HEADER VIRAL PROTEIN/IMMUNE SYSTEM 14-DEC-21 7T75 TITLE HIV-1 ENVELOPE APEXGT2 IN COMPLEX WITH RM20A3 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: HIV ENVELOPE APEXGT2 GP120; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: HIV ENVELOPE APEXGT2 GP41; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: RM20A3 FAB HEAVY CHAIN; COMPND 11 CHAIN: H; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: RM20A3 FAB LIGHT CHAIN; COMPND 15 CHAIN: L; COMPND 16 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_COMMON: HIV-1; SOURCE 4 ORGANISM_TAXID: 11676; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 11 ORGANISM_COMMON: HIV-1; SOURCE 12 ORGANISM_TAXID: 11676; SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 24 EXPRESSION_SYSTEM_CELL_LINE: HEK; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 27 ORGANISM_COMMON: HUMAN; SOURCE 28 ORGANISM_TAXID: 9606; SOURCE 29 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 30 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 31 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 32 EXPRESSION_SYSTEM_CELL_LINE: HEK KEYWDS HIV, GERMLINE TARGETING VACCINE, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Z.T.BERNDSEN JRNL AUTH J.R.WILLIS,Z.T.BERNDSEN,K.M.MA,J.M.STEICHEN,T.SCHIFNER, JRNL AUTH 2 E.LANDAIS,A.LIGUORI,O.KALYUZHNIY,J.D.ALLEN,S.BABOO, JRNL AUTH 3 O.OMORODION,J.K.DIEDRICH,X.HU,E.GEORGESON,N.PHELPS, JRNL AUTH 4 S.ESKANDARZADEH,B.GROSCHEL,M.KUBITZ,Y.ADACHI,T.M.MULLIN, JRNL AUTH 5 N.ALAVI,S.FALCONE,S.HIMANSU,A.CARFI,I.A.WILSON, JRNL AUTH 6 J.R.YATES III,J.C.PAULSON,M.CRISPIN,A.B.WARD,W.SCHIEF JRNL TITL HUMAN IMMUNOGLOBULIN REPERTOIRE ANALYSIS GUIDES DESIGN OF JRNL TITL 2 VACCINE PRIMING IMMUNOGENS TARGETING HIV V2-APEX BROADLY JRNL TITL 3 NEUTRALIZING ANTIBODY PRECURSORS JRNL REF IMMUNITY 2022 JRNL REFN ISSN 1074-7613 REMARK 2 REMARK 2 RESOLUTION. 2.70 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) : 2.700 REMARK 3 NUMBER OF PARTICLES : 229356 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 7T75 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000259225. 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 : HIV-1 ENVELOPE APEXGT2 IN REMARK 245 COMPLEX WITH RM20A3 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 : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : NULL REMARK 245 MAXIMUM DEFOCUS (NM) : NULL 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) : 50.00 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 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR REMARK 300 CYCLIC POINT SYMMETRY (SCHOENFLIES SYMBOL = C3). 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 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, C, D, E, F, G, I 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 350 BIOMT1 2 -0.499999 -0.866025 0.000710 426.37292 REMARK 350 BIOMT2 2 0.866025 -0.500000 -0.000900 114.40632 REMARK 350 BIOMT3 2 0.001135 0.000165 0.999999 -0.23417 REMARK 350 BIOMT1 3 -0.499999 0.866025 0.001135 114.10775 REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000165 426.45298 REMARK 350 BIOMT3 3 0.000710 -0.000900 0.999999 0.03440 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 MET A 0 REMARK 465 GLY A 1 REMARK 465 ILE A 2 REMARK 465 LEU A 3 REMARK 465 PRO A 4 REMARK 465 SER A 5 REMARK 465 PRO A 6 REMARK 465 GLY A 7 REMARK 465 MET A 8 REMARK 465 PRO A 9 REMARK 465 ALA A 10 REMARK 465 LEU A 11 REMARK 465 LEU A 12 REMARK 465 SER A 13 REMARK 465 LEU A 14 REMARK 465 VAL A 15 REMARK 465 SER A 16 REMARK 465 LEU A 17 REMARK 465 LEU A 18 REMARK 465 SER A 19 REMARK 465 VAL A 20 REMARK 465 LEU A 21 REMARK 465 LEU A 22 REMARK 465 MET A 23 REMARK 465 GLY A 24 REMARK 465 CYS A 25 REMARK 465 VAL A 26 REMARK 465 ALA A 27 REMARK 465 GLU A 28 REMARK 465 THR A 29 REMARK 465 GLY A 30 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 HIS A 66 REMARK 465 ASN A 67 REMARK 465 VAL A 68 REMARK 465 TRP A 69 REMARK 465 ALA A 70 REMARK 465 THR A 71 REMARK 465 HIS A 72 REMARK 465 ALA A 73 REMARK 465 CYS A 74 REMARK 465 VAL A 75 REMARK 465 PRO A 76 REMARK 465 THR A 77 REMARK 465 ASP A 78 REMARK 465 PRO A 79 REMARK 465 ASN A 80 REMARK 465 PRO A 81 REMARK 465 ASN A 397A REMARK 465 THR A 397B REMARK 465 SER A 397C REMARK 465 VAL A 397D REMARK 465 GLN A 397E REMARK 465 GLY A 397F REMARK 465 SER A 397G REMARK 465 ASN A 397H REMARK 465 SER A 397I REMARK 465 THR A 397J REMARK 465 GLY A 397K REMARK 465 SER A 397L REMARK 465 GLY A 458 REMARK 465 GLY A 459 REMARK 465 SER A 460 REMARK 465 THR A 461 REMARK 465 ASN A 462 REMARK 465 SER A 463 REMARK 465 ARG A 504 REMARK 465 VAL A 505 REMARK 465 VAL A 506 REMARK 465 GLY A 507 REMARK 465 ARG A 508 REMARK 465 ARG A 509 REMARK 465 ARG A 510 REMARK 465 ARG A 511 REMARK 465 ARG A 512 REMARK 465 ARG A 513 REMARK 465 ALA B 510 REMARK 465 VAL B 511 REMARK 465 GLY B 512 REMARK 465 ILE B 513 REMARK 465 GLY B 514 REMARK 465 ALA B 515 REMARK 465 VAL B 516 REMARK 465 SER B 517 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 PRO B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 ASP B 568 REMARK 465 THR B 569 REMARK 465 LEU B 663 REMARK 465 ASP B 664 REMARK 465 GLY B 665 REMARK 465 THR B 666 REMARK 465 LYS B 667 REMARK 465 HIS B 668 REMARK 465 HIS B 669 REMARK 465 HIS B 670 REMARK 465 HIS B 671 REMARK 465 HIS B 672 REMARK 465 HIS B 673 REMARK 465 SER H 113 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 SER L 113 REMARK 465 PRO L 114 REMARK 465 THR 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 TYR H 100G CG TYR H 100G CD2 -0.086 REMARK 500 ASP L 27B CB ASP L 27B CG -0.158 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 ARG A 143 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 CYS A 196 CB - CA - C ANGL. DEV. = 7.3 DEGREES REMARK 500 TYR A 217 CB - CG - CD1 ANGL. DEV. = -4.5 DEGREES REMARK 500 ARG A 456 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 ARG A 469 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 ARG A 476 NE - CZ - NH2 ANGL. DEV. = -3.8 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 ASN A 94 86.32 -150.26 REMARK 500 TRP A 96 -20.96 87.00 REMARK 500 THR A 257 -98.49 -95.31 REMARK 500 PHE A 391 64.94 -116.56 REMARK 500 MET A 426 -68.53 50.13 REMARK 500 THR A 465 114.32 92.59 REMARK 500 ASN B 625 -121.90 -128.20 REMARK 500 MET B 626 86.42 -0.21 REMARK 500 THR B 627 167.31 -34.62 REMARK 500 SER H 82B -4.66 73.43 REMARK 500 LEU H 82C 96.25 7.92 REMARK 500 ALA H 100 -35.10 72.84 REMARK 500 LYS H 100E -93.47 -111.12 REMARK 500 ASP L 27B -108.69 -163.80 REMARK 500 VAL L 51 -57.21 70.21 REMARK 500 SER L 76 -89.87 -89.69 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-25734 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-25732 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-25733 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-25735 RELATED DB: EMDB REMARK 900 RELATED ID: EMD-25736 RELATED DB: EMDB DBREF 7T75 A 0 513 PDB 7T75 7T75 0 513 DBREF 7T75 B 510 673 PDB 7T75 7T75 510 673 DBREF 7T75 H 1 113 PDB 7T75 7T75 1 113 DBREF 7T75 L 3 126 PDB 7T75 7T75 3 126 SEQRES 1 A 504 MET GLY ILE LEU PRO SER PRO GLY MET PRO ALA LEU LEU SEQRES 2 A 504 SER LEU VAL SER LEU LEU SER VAL LEU LEU MET GLY CYS SEQRES 3 A 504 VAL ALA GLU THR GLY ALA GLU ASN LEU TRP VAL THR VAL SEQRES 4 A 504 TYR TYR GLY VAL PRO VAL TRP LYS ASP ALA GLU THR THR SEQRES 5 A 504 LEU PHE CYS ALA SER ASP ALA LYS ALA TYR GLU THR GLU SEQRES 6 A 504 LYS HIS ASN VAL TRP ALA THR HIS ALA CYS VAL PRO THR SEQRES 7 A 504 ASP PRO ASN PRO GLN GLU ILE HIS LEU GLU ASN VAL THR SEQRES 8 A 504 GLU GLU PHE ASN MET TRP LYS ASN ASN MET VAL GLU GLN SEQRES 9 A 504 MET HIS GLU ASP ILE ILE SER LEU TRP ASP GLN SER LEU SEQRES 10 A 504 LYS PRO CYS VAL LYS LEU THR PRO LEU CYS VAL THR LEU SEQRES 11 A 504 GLN CYS THR ASN VAL THR ASN ASN ILE THR ASP ASP MET SEQRES 12 A 504 ARG GLY GLU LEU LYS ASN CYS SER PHE ASN ALA THR THR SEQRES 13 A 504 GLU LEU ARG ASN LYS ARG GLN LYS VAL TYR SER LEU PHE SEQRES 14 A 504 TYR ARG LEU ASP ILE VAL PRO MET GLY GLU ASN SER THR SEQRES 15 A 504 ASN TYR ARG LEU ILE ASN CYS ASN THR SER ALA ILE THR SEQRES 16 A 504 GLN ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE SEQRES 17 A 504 HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS SEQRES 18 A 504 LYS ASP LYS LYS PHE ASN GLY THR GLY PRO CYS PRO SER SEQRES 19 A 504 VAL SER THR VAL GLN CYS THR HIS GLY ILE LYS PRO VAL SEQRES 20 A 504 VAL SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU SEQRES 21 A 504 GLU GLU VAL ILE ILE ARG SER GLU ASN ILE THR ASN ASN SEQRES 22 A 504 ALA LYS ASN ILE LEU VAL GLN LEU ASN THR PRO VAL GLN SEQRES 23 A 504 ILE ASN CYS THR ARG PRO ASN ASN ASN THR VAL LYS SER SEQRES 24 A 504 ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR TYR THR GLY SEQRES 25 A 504 ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN VAL SEQRES 26 A 504 SER LYS ALA THR TRP ASN GLU THR LEU GLY LYS VAL VAL SEQRES 27 A 504 LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN THR ILE ILE SEQRES 28 A 504 ARG PHE ALA GLN SER SER GLY GLY ASP LEU GLU VAL THR SEQRES 29 A 504 THR HIS SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS SEQRES 30 A 504 ASN THR SER GLY LEU PHE ASN SER THR TRP ILE SER ASN SEQRES 31 A 504 THR SER VAL GLN GLY SER ASN SER THR GLY SER ASN ASP SEQRES 32 A 504 SER ILE THR LEU PRO CYS ARG ILE LYS GLN ILE ILE ASN SEQRES 33 A 504 MET TRP GLN ARG ILE GLY GLN ALA MET TYR ALA PRO PRO SEQRES 34 A 504 ILE GLN GLY VAL ILE ARG CYS VAL SER ASN ILE THR GLY SEQRES 35 A 504 LEU ILE LEU THR ARG ASP GLY GLY SER THR ASN SER THR SEQRES 36 A 504 THR GLU THR PHE ARG PRO GLY GLY GLY ASP MET ARG ASP SEQRES 37 A 504 ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL LYS SEQRES 38 A 504 ILE GLU PRO LEU GLY VAL ALA PRO THR ARG CYS LYS ARG SEQRES 39 A 504 ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 B 162 ALA VAL GLY ILE GLY ALA VAL SER LEU GLY PHE LEU GLY SEQRES 2 B 162 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 B 162 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 B 162 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU PRO GLN GLN SEQRES 5 B 162 HIS LEU LEU LYS ASP THR HIS TRP GLY ILE LYS GLN LEU SEQRES 6 B 162 GLN ALA ARG VAL LEU ALA VAL GLU HIS TYR LEU ARG ASP SEQRES 7 B 162 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 B 162 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 B 162 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 B 162 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 B 162 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 B 162 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP GLY THR LYS SEQRES 13 B 162 HIS HIS HIS HIS HIS HIS SEQRES 1 H 125 GLU VAL GLN LEU VAL GLU THR GLY GLY GLY LEU VAL GLN SEQRES 2 H 125 PRO GLY GLY SER LEU LYS LEU SER CYS ARG ALA SER GLY SEQRES 3 H 125 TYR THR PHE SER SER PHE ALA MET SER TRP VAL ARG GLN SEQRES 4 H 125 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER LEU ILE ASN SEQRES 5 H 125 ASP ARG GLY GLY LEU THR PHE TYR VAL ASP SER VAL LYS SEQRES 6 H 125 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 H 125 LEU SER LEU GLN MET HIS SER LEU ARG ASP GLY ASP THR SEQRES 8 H 125 ALA VAL TYR TYR CYS ALA THR GLY GLY MET SER SER ALA SEQRES 9 H 125 LEU GLN SER SER LYS TYR TYR PHE ASP PHE TRP GLY GLN SEQRES 10 H 125 GLY ALA LEU VAL THR VAL SER SER SEQRES 1 L 128 ALA LEU THR GLN PRO PRO SER VAL SER GLY SER PRO GLY SEQRES 2 L 128 GLN SER VAL THR ILE SER CYS THR GLY THR SER SER ASP SEQRES 3 L 128 ILE GLY SER TYR ASN TYR VAL SER TRP TYR GLN GLN HIS SEQRES 4 L 128 PRO GLY LYS ALA PRO LYS LEU MET ILE TYR ASP VAL THR SEQRES 5 L 128 GLN ARG PRO SER GLY VAL SER ASP ARG PHE SER GLY SER SEQRES 6 L 128 LYS SER GLY ASN THR ALA SER LEU THR ILE SER GLY LEU SEQRES 7 L 128 GLN ALA ASP ASP GLU ALA ASP TYR TYR CYS SER ALA TYR SEQRES 8 L 128 ALA GLY ARG GLN THR PHE TYR ILE PHE GLY GLY GLY THR SEQRES 9 L 128 ARG LEU THR VAL LEU GLY GLN PRO LYS ALA SER PRO THR SEQRES 10 L 128 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU 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 A 609 14 HET NAG A 610 14 HET NAG A 611 14 HET NAG A 612 14 HET NAG A 613 14 HET NAG B 701 14 HET NAG B 702 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 BMA E 3 11 HET MAN E 4 11 HET NAG F 1 14 HET NAG F 2 14 HET NAG G 1 14 HET FUC G 2 10 HET NAG I 1 14 HET FUC I 2 10 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE HETNAM FUC ALPHA-L-FUCOSE FORMUL 5 NAG 25(C8 H15 N O6) FORMUL 22 BMA C6 H12 O6 FORMUL 22 MAN C6 H12 O6 FORMUL 24 FUC 2(C6 H12 O5) HELIX 1 AA1 ASN A 98 SER A 115 1 18 HELIX 2 AA2 THR A 139 ARG A 143 5 5 HELIX 3 AA3 LYS A 335 ARG A 350 1 16 HELIX 4 AA4 ASP A 368 THR A 373 1 6 HELIX 5 AA5 MET A 475 TYR A 484 1 10 HELIX 6 AA6 LEU B 521 SER B 526 5 6 HELIX 7 AA7 THR B 527 SER B 532 1 6 HELIX 8 AA8 THR B 534 ARG B 540 1 7 HELIX 9 AA9 GLY B 572 TRP B 596 1 25 HELIX 10 AB1 ASN B 618 ASP B 624 1 7 HELIX 11 AB2 THR B 627 SER B 636 1 10 HELIX 12 AB3 TYR B 638 ASP B 659 1 22 HELIX 13 AB4 THR H 28 PHE H 32 5 5 HELIX 14 AB5 ASP H 61 LYS H 64 5 4 HELIX 15 AB6 ARG H 83 THR H 87 5 5 HELIX 16 AB7 GLN L 79 GLU L 83 5 5 SHEET 1 AA1 3 LEU A 494 THR A 499 0 SHEET 2 AA1 3 TRP A 35 TYR A 40 -1 N TYR A 39 O GLY A 495 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O VAL B 608 N VAL A 36 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 PHE A 223 CYS A 228 -1 N LEU A 226 O LYS A 487 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 ILE A 84 -1 N ILE A 84 O THR A 244 SHEET 1 AA3 2 PHE A 53 ALA A 55 0 SHEET 2 AA3 2 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 GLY A 237 N PHE A 93 SHEET 1 AA5 5 ARG A 169 TYR A 177 0 SHEET 2 AA5 5 LEU A 154 THR A 162 -1 N PHE A 159 O VAL A 172 SHEET 3 AA5 5 LEU A 129 ASN A 133 -1 N THR A 132 O ASN A 156 SHEET 4 AA5 5 ASN A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA5 5 ILE A 181 PRO A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA6 3 ILE A 201 GLN A 203 0 SHEET 2 AA6 3 ALA A 433 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA6 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA712 LEU A 259 LEU A 261 0 SHEET 2 AA712 ILE A 271 SER A 274 0 SHEET 3 AA712 ILE A 284 GLY A 312 -1 O LEU A 285 N ARG A 273 SHEET 4 AA712 GLN A 315 ILE A 323A-1 O GLY A 321 N THR A 303 SHEET 5 AA712 ALA A 329 SER A 334 -1 O HIS A 330 N THR A 297 SHEET 6 AA712 ILE A 358 PHE A 361 0 SHEET 7 AA712 HIS A 374 CYS A 378 0 SHEET 8 AA712 GLU A 381 CYS A 385 -1 O CYS A 385 N HIS A 374 SHEET 9 AA712 SER A 393 ILE A 396 -1 O TRP A 395 N ILE A 359 SHEET 10 AA712 SER A 413 LYS A 421 -1 O ARG A 419 N TYR A 384 SHEET 11 AA712 GLY A 441 ARG A 456 -1 O LEU A 454 N ILE A 284 SHEET 12 AA712 GLU A 466 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 1 AA8 4 GLN H 3 GLU H 6 0 SHEET 2 AA8 4 SER H 17 SER H 25 -1 O ARG H 23 N VAL H 5 SHEET 3 AA8 4 THR H 77 HIS H 82A-1 O LEU H 80 N LEU H 20 SHEET 4 AA8 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AA9 7 LEU H 11 VAL H 12 0 SHEET 2 AA9 7 MET H 34 GLN H 39 0 SHEET 3 AA9 7 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 4 AA9 7 THR H 57 TYR H 59 -1 O PHE H 58 N LEU H 50 SHEET 5 AA9 7 ALA H 88 GLY H 95 -1 O TYR H 91 N VAL H 37 SHEET 6 AA9 7 PHE H 100H TRP H 103 -1 O PHE H 102 N THR H 94 SHEET 7 AA9 7 ALA H 107 VAL H 111 -1 O ALA H 107 N TYR H 90 SHEET 1 AB1 6 SER L 12 GLY L 13 0 SHEET 2 AB1 6 VAL L 33 GLN L 38 0 SHEET 3 AB1 6 LYS L 45 ILE L 48 -1 O MET L 47 N TRP L 35 SHEET 4 AB1 6 ALA L 84 TYR L 91 -1 O TYR L 87 N TYR L 36 SHEET 5 AB1 6 TYR L 96 PHE L 98 -1 O ILE L 97 N ALA L 90 SHEET 6 AB1 6 THR L 102 VAL L 106 -1 O THR L 102 N TYR L 86 SHEET 1 AB2 3 VAL L 19 THR L 24 0 SHEET 2 AB2 3 THR L 70 ILE L 75 -1 O ALA L 71 N CYS L 23 SHEET 3 AB2 3 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SSBOND 1 CYS A 119 CYS A 205 1555 1555 2.06 SSBOND 2 CYS A 126 CYS A 196 1555 1555 2.05 SSBOND 3 CYS A 131 CYS A 157 1555 1555 2.04 SSBOND 4 CYS A 218 CYS A 247 1555 1555 2.05 SSBOND 5 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 6 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 7 CYS A 378 CYS A 445 1555 1555 2.04 SSBOND 8 CYS A 385 CYS A 418 1555 1555 2.02 SSBOND 9 CYS A 501 CYS B 605 1555 1555 2.02 SSBOND 10 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 11 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 12 CYS L 23 CYS L 88 1555 1555 2.02 LINK ND2 ASN A 88 C1 NAG A 601 1555 1555 1.51 LINK ND2 ASN A 133 C1 NAG A 613 1555 1555 1.52 LINK ND2 ASN A 137 C1 NAG A 604 1555 1555 1.52 LINK ND2 ASN A 156 C1 NAG F 1 1555 1555 1.51 LINK ND2 ASN A 160 C1 NAG A 602 1555 1555 1.51 LINK ND2 ASN A 197 C1 NAG A 612 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG A 603 1555 1555 1.51 LINK ND2 ASN A 262 C1 NAG E 1 1555 1555 1.51 LINK ND2 ASN A 276 C1 NAG A 606 1555 1555 1.52 LINK ND2 ASN A 295 C1 NAG A 609 1555 1555 1.51 LINK ND2 ASN A 301 C1 NAG A 611 1555 1555 1.52 LINK ND2 ASN A 332 C1 NAG D 1 1555 1555 1.50 LINK ND2 ASN A 339 C1 NAG A 608 1555 1555 1.53 LINK ND2 ASN A 355 C1 NAG A 605 1555 1555 1.52 LINK ND2 ASN A 386 C1 NAG C 1 1555 1555 1.52 LINK ND2 ASN A 392 C1 NAG A 607 1555 1555 1.52 LINK ND2 ASN A 448 C1 NAG A 610 1555 1555 1.52 LINK ND2 ASN B 611 C1 NAG I 1 1555 1555 1.43 LINK ND2 ASN B 618 C1 NAG G 1 1555 1555 1.52 LINK ND2 ASN B 625 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 637 C1 NAG B 702 1555 1555 1.43 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.51 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.51 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.51 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.51 LINK O3 BMA E 3 C1 MAN E 4 1555 1555 1.52 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.51 LINK O6 NAG G 1 C1 FUC G 2 1555 1555 1.51 LINK O6 NAG I 1 C1 FUC I 2 1555 1555 1.43 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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