR B 621 OG1 CG2 REMARK 470 ARG B 649 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 664 CG CD OE1 OE2 REMARK 470 ASP B 666 CG OD1 OD2 REMARK 470 SER B 676 OG REMARK 470 GLN B 678 CG CD OE1 NE2 REMARK 470 THR B 679 OG1 CG2 REMARK 470 GLU B 705 CG CD OE1 OE2 REMARK 470 MET B 743 CG SD CE REMARK 470 LYS B 789 CG CD CE NZ REMARK 470 LYS B 793 CG CD CE NZ REMARK 470 ILE B 797 CG1 CG2 CD1 REMARK 470 LYS B 798 CG CD CE NZ REMARK 470 ASP B 811 CG OD1 OD2 REMARK 470 GLU B 822 CG CD OE1 OE2 REMARK 470 LYS B 828 CG CD CE NZ REMARK 470 LYS B 857 CG CD CE NZ REMARK 470 GLU B 921 CG CD OE1 OE2 REMARK 470 LYS B 924 CG CD CE NZ REMARK 470 LYS B 936 CG CD CE NZ REMARK 470 ASP B 939 CG OD1 OD2 REMARK 470 SER B 943 OG REMARK 470 THR B 944 OG1 CG2 REMARK 470 SER B 946 OG REMARK 470 LYS B 950 CG CD CE NZ REMARK 470 LYS B 967 CG CD CE NZ REMARK 470 LYS B1048 CG CD CE NZ REMARK 470 LYS B1076 CG CD CE NZ REMARK 470 ARG B1110 CG CD NE CZ NH1 NH2 REMARK 470 TYR B1141 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU B1144 CG CD1 CD2 REMARK 470 GLN B1145 CG CD OE1 NE2 REMARK 470 LEU B1148 CG CD1 CD2 REMARK 470 ASP B1149 CG OD1 OD2 REMARK 470 SER C 46 OG REMARK 470 ASP C 53 CG OD1 OD2 REMARK 470 GLU C 96 CG CD OE1 OE2 REMARK 470 LYS C 97 CG CD CE NZ REMARK 470 SER C 98 OG REMARK 470 THR C 109 OG1 CG2 REMARK 470 LEU C 110 CG CD1 CD2 REMARK 470 ASP C 111 CG OD1 OD2 REMARK 470 LYS C 113 CG CD CE NZ REMARK 470 THR C 124 OG1 CG2 REMARK 470 GLU C 132 CG CD OE1 OE2 REMARK 470 PHE C 133 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLN C 134 CG CD OE1 NE2 REMARK 470 CYS C 136 SG REMARK 470 ASN C 137 CG OD1 ND2 REMARK 470 ASP C 138 CG OD1 OD2 REMARK 470 ARG C 158 CG CD NE CZ NH1 NH2 REMARK 470 TYR C 160 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ASN C 164 CG OD1 ND2 REMARK 470 GLN C 173 CG CD OE1 NE2 REMARK 470 LEU C 176 CG CD1 CD2 REMARK 470 LYS C 187 CG CD CE NZ REMARK 470 LYS C 206 CG CD CE NZ REMARK 470 ILE C 210 CG1 CG2 CD1 REMARK 470 LEU C 247 CG CD1 CD2 REMARK 470 HIS C 248 CG ND1 CD2 CE1 NE2 REMARK 470 ARG C 249 CG CD NE CZ NH1 NH2 REMARK 470 TYR C 251 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 THR C 262 OG1 CG2 REMARK 470 GLU C 284 CG CD OE1 OE2 REMARK 470 ASP C 290 CG OD1 OD2 REMARK 470 LYS C 307 CG CD CE NZ REMARK 470 GLU C 312 CG CD OE1 OE2 REMARK 470 LYS C 313 CG CD CE NZ REMARK 470 ARG C 322 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 327 CG CD OE1 OE2 REMARK 470 ARG C 349 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 359 CG CD CE NZ REMARK 470 TYR C 372 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS C 389 CG CD CE NZ REMARK 470 ASN C 391 CG OD1 ND2 REMARK 470 GLU C 409 CG CD OE1 OE2 REMARK 470 ASP C 430 CG OD1 OD2 REMARK 470 ASP C 431 CG OD1 OD2 REMARK 470 ASN C 442 CG OD1 ND2 REMARK 470 LEU C 444 CG CD1 CD2 REMARK 470 ASP C 445 CG OD1 OD2 REMARK 470 LYS C 447 CG CD CE NZ REMARK 470 ASN C 451 CG OD1 ND2 REMARK 470 LYS C 465 CG CD CE NZ REMARK 470 GLN C 477 CG CD OE1 NE2 REMARK 470 GLU C 519 CG CD OE1 OE2 REMARK 470 THR C 526 OG1 CG2 REMARK 470 LYS C 531 CG CD CE NZ REMARK 470 LYS C 532 CG CD CE NZ REMARK 470 ASN C 535 CG OD1 ND2 REMARK 470 LYS C 540 CG CD CE NZ REMARK 470 GLU C 557 CG CD OE1 OE2 REMARK 470 ASN C 559 CG OD1 ND2 REMARK 470 LYS C 560 CG CD CE NZ REMARK 470 LYS C 561 CG CD CE NZ REMARK 470 ASP C 571 CG OD1 OD2 REMARK 470 ASP C 574 CG OD1 OD2 REMARK 470 GLN C 616 CG CD OE1 NE2 REMARK 470 THR C 641 OG1 CG2 REMARK 470 SER C 643 OG REMARK 470 ARG C 649 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 664 CG CD OE1 OE2 REMARK 470 ASP C 666 CG OD1 OD2 REMARK 470 SER C 676 OG REMARK 470 GLN C 678 CG CD OE1 NE2 REMARK 470 THR C 679 OG1 CG2 REMARK 470 GLN C 693 CG CD OE1 NE2 REMARK 470 GLU C 705 CG CD OE1 OE2 REMARK 470 ASP C 740 CG OD1 OD2 REMARK 470 ASP C 748 CG OD1 OD2 REMARK 470 LYS C 779 CG CD CE NZ REMARK 470 GLN C 782 CG CD OE1 NE2 REMARK 470 GLU C 783 CG CD OE1 OE2 REMARK 470 LYS C 789 CG CD CE NZ REMARK 470 LYS C 793 CG CD CE NZ REMARK 470 ILE C 797 CG1 CG2 CD1 REMARK 470 LYS C 798 CG CD CE NZ REMARK 470 LYS C 814 CG CD CE NZ REMARK 470 LEU C 831 CG CD1 CD2 REMARK 470 LYS C 857 CG CD CE NZ REMARK 470 PHE C 858 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU C 871 CG CD OE1 OE2 REMARK 470 SER C 942 OG REMARK 470 SER C 943 OG REMARK 470 SER C 946 OG REMARK 470 ASP C 988 CG OD1 OD2 REMARK 470 GLU C 991 CG CD OE1 OE2 REMARK 470 ARG C 998 CG CD NE CZ NH1 NH2 REMARK 470 ARG C1017 CG CD NE CZ NH1 NH2 REMARK 470 ARG C1022 CG CD NE CZ NH1 NH2 REMARK 470 LYS C1041 CG CD CE NZ REMARK 470 LYS C1048 CG CD CE NZ REMARK 470 LYS C1076 CG CD CE NZ REMARK 470 GLU C1095 CG CD OE1 OE2 REMARK 470 LEU C1144 CG CD1 CD2 REMARK 470 GLN C1145 CG CD OE1 NE2 REMARK 470 LYS F 13 CG CD CE NZ REMARK 470 LYS F 67 CG CD CE NZ REMARK 470 LYS F 78 CG CD CE NZ REMARK 470 GLN F 84 CG CD OE1 NE2 REMARK 470 LYS F 89 CG CD CE NZ REMARK 470 LYS H 13 CG CD CE NZ REMARK 470 LYS H 67 CG CD CE NZ REMARK 470 LYS H 78 CG CD CE NZ REMARK 470 GLN H 84 CG CD OE1 NE2 REMARK 470 LYS H 89 CG CD CE NZ 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 OH TYR B 759 OD1 ASP B 997 2.14 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 CYS B 336 CA - CB - SG ANGL. DEV. = 6.9 DEGREES REMARK 500 PRO C 415 CA - N - CD ANGL. DEV. = -11.2 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 PHE A 32 -137.48 61.42 REMARK 500 ASN A 87 -63.32 -95.55 REMARK 500 GLN A 115 64.37 60.37 REMARK 500 LEU A 229 -62.41 -101.06 REMARK 500 PHE A 338 22.27 -140.14 REMARK 500 GLU A 340 -59.07 34.14 REMARK 500 ASN A 360 40.82 73.94 REMARK 500 CYS A 361 -174.12 -173.81 REMARK 500 ILE A 418 -54.60 64.63 REMARK 500 ASP A 428 31.93 -97.96 REMARK 500 LYS A 478 146.50 74.22 REMARK 500 CYS A 525 -179.39 -174.00 REMARK 500 ALA A 786 36.55 -99.22 REMARK 500 PHE B 32 -125.79 57.42 REMARK 500 ASN B 99 63.86 60.12 REMARK 500 ASP B 339 -37.63 -132.52 REMARK 500 CYS B 361 141.95 -171.49 REMARK 500 ILE B 418 -53.55 65.24 REMARK 500 LYS B 478 147.91 74.16 REMARK 500 ALA B 484 61.06 60.42 REMARK 500 CYS B 525 146.76 -174.43 REMARK 500 THR B 607 -61.95 -93.33 REMARK 500 ALA B 786 30.43 -93.17 REMARK 500 PHE B 805 31.15 -99.66 REMARK 500 LYS B1041 50.04 -93.95 REMARK 500 GLU B1114 84.29 -151.39 REMARK 500 CYS B1129 30.01 -96.83 REMARK 500 PHE C 32 -140.36 59.04 REMARK 500 ASP C 53 -165.88 -161.26 REMARK 500 ASN C 87 -148.16 57.24 REMARK 500 SER C 98 -3.09 66.85 REMARK 500 PRO C 233 0.52 -68.84 REMARK 500 HIS C 522 -167.22 -79.48 REMARK 500 CYS C 620 36.16 -94.68 REMARK 500 LYS C 798 58.79 -91.84 REMARK 500 ASN C1101 15.31 57.46 REMARK 500 GLU C1114 83.01 -152.68 REMARK 500 SER F 52 -167.35 57.90 REMARK 500 MET F 107 -60.83 -92.45 REMARK 500 MET F 108 24.29 44.46 REMARK 500 VAL G 46 -52.48 -121.22 REMARK 500 ILE G 98 -28.30 53.96 REMARK 500 PHE G 99 -170.40 59.20 REMARK 500 LEU G 108 30.44 -95.71 REMARK 500 ALA H 32 149.62 68.53 REMARK 500 SER H 52 -162.44 57.56 REMARK 500 MET H 108 14.87 55.39 REMARK 500 ILE J 98 -29.26 53.07 REMARK 500 PHE J 99 -171.26 58.60 REMARK 500 LEU J 108 31.88 -96.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 ASN A 360 CYS A 361 142.50 REMARK 500 CYS A 620 THR A 621 149.41 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH F 216 DISTANCE = 9.57 ANGSTROMS REMARK 525 HOH F 217 DISTANCE = 18.09 ANGSTROMS REMARK 525 HOH F 218 DISTANCE = 18.38 ANGSTROMS REMARK 525 HOH F 219 DISTANCE = 20.16 ANGSTROMS REMARK 525 HOH G 201 DISTANCE = 9.72 ANGSTROMS REMARK 525 HOH G 202 DISTANCE = 13.49 ANGSTROMS REMARK 525 HOH G 203 DISTANCE = 19.38 ANGSTROMS REMARK 525 HOH G 204 DISTANCE = 24.96 ANGSTROMS REMARK 525 HOH G 205 DISTANCE = 26.28 ANGSTROMS REMARK 525 HOH G 206 DISTANCE = 32.19 ANGSTROMS REMARK 525 HOH H 213 DISTANCE = 8.51 ANGSTROMS REMARK 525 HOH H 214 DISTANCE = 17.38 ANGSTROMS REMARK 525 HOH H 215 DISTANCE = 18.20 ANGSTROMS REMARK 525 HOH H 216 DISTANCE = 20.57 ANGSTROMS REMARK 525 HOH J 203 DISTANCE = 9.22 ANGSTROMS REMARK 525 HOH J 204 DISTANCE = 12.66 ANGSTROMS REMARK 525 HOH J 205 DISTANCE = 20.08 ANGSTROMS REMARK 525 HOH J 206 DISTANCE = 25.95 ANGSTROMS REMARK 525 HOH J 207 DISTANCE = 26.36 ANGSTROMS REMARK 525 HOH J 208 DISTANCE = 32.10 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-37240 RELATED DB: EMDB REMARK 900 SARS-COV-2 OMICRON SPIKE IN COMPLEX WITH 5817 FAB DBREF 8KHC A 27 1149 UNP P0DTC2 SPIKE_SARS2 27 1146 DBREF 8KHC B 27 1149 UNP P0DTC2 SPIKE_SARS2 27 1146 DBREF 8KHC C 27 1149 UNP P0DTC2 SPIKE_SARS2 27 1146 DBREF 8KHC F 1 125 PDB 8KHC 8KHC 1 125 DBREF 8KHC G 3 110 PDB 8KHC 8KHC 3 110 DBREF 8KHC H 1 125 PDB 8KHC 8KHC 1 125 DBREF 8KHC J 3 110 PDB 8KHC 8KHC 3 110 SEQADV 8KHC VAL A 67 UNP P0DTC2 ALA 67 CONFLICT SEQADV 8KHC ILE A 95 UNP P0DTC2 THR 95 CONFLICT SEQADV 8KHC ASP A 142 UNP P0DTC2 GLY 142 CONFLICT SEQADV 8KHC ASP A 156 UNP P0DTC2 GLU 156 CONFLICT SEQADV 8KHC ASP A 339 UNP P0DTC2 GLY 339 CONFLICT SEQADV 8KHC LEU A 371 UNP P0DTC2 SER 371 CONFLICT SEQADV 8KHC PRO A 373 UNP P0DTC2 SER 373 CONFLICT SEQADV 8KHC PHE A 375 UNP P0DTC2 SER 375 CONFLICT SEQADV 8KHC ASN A 417 UNP P0DTC2 LYS 417 CONFLICT SEQADV 8KHC LYS A 440 UNP P0DTC2 ASN 440 CONFLICT SEQADV 8KHC SER A 446 UNP P0DTC2 GLY 446 CONFLICT SEQADV 8KHC ASN A 477 UNP P0DTC2 SER 477 CONFLICT SEQADV 8KHC LYS A 478 UNP P0DTC2 THR 478 CONFLICT SEQADV 8KHC ALA A 484 UNP P0DTC2 GLU 484 CONFLICT SEQADV 8KHC ARG A 493 UNP P0DTC2 GLN 493 CONFLICT SEQADV 8KHC SER A 496 UNP P0DTC2 GLY 496 CONFLICT SEQADV 8KHC ARG A 498 UNP P0DTC2 GLN 498 CONFLICT SEQADV 8KHC TYR A 501 UNP P0DTC2 ASN 501 CONFLICT SEQADV 8KHC HIS A 505 UNP P0DTC2 TYR 505 CONFLICT SEQADV 8KHC LYS A 550 UNP P0DTC2 THR 547 CONFLICT SEQADV 8KHC GLY A 617 UNP P0DTC2 ASP 614 CONFLICT SEQADV 8KHC TYR A 658 UNP P0DTC2 HIS 655 CONFLICT SEQADV 8KHC LYS A 767 UNP P0DTC2 ASN 764 CONFLICT SEQADV 8KHC TYR A 799 UNP P0DTC2 ASP 796 CONFLICT SEQADV 8KHC LYS A 859 UNP P0DTC2 ASN 856 CONFLICT SEQADV 8KHC HIS A 957 UNP P0DTC2 GLN 954 CONFLICT SEQADV 8KHC LYS A 972 UNP P0DTC2 ASN 969 CONFLICT SEQADV 8KHC PHE A 984 UNP P0DTC2 LEU 981 CONFLICT SEQADV 8KHC PRO A 989 UNP P0DTC2 LYS 986 CONFLICT SEQADV 8KHC PRO A 990 UNP P0DTC2 VAL 987 CONFLICT SEQADV 8KHC VAL B 67 UNP P0DTC2 ALA 67 CONFLICT SEQADV 8KHC ILE B 95 UNP P0DTC2 THR 95 CONFLICT SEQADV 8KHC ASP B 142 UNP P0DTC2 GLY 142 CONFLICT SEQADV 8KHC ASP B 156 UNP P0DTC2 GLU 156 CONFLICT SEQADV 8KHC ASP B 339 UNP P0DTC2 GLY 339 CONFLICT SEQADV 8KHC LEU B 371 UNP P0DTC2 SER 371 CONFLICT SEQADV 8KHC PRO B 373 UNP P0DTC2 SER 373 CONFLICT SEQADV 8KHC PHE B 375 UNP P0DTC2 SER 375 CONFLICT SEQADV 8KHC ASN B 417 UNP P0DTC2 LYS 417 CONFLICT SEQADV 8KHC LYS B 440 UNP P0DTC2 ASN 440 CONFLICT SEQADV 8KHC SER B 446 UNP P0DTC2 GLY 446 CONFLICT SEQADV 8KHC ASN B 477 UNP P0DTC2 SER 477 CONFLICT SEQADV 8KHC LYS B 478 UNP P0DTC2 THR 478 CONFLICT SEQADV 8KHC ALA B 484 UNP P0DTC2 GLU 484 CONFLICT SEQADV 8KHC ARG B 493 UNP P0DTC2 GLN 493 CONFLICT SEQADV 8KHC SER B 496 UNP P0DTC2 GLY 496 CONFLICT SEQADV 8KHC ARG B 498 UNP P0DTC2 GLN 498 CONFLICT SEQADV 8KHC TYR B 501 UNP P0DTC2 ASN 501 CONFLICT SEQADV 8KHC HIS B 505 UNP P0DTC2 TYR 505 CONFLICT SEQADV 8KHC LYS B 550 UNP P0DTC2 THR 547 CONFLICT SEQADV 8KHC GLY B 617 UNP P0DTC2 ASP 614 CONFLICT SEQADV 8KHC TYR B 658 UNP P0DTC2 HIS 655 CONFLICT SEQADV 8KHC LYS B 767 UNP P0DTC2 ASN 764 CONFLICT SEQADV 8KHC TYR B 799 UNP P0DTC2 ASP 796 CONFLICT SEQADV 8KHC LYS B 859 UNP P0DTC2 ASN 856 CONFLICT SEQADV 8KHC HIS B 957 UNP P0DTC2 GLN 954 CONFLICT SEQADV 8KHC LYS B 972 UNP P0DTC2 ASN 969 CONFLICT SEQADV 8KHC PHE B 984 UNP P0DTC2 LEU 981 CONFLICT SEQADV 8KHC PRO B 989 UNP P0DTC2 LYS 986 CONFLICT SEQADV 8KHC PRO B 990 UNP P0DTC2 VAL 987 CONFLICT SEQADV 8KHC VAL C 67 UNP P0DTC2 ALA 67 CONFLICT SEQADV 8KHC ILE C 95 UNP P0DTC2 THR 95 CONFLICT SEQADV 8KHC ASP C 142 UNP P0DTC2 GLY 142 CONFLICT SEQADV 8KHC ASP C 156 UNP P0DTC2 GLU 156 CONFLICT SEQADV 8KHC ASP C 342 UNP P0DTC2 GLY 339 CONFLICT SEQADV 8KHC LEU C 374 UNP P0DTC2 SER 371 CONFLICT SEQADV 8KHC PRO C 376 UNP P0DTC2 SER 373 CONFLICT SEQADV 8KHC PHE C 378 UNP P0DTC2 SER 375 CONFLICT SEQADV 8KHC ASN C 420 UNP P0DTC2 LYS 417 CONFLICT SEQADV 8KHC LYS C 443 UNP P0DTC2 ASN 440 CONFLICT SEQADV 8KHC SER C 449 UNP P0DTC2 GLY 446 CONFLICT SEQADV 8KHC ASN C 480 UNP P0DTC2 SER 477 CONFLICT SEQADV 8KHC LYS C 481 UNP P0DTC2 THR 478 CONFLICT SEQADV 8KHC ALA C 487 UNP P0DTC2 GLU 484 CONFLICT SEQADV 8KHC ARG C 496 UNP P0DTC2 GLN 493 CONFLICT SEQADV 8KHC SER C 499 UNP P0DTC2 GLY 496 CONFLICT SEQADV 8KHC ARG C 501 UNP P0DTC2 GLN 498 CONFLICT SEQADV 8KHC TYR C 504 UNP P0DTC2 ASN 501 CONFLICT SEQADV 8KHC HIS C 508 UNP P0DTC2 TYR 505 CONFLICT SEQADV 8KHC LYS C 550 UNP P0DTC2 THR 547 CONFLICT SEQADV 8KHC GLY C 617 UNP P0DTC2 ASP 614 CONFLICT SEQADV 8KHC TYR C 658 UNP P0DTC2 HIS 655 CONFLICT SEQADV 8KHC LYS C 767 UNP P0DTC2 ASN 764 CONFLICT SEQADV 8KHC TYR C 799 UNP P0DTC2 ASP 796 CONFLICT SEQADV 8KHC LYS C 859 UNP P0DTC2 ASN 856 CONFLICT SEQADV 8KHC HIS C 957 UNP P0DTC2 GLN 954 CONFLICT SEQADV 8KHC LYS C 972 UNP P0DTC2 ASN 969 CONFLICT SEQADV 8KHC PHE C 984 UNP P0DTC2 LEU 981 CONFLICT SEQADV 8KHC PRO C 989 UNP P0DTC2 LYS 986 CONFLICT SEQADV 8KHC PRO C 990 UNP P0DTC2 VAL 987 CONFLICT SEQRES 1 A 1120 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 2 A 1120 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 3 A 1120 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 4 A 1120 HIS VAL ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG SEQRES 5 A 1120 PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR SEQRES 6 A 1120 PHE ALA SER ILE GLU LYS SER ASN ILE ILE ARG GLY TRP SEQRES 7 A 1120 ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU SEQRES 8 A 1120 LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL SEQRES 9 A 1120 CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU ASP VAL SEQRES 10 A 1120 TYR TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER ASP SEQRES 11 A 1120 PHE ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU SEQRES 12 A 1120 TYR VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS SEQRES 13 A 1120 GLN GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS SEQRES 14 A 1120 ASN ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR SEQRES 15 A 1120 PRO ILE ASN LEU VAL ARG ASP LEU PRO GLN GLY PHE SER SEQRES 16 A 1120 ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN SEQRES 17 A 1120 ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS ARG SER SEQRES 18 A 1120 TYR LEU THR PRO GLY ASP SER SER SER GLY TRP THR ALA SEQRES 19 A 1120 GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG SEQRES 20 A 1120 THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR ILE THR SEQRES 21 A 1120 ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER GLU THR SEQRES 22 A 1120 LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS GLY ILE SEQRES 23 A 1120 TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR GLU SER SEQRES 24 A 1120 ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE SEQRES 25 A 1120 ASP GLU VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR SEQRES 26 A 1120 ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP SEQRES 27 A 1120 TYR SER VAL LEU TYR ASN LEU ALA PRO PHE PHE THR PHE SEQRES 28 A 1120 LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU SEQRES 29 A 1120 CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG SEQRES 30 A 1120 GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY SEQRES 31 A 1120 ASN ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE SEQRES 32 A 1120 THR GLY CYS VAL ILE ALA TRP ASN SER ASN LYS LEU ASP SEQRES 33 A 1120 SER LYS VAL SER GLY ASN TYR ASN TYR LEU TYR ARG LEU SEQRES 34 A 1120 PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SEQRES 35 A 1120 SER THR GLU ILE TYR GLN ALA GLY ASN LYS PRO CYS ASN SEQRES 36 A 1120 GLY VAL ALA GLY PHE ASN CYS TYR PHE PRO LEU ARG SER SEQRES 37 A 1120 TYR SER PHE ARG PRO THR TYR GLY VAL GLY HIS GLN PRO SEQRES 38 A 1120 TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA SEQRES 39 A 1120 PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU SEQRES 40 A 1120 VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU SEQRES 41 A 1120 LYS GLY THR GLY VAL LEU THR GLU SER ASN LYS LYS PHE SEQRES 42 A 1120 LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA ASP THR SEQRES 43 A 1120 THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU ILE LEU SEQRES 44 A 1120 ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER VAL ILE SEQRES 45 A 1120 THR PRO GLY THR ASN THR SER ASN GLN VAL ALA VAL LEU SEQRES 46 A 1120 TYR GLN GLY VAL ASN CYS THR GLU VAL PRO VAL ALA ILE SEQRES 47 A 1120 HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL TYR SER SEQRES 48 A 1120 THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY CYS LEU SEQRES 49 A 1120 ILE GLY ALA GLU TYR VAL ASN ASN SER TYR GLU CYS ASP SEQRES 50 A 1120 ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR GLN THR SEQRES 51 A 1120 GLN THR ASN SER PRO ARG ARG ALA ARG SER VAL ALA SER SEQRES 52 A 1120 GLN SER ILE ILE ALA TYR THR MET SER LEU GLY ALA GLU SEQRES 53 A 1120 ASN SER VAL ALA TYR SER ASN ASN SER ILE ALA ILE PRO SEQRES 54 A 1120 THR ASN PHE THR ILE SER VAL THR THR GLU ILE LEU PRO SEQRES 55 A 1120 VAL SER MET THR LYS THR SER VAL ASP CYS THR MET TYR SEQRES 56 A 1120 ILE CYS GLY ASP SER THR GLU CYS SER ASN LEU LEU LEU SEQRES 57 A 1120 GLN TYR GLY SER PHE CYS THR GLN LEU LYS ARG ALA LEU SEQRES 58 A 1120 THR GLY ILE ALA VAL GLU GLN ASP LYS ASN THR GLN GLU SEQRES 59 A 1120 VAL PHE ALA GLN VAL LYS GLN ILE TYR LYS THR PRO PRO SEQRES 60 A 1120 ILE LYS TYR PHE GLY GLY PHE ASN PHE SER GLN ILE LEU SEQRES 61 A 1120 PRO ASP PRO SER LYS PRO SER LYS ARG SER PHE ILE GLU SEQRES 62 A 1120 ASP LEU LEU PHE ASN LYS VAL THR LEU ALA ASP ALA GLY SEQRES 63 A 1120 PHE ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA SEQRES 64 A 1120 ALA ARG ASP LEU ILE CYS ALA GLN LYS PHE LYS GLY LEU SEQRES 65 A 1120 THR VAL LEU PRO PRO LEU LEU THR ASP GLU MET ILE ALA SEQRES 66 A 1120 GLN TYR THR SER ALA LEU LEU ALA GLY THR ILE THR SER SEQRES 67 A 1120 GLY TRP THR PHE GLY ALA GLY ALA ALA LEU GLN ILE PRO SEQRES 68 A 1120 PHE ALA MET GLN MET ALA TYR ARG PHE ASN GLY ILE GLY SEQRES 69 A 1120 VAL THR GLN ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE SEQRES 70 A 1120 ALA ASN GLN PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SEQRES 71 A 1120 SER LEU SER SER THR ALA SER ALA LEU GLY LYS LEU GLN SEQRES 72 A 1120 ASP VAL VAL ASN HIS ASN ALA GLN ALA LEU ASN THR LEU SEQRES 73 A 1120 VAL LYS GLN LEU SER SER LYS PHE GLY ALA ILE SER SER SEQRES 74 A 1120 VAL LEU ASN ASP ILE PHE SER ARG LEU ASP PRO PRO GLU SEQRES 75 A 1120 ALA GLU VAL GLN ILE ASP ARG LEU ILE THR GLY ARG LEU SEQRES 76 A 1120 GLN SER LEU GLN THR TYR VAL THR GLN GLN LEU ILE ARG SEQRES 77 A 1120 ALA ALA GLU ILE ARG ALA SER ALA ASN LEU ALA ALA THR SEQRES 78 A 1120 LYS MET SER GLU CYS VAL LEU GLY GLN SER LYS ARG VAL SEQRES 79 A 1120 ASP PHE CYS GLY LYS GLY TYR HIS LEU MET SER PHE PRO SEQRES 80 A 1120 GLN SER ALA PRO HIS GLY VAL VAL PHE LEU HIS VAL THR SEQRES 81 A 1120 TYR VAL PRO ALA GLN GLU LYS ASN PHE THR THR ALA PRO SEQRES 82 A 1120 ALA ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU SEQRES 83 A 1120 GLY VAL PHE VAL SER ASN GLY THR HIS TRP PHE VAL THR SEQRES 84 A 1120 GLN ARG ASN PHE TYR GLU PRO GLN ILE ILE THR THR ASP SEQRES 85 A 1120 ASN THR PHE VAL SER GLY ASN CYS ASP VAL VAL ILE GLY SEQRES 86 A 1120 ILE VAL ASN ASN THR VAL TYR ASP PRO LEU GLN PRO GLU SEQRES 87 A 1120 LEU ASP SEQRES 1 B 1120 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 2 B 1120 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 3 B 1120 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 4 B 1120 HIS VAL ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG SEQRES 5 B 1120 PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR SEQRES 6 B 1120 PHE ALA SER ILE GLU LYS SER ASN ILE ILE ARG GLY TRP SEQRES 7 B 1120 ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU SEQRES 8 B 1120 LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL SEQRES 9 B 1120 CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU ASP VAL SEQRES 10 B 1120 TYR TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER ASP SEQRES 11 B 1120 PHE ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU SEQRES 12 B 1120 TYR VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS SEQRES 13 B 1120 GLN GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS SEQRES 14 B 1120 ASN ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR SEQRES 15 B 1120 PRO ILE ASN LEU VAL ARG ASP LEU PRO GLN GLY PHE SER SEQRES 16 B 1120 ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN SEQRES 17 B 1120 ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS ARG SER SEQRES 18 B 1120 TYR LEU THR PRO GLY ASP SER SER SER GLY TRP THR ALA SEQRES 19 B 1120 GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG SEQRES 20 B 1120 THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR ILE THR SEQRES 21 B 1120 ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER GLU THR SEQRES 22 B 1120 LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS GLY ILE SEQRES 23 B 1120 TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR GLU SER SEQRES 24 B 1120 ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE SEQRES 25 B 1120 ASP GLU VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR SEQRES 26 B 1120 ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP SEQRES 27 B 1120 TYR SER VAL LEU TYR ASN LEU ALA PRO PHE PHE THR PHE SEQRES 28 B 1120 LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU SEQRES 29 B 1120 CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG SEQRES 30 B 1120 GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY SEQRES 31 B 1120 ASN ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE SEQRES 32 B 1120 THR GLY CYS VAL ILE ALA TRP ASN SER ASN LYS LEU ASP SEQRES 33 B 1120 SER LYS VAL SER GLY ASN TYR ASN TYR LEU TYR ARG LEU SEQRES 34 B 1120 PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SEQRES 35 B 1120 SER THR GLU ILE TYR GLN ALA GLY ASN LYS PRO CYS ASN SEQRES 36 B 1120 GLY VAL ALA GLY PHE ASN CYS TYR PHE PRO LEU ARG SER SEQRES 37 B 1120 TYR SER PHE ARG PRO THR TYR GLY VAL GLY HIS GLN PRO SEQRES 38 B 1120 TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA SEQRES 39 B 1120 PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU SEQRES 40 B 1120 VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU SEQRES 41 B 1120 LYS GLY THR GLY VAL LEU THR GLU SER ASN LYS LYS PHE SEQRES 42 B 1120 LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA ASP THR SEQRES 43 B 1120 THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU ILE LEU SEQRES 44 B 1120 ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER VAL ILE SEQRES 45 B 1120 THR PRO GLY THR ASN THR SER ASN GLN VAL ALA VAL LEU SEQRES 46 B 1120 TYR GLN GLY VAL ASN CYS THR GLU VAL PRO VAL ALA ILE SEQRES 47 B 1120 HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL TYR SER SEQRES 48 B 1120 THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY CYS LEU SEQRES 49 B 1120 ILE GLY ALA GLU TYR VAL ASN ASN SER TYR GLU CYS ASP SEQRES 50 B 1120 ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR GLN THR SEQRES 51 B 1120 GLN THR ASN SER PRO ARG ARG ALA ARG SER VAL ALA SER SEQRES 52 B 1120 GLN SER ILE ILE ALA TYR THR MET SER LEU GLY ALA GLU SEQRES 53 B 1120 ASN SER VAL ALA TYR SER ASN ASN SER ILE ALA ILE PRO SEQRES 54 B 1120 THR ASN PHE THR ILE SER VAL THR THR GLU ILE LEU PRO SEQRES 55 B 1120 VAL SER MET THR LYS THR SER VAL ASP CYS THR MET TYR SEQRES 56 B 1120 ILE CYS GLY ASP SER THR GLU CYS SER ASN LEU LEU LEU SEQRES 57 B 1120 GLN TYR GLY SER PHE CYS THR GLN LEU LYS ARG ALA LEU SEQRES 58 B 1120 THR GLY ILE ALA VAL GLU GLN ASP LYS ASN THR GLN GLU SEQRES 59 B 1120 VAL PHE ALA GLN VAL LYS GLN ILE TYR LYS THR PRO PRO SEQRES 60 B 1120 ILE LYS TYR PHE GLY GLY PHE ASN PHE SER GLN ILE LEU SEQRES 61 B 1120 PRO ASP PRO SER LYS PRO SER LYS ARG SER PHE ILE GLU SEQRES 62 B 1120 ASP LEU LEU PHE ASN LYS VAL THR LEU ALA ASP ALA GLY SEQRES 63 B 1120 PHE ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA SEQRES 64 B 1120 ALA ARG ASP LEU ILE CYS ALA GLN LYS PHE LYS GLY LEU SEQRES 65 B 1120 THR VAL LEU PRO PRO LEU LEU THR ASP GLU MET ILE ALA SEQRES 66 B 1120 GLN TYR THR SER ALA LEU LEU ALA GLY THR ILE THR SER SEQRES 67 B 1120 GLY TRP THR PHE GLY ALA GLY ALA ALA LEU GLN ILE PRO SEQRES 68 B 1120 PHE ALA MET GLN MET ALA TYR ARG PHE ASN GLY ILE GLY SEQRES 69 B 1120 VAL THR GLN ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE SEQRES 70 B 1120 ALA ASN GLN PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SEQRES 71 B 1120 SER LEU SER SER THR ALA SER ALA LEU GLY LYS LEU GLN SEQRES 72 B 1120 ASP VAL VAL ASN HIS ASN ALA GLN ALA LEU ASN THR LEU SEQRES 73 B 1120 VAL LYS GLN LEU SER SER LYS PHE GLY ALA ILE SER SER SEQRES 74 B 1120 VAL LEU ASN ASP ILE PHE SER ARG LEU ASP PRO PRO GLU SEQRES 75 B 1120 ALA GLU VAL GLN ILE ASP ARG LEU ILE THR GLY ARG LEU SEQRES 76 B 1120 GLN SER LEU GLN THR TYR VAL THR GLN GLN LEU ILE ARG SEQRES 77 B 1120 ALA ALA GLU ILE ARG ALA SER ALA ASN LEU ALA ALA THR SEQRES 78 B 1120 LYS MET SER GLU CYS VAL LEU GLY GLN SER LYS ARG VAL SEQRES 79 B 1120 ASP PHE CYS GLY LYS GLY TYR HIS LEU MET SER PHE PRO SEQRES 80 B 1120 GLN SER ALA PRO HIS GLY VAL VAL PHE LEU HIS VAL THR SEQRES 81 B 1120 TYR VAL PRO ALA GLN GLU LYS ASN PHE THR THR ALA PRO SEQRES 82 B 1120 ALA ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU SEQRES 83 B 1120 GLY VAL PHE VAL SER ASN GLY THR HIS TRP PHE VAL THR SEQRES 84 B 1120 GLN ARG ASN PHE TYR GLU PRO GLN ILE ILE THR THR ASP SEQRES 85 B 1120 ASN THR PHE VAL SER GLY ASN CYS ASP VAL VAL ILE GLY SEQRES 86 B 1120 ILE VAL ASN ASN THR VAL TYR ASP PRO LEU GLN PRO GLU SEQRES 87 B 1120 LEU ASP SEQRES 1 C 1120 ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO SEQRES 2 C 1120 ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN SEQRES 3 C 1120 ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE SEQRES 4 C 1120 HIS VAL ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG SEQRES 5 C 1120 PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR SEQRES 6 C 1120 PHE ALA SER ILE GLU LYS SER ASN ILE ILE ARG GLY TRP SEQRES 7 C 1120 ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU SEQRES 8 C 1120 LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL SEQRES 9 C 1120 CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU ASP VAL SEQRES 10 C 1120 TYR TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER ASP SEQRES 11 C 1120 PHE ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU SEQRES 12 C 1120 TYR VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS SEQRES 13 C 1120 GLN GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS SEQRES 14 C 1120 ASN ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR SEQRES 15 C 1120 PRO ILE ASN LEU VAL ARG ASP LEU PRO GLN GLY PHE SER SEQRES 16 C 1120 ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN SEQRES 17 C 1120 ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS ARG SER SEQRES 18 C 1120 TYR LEU THR PRO GLY ASP SER SER SER GLY TRP THR ALA SEQRES 19 C 1120 GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG SEQRES 20 C 1120 THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR ILE THR SEQRES 21 C 1120 ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER GLU THR SEQRES 22 C 1120 LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS GLY ILE SEQRES 23 C 1120 TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR GLU SER SEQRES 24 C 1120 ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE SEQRES 25 C 1120 ASP GLU VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR SEQRES 26 C 1120 ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP SEQRES 27 C 1120 TYR SER VAL LEU TYR ASN LEU ALA PRO PHE PHE THR PHE SEQRES 28 C 1120 LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU SEQRES 29 C 1120 CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG SEQRES 30 C 1120 GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY SEQRES 31 C 1120 ASN ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE SEQRES 32 C 1120 THR GLY CYS VAL ILE ALA TRP ASN SER ASN LYS LEU ASP SEQRES 33 C 1120 SER LYS VAL SER GLY ASN TYR ASN TYR LEU TYR ARG LEU SEQRES 34 C 1120 PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SEQRES 35 C 1120 SER THR GLU ILE TYR GLN ALA GLY ASN LYS PRO CYS ASN SEQRES 36 C 1120 GLY VAL ALA GLY PHE ASN CYS TYR PHE PRO LEU ARG SER SEQRES 37 C 1120 TYR SER PHE ARG PRO THR TYR GLY VAL GLY HIS GLN PRO SEQRES 38 C 1120 TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA SEQRES 39 C 1120 PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU SEQRES 40 C 1120 VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU SEQRES 41 C 1120 LYS GLY THR GLY VAL LEU THR GLU SER ASN LYS LYS PHE SEQRES 42 C 1120 LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA ASP THR SEQRES 43 C 1120 THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU ILE LEU SEQRES 44 C 1120 ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER VAL ILE SEQRES 45 C 1120 THR PRO GLY THR ASN THR SER ASN GLN VAL ALA VAL LEU SEQRES 46 C 1120 TYR GLN GLY VAL ASN CYS THR GLU VAL PRO VAL ALA ILE SEQRES 47 C 1120 HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL TYR SER SEQRES 48 C 1120 THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY CYS LEU SEQRES 49 C 1120 ILE GLY ALA GLU TYR VAL ASN ASN SER TYR GLU CYS ASP SEQRES 50 C 1120 ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR GLN THR SEQRES 51 C 1120 GLN THR ASN SER PRO ARG ARG ALA ARG SER VAL ALA SER SEQRES 52 C 1120 GLN SER ILE ILE ALA TYR THR MET SER LEU GLY ALA GLU SEQRES 53 C 1120 ASN SER VAL ALA TYR SER ASN ASN SER ILE ALA ILE PRO SEQRES 54 C 1120 THR ASN PHE THR ILE SER VAL THR THR GLU ILE LEU PRO SEQRES 55 C 1120 VAL SER MET THR LYS THR SER VAL ASP CYS THR MET TYR SEQRES 56 C 1120 ILE CYS GLY ASP SER THR GLU CYS SER ASN LEU LEU LEU SEQRES 57 C 1120 GLN TYR GLY SER PHE CYS THR GLN LEU LYS ARG ALA LEU SEQRES 58 C 1120 THR GLY ILE ALA VAL GLU GLN ASP LYS ASN THR GLN GLU SEQRES 59 C 1120 VAL PHE ALA GLN VAL LYS GLN ILE TYR LYS THR PRO PRO SEQRES 60 C 1120 ILE LYS TYR PHE GLY GLY PHE ASN PHE SER GLN ILE LEU SEQRES 61 C 1120 PRO ASP PRO SER LYS PRO SER LYS ARG SER PHE ILE GLU SEQRES 62 C 1120 ASP LEU LEU PHE ASN LYS VAL THR LEU ALA ASP ALA GLY SEQRES 63 C 1120 PHE ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA SEQRES 64 C 1120 ALA ARG ASP LEU ILE CYS ALA GLN LYS PHE LYS GLY LEU SEQRES 65 C 1120 THR VAL LEU PRO PRO LEU LEU THR ASP GLU MET ILE ALA SEQRES 66 C 1120 GLN TYR THR SER ALA LEU LEU ALA GLY THR ILE THR SER SEQRES 67 C 1120 GLY TRP THR PHE GLY ALA GLY ALA ALA LEU GLN ILE PRO SEQRES 68 C 1120 PHE ALA MET GLN MET ALA TYR ARG PHE ASN GLY ILE GLY SEQRES 69 C 1120 VAL THR GLN ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE SEQRES 70 C 1120 ALA ASN GLN PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SEQRES 71 C 1120 SER LEU SER SER THR ALA SER ALA LEU GLY LYS LEU GLN SEQRES 72 C 1120 ASP VAL VAL ASN HIS ASN ALA GLN ALA LEU ASN THR LEU SEQRES 73 C 1120 VAL LYS GLN LEU SER SER LYS PHE GLY ALA ILE SER SER SEQRES 74 C 1120 VAL LEU ASN ASP ILE PHE SER ARG LEU ASP PRO PRO GLU SEQRES 75 C 1120 ALA GLU VAL GLN ILE ASP ARG LEU ILE THR GLY ARG LEU SEQRES 76 C 1120 GLN SER LEU GLN THR TYR VAL THR GLN GLN LEU ILE ARG SEQRES 77 C 1120 ALA ALA GLU ILE ARG ALA SER ALA ASN LEU ALA ALA THR SEQRES 78 C 1120 LYS MET SER GLU CYS VAL LEU GLY GLN SER LYS ARG VAL SEQRES 79 C 1120 ASP PHE CYS GLY LYS GLY TYR HIS LEU MET SER PHE PRO SEQRES 80 C 1120 GLN SER ALA PRO HIS GLY VAL VAL PHE LEU HIS VAL THR SEQRES 81 C 1120 TYR VAL PRO ALA GLN GLU LYS ASN PHE THR THR ALA PRO SEQRES 82 C 1120 ALA ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU SEQRES 83 C 1120 GLY VAL PHE VAL SER ASN GLY THR HIS TRP PHE VAL THR SEQRES 84 C 1120 GLN ARG ASN PHE TYR GLU PRO GLN ILE ILE THR THR ASP SEQRES 85 C 1120 ASN THR PHE VAL SER GLY ASN CYS ASP VAL VAL ILE GLY SEQRES 86 C 1120 ILE VAL ASN ASN THR VAL TYR ASP PRO LEU GLN PRO GLU SEQRES 87 C 1120 LEU ASP SEQRES 1 F 125 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 F 125 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 125 PHE SER PHE SER ASP ALA TRP MET SER TRP VAL ARG GLN SEQRES 4 F 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY ARG VAL SER SEQRES 5 F 125 SER GLU ILE GLY GLY GLY THR THR ASP TYR ALA ALA PRO SEQRES 6 F 125 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS SEQRES 7 F 125 ASN THR LEU PHE LEU GLN MET SER SER LEU LYS THR GLU SEQRES 8 F 125 ASP THR ALA VAL TYR TYR CYS THR THR GLY VAL ASP ILE SEQRES 9 F 125 VAL VAL MET MET TYR ALA ASP ASP ALA PHE ASP ILE TRP SEQRES 10 F 125 GLY GLN GLY THR MET VAL THR VAL SEQRES 1 G 108 GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA LEU GLY SEQRES 2 G 108 GLN THR VAL ARG ILE THR CYS GLN GLY ASP SER LEU ARG SEQRES 3 G 108 SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO GLY GLN SEQRES 4 G 108 ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN ARG PRO SEQRES 5 G 108 SER GLY ILE PRO ASP ARG PHE SER GLY SER SER SER GLY SEQRES 6 G 108 ASN THR ALA SER LEU THR ILE THR GLY PRO GLN ALA GLU SEQRES 7 G 108 ASP GLU ALA ASP TYR TYR CYS THR SER ARG ASP SER SER SEQRES 8 G 108 GLY ASN HIS VAL ILE PHE GLY GLY GLY THR LYS LEU THR SEQRES 9 G 108 VAL LEU GLY GLN SEQRES 1 H 125 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 125 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 125 PHE SER PHE SER ASP ALA TRP MET SER TRP VAL ARG GLN SEQRES 4 H 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL GLY ARG VAL SER SEQRES 5 H 125 SER GLU ILE GLY GLY GLY THR THR ASP TYR ALA ALA PRO SEQRES 6 H 125 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASP SER LYS SEQRES 7 H 125 ASN THR LEU PHE LEU GLN MET SER SER LEU LYS THR GLU SEQRES 8 H 125 ASP THR ALA VAL TYR TYR CYS THR THR GLY VAL ASP ILE SEQRES 9 H 125 VAL VAL MET MET TYR ALA ASP ASP ALA PHE ASP ILE TRP SEQRES 10 H 125 GLY GLN GLY THR MET VAL THR VAL SEQRES 1 J 108 GLU LEU THR GLN ASP PRO ALA VAL SER VAL ALA LEU GLY SEQRES 2 J 108 GLN THR VAL ARG ILE THR CYS GLN GLY ASP SER LEU ARG SEQRES 3 J 108 SER TYR TYR ALA SER TRP TYR GLN GLN LYS PRO GLY GLN SEQRES 4 J 108 ALA PRO VAL LEU VAL ILE TYR GLY LYS ASN ASN ARG PRO SEQRES 5 J 108 SER GLY ILE PRO ASP ARG PHE SER GLY SER SER SER GLY SEQRES 6 J 108 ASN THR ALA SER LEU THR ILE THR GLY PRO GLN ALA GLU SEQRES 7 J 108 ASP GLU ALA ASP TYR TYR CYS THR SER ARG ASP SER SER SEQRES 8 J 108 GLY ASN HIS VAL ILE PHE GLY GLY GLY THR LYS LEU THR SEQRES 9 J 108 VAL LEU GLY GLN HET NAG D 1 14 HET NAG D 2 14 HET NAG E 1 14 HET NAG E 2 14 HET NAG A1301 14 HET NAG A1302 14 HET NAG A1303 14 HET NAG A1304 14 HET NAG A1305 14 HET NAG A1306 14 HET NAG A1307 14 HET NAG A1308 14 HET NAG A1309 14 HET NAG A1310 14 HET NAG A1311 14 HET NAG A1312 14 HET NAG B1301 14 HET NAG B1302 14 HET NAG B1303 14 HET NAG B1304 14 HET NAG B1305 14 HET NAG B1306 14 HET NAG B1307 14 HET NAG B1308 14 HET NAG B1309 14 HET NAG B1310 14 HET NAG B1311 14 HET NAG B1312 14 HET NAG C1301 14 HET NAG C1302 14 HET NAG C1303 14 HET NAG C1304 14 HET NAG C1305 14 HET NAG C1306 14 HET NAG C1307 14 HET NAG C1308 14 HET NAG C1309 14 HET NAG C1310 14 HET NAG C1311 14 HET NAG C1312 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE 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 FORMUL 8 NAG 40(C8 H15 N O6) FORMUL 46 HOH *58(H2 O) HELIX 1 AA1 ASP A 111 GLN A 115 5 5 HELIX 2 AA2 ASP A 297 LYS A 307 1 11 HELIX 3 AA3 ASP A 339 ASN A 343 5 5 HELIX 4 AA4 TYR A 365 ASN A 370 1 6 HELIX 5 AA5 VAL A 407 ALA A 411 5 5 HELIX 6 AA6 ILE A 572 ASP A 574 5 3 HELIX 7 AA7 ASP A 740 CYS A 746 1 7 HELIX 8 AA8 SER A 749 LEU A 757 1 9 HELIX 9 AA9 GLN A 758 GLY A 760 5 3 HELIX 10 AB1 SER A 761 ALA A 786 1 26 HELIX 11 AB2 SER A 819 VAL A 829 1 11 HELIX 12 AB3 THR A 869 GLY A 888 1 20 HELIX 13 AB4 TRP A 889 ALA A 893 5 5 HELIX 14 AB5 PRO A 900 GLY A 911 1 12 HELIX 15 AB6 THR A 915 THR A 944 1 30 HELIX 16 AB7 LEU A 948 GLN A 968 1 21 HELIX 17 AB8 LEU A 969 SER A 971 5 3 HELIX 18 AB9 VAL A 979 ARG A 986 1 8 HELIX 19 AC1 ASP A 988 VAL A 1036 1 49 HELIX 20 AC2 PRO A 1143 LEU A 1148 1 6 HELIX 21 AC3 ASP B 297 LYS B 307 1 11 HELIX 22 AC4 ASP B 339 ASN B 343 5 5 HELIX 23 AC5 SER B 349 TRP B 353 5 5 HELIX 24 AC6 TYR B 365 ASN B 370 1 6 HELIX 25 AC7 ASP B 405 ALA B 411 5 7 HELIX 26 AC8 ASP B 740 CYS B 746 1 7 HELIX 27 AC9 SER B 749 LEU B 757 1 9 HELIX 28 AD1 GLN B 758 GLY B 760 5 3 HELIX 29 AD2 SER B 761 ALA B 786 1 26 HELIX 30 AD3 SER B 819 VAL B 829 1 11 HELIX 31 AD4 LYS B 857 LYS B 859 5 3 HELIX 32 AD5 THR B 869 GLY B 888 1 20 HELIX 33 AD6 TRP B 889 ALA B 893 5 5 HELIX 34 AD7 PRO B 900 ILE B 912 1 13 HELIX 35 AD8 THR B 915 THR B 944 1 30 HELIX 36 AD9 LEU B 948 GLN B 968 1 21 HELIX 37 AE1 LEU B 969 SER B 971 5 3 HELIX 38 AE2 VAL B 979 LEU B 987 1 9 HELIX 39 AE3 ASP B 988 VAL B 1036 1 49 HELIX 40 AE4 PRO B 1143 ASP B 1149 1 7 HELIX 41 AE5 ASP C 297 LYS C 307 1 11 HELIX 42 AE6 PRO C 340 ASN C 346 1 7 HELIX 43 AE7 TYR C 368 ASN C 373 1 6 HELIX 44 AE8 SER C 386 ASP C 392 5 7 HELIX 45 AE9 ASP C 408 GLN C 412 5 5 HELIX 46 AF1 GLY C 419 ASN C 425 1 7 HELIX 47 AF2 ASN C 480 ASN C 484 5 5 HELIX 48 AF3 ASP C 740 GLY C 747 1 8 HELIX 49 AF4 SER C 749 LEU C 757 1 9 HELIX 50 AF5 GLN C 758 GLY C 760 5 3 HELIX 51 AF6 SER C 761 ALA C 786 1 26 HELIX 52 AF7 SER C 819 VAL C 829 1 11 HELIX 53 AF8 THR C 869 SER C 887 1 19 HELIX 54 AF9 TRP C 889 ALA C 893 5 5 HELIX 55 AG1 PRO C 900 ILE C 912 1 13 HELIX 56 AG2 THR C 915 GLU C 921 1 7 HELIX 57 AG3 ASN C 922 THR C 944 1 23 HELIX 58 AG4 LEU C 948 GLN C 968 1 21 HELIX 59 AG5 LEU C 969 SER C 971 5 3 HELIX 60 AG6 VAL C 979 LEU C 987 1 9 HELIX 61 AG7 ASP C 988 LEU C 1037 1 50 SHEET 1 AA1 7 TYR A 28 ASN A 30 0 SHEET 2 AA1 7 ASN A 61 HIS A 66 -1 O VAL A 62 N THR A 29 SHEET 3 AA1 7 ALA A 267 TYR A 272 -1 O TYR A 268 N PHE A 65 SHEET 4 AA1 7 VAL A 90 ILE A 95 -1 N TYR A 91 O GLY A 271 SHEET 5 AA1 7 ASN A 188 LYS A 195 -1 O PHE A 192 N PHE A 92 SHEET 6 AA1 7 PHE A 201 PRO A 209 -1 O THR A 208 N LEU A 189 SHEET 7 AA1 7 PRO A 228 LEU A 232 -1 O LEU A 232 N PHE A 201 SHEET 1 AA2 3 LEU A 48 THR A 51 0 SHEET 2 AA2 3 PHE A 278 TYR A 282 -1 O LEU A 280 N HIS A 49 SHEET 3 AA2 3 ILE A 288 ASP A 293 -1 O VAL A 292 N LEU A 279 SHEET 1 AA3 2 LEU A 54 PHE A 55 0 SHEET 2 AA3 2 GLN A 274 PRO A 275 -1 O GLN A 274 N PHE A 55 SHEET 1 AA4 3 LEU A 84 PRO A 85 0 SHEET 2 AA4 3 ARG A 240 ALA A 246 -1 O PHE A 241 N LEU A 84 SHEET 3 AA4 3 LEU A 141 ASP A 142 1 N ASP A 142 O LEU A 245 SHEET 1 AA5 6 LEU A 84 PRO A 85 0 SHEET 2 AA5 6 ARG A 240 ALA A 246 -1 O PHE A 241 N LEU A 84 SHEET 3 AA5 6 GLY A 103 GLY A 107 -1 N ILE A 105 O GLN A 242 SHEET 4 AA5 6 LEU A 117 ASN A 121 -1 O LEU A 117 N PHE A 106 SHEET 5 AA5 6 VAL A 126 ILE A 128 -1 O VAL A 127 N VAL A 120 SHEET 6 AA5 6 TYR A 170 SER A 172 -1 O TYR A 170 N ILE A 128 SHEET 1 AA6 5 GLY A 314 ARG A 322 0 SHEET 2 AA6 5 PHE A 595 THR A 602 -1 O VAL A 600 N TYR A 316 SHEET 3 AA6 5 ALA A 612 TYR A 615 -1 O ALA A 612 N ILE A 601 SHEET 4 AA6 5 GLY A 651 ILE A 654 -1 O ILE A 654 N VAL A 613 SHEET 5 AA6 5 VAL A 645 THR A 648 -1 N PHE A 646 O LEU A 653 SHEET 1 AA7 5 ASN A 354 ILE A 358 0 SHEET 2 AA7 5 ASN A 394 ARG A 403 -1 O ALA A 397 N LYS A 356 SHEET 3 AA7 5 PRO A 507 GLU A 516 -1 O VAL A 512 N ASP A 398 SHEET 4 AA7 5 GLY A 431 TRP A 436 -1 N CYS A 432 O LEU A 513 SHEET 5 AA7 5 PHE A 374 PHE A 377 -1 N THR A 376 O ALA A 435 SHEET 1 AA8 2 LEU A 452 ARG A 454 0 SHEET 2 AA8 2 LEU A 492 SER A 494 -1 O ARG A 493 N TYR A 453 SHEET 1 AA9 6 CYS A 541 PHE A 546 0 SHEET 2 AA9 6 LEU A 549 GLU A 557 -1 O GLY A 553 N VAL A 542 SHEET 3 AA9 6 ILE A 587 THR A 591 -1 O THR A 591 N VAL A 554 SHEET 4 AA9 6 THR A 576 ARG A 580 -1 N VAL A 579 O LEU A 588 SHEET 5 AA9 6 PHE A 568 ARG A 570 -1 N GLY A 569 O ALA A 578 SHEET 6 AA9 6 VAL B 42 PHE B 43 1 O PHE B 43 N PHE A 568 SHEET 1 AB1 4 GLU A 657 TYR A 663 0 SHEET 2 AB1 4 ILE A 695 MET A 700 1 O ALA A 697 N GLU A 657 SHEET 3 AB1 4 ILE A 673 TYR A 677 -1 N SER A 676 O ILE A 696 SHEET 4 AB1 4 ILE A 667 GLY A 670 -1 N ILE A 669 O ILE A 673 SHEET 1 AB2 2 GLU A 705 ASN A 706 0 SHEET 2 AB2 2 ILE B 791 TYR B 792 1 O ILE B 791 N ASN A 706 SHEET 1 AB3 3 SER A 714 PRO A 731 0 SHEET 2 AB3 3 GLY A1062 ALA A1081 -1 O HIS A1067 N THR A 726 SHEET 3 AB3 3 TYR A1050 ALA A1059 -1 N MET A1053 O VAL A1068 SHEET 1 AB4 5 SER A 714 PRO A 731 0 SHEET 2 AB4 5 GLY A1062 ALA A1081 -1 O HIS A1067 N THR A 726 SHEET 3 AB4 5 VAL A1097 SER A1100 -1 O SER A1100 N THR A1079 SHEET 4 AB4 5 TRP A1105 THR A1108 -1 O PHE A1106 N VAL A1099 SHEET 5 AB4 5 GLN A1116 ILE A1117 -1 O GLN A1116 N VAL A1107 SHEET 1 AB5 2 LYS A 736 SER A 738 0 SHEET 2 AB5 2 THR A 862 LEU A 864 -1 O THR A 862 N SER A 738 SHEET 1 AB6 2 ILE A 791 LYS A 793 0 SHEET 2 AB6 2 GLU C 705 SER C 707 1 O ASN C 706 N ILE A 791 SHEET 1 AB7 4 THR A1123 ASN A1128 0 SHEET 2 AB7 4 LYS A1089 PRO A1093 -1 N PHE A1092 O PHE A1124 SHEET 3 AB7 4 ILE A1084 HIS A1086 -1 N ILE A1084 O HIS A1091 SHEET 4 AB7 4 VAL A1136 ASN A1137 1 O VAL A1136 N CYS A1085 SHEET 1 AB8 7 TYR B 28 ASN B 30 0 SHEET 2 AB8 7 ASN B 61 HIS B 66 -1 O VAL B 62 N THR B 29 SHEET 3 AB8 7 ALA B 267 TYR B 272 -1 O TYR B 268 N PHE B 65 SHEET 4 AB8 7 VAL B 90 GLU B 96 -1 N ALA B 93 O TYR B 269 SHEET 5 AB8 7 ASN B 188 ILE B 197 -1 O PHE B 192 N PHE B 92 SHEET 6 AB8 7 TYR B 200 PRO B 209 -1 O THR B 208 N LEU B 189 SHEET 7 AB8 7 GLU B 227 LEU B 232 -1 O VAL B 230 N ILE B 203 SHEET 1 AB9 3 VAL B 47 PHE B 55 0 SHEET 2 AB9 3 GLN B 274 TYR B 282 -1 O GLN B 274 N PHE B 55 SHEET 3 AB9 3 ILE B 288 ASP B 293 -1 O ASP B 290 N LYS B 281 SHEET 1 AC1 6 LEU B 84 PRO B 85 0 SHEET 2 AC1 6 ARG B 240 LEU B 245 -1 O PHE B 241 N LEU B 84 SHEET 3 AC1 6 ILE B 101 GLY B 107 -1 N ILE B 105 O GLN B 242 SHEET 4 AC1 6 SER B 116 ASN B 121 -1 O LEU B 117 N PHE B 106 SHEET 5 AC1 6 VAL B 126 VAL B 130 -1 O LYS B 129 N LEU B 118 SHEET 6 AC1 6 PHE B 168 SER B 172 -1 O TYR B 170 N ILE B 128 SHEET 1 AC2 5 GLY B 314 ARG B 322 0 SHEET 2 AC2 5 PHE B 595 THR B 602 -1 O VAL B 598 N SER B 319 SHEET 3 AC2 5 ALA B 612 GLN B 616 -1 O ALA B 612 N ILE B 601 SHEET 4 AC2 5 GLY B 651 ILE B 654 -1 O ILE B 654 N VAL B 613 SHEET 5 AC2 5 VAL B 645 GLN B 647 -1 N PHE B 646 O LEU B 653 SHEET 1 AC3 5 ASN B 354 ILE B 358 0 SHEET 2 AC3 5 ASN B 394 ARG B 403 -1 O SER B 399 N ASN B 354 SHEET 3 AC3 5 PRO B 507 GLU B 516 -1 O VAL B 512 N ASP B 398 SHEET 4 AC3 5 VAL B 433 ASN B 437 -1 N ILE B 434 O VAL B 511 SHEET 5 AC3 5 THR B 376 LYS B 378 -1 N THR B 376 O ALA B 435 SHEET 1 AC4 2 LEU B 452 ARG B 454 0 SHEET 2 AC4 2 LEU B 492 SER B 494 -1 O ARG B 493 N TYR B 453 SHEET 1 AC5 2 GLU B 465 ASP B 467 0 SHEET 2 AC5 2 ILE F 104 VAL F 106 -1 O VAL F 105 N ARG B 466 SHEET 1 AC6 5 VAL B 542 PHE B 544 0 SHEET 2 AC6 5 GLY B 551 GLU B 557 -1 O GLY B 553 N VAL B 542 SHEET 3 AC6 5 ILE B 587 THR B 591 -1 O ASP B 589 N THR B 556 SHEET 4 AC6 5 THR B 576 ARG B 580 -1 N VAL B 579 O LEU B 588 SHEET 5 AC6 5 PHE B 568 ARG B 570 -1 N GLY B 569 O ASP B 577 SHEET 1 AC7 4 GLU B 657 TYR B 658 0 SHEET 2 AC7 4 ILE B 695 THR B 699 1 O ALA B 697 N GLU B 657 SHEET 3 AC7 4 ILE B 673 TYR B 677 -1 N CYS B 674 O TYR B 698 SHEET 4 AC7 4 ILE B 667 GLY B 670 -1 N ILE B 667 O ALA B 675 SHEET 1 AC8 2 ALA B 704 SER B 707 0 SHEET 2 AC8 2 GLN C 790 LYS C 793 1 O ILE C 791 N ALA B 704 SHEET 1 AC9 3 SER B 714 PRO B 731 0 SHEET 2 AC9 3 GLY B1062 THR B1080 -1 O HIS B1067 N THR B 726 SHEET 3 AC9 3 TYR B1050 ALA B1059 -1 N MET B1053 O VAL B1068 SHEET 1 AD1 5 SER B 714 PRO B 731 0 SHEET 2 AD1 5 GLY B1062 THR B1080 -1 O HIS B1067 N THR B 726 SHEET 3 AD1 5 VAL B1097 SER B1100 -1 O SER B1100 N THR B1079 SHEET 4 AD1 5 TRP B1105 THR B1108 -1 O PHE B1106 N VAL B1099 SHEET 5 AD1 5 GLN B1116 ILE B1117 -1 O GLN B1116 N VAL B1107 SHEET 1 AD2 2 LYS B 736 VAL B 739 0 SHEET 2 AD2 2 LEU B 861 LEU B 864 -1 O THR B 862 N SER B 738 SHEET 1 AD3 4 THR B1123 ASN B1128 0 SHEET 2 AD3 4 LYS B1089 PRO B1093 -1 N PHE B1092 O PHE B1124 SHEET 3 AD3 4 ILE B1084 HIS B1086 -1 N ILE B1084 O HIS B1091 SHEET 4 AD3 4 VAL B1136 ASN B1137 1 O VAL B1136 N CYS B1085 SHEET 1 AD4 7 TYR C 28 ASN C 30 0 SHEET 2 AD4 7 ASN C 61 HIS C 66 -1 O VAL C 62 N THR C 29 SHEET 3 AD4 7 ALA C 267 TYR C 272 -1 O TYR C 268 N PHE C 65 SHEET 4 AD4 7 VAL C 90 SER C 94 -1 N TYR C 91 O GLY C 271 SHEET 5 AD4 7 ASN C 188 ILE C 197 -1 O PHE C 192 N PHE C 92 SHEET 6 AD4 7 TYR C 200 PRO C 209 -1 O THR C 208 N LEU C 189 SHEET 7 AD4 7 GLU C 227 LEU C 232 -1 O LEU C 232 N PHE C 201 SHEET 1 AD5 3 LEU C 48 PHE C 55 0 SHEET 2 AD5 3 GLN C 274 TYR C 282 -1 O PHE C 278 N THR C 51 SHEET 3 AD5 3 ILE C 288 ASP C 293 -1 O ASP C 290 N LYS C 281 SHEET 1 AD6 6 LEU C 84 PRO C 85 0 SHEET 2 AD6 6 ARG C 240 LEU C 245 -1 O PHE C 241 N LEU C 84 SHEET 3 AD6 6 ILE C 101 GLY C 107 -1 N GLY C 103 O LEU C 244 SHEET 4 AD6 6 SER C 116 ASN C 121 -1 O LEU C 117 N PHE C 106 SHEET 5 AD6 6 VAL C 126 VAL C 130 -1 O VAL C 127 N VAL C 120 SHEET 6 AD6 6 PHE C 168 SER C 172 -1 O TYR C 170 N ILE C 128 SHEET 1 AD7 5 GLY C 314 ARG C 322 0 SHEET 2 AD7 5 PHE C 595 THR C 602 -1 O GLY C 596 N PHE C 321 SHEET 3 AD7 5 ALA C 612 GLN C 616 -1 O ALA C 612 N ILE C 601 SHEET 4 AD7 5 GLY C 651 ILE C 654 -1 O ILE C 654 N VAL C 613 SHEET 5 AD7 5 VAL C 645 THR C 648 -1 N THR C 648 O GLY C 651 SHEET 1 AD8 6 SER C 328 ARG C 331 0 SHEET 2 AD8 6 VAL C 542 PHE C 546 1 O ASN C 545 N ARG C 331 SHEET 3 AD8 6 LEU C 549 THR C 556 -1 O LEU C 549 N PHE C 546 SHEET 4 AD8 6 ILE C 587 THR C 591 -1 O THR C 591 N VAL C 554 SHEET 5 AD8 6 ALA C 578 ARG C 580 -1 N VAL C 579 O LEU C 588 SHEET 6 AD8 6 PHE C 568 GLY C 569 -1 N GLY C 569 O ALA C 578 SHEET 1 AD9 5 ARG C 360 ILE C 361 0 SHEET 2 AD9 5 VAL C 398 ILE C 405 -1 O VAL C 398 N ILE C 361 SHEET 3 AD9 5 TYR C 511 PHE C 518 -1 O VAL C 515 N ASP C 401 SHEET 4 AD9 5 GLY C 434 ASN C 440 -1 N CYS C 435 O LEU C 516 SHEET 5 AD9 5 PHE C 377 THR C 379 -1 N PHE C 378 O ALA C 438 SHEET 1 AE1 5 ARG C 360 ILE C 361 0 SHEET 2 AE1 5 VAL C 398 ILE C 405 -1 O VAL C 398 N ILE C 361 SHEET 3 AE1 5 TYR C 511 PHE C 518 -1 O VAL C 515 N ASP C 401 SHEET 4 AE1 5 GLY C 434 ASN C 440 -1 N CYS C 435 O LEU C 516 SHEET 5 AE1 5 CYS C 382 TYR C 383 -1 N TYR C 383 O GLY C 434 SHEET 1 AE2 3 CYS C 364 VAL C 365 0 SHEET 2 AE2 3 VAL C 527 CYS C 528 1 O CYS C 528 N CYS C 364 SHEET 3 AE2 3 CYS C 394 PHE C 395 -1 N PHE C 395 O VAL C 527 SHEET 1 AE3 2 LEU C 455 ARG C 457 0 SHEET 2 AE3 2 LEU C 495 SER C 497 -1 O ARG C 496 N TYR C 456 SHEET 1 AE4 4 GLU C 657 TYR C 658 0 SHEET 2 AE4 4 SER C 694 THR C 699 1 O ALA C 697 N GLU C 657 SHEET 3 AE4 4 ILE C 673 GLN C 678 -1 N CYS C 674 O TYR C 698 SHEET 4 AE4 4 ILE C 667 GLY C 670 -1 N ILE C 667 O ALA C 675 SHEET 1 AE5 3 SER C 714 PRO C 731 0 SHEET 2 AE5 3 GLY C1062 THR C1079 -1 O VAL C1071 N THR C 722 SHEET 3 AE5 3 TYR C1050 ALA C1059 -1 N GLN C1057 O VAL C1064 SHEET 1 AE6 2 LYS C 736 VAL C 739 0 SHEET 2 AE6 2 LEU C 861 LEU C 864 -1 O LEU C 864 N LYS C 736 SHEET 1 AE7 4 THR C1123 VAL C1125 0 SHEET 2 AE7 4 LYS C1089 PRO C1093 -1 N PHE C1092 O PHE C1124 SHEET 3 AE7 4 ILE C1084 HIS C1086 -1 N HIS C1086 O LYS C1089 SHEET 4 AE7 4 VAL C1136 ASN C1137 1 O VAL C1136 N CYS C1085 SHEET 1 AE8 2 VAL C1097 VAL C1099 0 SHEET 2 AE8 2 PHE C1106 THR C1108 -1 O PHE C1106 N VAL C1099 SHEET 1 AE9 4 GLN F 3 SER F 7 0 SHEET 2 AE9 4 LEU F 18 SER F 25 -1 O SER F 21 N SER F 7 SHEET 3 AE9 4 THR F 80 MET F 85 -1 O MET F 85 N LEU F 18 SHEET 4 AE9 4 PHE F 70 ASP F 75 -1 N THR F 71 O GLN F 84 SHEET 1 AF1 4 LEU F 45 ARG F 50 0 SHEET 2 AF1 4 MET F 34 GLN F 39 -1 N ARG F 38 O GLU F 46 SHEET 3 AF1 4 ALA F 94 THR F 100 -1 O TYR F 97 N VAL F 37 SHEET 4 AF1 4 THR F 121 VAL F 123 -1 O THR F 121 N TYR F 96 SHEET 1 AF2 5 ALA G 9 VAL G 10 0 SHEET 2 AF2 5 THR G 103 LEU G 105 1 O LYS G 104 N VAL G 10 SHEET 3 AF2 5 ASP G 84 THR G 88 -1 N TYR G 85 O THR G 103 SHEET 4 AF2 5 SER G 33 GLN G 37 -1 N GLN G 37 O ASP G 84 SHEET 5 AF2 5 PRO G 43 ILE G 47 -1 O ILE G 47 N TRP G 34 SHEET 1 AF3 3 VAL G 18 GLN G 23 0 SHEET 2 AF3 3 THR G 69 ILE G 74 -1 O LEU G 72 N ILE G 20 SHEET 3 AF3 3 PHE G 61 SER G 66 -1 N SER G 62 O THR G 73 SHEET 1 AF4 4 GLN H 3 SER H 7 0 SHEET 2 AF4 4 LEU H 18 SER H 25 -1 O SER H 25 N GLN H 3 SHEET 3 AF4 4 THR H 80 MET H 85 -1 O LEU H 81 N CYS H 22 SHEET 4 AF4 4 PHE H 70 ASP H 75 -1 N THR H 71 O GLN H 84 SHEET 1 AF5 4 LEU H 45 SER H 52 0 SHEET 2 AF5 4 MET H 34 GLN H 39 -1 N ARG H 38 O GLU H 46 SHEET 3 AF5 4 ALA H 94 THR H 100 -1 O TYR H 97 N VAL H 37 SHEET 4 AF5 4 THR H 121 VAL H 123 -1 O THR H 121 N TYR H 96 SHEET 1 AF6 5 ALA J 9 VAL J 10 0 SHEET 2 AF6 5 THR J 103 LEU J 105 1 O LYS J 104 N VAL J 10 SHEET 3 AF6 5 ASP J 84 THR J 88 -1 N TYR J 85 O THR J 103 SHEET 4 AF6 5 SER J 33 GLN J 37 -1 N GLN J 37 O ASP J 84 SHEET 5 AF6 5 VAL J 44 ILE J 47 -1 O VAL J 44 N GLN J 36 SHEET 1 AF7 3 VAL J 18 GLN J 23 0 SHEET 2 AF7 3 THR J 69 ILE J 74 -1 O ALA J 70 N CYS J 22 SHEET 3 AF7 3 PHE J 61 SER J 66 -1 N SER J 62 O THR J 73 SSBOND 1 CYS A 131 CYS A 166 1555 1555 2.04 SSBOND 2 CYS A 294 CYS A 304 1555 1555 2.03 SSBOND 3 CYS A 336 CYS A 361 1555 1555 2.04 SSBOND 4 CYS A 379 CYS A 432 1555 1555 2.03 SSBOND 5 CYS A 391 CYS A 525 1555 1555 2.04 SSBOND 6 CYS A 480 CYS A 488 1555 1555 2.03 SSBOND 7 CYS A 541 CYS A 593 1555 1555 2.04 SSBOND 8 CYS A 620 CYS A 652 1555 1555 2.03 SSBOND 9 CYS A 665 CYS A 674 1555 1555 2.03 SSBOND 10 CYS A 741 CYS A 763 1555 1555 2.03 SSBOND 11 CYS A 746 CYS A 752 1555 1555 2.03 SSBOND 12 CYS A 1035 CYS A 1046 1555 1555 2.03 SSBOND 13 CYS A 1085 CYS A 1129 1555 1555 2.03 SSBOND 14 CYS B 131 CYS B 166 1555 1555 2.03 SSBOND 15 CYS B 294 CYS B 304 1555 1555 2.03 SSBOND 16 CYS B 336 CYS B 361 1555 1555 2.03 SSBOND 17 CYS B 379 CYS B 432 1555 1555 2.03 SSBOND 18 CYS B 391 CYS B 525 1555 1555 2.04 SSBOND 19 CYS B 480 CYS B 488 1555 1555 2.03 SSBOND 20 CYS B 541 CYS B 593 1555 1555 2.03 SSBOND 21 CYS B 620 CYS B 652 1555 1555 2.03 SSBOND 22 CYS B 665 CYS B 674 1555 1555 2.03 SSBOND 23 CYS B 741 CYS B 763 1555 1555 2.02 SSBOND 24 CYS B 746 CYS B 752 1555 1555 2.03 SSBOND 25 CYS B 1035 CYS B 1046 1555 1555 2.03 SSBOND 26 CYS B 1085 CYS B 1129 1555 1555 2.03 SSBOND 27 CYS C 131 CYS C 166 1555 1555 2.03 SSBOND 28 CYS C 294 CYS C 304 1555 1555 2.03 SSBOND 29 CYS C 339 CYS C 364 1555 1555 2.03 SSBOND 30 CYS C 382 CYS C 435 1555 1555 2.03 SSBOND 31 CYS C 394 CYS C 528 1555 1555 2.03 SSBOND 32 CYS C 483 CYS C 491 1555 1555 2.03 SSBOND 33 CYS C 541 CYS C 593 1555 1555 2.04 SSBOND 34 CYS C 620 CYS C 652 1555 1555 2.03 SSBOND 35 CYS C 665 CYS C 674 1555 1555 2.03 SSBOND 36 CYS C 741 CYS C 763 1555 1555 2.03 SSBOND 37 CYS C 746 CYS C 752 1555 1555 2.03 SSBOND 38 CYS C 1035 CYS C 1046 1555 1555 2.03 SSBOND 39 CYS C 1085 CYS C 1129 1555 1555 2.03 SSBOND 40 CYS F 22 CYS F 98 1555 1555 2.03 SSBOND 41 CYS G 22 CYS G 87 1555 1555 2.03 SSBOND 42 CYS H 22 CYS H 98 1555 1555 2.03 SSBOND 43 CYS J 22 CYS J 87 1555 1555 2.03 LINK ND2 ASN A 165 C1 NAG A1308 1555 1555 1.44 LINK ND2 ASN A 237 C1 NAG A1303 1555 1555 1.44 LINK ND2 ASN A 285 C1 NAG A1312 1555 1555 1.44 LINK ND2 ASN A 334 C1 NAG A1302 1555 1555 1.44 LINK ND2 ASN A 606 C1 NAG A1304 1555 1555 1.44 LINK ND2 ASN A 619 C1 NAG A1309 1555 1555 1.45 LINK ND2 ASN A 660 C1 NAG A1301 1555 1555 1.44 LINK ND2 ASN A 712 C1 NAG A1310 1555 1555 1.44 LINK ND2 ASN A 720 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 804 C1 NAG A1311 1555 1555 1.43 LINK ND2 ASN A1077 C1 NAG A1305 1555 1555 1.44 LINK ND2 ASN A1101 C1 NAG A1307 1555 1555 1.44 LINK ND2 ASN A1137 C1 NAG A1306 1555 1555 1.44 LINK ND2 ASN B 165 C1 NAG B1311 1555 1555 1.44 LINK ND2 ASN B 237 C1 NAG B1302 1555 1555 1.44 LINK ND2 ASN B 285 C1 NAG B1303 1555 1555 1.45 LINK ND2 ASN B 334 C1 NAG B1310 1555 1555 1.44 LINK ND2 ASN B 606 C1 NAG B1309 1555 1555 1.44 LINK ND2 ASN B 619 C1 NAG B1308 1555 1555 1.44 LINK ND2 ASN B 660 C1 NAG B1307 1555 1555 1.44 LINK ND2 ASN B 712 C1 NAG B1306 1555 1555 1.44 LINK ND2 ASN B 720 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN B 804 C1 NAG B1305 1555 1555 1.45 LINK ND2 ASN B1077 C1 NAG B1301 1555 1555 1.44 LINK ND2 ASN B1101 C1 NAG B1304 1555 1555 1.44 LINK ND2 ASN B1137 C1 NAG B1312 1555 1555 1.44 LINK ND2 ASN C 165 C1 NAG C1308 1555 1555 1.44 LINK ND2 ASN C 237 C1 NAG C1306 1555 1555 1.44 LINK ND2 ASN C 285 C1 NAG C1302 1555 1555 1.44 LINK ND2 ASN C 334 C1 NAG C1304 1555 1555 1.44 LINK ND2 ASN C 606 C1 NAG C1301 1555 1555 1.46 LINK ND2 ASN C 619 C1 NAG C1312 1555 1555 1.44 LINK ND2 ASN C 660 C1 NAG C1303 1555 1555 1.44 LINK ND2 ASN C 712 C1 NAG C1307 1555 1555 1.46 LINK ND2 ASN C 804 C1 NAG C1310 1555 1555 1.44 LINK ND2 ASN C1077 C1 NAG C1311 1555 1555 1.44 LINK ND2 ASN C1101 C1 NAG C1309 1555 1555 1.44 LINK ND2 ASN C1137 C1 NAG C1305 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 1.44 CISPEP 1 ALA C 523 PRO C 524 0 5.78 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