HEADER VIRAL PROTEIN 12-NOV-18 6N1V TITLE CRYO-EM STRUCTURE AT 4.0 A RESOLUTION OF VACCINE-ELICITED ANTIBODY TITLE 2 A12V163-A.01 IN COMPLEX WITH HIV-1 ENV BG505 DS-SOSIP, AND ANTIBODIES TITLE 3 VRC03 AND PGT122 COMPND MOL_ID: 1; COMPND 2 MOLECULE: A12V163-A.01 HEAVY CHAIN; COMPND 3 CHAIN: 3, 1, H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: A12V163-A.01 LIGHT CHAIN; COMPND 7 CHAIN: 4, 2, L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 11 CHAIN: B, A, C; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 15 CHAIN: F, E, D; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: PGT122 HEAVY CHAIN; COMPND 19 CHAIN: Y, X, M; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: PGT122 LIGHT CHAIN; COMPND 23 CHAIN: a, Z, N; COMPND 24 ENGINEERED: YES; COMPND 25 MOL_ID: 7; COMPND 26 MOLECULE: VRC03 HEAVY CHAIN; COMPND 27 CHAIN: g, f, Q; COMPND 28 ENGINEERED: YES; COMPND 29 MOL_ID: 8; COMPND 30 MOLECULE: VRC03 LIGHT CHAIN; COMPND 31 CHAIN: i, h, R; COMPND 32 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_TAXID: 9544; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 9 ORGANISM_TAXID: 9544; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 15 ORGANISM_TAXID: 11676; SOURCE 16 GENE: ENV; SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 18 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 22 ORGANISM_TAXID: 11676; SOURCE 23 GENE: ENV; SOURCE 24 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 25 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 26 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 27 MOL_ID: 5; SOURCE 28 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 29 ORGANISM_COMMON: HUMAN; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 34 MOL_ID: 6; SOURCE 35 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 36 ORGANISM_COMMON: HUMAN; SOURCE 37 ORGANISM_TAXID: 9606; SOURCE 38 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 39 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 40 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 41 MOL_ID: 7; SOURCE 42 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 43 ORGANISM_COMMON: HUMAN; SOURCE 44 ORGANISM_TAXID: 9606; SOURCE 45 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 46 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 47 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 48 MOL_ID: 8; SOURCE 49 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 50 ORGANISM_COMMON: HUMAN; SOURCE 51 ORGANISM_TAXID: 9606; SOURCE 52 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 53 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 54 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1 ENV COMPLEX, NEUTRALIZING ANTIBODY, FUSION PEPTIDE-DIRECTED, KEYWDS 2 VIRAL PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR P.ACHARYA,P.D.KWONG REVDAT 1 24-JUL-19 6N1V 0 JRNL AUTH R.KONG,P.ACHARYA,K.XU,B.ZHANG,V.P.DANDEY,E.T.ENG,H.WEI, JRNL AUTH 2 B.CARRAGHER,C.S.POTTER,J.MASCOLA,P.D.KWONG JRNL TITL VACCINE-INDUCED DEVELOPMENTAL PATHWAYS FOR JRNL TITL 2 HIV-1-NEUTRALIZING FUSION PEPTIDE-DIRECTED ANTIBODIES IN JRNL TITL 3 RHESUS MACAQUES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 4.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LEGINON, GCTF, COOT, PHENIX, CRYOSPARC, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT REMARK 3 REFINEMENT TARGET : CORRELATION COEFFICIENT 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) : 4.000 REMARK 3 NUMBER OF PARTICLES : 43895 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 6N1V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-NOV-18. REMARK 100 THE DEPOSITION ID IS D_1000238027. 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 : QUATERNARY COMPLEX OF HIV-1 ENV REMARK 245 BG505 DS-SOSIP WITH ANTIBODIES REMARK 245 17D4, VRC03 AND PGT122.; REMARK 245 A12V163-A.01; ENVELOPE REMARK 245 GLYCOPROTEIN GP120; ENVELOPE REMARK 245 GLYCOPROTEIN GP4; PGT122; VRC03 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.50 REMARK 245 SAMPLE SUPPORT DETAILS : UNSPECIFIED 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 K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 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 : 2.70 REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 69.98 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : 22500 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: 24-MERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: 3, 4, B, F, Y, a, g, i, 1, 2, REMARK 350 AND CHAINS: A, E, X, Z, f, h, C, D, H, REMARK 350 AND CHAINS: L, M, N, Q, R 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 GLN 3 1 REMARK 465 GLU B 185A REMARK 465 ASN B 185B REMARK 465 GLN B 185C REMARK 465 GLY B 185D REMARK 465 ASN B 185E REMARK 465 ARG B 185F REMARK 465 SER B 185G REMARK 465 ASN B 185H REMARK 465 ASN B 185I REMARK 465 THR B 400 REMARK 465 SER B 401 REMARK 465 VAL B 402 REMARK 465 GLN B 403 REMARK 465 GLY B 404 REMARK 465 SER B 405 REMARK 465 ASN B 406 REMARK 465 SER B 407 REMARK 465 THR B 408 REMARK 465 GLY B 409 REMARK 465 SER B 410 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 ILE F 559 REMARK 465 GLU F 560 REMARK 465 ALA F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 LEU F 568 REMARK 465 ALA a 7 REMARK 465 PRO a 8 REMARK 465 THR a 9 REMARK 465 PHE a 10 REMARK 465 GLN 1 1 REMARK 465 GLU A 185A REMARK 465 ASN A 185B REMARK 465 GLN A 185C REMARK 465 GLY A 185D REMARK 465 ASN A 185E REMARK 465 ARG A 185F REMARK 465 SER A 185G REMARK 465 ASN A 185H REMARK 465 ASN A 185I REMARK 465 THR A 400 REMARK 465 SER A 401 REMARK 465 VAL A 402 REMARK 465 GLN A 403 REMARK 465 GLY A 404 REMARK 465 SER A 405 REMARK 465 ASN A 406 REMARK 465 SER A 407 REMARK 465 THR A 408 REMARK 465 GLY A 409 REMARK 465 SER A 410 REMARK 465 ILE E 548 REMARK 465 VAL E 549 REMARK 465 GLN E 550 REMARK 465 GLN E 551 REMARK 465 GLN E 552 REMARK 465 SER E 553 REMARK 465 ASN E 554 REMARK 465 LEU E 555 REMARK 465 LEU E 556 REMARK 465 ARG E 557 REMARK 465 ALA E 558 REMARK 465 ILE E 559 REMARK 465 GLU E 560 REMARK 465 ALA E 561 REMARK 465 GLN E 562 REMARK 465 GLN E 563 REMARK 465 HIS E 564 REMARK 465 LEU E 565 REMARK 465 LEU E 566 REMARK 465 LYS E 567 REMARK 465 LEU E 568 REMARK 465 ALA Z 7 REMARK 465 PRO Z 8 REMARK 465 THR Z 9 REMARK 465 PHE Z 10 REMARK 465 GLU C 185A REMARK 465 ASN C 185B REMARK 465 GLN C 185C REMARK 465 GLY C 185D REMARK 465 ASN C 185E REMARK 465 ARG C 185F REMARK 465 SER C 185G REMARK 465 ASN C 185H REMARK 465 ASN C 185I REMARK 465 THR C 400 REMARK 465 SER C 401 REMARK 465 VAL C 402 REMARK 465 GLN C 403 REMARK 465 GLY C 404 REMARK 465 SER C 405 REMARK 465 ASN C 406 REMARK 465 SER C 407 REMARK 465 THR C 408 REMARK 465 GLY C 409 REMARK 465 SER C 410 REMARK 465 ILE D 548 REMARK 465 VAL D 549 REMARK 465 GLN D 550 REMARK 465 GLN D 551 REMARK 465 GLN D 552 REMARK 465 SER D 553 REMARK 465 ASN D 554 REMARK 465 LEU D 555 REMARK 465 LEU D 556 REMARK 465 ARG D 557 REMARK 465 ALA D 558 REMARK 465 ILE D 559 REMARK 465 GLU D 560 REMARK 465 ALA D 561 REMARK 465 GLN D 562 REMARK 465 GLN D 563 REMARK 465 HIS D 564 REMARK 465 LEU D 565 REMARK 465 LEU D 566 REMARK 465 LYS D 567 REMARK 465 LEU D 568 REMARK 465 GLN H 1 REMARK 465 ALA N 7 REMARK 465 PRO N 8 REMARK 465 THR N 9 REMARK 465 PHE N 10 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 CYS g 121 CB SG REMARK 470 CYS f 121 CB SG REMARK 470 CYS Q 121 CB SG REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 LEU B 494 CA - CB - CG ANGL. DEV. = 15.3 DEGREES REMARK 500 LEU A 494 CA - CB - CG ANGL. DEV. = 15.3 DEGREES REMARK 500 LEU C 494 CA - CB - CG ANGL. DEV. = 15.3 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 ILE 3 49 -61.71 -105.56 REMARK 500 THR 3 104 -169.61 -128.89 REMARK 500 LEU 3 133 90.17 -69.40 REMARK 500 ASP 3 153 62.83 60.00 REMARK 500 PRO 3 156 -159.90 -85.02 REMARK 500 ASN 4 52 -13.15 72.45 REMARK 500 TYR 4 53 -2.86 -148.12 REMARK 500 PRO 4 168 109.94 -57.55 REMARK 500 ASN 4 174 11.53 59.84 REMARK 500 ASN B 80 71.32 37.31 REMARK 500 GLU B 87 -151.24 -88.77 REMARK 500 ASN B 88 -38.43 -24.27 REMARK 500 MET B 100 -14.76 72.33 REMARK 500 CYS B 126 98.90 -68.20 REMARK 500 PHE B 353 22.54 -140.89 REMARK 500 PHE B 391 56.20 -100.59 REMARK 500 TRP B 427 -2.89 68.23 REMARK 500 LEU B 494 72.70 57.42 REMARK 500 VAL F 518 -71.66 -77.17 REMARK 500 PHE F 519 159.79 179.96 REMARK 500 LEU F 544 -16.24 -141.80 REMARK 500 LEU F 602 -14.08 71.82 REMARK 500 ASN F 607 50.45 -119.37 REMARK 500 ASN F 625 -39.36 -131.54 REMARK 500 GLN F 640 -5.27 70.09 REMARK 500 LYS Y 64 -8.71 69.51 REMARK 500 GLU Y 100I 58.95 -92.57 REMARK 500 CYS a 23 118.16 -160.35 REMARK 500 ILE a 47 -61.69 -123.79 REMARK 500 ASN a 52 30.04 -140.57 REMARK 500 ILE g 48 -66.35 -101.67 REMARK 500 PRO g 116 84.03 -68.20 REMARK 500 PRO i 8 -50.25 -21.66 REMARK 500 THR i 51 -12.74 69.53 REMARK 500 SER i 52 -5.36 -143.97 REMARK 500 LYS i 77 66.82 60.00 REMARK 500 PHE i 91 -153.36 -37.36 REMARK 500 ILE 1 49 -61.75 -105.57 REMARK 500 THR 1 104 -169.59 -128.87 REMARK 500 LEU 1 133 90.22 -69.42 REMARK 500 PRO 1 156 -159.91 -84.98 REMARK 500 ASN 2 52 -13.11 72.41 REMARK 500 TYR 2 53 -2.84 -148.12 REMARK 500 PRO 2 168 109.93 -57.59 REMARK 500 ASN 2 174 11.55 59.83 REMARK 500 ASN A 80 71.35 37.28 REMARK 500 GLU A 87 -151.22 -88.76 REMARK 500 ASN A 88 -38.45 -24.27 REMARK 500 MET A 100 -14.75 72.33 REMARK 500 CYS A 126 98.91 -68.22 REMARK 500 REMARK 500 THIS ENTRY HAS 110 RAMACHANDRAN OUTLIERS. 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 SER i 7 PRO i 8 -98.59 REMARK 500 GLN i 89 GLN i 90 142.16 REMARK 500 SER h 7 PRO h 8 -98.63 REMARK 500 GLN h 89 GLN h 90 142.17 REMARK 500 SER R 7 PRO R 8 -98.58 REMARK 500 GLN R 89 GLN R 90 142.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 PHE i 91 11.96 REMARK 500 PHE h 91 11.94 REMARK 500 PHE R 91 11.96 REMARK 500 REMARK 500 REMARK: NULL REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 646 through BMA A 648 bound to ASN A 88 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 618 through NAG A 619 bound to ASN A 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 620 through BMA A 622 bound to ASN A 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 624 through BMA A 626 bound to ASN A 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 601 through BMA A 603 bound to ASN A 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 623 bound REMARK 800 to ASN A 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 643 through BMA A 645 bound to ASN A 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 634 through MAN A 638 bound to ASN A 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 639 through MAN A 642 bound to ASN A 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 604 through MAN A 607 bound to ASN A 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 627 through NAG A 628 bound to ASN A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 629 through BMA A 631 bound to ASN A 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 608 bound REMARK 800 to ASN A 339 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 609 through BMA A 611 bound to ASN A 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 612 through MAN A 616 bound to ASN A 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 617 bound REMARK 800 to ASN A 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A REMARK 800 632 through NAG A 633 bound to ASN A 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 646 through BMA B 648 bound to ASN B 88 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 618 through NAG B 619 bound to ASN B 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 620 through BMA B 622 bound to ASN B 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 624 through BMA B 626 bound to ASN B 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 601 through BMA B 603 bound to ASN B 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 623 bound REMARK 800 to ASN B 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 643 through BMA B 645 bound to ASN B 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 634 through MAN B 638 bound to ASN B 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 639 through MAN B 642 bound to ASN B 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 604 through MAN B 607 bound to ASN B 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 627 through NAG B 628 bound to ASN B 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 629 through BMA B 631 bound to ASN B 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 608 bound REMARK 800 to ASN B 339 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 609 through BMA B 611 bound to ASN B 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 612 through MAN B 616 bound to ASN B 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 617 bound REMARK 800 to ASN B 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B REMARK 800 632 through NAG B 633 bound to ASN B 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 646 through BMA C 648 bound to ASN C 88 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 618 through NAG C 619 bound to ASN C 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 620 through BMA C 622 bound to ASN C 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 624 through BMA C 626 bound to ASN C 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 601 through BMA C 603 bound to ASN C 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 623 bound REMARK 800 to ASN C 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 643 through BMA C 645 bound to ASN C 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 634 through MAN C 638 bound to ASN C 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 639 through MAN C 642 bound to ASN C 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 604 through MAN C 607 bound to ASN C 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 627 through NAG C 628 bound to ASN C 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 629 through BMA C 631 bound to ASN C 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 608 bound REMARK 800 to ASN C 339 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 609 through BMA C 611 bound to ASN C 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 612 through MAN C 616 bound to ASN C 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 617 bound REMARK 800 to ASN C 392 REMARK 800 REMARK 800 SITE_IDENTIFIER: AH6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 632 through NAG C 633 bound to ASN C 448 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-9319 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE AT 4.0 A RESOLUTION OF VACCINE-ELICITED ANTIBODY REMARK 900 17D4 IN COMPLEX WITH HIV-1 ENV BG505 DS-SOSIP, AND ANTIBODIES VRC03 REMARK 900 AND PGT122 DBREF 6N1V 3 1 225 PDB 6N1V 6N1V 1 225 DBREF 6N1V 4 1 215 PDB 6N1V 6N1V 1 215 DBREF 6N1V B 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6N1V F 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 6N1V Y 1 111 PDB 6N1V 6N1V 1 111 DBREF 6N1V a 7 107 PDB 6N1V 6N1V 7 107 DBREF 6N1V g 1 129 PDB 6N1V 6N1V 1 129 DBREF 6N1V i 1 107 PDB 6N1V 6N1V 1 107 DBREF 6N1V 1 1 225 PDB 6N1V 6N1V 1 225 DBREF 6N1V 2 1 215 PDB 6N1V 6N1V 1 215 DBREF 6N1V A 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6N1V E 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 6N1V X 1 111 PDB 6N1V 6N1V 1 111 DBREF 6N1V Z 7 107 PDB 6N1V 6N1V 7 107 DBREF 6N1V f 1 129 PDB 6N1V 6N1V 1 129 DBREF 6N1V h 1 107 PDB 6N1V 6N1V 1 107 DBREF 6N1V C 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6N1V D 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 6N1V H 1 225 PDB 6N1V 6N1V 1 225 DBREF 6N1V L 1 215 PDB 6N1V 6N1V 1 215 DBREF 6N1V M 1 111 PDB 6N1V 6N1V 1 111 DBREF 6N1V N 7 107 PDB 6N1V 6N1V 7 107 DBREF 6N1V Q 1 129 PDB 6N1V 6N1V 1 129 DBREF 6N1V R 1 107 PDB 6N1V 6N1V 1 107 SEQADV 6N1V ASN B 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6N1V CYS B 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6N1V CYS F 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 6N1V ASN A 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6N1V CYS A 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6N1V CYS E 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 6N1V ASN C 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6N1V CYS C 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6N1V CYS D 605 UNP Q2N0S6 THR 602 CONFLICT SEQRES 1 3 225 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 3 225 PRO SER GLU THR LEU SER LEU THR CYS GLY VAL SER GLY SEQRES 3 3 225 GLY SER ILE SER ASP ALA TYR TYR TRP SER TRP ILE ARG SEQRES 4 3 225 GLN SER PRO GLY LYS ARG LEU GLU TRP ILE GLY TYR ILE SEQRES 5 3 225 PHE GLY SER ASN GLY GLY THR ARG TYR ASN PRO SER LEU SEQRES 6 3 225 ARG SER ARG VAL SER ILE SER ILE ASP THR SER LYS ASN SEQRES 7 3 225 GLN LEU SER LEU LYS LEU THR SER VAL THR ALA ALA ASP SEQRES 8 3 225 THR ALA VAL TYR TYR CYS VAL ARG GLU GLY VAL PRO THR SEQRES 9 3 225 GLU ALA THR THR GLY ASP HIS TRP GLY GLN GLY VAL PRO SEQRES 10 3 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 3 225 PHE PRO LEU ALA PRO SER SER ARG SER THR SER GLU SER SEQRES 12 3 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 3 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY SER LEU THR SEQRES 14 3 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 3 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 3 225 SER SER LEU GLY THR GLN THR TYR VAL CYS ASN VAL ASN SEQRES 17 3 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 3 225 ILE LYS THR CYS SEQRES 1 4 215 GLN PHE VAL LEU THR GLN PRO PRO SER MET SER GLY ALA SEQRES 2 4 215 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY THR ASN SEQRES 3 4 215 SER ASN ILE GLY VAL ASN TYR VAL GLN TRP TYR GLN GLN SEQRES 4 4 215 PHE PRO GLY THR ALA PRO LYS LEU LEU ILE TYR GLU ASN SEQRES 5 4 215 TYR LYS ARG PRO SER GLY ILE SER ASP ARG PHE SER GLY SEQRES 6 4 215 SER GLN SER GLY SER SER ALA SER LEU THR ILE THR GLY SEQRES 7 4 215 LEU GLN SER GLU ASP GLU ALA ASP TYR TYR CYS GLN SER SEQRES 8 4 215 TYR ASP ILE SER LEU GLY ALA HIS VAL PHE GLY SER GLY SEQRES 9 4 215 THR GLU LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 4 215 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 4 215 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 4 215 TYR PRO GLY ALA VAL GLU VAL ALA TRP LYS ALA ASP GLY SEQRES 13 4 215 SER ALA VAL ASN ALA GLY VAL GLU THR THR LYS PRO SER SEQRES 14 4 215 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 4 215 SER LEU THR SER ASP GLN TRP LYS SER HIS LYS SER TYR SEQRES 16 4 215 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 4 215 THR VAL ALA PRO ALA GLU CYS SEQRES 1 B 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 B 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 B 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 B 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 B 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 B 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 B 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 B 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 B 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 B 473 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 B 473 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 B 473 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 B 473 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 B 473 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 B 473 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 B 473 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 B 473 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 B 473 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 B 473 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 B 473 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 B 473 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 B 473 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 B 473 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 B 473 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 B 473 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 B 473 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 B 473 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 B 473 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 B 473 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 B 473 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 B 473 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 B 473 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 B 473 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 B 473 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 B 473 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 B 473 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 B 473 CYS LYS ARG ARG VAL SEQRES 1 F 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 F 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 F 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 F 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 F 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 F 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 F 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 F 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 F 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 F 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 F 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 F 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 Y 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 Y 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 Y 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 Y 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 Y 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 Y 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 Y 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 Y 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 Y 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 Y 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 Y 132 SER SER SEQRES 1 a 107 ALA PRO THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 2 a 107 ARG ILE THR CYS GLY GLU GLU SER LEU GLY SER ARG SER SEQRES 3 a 107 VAL ILE TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER SEQRES 4 a 107 LEU ILE ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE SEQRES 5 a 107 PRO ASP ARG PHE SER GLY SER PRO GLY SER THR PHE GLY SEQRES 6 a 107 THR THR ALA THR LEU THR ILE THR SER VAL GLU ALA GLY SEQRES 7 a 107 ASP GLU ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG SEQRES 8 a 107 ARG PRO THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU SEQRES 9 a 107 ILE VAL LEU SEQRES 1 g 129 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 g 129 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 g 129 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 g 129 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 g 129 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 g 129 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 g 129 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 g 129 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 g 129 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 g 129 GLN TYR TRP CYS GLN GLY THR VAL VAL VAL VAL SER SEQRES 1 i 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 i 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 i 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 i 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 i 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 i 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 i 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 i 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS SEQRES 1 1 225 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 1 225 PRO SER GLU THR LEU SER LEU THR CYS GLY VAL SER GLY SEQRES 3 1 225 GLY SER ILE SER ASP ALA TYR TYR TRP SER TRP ILE ARG SEQRES 4 1 225 GLN SER PRO GLY LYS ARG LEU GLU TRP ILE GLY TYR ILE SEQRES 5 1 225 PHE GLY SER ASN GLY GLY THR ARG TYR ASN PRO SER LEU SEQRES 6 1 225 ARG SER ARG VAL SER ILE SER ILE ASP THR SER LYS ASN SEQRES 7 1 225 GLN LEU SER LEU LYS LEU THR SER VAL THR ALA ALA ASP SEQRES 8 1 225 THR ALA VAL TYR TYR CYS VAL ARG GLU GLY VAL PRO THR SEQRES 9 1 225 GLU ALA THR THR GLY ASP HIS TRP GLY GLN GLY VAL PRO SEQRES 10 1 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 1 225 PHE PRO LEU ALA PRO SER SER ARG SER THR SER GLU SER SEQRES 12 1 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 1 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY SER LEU THR SEQRES 14 1 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 1 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 1 225 SER SER LEU GLY THR GLN THR TYR VAL CYS ASN VAL ASN SEQRES 17 1 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 1 225 ILE LYS THR CYS SEQRES 1 2 215 GLN PHE VAL LEU THR GLN PRO PRO SER MET SER GLY ALA SEQRES 2 2 215 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY THR ASN SEQRES 3 2 215 SER ASN ILE GLY VAL ASN TYR VAL GLN TRP TYR GLN GLN SEQRES 4 2 215 PHE PRO GLY THR ALA PRO LYS LEU LEU ILE TYR GLU ASN SEQRES 5 2 215 TYR LYS ARG PRO SER GLY ILE SER ASP ARG PHE SER GLY SEQRES 6 2 215 SER GLN SER GLY SER SER ALA SER LEU THR ILE THR GLY SEQRES 7 2 215 LEU GLN SER GLU ASP GLU ALA ASP TYR TYR CYS GLN SER SEQRES 8 2 215 TYR ASP ILE SER LEU GLY ALA HIS VAL PHE GLY SER GLY SEQRES 9 2 215 THR GLU LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 2 215 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 2 215 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 2 215 TYR PRO GLY ALA VAL GLU VAL ALA TRP LYS ALA ASP GLY SEQRES 13 2 215 SER ALA VAL ASN ALA GLY VAL GLU THR THR LYS PRO SER SEQRES 14 2 215 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 2 215 SER LEU THR SER ASP GLN TRP LYS SER HIS LYS SER TYR SEQRES 16 2 215 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 2 215 THR VAL ALA PRO ALA GLU CYS SEQRES 1 A 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 A 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 A 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 A 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 A 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 A 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 A 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 A 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 A 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 A 473 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 A 473 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 A 473 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 A 473 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 A 473 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 A 473 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 A 473 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 A 473 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 A 473 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 A 473 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 A 473 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 A 473 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 A 473 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 A 473 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 A 473 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 A 473 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 A 473 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 A 473 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 A 473 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 A 473 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 A 473 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 A 473 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 A 473 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 A 473 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 A 473 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 A 473 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 A 473 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 A 473 CYS LYS ARG ARG VAL SEQRES 1 E 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 E 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 E 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 E 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 E 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 E 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 E 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 E 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 E 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 E 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 E 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 E 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 X 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 X 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 X 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 X 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 X 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 X 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 X 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 X 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 X 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 X 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 X 132 SER SER SEQRES 1 Z 107 ALA PRO THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 2 Z 107 ARG ILE THR CYS GLY GLU GLU SER LEU GLY SER ARG SER SEQRES 3 Z 107 VAL ILE TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER SEQRES 4 Z 107 LEU ILE ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE SEQRES 5 Z 107 PRO ASP ARG PHE SER GLY SER PRO GLY SER THR PHE GLY SEQRES 6 Z 107 THR THR ALA THR LEU THR ILE THR SER VAL GLU ALA GLY SEQRES 7 Z 107 ASP GLU ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG SEQRES 8 Z 107 ARG PRO THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU SEQRES 9 Z 107 ILE VAL LEU SEQRES 1 f 129 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 f 129 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 f 129 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 f 129 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 f 129 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 f 129 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 f 129 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 f 129 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 f 129 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 f 129 GLN TYR TRP CYS GLN GLY THR VAL VAL VAL VAL SER SEQRES 1 h 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 h 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 h 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 h 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 h 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 h 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 h 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 h 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS SEQRES 1 C 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 C 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 C 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 C 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 C 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 C 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 C 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 C 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 C 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 C 473 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 C 473 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 C 473 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 C 473 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 C 473 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 C 473 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 C 473 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 C 473 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 C 473 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 C 473 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 C 473 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 C 473 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 C 473 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 C 473 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 C 473 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 C 473 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 C 473 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 C 473 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 C 473 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 C 473 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 C 473 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 C 473 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 C 473 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 C 473 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 C 473 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 C 473 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 C 473 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 C 473 CYS LYS ARG ARG VAL SEQRES 1 D 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 D 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 D 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 D 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 D 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 D 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 D 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 D 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 D 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 D 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 D 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 D 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 H 225 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 225 PRO SER GLU THR LEU SER LEU THR CYS GLY VAL SER GLY SEQRES 3 H 225 GLY SER ILE SER ASP ALA TYR TYR TRP SER TRP ILE ARG SEQRES 4 H 225 GLN SER PRO GLY LYS ARG LEU GLU TRP ILE GLY TYR ILE SEQRES 5 H 225 PHE GLY SER ASN GLY GLY THR ARG TYR ASN PRO SER LEU SEQRES 6 H 225 ARG SER ARG VAL SER ILE SER ILE ASP THR SER LYS ASN SEQRES 7 H 225 GLN LEU SER LEU LYS LEU THR SER VAL THR ALA ALA ASP SEQRES 8 H 225 THR ALA VAL TYR TYR CYS VAL ARG GLU GLY VAL PRO THR SEQRES 9 H 225 GLU ALA THR THR GLY ASP HIS TRP GLY GLN GLY VAL PRO SEQRES 10 H 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 225 PHE PRO LEU ALA PRO SER SER ARG SER THR SER GLU SER SEQRES 12 H 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY SER LEU THR SEQRES 14 H 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 225 SER SER LEU GLY THR GLN THR TYR VAL CYS ASN VAL ASN SEQRES 17 H 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 H 225 ILE LYS THR CYS SEQRES 1 L 215 GLN PHE VAL LEU THR GLN PRO PRO SER MET SER GLY ALA SEQRES 2 L 215 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY THR ASN SEQRES 3 L 215 SER ASN ILE GLY VAL ASN TYR VAL GLN TRP TYR GLN GLN SEQRES 4 L 215 PHE PRO GLY THR ALA PRO LYS LEU LEU ILE TYR GLU ASN SEQRES 5 L 215 TYR LYS ARG PRO SER GLY ILE SER ASP ARG PHE SER GLY SEQRES 6 L 215 SER GLN SER GLY SER SER ALA SER LEU THR ILE THR GLY SEQRES 7 L 215 LEU GLN SER GLU ASP GLU ALA ASP TYR TYR CYS GLN SER SEQRES 8 L 215 TYR ASP ILE SER LEU GLY ALA HIS VAL PHE GLY SER GLY SEQRES 9 L 215 THR GLU LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SEQRES 10 L 215 SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN SEQRES 11 L 215 ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE SEQRES 12 L 215 TYR PRO GLY ALA VAL GLU VAL ALA TRP LYS ALA ASP GLY SEQRES 13 L 215 SER ALA VAL ASN ALA GLY VAL GLU THR THR LYS PRO SER SEQRES 14 L 215 LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SEQRES 15 L 215 SER LEU THR SER ASP GLN TRP LYS SER HIS LYS SER TYR SEQRES 16 L 215 SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS SEQRES 17 L 215 THR VAL ALA PRO ALA GLU CYS SEQRES 1 M 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 M 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 M 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 M 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 M 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 M 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 M 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 M 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 M 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 M 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 M 132 SER SER SEQRES 1 N 107 ALA PRO THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 2 N 107 ARG ILE THR CYS GLY GLU GLU SER LEU GLY SER ARG SER SEQRES 3 N 107 VAL ILE TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER SEQRES 4 N 107 LEU ILE ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE SEQRES 5 N 107 PRO ASP ARG PHE SER GLY SER PRO GLY SER THR PHE GLY SEQRES 6 N 107 THR THR ALA THR LEU THR ILE THR SER VAL GLU ALA GLY SEQRES 7 N 107 ASP GLU ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG SEQRES 8 N 107 ARG PRO THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU SEQRES 9 N 107 ILE VAL LEU SEQRES 1 Q 129 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 Q 129 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 Q 129 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 Q 129 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 Q 129 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 Q 129 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 Q 129 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 Q 129 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 Q 129 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 Q 129 GLN TYR TRP CYS GLN GLY THR VAL VAL VAL VAL SER SEQRES 1 R 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 R 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 R 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 R 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 R 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 R 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 R 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 R 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS HET NAG B 601 14 HET NAG B 602 14 HET BMA B 603 11 HET NAG B 604 14 HET NAG B 605 14 HET BMA B 606 11 HET MAN B 607 11 HET NAG B 608 14 HET NAG B 609 14 HET NAG B 610 14 HET BMA B 611 11 HET NAG B 612 14 HET NAG B 613 14 HET BMA B 614 11 HET MAN B 615 11 HET MAN B 616 11 HET NAG B 617 14 HET NAG B 618 14 HET NAG B 619 14 HET NAG B 620 14 HET NAG B 621 14 HET BMA B 622 11 HET NAG B 623 14 HET NAG B 624 14 HET NAG B 625 14 HET BMA B 626 11 HET NAG B 627 14 HET NAG B 628 14 HET NAG B 629 14 HET NAG B 630 14 HET BMA B 631 11 HET NAG B 632 14 HET NAG B 633 14 HET NAG B 634 14 HET NAG B 635 14 HET BMA B 636 11 HET MAN B 637 11 HET MAN B 638 11 HET NAG B 639 14 HET NAG B 640 14 HET BMA B 641 11 HET MAN B 642 11 HET NAG B 643 14 HET NAG B 644 14 HET BMA B 645 11 HET NAG B 646 14 HET NAG B 647 14 HET BMA B 648 11 HET NAG A 601 14 HET NAG A 602 14 HET BMA A 603 11 HET NAG A 604 14 HET NAG A 605 14 HET BMA A 606 11 HET MAN A 607 11 HET NAG A 608 14 HET NAG A 609 14 HET NAG A 610 14 HET BMA A 611 11 HET NAG A 612 14 HET NAG A 613 14 HET BMA A 614 11 HET MAN A 615 11 HET MAN A 616 11 HET NAG A 617 14 HET NAG A 618 14 HET NAG A 619 14 HET NAG A 620 14 HET NAG A 621 14 HET BMA A 622 11 HET NAG A 623 14 HET NAG A 624 14 HET NAG A 625 14 HET BMA A 626 11 HET NAG A 627 14 HET NAG A 628 14 HET NAG A 629 14 HET NAG A 630 14 HET BMA A 631 11 HET NAG A 632 14 HET NAG A 633 14 HET NAG A 634 14 HET NAG A 635 14 HET BMA A 636 11 HET MAN A 637 11 HET MAN A 638 11 HET NAG A 639 14 HET NAG A 640 14 HET BMA A 641 11 HET MAN A 642 11 HET NAG A 643 14 HET NAG A 644 14 HET BMA A 645 11 HET NAG A 646 14 HET NAG A 647 14 HET BMA A 648 11 HET NAG C 601 14 HET NAG C 602 14 HET BMA C 603 11 HET NAG C 604 14 HET NAG C 605 14 HET BMA C 606 11 HET MAN C 607 11 HET NAG C 608 14 HET NAG C 609 14 HET NAG C 610 14 HET BMA C 611 11 HET NAG C 612 14 HET NAG C 613 14 HET BMA C 614 11 HET MAN C 615 11 HET MAN C 616 11 HET NAG C 617 14 HET NAG C 618 14 HET NAG C 619 14 HET NAG C 620 14 HET NAG C 621 14 HET BMA C 622 11 HET NAG C 623 14 HET NAG C 624 14 HET NAG C 625 14 HET BMA C 626 11 HET NAG C 627 14 HET NAG C 628 14 HET NAG C 629 14 HET NAG C 630 14 HET BMA C 631 11 HET NAG C 632 14 HET NAG C 633 14 HET NAG C 634 14 HET NAG C 635 14 HET BMA C 636 11 HET MAN C 637 11 HET MAN C 638 11 HET NAG C 639 14 HET NAG C 640 14 HET BMA C 641 11 HET MAN C 642 11 HET NAG C 643 14 HET NAG C 644 14 HET BMA C 645 11 HET NAG C 646 14 HET NAG C 647 14 HET BMA C 648 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 25 NAG 93(C8 H15 N O6) FORMUL 25 BMA 33(C6 H12 O6) FORMUL 26 MAN 18(C6 H12 O6) HELIX 1 AA1 PRO 3 63 ARG 3 66 5 4 HELIX 2 AA2 THR 3 88 THR 3 92 5 5 HELIX 3 AA3 THR 3 140 GLU 3 142 5 3 HELIX 4 AA4 SER 3 196 GLY 3 199 5 4 HELIX 5 AA5 GLN 4 80 GLU 4 84 5 5 HELIX 6 AA6 SER 4 125 ALA 4 131 1 7 HELIX 7 AA7 SER 4 186 LYS 4 190 1 5 HELIX 8 AA8 ALA 4 211 CYS 4 215 5 5 HELIX 9 AA9 ALA B 58 GLU B 62 5 5 HELIX 10 AB1 MET B 100 SER B 115 1 16 HELIX 11 AB2 LEU B 122 CYS B 126 5 5 HELIX 12 AB3 LYS B 335 ARG B 350 1 16 HELIX 13 AB4 LYS B 351 PHE B 353 5 3 HELIX 14 AB5 ASP B 368 THR B 373 1 6 HELIX 15 AB6 MET B 475 SER B 481 1 7 HELIX 16 AB7 GLY F 524 SER F 528 5 5 HELIX 17 AB8 THR F 529 SER F 534 1 6 HELIX 18 AB9 LEU F 537 ASN F 543 1 7 HELIX 19 AC1 VAL F 570 ILE F 595 1 26 HELIX 20 AC2 ASN F 611 ASN F 616 1 6 HELIX 21 AC3 ASN F 618 TRP F 623 1 6 HELIX 22 AC4 THR F 627 ILE F 635 1 9 HELIX 23 AC5 ILE F 641 ASP F 664 1 24 HELIX 24 AC6 THR Y 83 SER Y 87 5 5 HELIX 25 AC7 GLU a 79 GLU a 83 5 5 HELIX 26 AC8 ASN g 28 TYR g 32 5 5 HELIX 27 AC9 THR g 94 THR g 98 5 5 HELIX 28 AD1 ASP i 79 PHE i 83 5 5 HELIX 29 AD2 PRO 1 63 ARG 1 66 5 4 HELIX 30 AD3 THR 1 88 THR 1 92 5 5 HELIX 31 AD4 THR 1 140 GLU 1 142 5 3 HELIX 32 AD5 SER 1 196 GLY 1 199 5 4 HELIX 33 AD6 GLN 2 80 GLU 2 84 5 5 HELIX 34 AD7 SER 2 125 ALA 2 131 1 7 HELIX 35 AD8 SER 2 186 LYS 2 190 1 5 HELIX 36 AD9 ALA 2 211 CYS 2 215 5 5 HELIX 37 AE1 ALA A 58 GLU A 62 5 5 HELIX 38 AE2 MET A 100 SER A 115 1 16 HELIX 39 AE3 LEU A 122 CYS A 126 5 5 HELIX 40 AE4 LYS A 335 ARG A 350 1 16 HELIX 41 AE5 LYS A 351 PHE A 353 5 3 HELIX 42 AE6 ASP A 368 THR A 373 1 6 HELIX 43 AE7 MET A 475 SER A 481 1 7 HELIX 44 AE8 GLY E 524 SER E 528 5 5 HELIX 45 AE9 THR E 529 SER E 534 1 6 HELIX 46 AF1 LEU E 537 ASN E 543 1 7 HELIX 47 AF2 VAL E 570 ILE E 595 1 26 HELIX 48 AF3 ASN E 611 ASN E 616 1 6 HELIX 49 AF4 ASN E 618 TRP E 623 1 6 HELIX 50 AF5 THR E 627 ILE E 635 1 9 HELIX 51 AF6 ILE E 641 ASP E 664 1 24 HELIX 52 AF7 THR X 83 SER X 87 5 5 HELIX 53 AF8 GLU Z 79 GLU Z 83 5 5 HELIX 54 AF9 ASN f 28 TYR f 32 5 5 HELIX 55 AG1 THR f 94 THR f 98 5 5 HELIX 56 AG2 ASP h 79 PHE h 83 5 5 HELIX 57 AG3 ALA C 58 GLU C 62 5 5 HELIX 58 AG4 MET C 100 SER C 115 1 16 HELIX 59 AG5 LEU C 122 CYS C 126 5 5 HELIX 60 AG6 LYS C 335 ARG C 350 1 16 HELIX 61 AG7 LYS C 351 PHE C 353 5 3 HELIX 62 AG8 ASP C 368 THR C 373 1 6 HELIX 63 AG9 MET C 475 SER C 481 1 7 HELIX 64 AH1 GLY D 524 SER D 528 5 5 HELIX 65 AH2 THR D 529 SER D 534 1 6 HELIX 66 AH3 LEU D 537 ASN D 543 1 7 HELIX 67 AH4 VAL D 570 ILE D 595 1 26 HELIX 68 AH5 ASN D 611 ASN D 616 1 6 HELIX 69 AH6 ASN D 618 TRP D 623 1 6 HELIX 70 AH7 THR D 627 ILE D 635 1 9 HELIX 71 AH8 ILE D 641 ASP D 664 1 24 HELIX 72 AH9 PRO H 63 ARG H 66 5 4 HELIX 73 AI1 THR H 88 THR H 92 5 5 HELIX 74 AI2 THR H 140 GLU H 142 5 3 HELIX 75 AI3 SER H 196 GLY H 199 5 4 HELIX 76 AI4 GLN L 80 GLU L 84 5 5 HELIX 77 AI5 SER L 125 ALA L 131 1 7 HELIX 78 AI6 SER L 186 LYS L 190 1 5 HELIX 79 AI7 ALA L 211 CYS L 215 5 5 HELIX 80 AI8 THR M 83 SER M 87 5 5 HELIX 81 AI9 GLU N 79 GLU N 83 5 5 HELIX 82 AJ1 ASN Q 28 TYR Q 32 5 5 HELIX 83 AJ2 THR Q 94 THR Q 98 5 5 HELIX 84 AJ3 ASP R 79 PHE R 83 5 5 SHEET 1 AA1 4 GLN 3 3 SER 3 7 0 SHEET 2 AA1 4 LEU 3 18 SER 3 25 -1 O THR 3 21 N SER 3 7 SHEET 3 AA1 4 GLN 3 79 LEU 3 84 -1 O LEU 3 80 N CYS 3 22 SHEET 4 AA1 4 VAL 3 69 ASP 3 74 -1 N ASP 3 74 O GLN 3 79 SHEET 1 AA2 6 LEU 3 11 VAL 3 12 0 SHEET 2 AA2 6 VAL 3 116 VAL 3 120 1 O THR 3 119 N VAL 3 12 SHEET 3 AA2 6 ALA 3 93 ARG 3 99 -1 N ALA 3 93 O VAL 3 118 SHEET 4 AA2 6 TYR 3 34 GLN 3 40 -1 N ILE 3 38 O TYR 3 96 SHEET 5 AA2 6 LEU 3 46 PHE 3 53 -1 O GLY 3 50 N TRP 3 37 SHEET 6 AA2 6 THR 3 59 TYR 3 61 -1 O ARG 3 60 N TYR 3 51 SHEET 1 AA3 4 SER 3 129 LEU 3 133 0 SHEET 2 AA3 4 THR 3 144 TYR 3 154 -1 O LYS 3 152 N SER 3 129 SHEET 3 AA3 4 TYR 3 185 PRO 3 194 -1 O VAL 3 193 N ALA 3 145 SHEET 4 AA3 4 VAL 3 172 THR 3 174 -1 N HIS 3 173 O VAL 3 190 SHEET 1 AA4 4 SER 3 129 LEU 3 133 0 SHEET 2 AA4 4 THR 3 144 TYR 3 154 -1 O LYS 3 152 N SER 3 129 SHEET 3 AA4 4 TYR 3 185 PRO 3 194 -1 O VAL 3 193 N ALA 3 145 SHEET 4 AA4 4 VAL 3 178 LEU 3 179 -1 N VAL 3 178 O SER 3 186 SHEET 1 AA5 3 VAL 3 159 TRP 3 163 0 SHEET 2 AA5 3 TYR 3 203 HIS 3 209 -1 O ASN 3 206 N SER 3 162 SHEET 3 AA5 3 THR 3 214 VAL 3 220 -1 O VAL 3 220 N TYR 3 203 SHEET 1 AA6 5 SER 4 9 GLY 4 12 0 SHEET 2 AA6 5 THR 4 105 VAL 4 109 1 O THR 4 108 N MET 4 10 SHEET 3 AA6 5 ALA 4 85 ASP 4 93 -1 N TYR 4 87 O THR 4 105 SHEET 4 AA6 5 GLN 4 35 GLN 4 39 -1 N GLN 4 39 O ASP 4 86 SHEET 5 AA6 5 LYS 4 46 ILE 4 49 -1 O LYS 4 46 N GLN 4 38 SHEET 1 AA7 4 SER 4 9 GLY 4 12 0 SHEET 2 AA7 4 THR 4 105 VAL 4 109 1 O THR 4 108 N MET 4 10 SHEET 3 AA7 4 ALA 4 85 ASP 4 93 -1 N TYR 4 87 O THR 4 105 SHEET 4 AA7 4 ALA 4 98 PHE 4 101 -1 O ALA 4 98 N ASP 4 93 SHEET 1 AA8 3 VAL 4 18 THR 4 23 0 SHEET 2 AA8 3 SER 4 71 ILE 4 76 -1 O ALA 4 72 N CYS 4 22 SHEET 3 AA8 3 PHE 4 63 SER 4 68 -1 N SER 4 68 O SER 4 71 SHEET 1 AA9 4 SER 4 118 PHE 4 122 0 SHEET 2 AA9 4 LYS 4 133 PHE 4 143 -1 O SER 4 141 N SER 4 118 SHEET 3 AA9 4 TYR 4 176 THR 4 185 -1 O SER 4 180 N CYS 4 138 SHEET 4 AA9 4 VAL 4 163 LYS 4 170 -1 N SER 4 169 O ALA 4 177 SHEET 1 AB1 3 VAL 4 148 LYS 4 153 0 SHEET 2 AB1 3 TYR 4 195 HIS 4 201 -1 O GLN 4 198 N ALA 4 151 SHEET 3 AB1 3 SER 4 204 VAL 4 210 -1 O VAL 4 210 N TYR 4 195 SHEET 1 AB2 2 TRP B 35 TYR B 39 0 SHEET 2 AB2 2 GLY B 495 THR B 499 -1 O GLY B 495 N TYR B 39 SHEET 1 AB3 4 TRP B 45 ASP B 47 0 SHEET 2 AB3 4 VAL B 488 ILE B 491 -1 O LYS B 490 N LYS B 46 SHEET 3 AB3 4 PHE B 223 CYS B 228 -1 N ALA B 224 O VAL B 489 SHEET 4 AB3 4 VAL B 242 VAL B 245 -1 O VAL B 245 N ILE B 225 SHEET 1 AB4 3 VAL B 75 PRO B 76 0 SHEET 2 AB4 3 PHE B 53 SER B 56 1 N SER B 56 O VAL B 75 SHEET 3 AB4 3 HIS B 216 CYS B 218 -1 O HIS B 216 N ALA B 55 SHEET 1 AB5 2 GLU B 91 ASN B 94 0 SHEET 2 AB5 2 THR B 236 CYS B 239 -1 O GLY B 237 N PHE B 93 SHEET 1 AB6 5 LYS B 169 TYR B 177 0 SHEET 2 AB6 5 LEU B 154 THR B 162 -1 N LYS B 155 O PHE B 176 SHEET 3 AB6 5 LEU B 129 ASN B 133 -1 N THR B 132 O ASN B 156 SHEET 4 AB6 5 GLU B 190 LEU B 193 -1 O TYR B 191 N LEU B 129 SHEET 5 AB6 5 VAL B 181 GLN B 183 -1 N VAL B 182 O ARG B 192 SHEET 1 AB7 2 THR B 202 GLN B 203 0 SHEET 2 AB7 2 MET B 434 TYR B 435 1 O TYR B 435 N THR B 202 SHEET 1 AB8 6 MET B 271 ARG B 273 0 SHEET 2 AB8 6 ILE B 284 ARG B 298 -1 O GLN B 287 N MET B 271 SHEET 3 AB8 6 HIS B 330 SER B 334 -1 O HIS B 330 N THR B 297 SHEET 4 AB8 6 SER B 413 ARG B 419 -1 O ILE B 414 N VAL B 333 SHEET 5 AB8 6 GLU B 381 CYS B 385 -1 N TYR B 384 O ARG B 419 SHEET 6 AB8 6 HIS B 374 CYS B 378 -1 N PHE B 376 O PHE B 383 SHEET 1 AB9 6 MET B 271 ARG B 273 0 SHEET 2 AB9 6 ILE B 284 ARG B 298 -1 O GLN B 287 N MET B 271 SHEET 3 AB9 6 ILE B 443 ARG B 456 -1 O ILE B 449 N VAL B 292 SHEET 4 AB9 6 GLU B 466 PRO B 470 -1 O ARG B 469 N THR B 455 SHEET 5 AB9 6 ILE B 359 PHE B 361 1 N ARG B 360 O PHE B 468 SHEET 6 AB9 6 SER B 393 TRP B 395 -1 O SER B 393 N PHE B 361 SHEET 1 AC1 2 ARG B 304 GLY B 312 0 SHEET 2 AC1 2 GLN B 315 THR B 320 -1 O PHE B 317 N ILE B 307 SHEET 1 AC2 4 GLN Y 5 SER Y 7 0 SHEET 2 AC2 4 SER Y 19 ASN Y 23 -1 O THR Y 21 N SER Y 7 SHEET 3 AC2 4 LEU Y 77 LEU Y 82 -1 O LEU Y 80 N LEU Y 20 SHEET 4 AC2 4 VAL Y 67 ASP Y 72 -1 N HIS Y 68 O ARG Y 81 SHEET 1 AC3 5 LEU Y 11 VAL Y 12 0 SHEET 2 AC3 5 THR Y 105 VAL Y 109 1 O THR Y 108 N VAL Y 12 SHEET 3 AC3 5 ALA Y 88 ILE Y 100A-1 N TYR Y 90 O THR Y 105 SHEET 4 AC3 5 TYR Y 33 GLN Y 39 -1 N GLN Y 39 O ILE Y 89 SHEET 5 AC3 5 GLU Y 46 VAL Y 51 -1 O GLU Y 46 N ARG Y 38 SHEET 1 AC4 4 LEU Y 11 VAL Y 12 0 SHEET 2 AC4 4 THR Y 105 VAL Y 109 1 O THR Y 108 N VAL Y 12 SHEET 3 AC4 4 ALA Y 88 ILE Y 100A-1 N TYR Y 90 O THR Y 105 SHEET 4 AC4 4 TRP Y 100J TYR Y 100O-1 O PHE Y 100K N ARG Y 100 SHEET 1 AC5 3 ALA a 19 ARG a 20 0 SHEET 2 AC5 3 LEU a 73 ILE a 75 -1 O ILE a 75 N ALA a 19 SHEET 3 AC5 3 PHE a 62 GLY a 64 -1 N SER a 63 O THR a 74 SHEET 1 AC6 3 PRO a 44 ILE a 48 0 SHEET 2 AC6 3 ARG a 31 GLN a 38 -1 N GLN a 37 O SER a 45 SHEET 3 AC6 3 ASP a 85 ASP a 92 -1 O TYR a 87 N TYR a 36 SHEET 1 AC7 4 GLN g 3 VAL g 5 0 SHEET 2 AC7 4 SER g 17 SER g 25 -1 O ARG g 23 N VAL g 5 SHEET 3 AC7 4 GLY g 84 SER g 91 -1 O GLY g 84 N ALA g 24 SHEET 4 AC7 4 VAL g 68 GLN g 73 -1 N THR g 71 O TYR g 87 SHEET 1 AC8 6 VAL g 10 LYS g 12 0 SHEET 2 AC8 6 THR g 124 VAL g 128 1 O VAL g 127 N LYS g 12 SHEET 3 AC8 6 ALA g 99 ARG g 106 -1 N ALA g 99 O VAL g 126 SHEET 4 AC8 6 ILE g 34 ILE g 40 -1 N VAL g 37 O PHE g 102 SHEET 5 AC8 6 GLY g 44 LYS g 52 -1 O GLY g 49 N TRP g 36 SHEET 6 AC8 6 ALA g 57 TYR g 60 -1 O ALA g 57 N LYS g 52 SHEET 1 AC9 4 VAL g 10 LYS g 12 0 SHEET 2 AC9 4 THR g 124 VAL g 128 1 O VAL g 127 N LYS g 12 SHEET 3 AC9 4 ALA g 99 ARG g 106 -1 N ALA g 99 O VAL g 126 SHEET 4 AC9 4 TRP g 117 TRP g 120 -1 O TYR g 119 N ARG g 105 SHEET 1 AD1 4 LEU i 4 SER i 7 0 SHEET 2 AD1 4 ALA i 19 ALA i 25 -1 O PHE i 22 N SER i 7 SHEET 3 AD1 4 ASP i 70 ILE i 75 -1 O PHE i 71 N CYS i 23 SHEET 4 AD1 4 PHE i 62 SER i 67 -1 N VAL i 63 O THR i 74 SHEET 1 AD2 6 ILE i 10 LEU i 13 0 SHEET 2 AD2 6 SER i 102 VAL i 106 1 O GLU i 103 N LEU i 11 SHEET 3 AD2 6 VAL i 85 GLN i 89 -1 N TYR i 86 O SER i 102 SHEET 4 AD2 6 THR i 34 LYS i 38 -1 N LYS i 38 O VAL i 85 SHEET 5 AD2 6 ARG i 45 TYR i 49 -1 O ARG i 45 N GLN i 37 SHEET 6 AD2 6 ARG i 53 ARG i 54 -1 O ARG i 53 N TYR i 49 SHEET 1 AD3 4 GLN 1 3 SER 1 7 0 SHEET 2 AD3 4 LEU 1 18 SER 1 25 -1 O THR 1 21 N SER 1 7 SHEET 3 AD3 4 GLN 1 79 LEU 1 84 -1 O LEU 1 80 N CYS 1 22 SHEET 4 AD3 4 VAL 1 69 ASP 1 74 -1 N ASP 1 74 O GLN 1 79 SHEET 1 AD4 6 LEU 1 11 VAL 1 12 0 SHEET 2 AD4 6 VAL 1 116 VAL 1 120 1 O THR 1 119 N VAL 1 12 SHEET 3 AD4 6 ALA 1 93 ARG 1 99 -1 N ALA 1 93 O VAL 1 118 SHEET 4 AD4 6 TYR 1 34 GLN 1 40 -1 N ILE 1 38 O TYR 1 96 SHEET 5 AD4 6 LEU 1 46 PHE 1 53 -1 O GLY 1 50 N TRP 1 37 SHEET 6 AD4 6 THR 1 59 TYR 1 61 -1 O ARG 1 60 N TYR 1 51 SHEET 1 AD5 4 SER 1 129 LEU 1 133 0 SHEET 2 AD5 4 THR 1 144 TYR 1 154 -1 O LYS 1 152 N SER 1 129 SHEET 3 AD5 4 TYR 1 185 PRO 1 194 -1 O VAL 1 193 N ALA 1 145 SHEET 4 AD5 4 VAL 1 172 THR 1 174 -1 N HIS 1 173 O VAL 1 190 SHEET 1 AD6 4 SER 1 129 LEU 1 133 0 SHEET 2 AD6 4 THR 1 144 TYR 1 154 -1 O LYS 1 152 N SER 1 129 SHEET 3 AD6 4 TYR 1 185 PRO 1 194 -1 O VAL 1 193 N ALA 1 145 SHEET 4 AD6 4 VAL 1 178 LEU 1 179 -1 N VAL 1 178 O SER 1 186 SHEET 1 AD7 3 VAL 1 159 TRP 1 163 0 SHEET 2 AD7 3 TYR 1 203 HIS 1 209 -1 O ASN 1 206 N SER 1 162 SHEET 3 AD7 3 THR 1 214 VAL 1 220 -1 O VAL 1 220 N TYR 1 203 SHEET 1 AD8 5 SER 2 9 GLY 2 12 0 SHEET 2 AD8 5 THR 2 105 VAL 2 109 1 O THR 2 108 N MET 2 10 SHEET 3 AD8 5 ALA 2 85 ASP 2 93 -1 N TYR 2 87 O THR 2 105 SHEET 4 AD8 5 GLN 2 35 GLN 2 39 -1 N GLN 2 39 O ASP 2 86 SHEET 5 AD8 5 LYS 2 46 ILE 2 49 -1 O LYS 2 46 N GLN 2 38 SHEET 1 AD9 4 SER 2 9 GLY 2 12 0 SHEET 2 AD9 4 THR 2 105 VAL 2 109 1 O THR 2 108 N MET 2 10 SHEET 3 AD9 4 ALA 2 85 ASP 2 93 -1 N TYR 2 87 O THR 2 105 SHEET 4 AD9 4 ALA 2 98 PHE 2 101 -1 O ALA 2 98 N ASP 2 93 SHEET 1 AE1 3 VAL 2 18 THR 2 23 0 SHEET 2 AE1 3 SER 2 71 ILE 2 76 -1 O ALA 2 72 N CYS 2 22 SHEET 3 AE1 3 PHE 2 63 SER 2 68 -1 N SER 2 68 O SER 2 71 SHEET 1 AE2 4 SER 2 118 PHE 2 122 0 SHEET 2 AE2 4 LYS 2 133 PHE 2 143 -1 O SER 2 141 N SER 2 118 SHEET 3 AE2 4 TYR 2 176 THR 2 185 -1 O SER 2 180 N CYS 2 138 SHEET 4 AE2 4 VAL 2 163 LYS 2 170 -1 N SER 2 169 O ALA 2 177 SHEET 1 AE3 3 VAL 2 148 LYS 2 153 0 SHEET 2 AE3 3 TYR 2 195 HIS 2 201 -1 O GLN 2 198 N ALA 2 151 SHEET 3 AE3 3 SER 2 204 VAL 2 210 -1 O VAL 2 210 N TYR 2 195 SHEET 1 AE4 2 TRP A 35 TYR A 39 0 SHEET 2 AE4 2 GLY A 495 THR A 499 -1 O GLY A 495 N TYR A 39 SHEET 1 AE5 4 TRP A 45 ASP A 47 0 SHEET 2 AE5 4 VAL A 488 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AE5 4 PHE A 223 CYS A 228 -1 N ALA A 224 O VAL A 489 SHEET 4 AE5 4 VAL A 242 VAL A 245 -1 O VAL A 245 N ILE A 225 SHEET 1 AE6 3 VAL A 75 PRO A 76 0 SHEET 2 AE6 3 PHE A 53 SER A 56 1 N SER A 56 O VAL A 75 SHEET 3 AE6 3 HIS A 216 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AE7 2 GLU A 91 ASN A 94 0 SHEET 2 AE7 2 THR A 236 CYS A 239 -1 O GLY A 237 N PHE A 93 SHEET 1 AE8 5 LYS A 169 TYR A 177 0 SHEET 2 AE8 5 LEU A 154 THR A 162 -1 N LYS A 155 O PHE A 176 SHEET 3 AE8 5 LEU A 129 ASN A 133 -1 N THR A 132 O ASN A 156 SHEET 4 AE8 5 GLU A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AE8 5 VAL A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AE9 2 THR A 202 GLN A 203 0 SHEET 2 AE9 2 MET A 434 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 1 AF1 6 MET A 271 ARG A 273 0 SHEET 2 AF1 6 ILE A 284 ARG A 298 -1 O GLN A 287 N MET A 271 SHEET 3 AF1 6 HIS A 330 SER A 334 -1 O HIS A 330 N THR A 297 SHEET 4 AF1 6 SER A 413 ILE A 420 -1 O ILE A 414 N VAL A 333 SHEET 5 AF1 6 GLU A 381 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 6 AF1 6 HIS A 374 CYS A 378 -1 N PHE A 376 O PHE A 383 SHEET 1 AF2 6 MET A 271 ARG A 273 0 SHEET 2 AF2 6 ILE A 284 ARG A 298 -1 O GLN A 287 N MET A 271 SHEET 3 AF2 6 ILE A 443 ARG A 456 -1 O ILE A 449 N VAL A 292 SHEET 4 AF2 6 GLU A 466 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 5 AF2 6 ILE A 359 PHE A 361 1 N ARG A 360 O PHE A 468 SHEET 6 AF2 6 SER A 393 TRP A 395 -1 O SER A 393 N PHE A 361 SHEET 1 AF3 2 ARG A 304 GLY A 312 0 SHEET 2 AF3 2 GLN A 315 THR A 320 -1 O PHE A 317 N ILE A 307 SHEET 1 AF4 4 GLN X 5 SER X 7 0 SHEET 2 AF4 4 SER X 19 ASN X 23 -1 O THR X 21 N SER X 7 SHEET 3 AF4 4 LEU X 77 LEU X 82 -1 O LEU X 80 N LEU X 20 SHEET 4 AF4 4 VAL X 67 ASP X 72 -1 N HIS X 68 O ARG X 81 SHEET 1 AF5 5 LEU X 11 VAL X 12 0 SHEET 2 AF5 5 THR X 105 VAL X 109 1 O THR X 108 N VAL X 12 SHEET 3 AF5 5 ALA X 88 ILE X 100A-1 N TYR X 90 O THR X 105 SHEET 4 AF5 5 TYR X 33 GLN X 39 -1 N GLN X 39 O ILE X 89 SHEET 5 AF5 5 GLU X 46 VAL X 51 -1 O GLU X 46 N ARG X 38 SHEET 1 AF6 4 LEU X 11 VAL X 12 0 SHEET 2 AF6 4 THR X 105 VAL X 109 1 O THR X 108 N VAL X 12 SHEET 3 AF6 4 ALA X 88 ILE X 100A-1 N TYR X 90 O THR X 105 SHEET 4 AF6 4 TRP X 100J TYR X 100O-1 O PHE X 100K N ARG X 100 SHEET 1 AF7 3 ALA Z 19 ARG Z 20 0 SHEET 2 AF7 3 LEU Z 73 ILE Z 75 -1 O ILE Z 75 N ALA Z 19 SHEET 3 AF7 3 PHE Z 62 GLY Z 64 -1 N SER Z 63 O THR Z 74 SHEET 1 AF8 3 PRO Z 44 ILE Z 48 0 SHEET 2 AF8 3 ARG Z 31 GLN Z 38 -1 N GLN Z 37 O SER Z 45 SHEET 3 AF8 3 ASP Z 85 ASP Z 92 -1 O TYR Z 87 N TYR Z 36 SHEET 1 AF9 4 GLN f 3 VAL f 5 0 SHEET 2 AF9 4 SER f 17 SER f 25 -1 O ARG f 23 N VAL f 5 SHEET 3 AF9 4 GLY f 84 SER f 91 -1 O GLY f 84 N ALA f 24 SHEET 4 AF9 4 VAL f 68 GLN f 73 -1 N THR f 71 O TYR f 87 SHEET 1 AG1 6 VAL f 10 LYS f 12 0 SHEET 2 AG1 6 THR f 124 VAL f 128 1 O VAL f 127 N LYS f 12 SHEET 3 AG1 6 ALA f 99 ARG f 106 -1 N ALA f 99 O VAL f 126 SHEET 4 AG1 6 ILE f 34 ILE f 40 -1 N VAL f 37 O PHE f 102 SHEET 5 AG1 6 GLY f 44 LYS f 52 -1 O GLY f 49 N TRP f 36 SHEET 6 AG1 6 ALA f 57 TYR f 60 -1 O ALA f 57 N LYS f 52 SHEET 1 AG2 4 VAL f 10 LYS f 12 0 SHEET 2 AG2 4 THR f 124 VAL f 128 1 O VAL f 127 N LYS f 12 SHEET 3 AG2 4 ALA f 99 ARG f 106 -1 N ALA f 99 O VAL f 126 SHEET 4 AG2 4 TRP f 117 TRP f 120 -1 O TYR f 119 N ARG f 105 SHEET 1 AG3 4 LEU h 4 SER h 7 0 SHEET 2 AG3 4 ALA h 19 ALA h 25 -1 O PHE h 22 N SER h 7 SHEET 3 AG3 4 ASP h 70 ILE h 75 -1 O PHE h 71 N CYS h 23 SHEET 4 AG3 4 PHE h 62 SER h 67 -1 N VAL h 63 O THR h 74 SHEET 1 AG4 6 ILE h 10 LEU h 13 0 SHEET 2 AG4 6 SER h 102 VAL h 106 1 O GLU h 103 N LEU h 11 SHEET 3 AG4 6 VAL h 85 GLN h 89 -1 N TYR h 86 O SER h 102 SHEET 4 AG4 6 THR h 34 LYS h 38 -1 N LYS h 38 O VAL h 85 SHEET 5 AG4 6 ARG h 45 TYR h 49 -1 O ARG h 45 N GLN h 37 SHEET 6 AG4 6 ARG h 53 ARG h 54 -1 O ARG h 53 N TYR h 49 SHEET 1 AG5 2 TRP C 35 TYR C 39 0 SHEET 2 AG5 2 GLY C 495 THR C 499 -1 O GLY C 495 N TYR C 39 SHEET 1 AG6 4 TRP C 45 ASP C 47 0 SHEET 2 AG6 4 VAL C 488 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AG6 4 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AG6 4 VAL C 242 VAL C 245 -1 O VAL C 245 N ILE C 225 SHEET 1 AG7 3 VAL C 75 PRO C 76 0 SHEET 2 AG7 3 PHE C 53 SER C 56 1 N SER C 56 O VAL C 75 SHEET 3 AG7 3 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AG8 2 GLU C 91 ASN C 94 0 SHEET 2 AG8 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AG9 5 LYS C 169 TYR C 177 0 SHEET 2 AG9 5 LEU C 154 THR C 162 -1 N LYS C 155 O PHE C 176 SHEET 3 AG9 5 LEU C 129 ASN C 133 -1 N THR C 132 O ASN C 156 SHEET 4 AG9 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AG9 5 VAL C 181 GLN C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AH1 2 THR C 202 GLN C 203 0 SHEET 2 AH1 2 MET C 434 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 1 AH2 6 MET C 271 ARG C 273 0 SHEET 2 AH2 6 ILE C 284 ARG C 298 -1 O GLN C 287 N MET C 271 SHEET 3 AH2 6 HIS C 330 SER C 334 -1 O HIS C 330 N THR C 297 SHEET 4 AH2 6 SER C 413 ARG C 419 -1 O ILE C 414 N VAL C 333 SHEET 5 AH2 6 GLU C 381 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 6 AH2 6 HIS C 374 CYS C 378 -1 N PHE C 376 O PHE C 383 SHEET 1 AH3 6 MET C 271 ARG C 273 0 SHEET 2 AH3 6 ILE C 284 ARG C 298 -1 O GLN C 287 N MET C 271 SHEET 3 AH3 6 ILE C 443 ARG C 456 -1 O ILE C 449 N VAL C 292 SHEET 4 AH3 6 GLU C 466 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 5 AH3 6 ILE C 359 PHE C 361 1 N ARG C 360 O PHE C 468 SHEET 6 AH3 6 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 AH4 2 ARG C 304 GLY C 312 0 SHEET 2 AH4 2 GLN C 315 THR C 320 -1 O PHE C 317 N ILE C 307 SHEET 1 AH5 4 GLN H 3 SER H 7 0 SHEET 2 AH5 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AH5 4 GLN H 79 LEU H 84 -1 O LEU H 80 N CYS H 22 SHEET 4 AH5 4 VAL H 69 ASP H 74 -1 N ASP H 74 O GLN H 79 SHEET 1 AH6 6 LEU H 11 VAL H 12 0 SHEET 2 AH6 6 VAL H 116 VAL H 120 1 O THR H 119 N VAL H 12 SHEET 3 AH6 6 ALA H 93 ARG H 99 -1 N ALA H 93 O VAL H 118 SHEET 4 AH6 6 TYR H 34 GLN H 40 -1 N ILE H 38 O TYR H 96 SHEET 5 AH6 6 LEU H 46 PHE H 53 -1 O GLY H 50 N TRP H 37 SHEET 6 AH6 6 THR H 59 TYR H 61 -1 O ARG H 60 N TYR H 51 SHEET 1 AH7 4 SER H 129 LEU H 133 0 SHEET 2 AH7 4 THR H 144 TYR H 154 -1 O LYS H 152 N SER H 129 SHEET 3 AH7 4 TYR H 185 PRO H 194 -1 O VAL H 193 N ALA H 145 SHEET 4 AH7 4 VAL H 172 THR H 174 -1 N HIS H 173 O VAL H 190 SHEET 1 AH8 4 SER H 129 LEU H 133 0 SHEET 2 AH8 4 THR H 144 TYR H 154 -1 O LYS H 152 N SER H 129 SHEET 3 AH8 4 TYR H 185 PRO H 194 -1 O VAL H 193 N ALA H 145 SHEET 4 AH8 4 VAL H 178 LEU H 179 -1 N VAL H 178 O SER H 186 SHEET 1 AH9 3 VAL H 159 TRP H 163 0 SHEET 2 AH9 3 TYR H 203 HIS H 209 -1 O ASN H 206 N SER H 162 SHEET 3 AH9 3 THR H 214 VAL H 220 -1 O VAL H 220 N TYR H 203 SHEET 1 AI1 5 SER L 9 GLY L 12 0 SHEET 2 AI1 5 THR L 105 VAL L 109 1 O THR L 108 N MET L 10 SHEET 3 AI1 5 ALA L 85 ASP L 93 -1 N TYR L 87 O THR L 105 SHEET 4 AI1 5 GLN L 35 GLN L 39 -1 N GLN L 39 O ASP L 86 SHEET 5 AI1 5 LYS L 46 ILE L 49 -1 O LYS L 46 N GLN L 38 SHEET 1 AI2 4 SER L 9 GLY L 12 0 SHEET 2 AI2 4 THR L 105 VAL L 109 1 O THR L 108 N MET L 10 SHEET 3 AI2 4 ALA L 85 ASP L 93 -1 N TYR L 87 O THR L 105 SHEET 4 AI2 4 ALA L 98 PHE L 101 -1 O ALA L 98 N ASP L 93 SHEET 1 AI3 3 VAL L 18 THR L 23 0 SHEET 2 AI3 3 SER L 71 ILE L 76 -1 O ALA L 72 N CYS L 22 SHEET 3 AI3 3 PHE L 63 SER L 68 -1 N SER L 68 O SER L 71 SHEET 1 AI4 4 SER L 118 PHE L 122 0 SHEET 2 AI4 4 LYS L 133 PHE L 143 -1 O SER L 141 N SER L 118 SHEET 3 AI4 4 TYR L 176 THR L 185 -1 O SER L 180 N CYS L 138 SHEET 4 AI4 4 VAL L 163 LYS L 170 -1 N SER L 169 O ALA L 177 SHEET 1 AI5 3 VAL L 148 LYS L 153 0 SHEET 2 AI5 3 TYR L 195 HIS L 201 -1 O GLN L 198 N ALA L 151 SHEET 3 AI5 3 SER L 204 VAL L 210 -1 O VAL L 210 N TYR L 195 SHEET 1 AI6 4 GLN M 5 SER M 7 0 SHEET 2 AI6 4 SER M 19 ASN M 23 -1 O THR M 21 N SER M 7 SHEET 3 AI6 4 LEU M 77 LEU M 82 -1 O LEU M 80 N LEU M 20 SHEET 4 AI6 4 VAL M 67 ASP M 72 -1 N HIS M 68 O ARG M 81 SHEET 1 AI7 5 LEU M 11 VAL M 12 0 SHEET 2 AI7 5 THR M 105 VAL M 109 1 O THR M 108 N VAL M 12 SHEET 3 AI7 5 ALA M 88 ILE M 100A-1 N TYR M 90 O THR M 105 SHEET 4 AI7 5 TYR M 33 GLN M 39 -1 N GLN M 39 O ILE M 89 SHEET 5 AI7 5 GLU M 46 VAL M 51 -1 O GLU M 46 N ARG M 38 SHEET 1 AI8 4 LEU M 11 VAL M 12 0 SHEET 2 AI8 4 THR M 105 VAL M 109 1 O THR M 108 N VAL M 12 SHEET 3 AI8 4 ALA M 88 ILE M 100A-1 N TYR M 90 O THR M 105 SHEET 4 AI8 4 TRP M 100J TYR M 100O-1 O PHE M 100K N ARG M 100 SHEET 1 AI9 3 ALA N 19 ARG N 20 0 SHEET 2 AI9 3 LEU N 73 ILE N 75 -1 O ILE N 75 N ALA N 19 SHEET 3 AI9 3 PHE N 62 GLY N 64 -1 N SER N 63 O THR N 74 SHEET 1 AJ1 3 PRO N 44 ILE N 48 0 SHEET 2 AJ1 3 ARG N 31 GLN N 38 -1 N GLN N 37 O SER N 45 SHEET 3 AJ1 3 ASP N 85 ASP N 92 -1 O TYR N 87 N TYR N 36 SHEET 1 AJ2 4 GLN Q 3 VAL Q 5 0 SHEET 2 AJ2 4 SER Q 17 SER Q 25 -1 O ARG Q 23 N VAL Q 5 SHEET 3 AJ2 4 GLY Q 84 SER Q 91 -1 O GLY Q 84 N ALA Q 24 SHEET 4 AJ2 4 VAL Q 68 GLN Q 73 -1 N THR Q 71 O TYR Q 87 SHEET 1 AJ3 6 VAL Q 10 LYS Q 12 0 SHEET 2 AJ3 6 THR Q 124 VAL Q 128 1 O VAL Q 127 N LYS Q 12 SHEET 3 AJ3 6 ALA Q 99 ARG Q 106 -1 N ALA Q 99 O VAL Q 126 SHEET 4 AJ3 6 ILE Q 34 ILE Q 40 -1 N VAL Q 37 O PHE Q 102 SHEET 5 AJ3 6 GLY Q 44 LYS Q 52 -1 O GLY Q 49 N TRP Q 36 SHEET 6 AJ3 6 ALA Q 57 TYR Q 60 -1 O ALA Q 57 N LYS Q 52 SHEET 1 AJ4 4 VAL Q 10 LYS Q 12 0 SHEET 2 AJ4 4 THR Q 124 VAL Q 128 1 O VAL Q 127 N LYS Q 12 SHEET 3 AJ4 4 ALA Q 99 ARG Q 106 -1 N ALA Q 99 O VAL Q 126 SHEET 4 AJ4 4 TRP Q 117 TRP Q 120 -1 O TYR Q 119 N ARG Q 105 SHEET 1 AJ5 4 LEU R 4 SER R 7 0 SHEET 2 AJ5 4 ALA R 19 ALA R 25 -1 O PHE R 22 N SER R 7 SHEET 3 AJ5 4 ASP R 70 ILE R 75 -1 O PHE R 71 N CYS R 23 SHEET 4 AJ5 4 PHE R 62 SER R 67 -1 N VAL R 63 O THR R 74 SHEET 1 AJ6 6 ILE R 10 LEU R 13 0 SHEET 2 AJ6 6 SER R 102 VAL R 106 1 O GLU R 103 N LEU R 11 SHEET 3 AJ6 6 VAL R 85 GLN R 89 -1 N TYR R 86 O SER R 102 SHEET 4 AJ6 6 THR R 34 LYS R 38 -1 N LYS R 38 O VAL R 85 SHEET 5 AJ6 6 ARG R 45 TYR R 49 -1 O ARG R 45 N GLN R 37 SHEET 6 AJ6 6 ARG R 53 ARG R 54 -1 O ARG R 53 N TYR R 49 SSBOND 1 CYS 3 22 CYS 3 97 1555 1555 2.03 SSBOND 2 CYS 3 149 CYS 3 205 1555 1555 2.03 SSBOND 3 CYS 3 225 CYS 4 215 1555 1555 2.03 SSBOND 4 CYS 4 22 CYS 4 89 1555 1555 2.03 SSBOND 5 CYS 4 138 CYS 4 197 1555 1555 2.03 SSBOND 6 CYS B 119 CYS B 205 1555 1555 2.03 SSBOND 7 CYS B 126 CYS B 196 1555 1555 2.03 SSBOND 8 CYS B 131 CYS B 157 1555 1555 2.03 SSBOND 9 CYS B 218 CYS B 247 1555 1555 2.03 SSBOND 10 CYS B 228 CYS B 239 1555 1555 2.04 SSBOND 11 CYS B 296 CYS B 331 1555 1555 2.03 SSBOND 12 CYS B 378 CYS B 445 1555 1555 2.03 SSBOND 13 CYS B 385 CYS B 418 1555 1555 2.03 SSBOND 14 CYS F 598 CYS F 604 1555 1555 2.01 SSBOND 15 CYS Y 22 CYS Y 92 1555 1555 2.03 SSBOND 16 CYS a 23 CYS a 88 1555 1555 2.03 SSBOND 17 CYS g 22 CYS g 103 1555 1555 2.04 SSBOND 18 CYS g 109 CYS g 112 1555 1555 2.03 SSBOND 19 CYS 1 22 CYS 1 97 1555 1555 2.03 SSBOND 20 CYS 1 149 CYS 1 205 1555 1555 2.03 SSBOND 21 CYS 1 225 CYS 2 215 1555 1555 2.03 SSBOND 22 CYS 2 22 CYS 2 89 1555 1555 2.03 SSBOND 23 CYS 2 138 CYS 2 197 1555 1555 2.03 SSBOND 24 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 25 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 26 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 27 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 28 CYS A 228 CYS A 239 1555 1555 2.04 SSBOND 29 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 30 CYS A 378 CYS A 445 1555 1555 2.03 SSBOND 31 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 32 CYS E 598 CYS E 604 1555 1555 2.01 SSBOND 33 CYS X 22 CYS X 92 1555 1555 2.03 SSBOND 34 CYS Z 23 CYS Z 88 1555 1555 2.03 SSBOND 35 CYS f 22 CYS f 103 1555 1555 2.04 SSBOND 36 CYS f 109 CYS f 112 1555 1555 2.03 SSBOND 37 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 38 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 39 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 40 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 41 CYS C 228 CYS C 239 1555 1555 2.04 SSBOND 42 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 43 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 44 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 45 CYS D 598 CYS D 604 1555 1555 2.01 SSBOND 46 CYS H 22 CYS H 97 1555 1555 2.03 SSBOND 47 CYS H 149 CYS H 205 1555 1555 2.03 SSBOND 48 CYS H 225 CYS L 215 1555 1555 2.03 SSBOND 49 CYS L 22 CYS L 89 1555 1555 2.03 SSBOND 50 CYS L 138 CYS L 197 1555 1555 2.03 SSBOND 51 CYS M 22 CYS M 92 1555 1555 2.03 SSBOND 52 CYS N 23 CYS N 88 1555 1555 2.03 SSBOND 53 CYS Q 22 CYS Q 103 1555 1555 2.04 SSBOND 54 CYS Q 109 CYS Q 112 1555 1555 2.03 LINK ND2 ASN B 88 C1 NAG B 646 1555 1555 1.43 LINK ND2 ASN B 133 C1 NAG B 618 1555 1555 1.43 LINK ND2 ASN B 137 C1 NAG B 620 1555 1555 1.44 LINK ND2 ASN B 156 C1 NAG B 624 1555 1555 1.45 LINK ND2 ASN B 160 C1 NAG B 601 1555 1555 1.44 LINK ND2 ASN B 197 C1 NAG B 623 1555 1555 1.44 LINK ND2 ASN B 234 C1 NAG B 643 1555 1555 1.44 LINK ND2 ASN B 262 C1 NAG B 634 1555 1555 1.44 LINK ND2 ASN B 276 C1 NAG B 639 1555 1555 1.45 LINK ND2 ASN B 295 C1 NAG B 604 1555 1555 1.43 LINK ND2 ASN B 301 C1 NAG B 627 1555 1555 1.44 LINK ND2 ASN B 332 C1 NAG B 629 1555 1555 1.43 LINK ND2 ASN B 339 C1 NAG B 608 1555 1555 1.44 LINK ND2 ASN B 363 C1 NAG B 609 1555 1555 1.43 LINK ND2 ASN B 386 C1 NAG B 612 1555 1555 1.43 LINK ND2 ASN B 392 C1 NAG B 617 1555 1555 1.45 LINK ND2 ASN B 448 C1 NAG B 632 1555 1555 1.44 LINK ND2 ASN A 88 C1 NAG A 646 1555 1555 1.43 LINK ND2 ASN A 133 C1 NAG A 618 1555 1555 1.43 LINK ND2 ASN A 137 C1 NAG A 620 1555 1555 1.44 LINK ND2 ASN A 156 C1 NAG A 624 1555 1555 1.45 LINK ND2 ASN A 160 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG A 623 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG A 643 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG A 634 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG A 639 1555 1555 1.45 LINK ND2 ASN A 295 C1 NAG A 604 1555 1555 1.43 LINK ND2 ASN A 301 C1 NAG A 627 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG A 629 1555 1555 1.43 LINK ND2 ASN A 339 C1 NAG A 608 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG A 609 1555 1555 1.43 LINK ND2 ASN A 386 C1 NAG A 612 1555 1555 1.43 LINK ND2 ASN A 392 C1 NAG A 617 1555 1555 1.45 LINK ND2 ASN A 448 C1 NAG A 632 1555 1555 1.44 LINK ND2 ASN C 88 C1 NAG C 646 1555 1555 1.43 LINK ND2 ASN C 133 C1 NAG C 618 1555 1555 1.43 LINK ND2 ASN C 137 C1 NAG C 620 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG C 624 1555 1555 1.45 LINK ND2 ASN C 160 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG C 623 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG C 643 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG C 634 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG C 639 1555 1555 1.45 LINK ND2 ASN C 295 C1 NAG C 604 1555 1555 1.43 LINK ND2 ASN C 301 C1 NAG C 627 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG C 629 1555 1555 1.43 LINK ND2 ASN C 339 C1 NAG C 608 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG C 609 1555 1555 1.43 LINK ND2 ASN C 386 C1 NAG C 612 1555 1555 1.43 LINK ND2 ASN C 392 C1 NAG C 617 1555 1555 1.45 LINK ND2 ASN C 448 C1 NAG C 632 1555 1555 1.44 LINK O4 NAG B 601 C1 NAG B 602 1555 1555 1.44 LINK O4 NAG B 602 C1 BMA B 603 1555 1555 1.44 LINK O4 NAG B 604 C1 NAG B 605 1555 1555 1.44 LINK O4 NAG B 605 C1 BMA B 606 1555 1555 1.45 LINK O3 BMA B 606 C1 MAN B 607 1555 1555 1.45 LINK O4 NAG B 609 C1 NAG B 610 1555 1555 1.45 LINK O4 NAG B 610 C1 BMA B 611 1555 1555 1.45 LINK O4 NAG B 612 C1 NAG B 613 1555 1555 1.43 LINK O4 NAG B 613 C1 BMA B 614 1555 1555 1.44 LINK O3 BMA B 614 C1 MAN B 615 1555 1555 1.44 LINK O6 BMA B 614 C1 MAN B 616 1555 1555 1.44 LINK O4 NAG B 618 C1 NAG B 619 1555 1555 1.45 LINK O4 NAG B 620 C1 NAG B 621 1555 1555 1.44 LINK O4 NAG B 621 C1 BMA B 622 1555 1555 1.44 LINK O4 NAG B 624 C1 NAG B 625 1555 1555 1.42 LINK O4 NAG B 625 C1 BMA B 626 1555 1555 1.45 LINK O4 NAG B 627 C1 NAG B 628 1555 1555 1.45 LINK O4 NAG B 629 C1 NAG B 630 1555 1555 1.45 LINK O4 NAG B 630 C1 BMA B 631 1555 1555 1.44 LINK O4 NAG B 632 C1 NAG B 633 1555 1555 1.44 LINK O4 NAG B 634 C1 NAG B 635 1555 1555 1.45 LINK O4 NAG B 635 C1 BMA B 636 1555 1555 1.44 LINK O3 BMA B 636 C1 MAN B 637 1555 1555 1.44 LINK O6 BMA B 636 C1 MAN B 638 1555 1555 1.44 LINK O4 NAG B 639 C1 NAG B 640 1555 1555 1.43 LINK O4 NAG B 640 C1 BMA B 641 1555 1555 1.44 LINK O3 BMA B 641 C1 MAN B 642 1555 1555 1.45 LINK O4 NAG B 643 C1 NAG B 644 1555 1555 1.44 LINK O4 NAG B 644 C1 BMA B 645 1555 1555 1.45 LINK O4 NAG B 646 C1 NAG B 647 1555 1555 1.45 LINK O4 NAG B 647 C1 BMA B 648 1555 1555 1.45 LINK O4 NAG A 601 C1 NAG A 602 1555 1555 1.44 LINK O4 NAG A 602 C1 BMA A 603 1555 1555 1.44 LINK O4 NAG A 604 C1 NAG A 605 1555 1555 1.44 LINK O4 NAG A 605 C1 BMA A 606 1555 1555 1.45 LINK O3 BMA A 606 C1 MAN A 607 1555 1555 1.45 LINK O4 NAG A 609 C1 NAG A 610 1555 1555 1.45 LINK O4 NAG A 610 C1 BMA A 611 1555 1555 1.45 LINK O4 NAG A 612 C1 NAG A 613 1555 1555 1.43 LINK O4 NAG A 613 C1 BMA A 614 1555 1555 1.44 LINK O3 BMA A 614 C1 MAN A 615 1555 1555 1.44 LINK O6 BMA A 614 C1 MAN A 616 1555 1555 1.44 LINK O4 NAG A 618 C1 NAG A 619 1555 1555 1.45 LINK O4 NAG A 620 C1 NAG A 621 1555 1555 1.44 LINK O4 NAG A 621 C1 BMA A 622 1555 1555 1.44 LINK O4 NAG A 624 C1 NAG A 625 1555 1555 1.42 LINK O4 NAG A 625 C1 BMA A 626 1555 1555 1.45 LINK O4 NAG A 627 C1 NAG A 628 1555 1555 1.45 LINK O4 NAG A 629 C1 NAG A 630 1555 1555 1.45 LINK O4 NAG A 630 C1 BMA A 631 1555 1555 1.44 LINK O4 NAG A 632 C1 NAG A 633 1555 1555 1.44 LINK O4 NAG A 634 C1 NAG A 635 1555 1555 1.45 LINK O4 NAG A 635 C1 BMA A 636 1555 1555 1.44 LINK O3 BMA A 636 C1 MAN A 637 1555 1555 1.44 LINK O6 BMA A 636 C1 MAN A 638 1555 1555 1.44 LINK O4 NAG A 639 C1 NAG A 640 1555 1555 1.43 LINK O4 NAG A 640 C1 BMA A 641 1555 1555 1.44 LINK O3 BMA A 641 C1 MAN A 642 1555 1555 1.45 LINK O4 NAG A 643 C1 NAG A 644 1555 1555 1.44 LINK O4 NAG A 644 C1 BMA A 645 1555 1555 1.45 LINK O4 NAG A 646 C1 NAG A 647 1555 1555 1.45 LINK O4 NAG A 647 C1 BMA A 648 1555 1555 1.45 LINK O4 NAG C 601 C1 NAG C 602 1555 1555 1.44 LINK O4 NAG C 602 C1 BMA C 603 1555 1555 1.44 LINK O4 NAG C 604 C1 NAG C 605 1555 1555 1.44 LINK O4 NAG C 605 C1 BMA C 606 1555 1555 1.45 LINK O3 BMA C 606 C1 MAN C 607 1555 1555 1.45 LINK O4 NAG C 609 C1 NAG C 610 1555 1555 1.45 LINK O4 NAG C 610 C1 BMA C 611 1555 1555 1.45 LINK O4 NAG C 612 C1 NAG C 613 1555 1555 1.43 LINK O4 NAG C 613 C1 BMA C 614 1555 1555 1.44 LINK O3 BMA C 614 C1 MAN C 615 1555 1555 1.44 LINK O6 BMA C 614 C1 MAN C 616 1555 1555 1.44 LINK O4 NAG C 618 C1 NAG C 619 1555 1555 1.45 LINK O4 NAG C 620 C1 NAG C 621 1555 1555 1.44 LINK O4 NAG C 621 C1 BMA C 622 1555 1555 1.44 LINK O4 NAG C 624 C1 NAG C 625 1555 1555 1.42 LINK O4 NAG C 625 C1 BMA C 626 1555 1555 1.45 LINK O4 NAG C 627 C1 NAG C 628 1555 1555 1.45 LINK O4 NAG C 629 C1 NAG C 630 1555 1555 1.45 LINK O4 NAG C 630 C1 BMA C 631 1555 1555 1.44 LINK O4 NAG C 632 C1 NAG C 633 1555 1555 1.44 LINK O4 NAG C 634 C1 NAG C 635 1555 1555 1.45 LINK O4 NAG C 635 C1 BMA C 636 1555 1555 1.44 LINK O3 BMA C 636 C1 MAN C 637 1555 1555 1.44 LINK O6 BMA C 636 C1 MAN C 638 1555 1555 1.44 LINK O4 NAG C 639 C1 NAG C 640 1555 1555 1.43 LINK O4 NAG C 640 C1 BMA C 641 1555 1555 1.44 LINK O3 BMA C 641 C1 MAN C 642 1555 1555 1.45 LINK O4 NAG C 643 C1 NAG C 644 1555 1555 1.44 LINK O4 NAG C 644 C1 BMA C 645 1555 1555 1.45 LINK O4 NAG C 646 C1 NAG C 647 1555 1555 1.45 LINK O4 NAG C 647 C1 BMA C 648 1555 1555 1.45 CISPEP 1 PHE 3 155 PRO 3 156 0 -9.93 CISPEP 2 GLU 3 157 PRO 3 158 0 -4.30 CISPEP 3 TYR 4 144 PRO 4 145 0 -2.68 CISPEP 4 PHE 1 155 PRO 1 156 0 -9.93 CISPEP 5 GLU 1 157 PRO 1 158 0 -4.25 CISPEP 6 TYR 2 144 PRO 2 145 0 -2.69 CISPEP 7 PHE H 155 PRO H 156 0 -9.90 CISPEP 8 GLU H 157 PRO H 158 0 -4.32 CISPEP 9 TYR L 144 PRO L 145 0 -2.65 SITE 1 AC1 5 ASN 1 56 THR 1 59 ARG 1 60 ASN A 88 SITE 2 AC1 5 SER E 528 SITE 1 AC2 3 ASN A 133 ASP A 140 MET A 150 SITE 1 AC3 5 ASN A 137 ASN X 58 PHE X 100K ASP Z 92 SITE 2 AC3 5 THR Z 95B SITE 1 AC4 3 ASN A 156 SER A 158 TYR A 173 SITE 1 AC5 4 GLN A 130 ASN A 160 LYS A 169 LYS A 171 SITE 1 AC6 3 ARG A 192 ASN A 197 ARG C 308 SITE 1 AC7 4 ASN A 234 THR A 236 ILE A 277 HIS A 352 SITE 1 AC8 4 GLU A 211 ASN A 262 SER A 447 NAG A 632 SITE 1 AC9 3 ASN A 276 GLY h 30 SER h 52 SITE 1 AD1 2 ASN A 295 ARG A 444 SITE 1 AD2 2 ASN A 301 ILE A 323 SITE 1 AD3 7 HIS A 330 ASN A 332 THR A 415 ILE X 100A SITE 2 AD3 7 TYR X 100B GLY X 100C VAL X 100E SITE 1 AD4 1 ASN A 339 SITE 1 AD5 5 ASN A 363 SER A 388 NAG A 612 NAG A 613 SITE 2 AD5 5 NAG A 617 SITE 1 AD6 6 ASP A 141 ASN A 386 SER A 388 NAG A 609 SITE 2 AD6 6 NAG A 610 NAG A 617 SITE 1 AD7 3 ASN A 392 NAG A 609 NAG A 613 SITE 1 AD8 2 ASN A 448 NAG A 634 SITE 1 AD9 5 ASN 3 56 THR 3 59 ARG 3 60 ASN B 88 SITE 2 AD9 5 SER F 528 SITE 1 AE1 3 ASN B 133 ASP B 140 MET B 150 SITE 1 AE2 5 ASN B 137 ASN Y 58 PHE Y 100K ASP a 92 SITE 2 AE2 5 THR a 95B SITE 1 AE3 3 ASN B 156 SER B 158 TYR B 173 SITE 1 AE4 4 GLN B 130 ASN B 160 LYS B 169 LYS B 171 SITE 1 AE5 3 ARG A 308 ARG B 192 ASN B 197 SITE 1 AE6 4 ASN B 234 THR B 236 ILE B 277 HIS B 352 SITE 1 AE7 4 GLU B 211 ASN B 262 SER B 447 NAG B 632 SITE 1 AE8 3 ASN B 276 GLY i 30 SER i 52 SITE 1 AE9 2 ASN B 295 ARG B 444 SITE 1 AF1 2 ASN B 301 ILE B 323 SITE 1 AF2 7 HIS B 330 ASN B 332 THR B 415 ILE Y 100A SITE 2 AF2 7 TYR Y 100B GLY Y 100C VAL Y 100E SITE 1 AF3 1 ASN B 339 SITE 1 AF4 5 ASN B 363 SER B 388 NAG B 612 NAG B 613 SITE 2 AF4 5 NAG B 617 SITE 1 AF5 6 ASP B 141 ASN B 386 SER B 388 NAG B 609 SITE 2 AF5 6 NAG B 610 NAG B 617 SITE 1 AF6 3 ASN B 392 NAG B 609 NAG B 613 SITE 1 AF7 2 ASN B 448 NAG B 634 SITE 1 AF8 5 ASN C 88 SER D 528 ASN H 56 THR H 59 SITE 2 AF8 5 ARG H 60 SITE 1 AF9 3 ASN C 133 ASP C 140 MET C 150 SITE 1 AG1 5 ASN C 137 ASN M 58 PHE M 100K ASP N 92 SITE 2 AG1 5 THR N 95B SITE 1 AG2 3 ASN C 156 SER C 158 TYR C 173 SITE 1 AG3 4 GLN C 130 ASN C 160 LYS C 169 LYS C 171 SITE 1 AG4 3 ARG B 308 ARG C 192 ASN C 197 SITE 1 AG5 4 ASN C 234 THR C 236 ILE C 277 HIS C 352 SITE 1 AG6 4 GLU C 211 ASN C 262 SER C 447 NAG C 632 SITE 1 AG7 3 ASN C 276 GLY R 30 SER R 52 SITE 1 AG8 2 ASN C 295 ARG C 444 SITE 1 AG9 2 ASN C 301 ILE C 323 SITE 1 AH1 7 HIS C 330 ASN C 332 THR C 415 ILE M 100A SITE 2 AH1 7 TYR M 100B GLY M 100C VAL M 100E SITE 1 AH2 1 ASN C 339 SITE 1 AH3 5 ASN C 363 SER C 388 NAG C 612 NAG C 613 SITE 2 AH3 5 NAG C 617 SITE 1 AH4 6 ASP C 141 ASN C 386 SER C 388 NAG C 609 SITE 2 AH4 6 NAG C 610 NAG C 617 SITE 1 AH5 3 ASN C 392 NAG C 609 NAG C 613 SITE 1 AH6 2 ASN C 448 NAG C 634 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