HEADER VIRAL PROTEIN 26-MAR-18 6CUE TITLE CRYO-EM STRUCTURE AT 4.0 A RESOLUTION OF VACCINE-ELICITED ANTIBODY TITLE 2 VFP7.04 IN COMPLEX WITH HIV-1 ENV BG505 DS-SOSIP, AND ANTIBODIES TITLE 3 VRC03 AND PGT122 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 3 CHAIN: c, 2, C; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 8 CHAIN: 1, D, d; COMPND 9 SYNONYM: ENV POLYPROTEIN; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: VFP7.04 HEAVY CHAIN; COMPND 13 CHAIN: 3, H, h; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: VFP7.04 LIGHT CHAIN; COMPND 17 CHAIN: 4, L, l; COMPND 18 ENGINEERED: YES; COMPND 19 MOL_ID: 5; COMPND 20 MOLECULE: PGT122 HEAVY CHAIN; COMPND 21 CHAIN: 5, M, m; COMPND 22 ENGINEERED: YES; COMPND 23 MOL_ID: 6; COMPND 24 MOLECULE: PGT122 LIGHT CHAIN; COMPND 25 CHAIN: 6, N, n; COMPND 26 ENGINEERED: YES; COMPND 27 MOL_ID: 7; COMPND 28 MOLECULE: VRC03 HEAVY CHAIN; COMPND 29 CHAIN: 7, Q, q; COMPND 30 ENGINEERED: YES; COMPND 31 MOL_ID: 8; COMPND 32 MOLECULE: VRC03 LIGHT CHAIN; COMPND 33 CHAIN: 8, R, r; COMPND 34 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 GENE: ENV; SOURCE 5 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 10 ORGANISM_TAXID: 11676; SOURCE 11 GENE: ENV; SOURCE 12 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 17 ORGANISM_COMMON: MOUSE; SOURCE 18 ORGANISM_TAXID: 10090; SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 24 ORGANISM_COMMON: MOUSE; SOURCE 25 ORGANISM_TAXID: 10090; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 31 ORGANISM_COMMON: HUMAN; SOURCE 32 ORGANISM_TAXID: 9606; SOURCE 33 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 34 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 35 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 36 MOL_ID: 6; SOURCE 37 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 38 ORGANISM_COMMON: HUMAN; SOURCE 39 ORGANISM_TAXID: 9606; SOURCE 40 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 41 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 42 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 43 MOL_ID: 7; SOURCE 44 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 45 ORGANISM_COMMON: HUMAN; SOURCE 46 ORGANISM_TAXID: 9606; SOURCE 47 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 48 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 49 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 50 MOL_ID: 8; SOURCE 51 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 52 ORGANISM_COMMON: HUMAN; SOURCE 53 ORGANISM_TAXID: 9606; SOURCE 54 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 55 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 56 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1 ENV, BG505 SOSIP, FUSION PEPTIDE, VRC03, PGT122, VFP7.04, VIRAL KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR P.ACHARYA,B.CARRAGHER,C.S.POTTER,P.D.KWONG REVDAT 1 11-JUL-18 6CUE 0 JRNL AUTH A.DINGENS,P.ACHARYA,B.CARRAGHER,C.S.POTTER,P.D.KWONG,J.BLOOM JRNL TITL COMPLETE FUNCTIONAL MAPPING OF INFECTION- AND JRNL TITL 2 VACCINE-ELICITED ANTIBODIES AGAINST THE FUSION PEPTIDE OF JRNL TITL 3 HIV 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, UCSF CHIMERA, CRYOSPARC, REMARK 3 CRYOSPARC, PHENIX 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 : 142.000 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 : 64580 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 6CUE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-18. REMARK 100 THE DEPOSITION ID IS D_1000233398. 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 : VFP7.04-BG505 DS-SOSIP-VRC03 REMARK 245 -PGT122; PGT122; VRC03; REMARK 245 GLYCOPROTEIN; VFP7.04 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.50 REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.00 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 978 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) : 53.11 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : 105000 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: c, 2, C, 1, 3, 4, 5, 6, 7, 8, REMARK 350 AND CHAINS: D, H, L, M, N, Q, R, 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 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 GLU 2 185A REMARK 465 ASN 2 185B REMARK 465 GLN 2 185C REMARK 465 GLY 2 185D REMARK 465 ASN 2 185E REMARK 465 ARG 2 185F REMARK 465 SER 2 185G REMARK 465 ASN 2 185H REMARK 465 ASN 2 185I REMARK 465 THR 2 400 REMARK 465 SER 2 401 REMARK 465 VAL 2 402 REMARK 465 GLN 2 403 REMARK 465 GLY 2 404 REMARK 465 SER 2 405 REMARK 465 ASN 2 406 REMARK 465 SER 2 407 REMARK 465 THR 2 408 REMARK 465 GLY 2 409 REMARK 465 SER 2 410 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 1 548 REMARK 465 VAL 1 549 REMARK 465 GLN 1 550 REMARK 465 GLN 1 551 REMARK 465 GLN 1 552 REMARK 465 SER 1 553 REMARK 465 ASN 1 554 REMARK 465 LEU 1 555 REMARK 465 LEU 1 556 REMARK 465 ARG 1 557 REMARK 465 ALA 1 558 REMARK 465 ILE 1 559 REMARK 465 GLU 1 560 REMARK 465 ALA 1 561 REMARK 465 GLN 1 562 REMARK 465 GLN 1 563 REMARK 465 HIS 1 564 REMARK 465 LEU 1 565 REMARK 465 LEU 1 566 REMARK 465 LYS 1 567 REMARK 465 LEU 1 568 REMARK 465 SER 3 118 REMARK 465 LYS 4 112 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 SER H 118 REMARK 465 LYS L 112 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 SER h 118 REMARK 465 LYS l 112 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 7 121 CB SG REMARK 470 CYS Q 121 CB SG REMARK 470 CYS q 121 CB SG REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 SG CYS d 598 CB CYS d 604 1.49 REMARK 500 NH2 ARG D 542 OE2 GLU d 647 2.12 REMARK 500 OD2 ASP c 457 NH1 ARG c 469 2.13 REMARK 500 NH2 ARG 1 542 OE2 GLU D 647 2.17 REMARK 500 OE2 GLU 1 647 NH2 ARG d 542 2.18 REMARK 500 N THR M 83 OD2 ASP M 86 2.18 REMARK 500 ND2 ASN C 276 O5 NAG C 635 2.19 REMARK 500 N THR m 83 OD2 ASP m 86 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS Q 109 CA - CB - SG ANGL. DEV. = 8.8 DEGREES REMARK 500 CYS R 23 CA - CB - SG ANGL. DEV. = 7.6 DEGREES REMARK 500 CYS r 23 CA - CB - SG ANGL. DEV. = 7.6 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 c 80 76.69 40.06 REMARK 500 MET c 100 -6.71 67.94 REMARK 500 LEU c 122 43.47 -108.48 REMARK 500 CYS c 126 99.26 -69.14 REMARK 500 LEU c 259 70.42 59.63 REMARK 500 ASN c 289 -61.79 -95.88 REMARK 500 ASN c 425 47.62 -140.43 REMARK 500 THR c 461 65.60 61.17 REMARK 500 ASN c 462 67.20 60.79 REMARK 500 PRO c 493 -166.49 -74.22 REMARK 500 LEU c 494 68.29 62.56 REMARK 500 LYS 2 65 68.50 60.63 REMARK 500 ASN 2 80 74.21 36.12 REMARK 500 MET 2 100 -5.62 66.79 REMARK 500 CYS 2 126 99.13 -68.69 REMARK 500 LEU 2 259 68.68 60.20 REMARK 500 PHE 2 391 52.76 -95.53 REMARK 500 THR 2 461 65.54 61.76 REMARK 500 PRO 2 493 -169.56 -74.07 REMARK 500 LEU 2 494 69.39 62.00 REMARK 500 LEU C 52 -169.53 -125.54 REMARK 500 LYS C 65 67.30 61.00 REMARK 500 ASN C 80 77.38 36.52 REMARK 500 LYS C 97 32.12 -96.99 REMARK 500 MET C 100 -8.18 67.93 REMARK 500 CYS C 126 99.03 -67.45 REMARK 500 THR C 198 -34.91 -130.54 REMARK 500 GLU C 268 -50.19 -121.60 REMARK 500 ASN C 356 77.36 -100.19 REMARK 500 THR C 373 -163.92 -78.42 REMARK 500 PHE C 391 51.26 -95.46 REMARK 500 ASN C 425 48.34 -140.60 REMARK 500 THR C 461 65.77 62.84 REMARK 500 PRO C 493 -167.01 -73.73 REMARK 500 LEU C 494 69.31 62.87 REMARK 500 LEU 1 602 -14.16 72.71 REMARK 500 GLN 1 640 -6.93 73.18 REMARK 500 THR 3 61 -169.04 -102.08 REMARK 500 LYS 4 55 -174.60 177.65 REMARK 500 SER 4 57 43.94 -140.30 REMARK 500 SER 5 54 67.81 61.43 REMARK 500 ASP 5 56 72.14 -100.53 REMARK 500 LYS 5 64 -16.26 70.02 REMARK 500 SER 5 65 -37.27 -131.45 REMARK 500 ASP 5 72 88.05 -152.85 REMARK 500 VAL 6 11 48.38 -95.38 REMARK 500 ASN 6 52 41.17 -140.59 REMARK 500 ALA 7 99 -165.99 -161.88 REMARK 500 ASP 8 50 -36.30 76.27 REMARK 500 THR 8 51 -50.84 -153.07 REMARK 500 REMARK 500 THIS ENTRY HAS 83 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 THR c 77 ASP c 78 146.19 REMARK 500 THR 2 77 ASP 2 78 147.87 REMARK 500 ASP 8 50 THR 8 51 147.85 REMARK 500 PHE 8 83 ALA 8 84 148.39 REMARK 500 GLN 8 90 PHE 8 91 -141.14 REMARK 500 GLN R 90 PHE R 91 -141.77 REMARK 500 GLN r 90 PHE r 91 -139.91 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 2 REMARK 800 601 through NAG 2 602 bound to ASN 2 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 603 through BMA 2 605 bound to ASN 2 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 606 through BMA 2 608 bound to ASN 2 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 609 through NAG 2 610 bound to ASN 2 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG 2 611 bound REMARK 800 to ASN 2 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 612 through NAG 2 613 bound to ASN 2 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 614 through MAN 2 618 bound to ASN 2 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 635 through MAN 2 638 bound to ASN 2 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 619 through NAG 2 620 bound to ASN 2 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 621 through NAG 2 622 bound to ASN 2 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 628 through MAN 2 632 bound to ASN 2 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 623 through BMA 2 625 bound to ASN 2 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 626 through NAG 2 627 bound to ASN 2 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG 2 REMARK 800 633 through NAG 2 634 bound to ASN 2 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 601 through NAG C 602 bound to ASN C 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 603 through BMA C 605 bound to ASN C 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 606 through BMA C 608 bound to ASN C 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 609 through NAG C 610 bound to ASN C 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 611 bound REMARK 800 to ASN C 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 612 through NAG C 613 bound to ASN C 234 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 614 through MAN C 618 bound to ASN C 262 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 635 through MAN C 638 bound to ASN C 276 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 619 through NAG C 620 bound to ASN C 295 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 621 through NAG C 622 bound to ASN C 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 628 through MAN C 632 bound to ASN C 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 623 through BMA C 625 bound to ASN C 363 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 626 through NAG C 627 bound to ASN C 386 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C REMARK 800 633 through NAG C 634 bound to ASN C 448 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 601 through NAG c 602 bound to ASN c 133 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 603 through BMA c 605 bound to ASN c 137 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 606 through BMA c 608 bound to ASN c 156 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 609 through NAG c 610 bound to ASN c 160 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG c 611 bound REMARK 800 to ASN c 197 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 612 through NAG c 613 bound to ASN c 234 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 800 614 through MAN c 618 bound to ASN c 262 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 800 635 through MAN c 638 bound to ASN c 276 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 800 619 through NAG c 620 bound to ASN c 295 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 800 621 through NAG c 622 bound to ASN c 301 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 800 628 through MAN c 632 bound to ASN c 332 REMARK 800 REMARK 800 SITE_IDENTIFIER: AG4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG c REMARK 800 623 through BMA c 625 bound to ASN c 363 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 800 626 through NAG c 627 bound to ASN c 386 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 800 633 through NAG c 634 bound to ASN c 448 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-7621 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE AT 4.2 A RESOLUTION OF VACCINE-ELICITED ANTIBODY REMARK 900 VFP7.04 IN COMPLEX WITH HIV-1 ENV BG505 DS-SOSIP, AND ANTIBODIES REMARK 900 VRC03 AND PGT122 DBREF 6CUE c 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6CUE 2 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6CUE C 31 505 UNP Q2N0S6 Q2N0S6_9HIV1 30 502 DBREF 6CUE 1 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6CUE 3 1 118 PDB 6CUE 6CUE 1 118 DBREF 6CUE 4 1 112 PDB 6CUE 6CUE 1 112 DBREF 6CUE 5 1 111 PDB 6CUE 6CUE 1 111 DBREF 6CUE 6 6 107 PDB 6CUE 6CUE 6 107 DBREF 6CUE 7 1 129 PDB 6CUE 6CUE 1 129 DBREF 6CUE 8 1 107 PDB 6CUE 6CUE 1 107 DBREF 6CUE D 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6CUE H 1 118 PDB 6CUE 6CUE 1 118 DBREF 6CUE L 1 112 PDB 6CUE 6CUE 1 112 DBREF 6CUE M 1 111 PDB 6CUE 6CUE 1 111 DBREF 6CUE N 6 107 PDB 6CUE 6CUE 6 107 DBREF 6CUE Q 1 129 PDB 6CUE 6CUE 1 129 DBREF 6CUE R 1 107 PDB 6CUE 6CUE 1 107 DBREF 6CUE d 512 664 UNP Q2N0S7 Q2N0S7_9HIV1 509 661 DBREF 6CUE h 1 118 PDB 6CUE 6CUE 1 118 DBREF 6CUE l 1 112 PDB 6CUE 6CUE 1 112 DBREF 6CUE m 1 111 PDB 6CUE 6CUE 1 111 DBREF 6CUE n 6 107 PDB 6CUE 6CUE 6 107 DBREF 6CUE q 1 129 PDB 6CUE 6CUE 1 129 DBREF 6CUE r 1 107 PDB 6CUE 6CUE 1 107 SEQADV 6CUE CYS c 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 6CUE ASN c 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6CUE CYS c 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 6CUE CYS c 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6CUE CYS 2 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 6CUE ASN 2 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6CUE CYS 2 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 6CUE CYS 2 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6CUE CYS C 201 UNP Q2N0S6 ILE 200 CONFLICT SEQADV 6CUE ASN C 332 UNP Q2N0S6 THR 330 CONFLICT SEQADV 6CUE CYS C 433 UNP Q2N0S6 ALA 430 CONFLICT SEQADV 6CUE CYS C 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 6CUE CYS 1 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 6CUE CYS D 605 UNP Q2N0S7 THR 602 CONFLICT SEQADV 6CUE CYS d 605 UNP Q2N0S7 THR 602 CONFLICT 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 CYS 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 CYS 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 2 473 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 2 473 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 2 473 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 2 473 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 2 473 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 2 473 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 2 473 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 2 473 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 2 473 THR ASN ASN ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 2 473 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 2 473 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 2 473 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 2 473 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 2 473 ALA CYS THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 2 473 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 2 473 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 2 473 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 2 473 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 2 473 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 2 473 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 2 473 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 2 473 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 2 473 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 2 473 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 2 473 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 2 473 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 2 473 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 2 473 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 2 473 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 2 473 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 2 473 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN CYS MET TYR SEQRES 32 2 473 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 2 473 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 2 473 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 2 473 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 2 473 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 2 473 CYS LYS ARG ARG VAL 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 CYS 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 CYS 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 1 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 1 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 1 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 1 153 GLN GLN SER ASN LEU LEU ARG ALA ILE GLU ALA GLN GLN SEQRES 5 1 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 1 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 1 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 1 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 1 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 1 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 1 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 1 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 3 118 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 3 118 PRO GLY ALA SER VAL THR LEU SER CYS LYS ALA SER GLY SEQRES 3 3 118 TYR THR PHE THR ASP TYR GLU MET HIS TRP VAL LYS GLN SEQRES 4 3 118 THR PRO VAL HIS GLY LEU GLU TRP ILE GLY ALA ILE VAL SEQRES 5 3 118 PRO GLU THR GLY PHE THR ALA TYR THR GLN LYS PHE LYS SEQRES 6 3 118 GLY LYS ALA MET LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 3 118 ALA TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 3 118 ALA VAL TYR PHE CYS SER ARG LEU ARG LEU TYR TRP TYR SEQRES 9 3 118 PHE ASP VAL TRP GLY THR GLY THR THR VAL THR VAL SER SEQRES 10 3 118 SER SEQRES 1 4 112 GLY VAL LEU MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 4 112 ARG LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER SEQRES 3 4 112 GLN SER ILE VAL TYR SER ASN GLY ASN THR TYR LEU GLU SEQRES 4 4 112 TRP TYR LEU GLN ARG PRO GLY GLN SER PRO LYS LEU LEU SEQRES 5 4 112 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 4 112 ARG VAL SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 4 112 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 4 112 TYR CYS PHE GLN GLY SER HIS VAL PRO TYR THR PHE GLY SEQRES 9 4 112 GLY GLY THR LYS LEU GLU ILE LYS SEQRES 1 5 132 GLN VAL HIS LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 5 132 PRO SER GLU THR LEU SER LEU THR CYS ASN VAL SER GLY SEQRES 3 5 132 THR LEU VAL ARG ASP ASN TYR TRP SER TRP ILE ARG GLN SEQRES 4 5 132 PRO LEU GLY LYS GLN PRO GLU TRP ILE GLY TYR VAL HIS SEQRES 5 5 132 ASP SER GLY ASP THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 5 132 ARG VAL HIS LEU SER LEU ASP LYS SER LYS ASN LEU VAL SEQRES 7 5 132 SER LEU ARG LEU THR GLY VAL THR ALA ALA ASP SER ALA SEQRES 8 5 132 ILE TYR TYR CYS ALA THR THR LYS HIS GLY ARG ARG ILE SEQRES 9 5 132 TYR GLY VAL VAL ALA PHE LYS GLU TRP PHE THR TYR PHE SEQRES 10 5 132 TYR MET ASP VAL TRP GLY LYS GLY THR SER VAL THR VAL SEQRES 11 5 132 SER SER SEQRES 1 6 107 ALA PRO THR PHE VAL SER VAL ALA PRO GLY GLN THR ALA SEQRES 2 6 107 ARG ILE THR CYS GLY GLU GLU SER LEU GLY SER ARG SER SEQRES 3 6 107 VAL ILE TRP TYR GLN GLN ARG PRO GLY GLN ALA PRO SER SEQRES 4 6 107 LEU ILE ILE TYR ASN ASN ASN ASP ARG PRO SER GLY ILE SEQRES 5 6 107 PRO ASP ARG PHE SER GLY SER PRO GLY SER THR PHE GLY SEQRES 6 6 107 THR THR ALA THR LEU THR ILE THR SER VAL GLU ALA GLY SEQRES 7 6 107 ASP GLU ALA ASP TYR TYR CYS HIS ILE TRP ASP SER ARG SEQRES 8 6 107 ARG PRO THR ASN TRP VAL PHE GLY GLU GLY THR THR LEU SEQRES 9 6 107 ILE VAL LEU SEQRES 1 7 129 GLN VAL GLN LEU VAL GLN SER GLY ALA VAL ILE LYS THR SEQRES 2 7 129 PRO GLY SER SER VAL LYS ILE SER CYS ARG ALA SER GLY SEQRES 3 7 129 TYR ASN PHE ARG ASP TYR SER ILE HIS TRP VAL ARG LEU SEQRES 4 7 129 ILE PRO ASP LYS GLY PHE GLU TRP ILE GLY TRP ILE LYS SEQRES 5 7 129 PRO LEU TRP GLY ALA VAL SER TYR ALA ARG GLN LEU GLN SEQRES 6 7 129 GLY ARG VAL SER MET THR ARG GLN LEU SER GLN ASP PRO SEQRES 7 7 129 ASP ASP PRO ASP TRP GLY VAL ALA TYR MET GLU PHE SER SEQRES 8 7 129 GLY LEU THR PRO ALA ASP THR ALA GLU TYR PHE CYS VAL SEQRES 9 7 129 ARG ARG GLY SER CYS ASP TYR CYS GLY ASP PHE PRO TRP SEQRES 10 7 129 GLN TYR TRP CYS GLN GLY THR VAL VAL VAL VAL SER SEQRES 1 8 102 GLU ILE VAL LEU THR GLN SER PRO GLY ILE LEU SER LEU SEQRES 2 8 102 SER PRO GLY GLU THR ALA THR LEU PHE CYS LYS ALA SER SEQRES 3 8 102 GLN GLY GLY ASN ALA MET THR TRP TYR GLN LYS ARG ARG SEQRES 4 8 102 GLY GLN VAL PRO ARG LEU LEU ILE TYR ASP THR SER ARG SEQRES 5 8 102 ARG ALA SER GLY VAL PRO ASP ARG PHE VAL GLY SER GLY SEQRES 6 8 102 SER GLY THR ASP PHE PHE LEU THR ILE ASN LYS LEU ASP SEQRES 7 8 102 ARG GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN PHE GLU SEQRES 8 8 102 PHE PHE GLY LEU GLY SER GLU LEU GLU VAL HIS 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 118 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 H 118 PRO GLY ALA SER VAL THR LEU SER CYS LYS ALA SER GLY SEQRES 3 H 118 TYR THR PHE THR ASP TYR GLU MET HIS TRP VAL LYS GLN SEQRES 4 H 118 THR PRO VAL HIS GLY LEU GLU TRP ILE GLY ALA ILE VAL SEQRES 5 H 118 PRO GLU THR GLY PHE THR ALA TYR THR GLN LYS PHE LYS SEQRES 6 H 118 GLY LYS ALA MET LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 H 118 ALA TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 H 118 ALA VAL TYR PHE CYS SER ARG LEU ARG LEU TYR TRP TYR SEQRES 9 H 118 PHE ASP VAL TRP GLY THR GLY THR THR VAL THR VAL SER SEQRES 10 H 118 SER SEQRES 1 L 112 GLY VAL LEU MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 L 112 ARG LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER SEQRES 3 L 112 GLN SER ILE VAL TYR SER ASN GLY ASN THR TYR LEU GLU SEQRES 4 L 112 TRP TYR LEU GLN ARG PRO GLY GLN SER PRO LYS LEU LEU SEQRES 5 L 112 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 L 112 ARG VAL SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 L 112 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 L 112 TYR CYS PHE GLN GLY SER HIS VAL PRO TYR THR PHE GLY SEQRES 9 L 112 GLY GLY THR LYS LEU GLU ILE LYS 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 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 118 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL ARG SEQRES 2 h 118 PRO GLY ALA SER VAL THR LEU SER CYS LYS ALA SER GLY SEQRES 3 h 118 TYR THR PHE THR ASP TYR GLU MET HIS TRP VAL LYS GLN SEQRES 4 h 118 THR PRO VAL HIS GLY LEU GLU TRP ILE GLY ALA ILE VAL SEQRES 5 h 118 PRO GLU THR GLY PHE THR ALA TYR THR GLN LYS PHE LYS SEQRES 6 h 118 GLY LYS ALA MET LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 h 118 ALA TYR MET GLU LEU ARG SER LEU THR SER GLU ASP SER SEQRES 8 h 118 ALA VAL TYR PHE CYS SER ARG LEU ARG LEU TYR TRP TYR SEQRES 9 h 118 PHE ASP VAL TRP GLY THR GLY THR THR VAL THR VAL SER SEQRES 10 h 118 SER SEQRES 1 l 112 GLY VAL LEU MET THR GLN SER PRO LEU SER LEU PRO VAL SEQRES 2 l 112 ARG LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SER SEQRES 3 l 112 GLN SER ILE VAL TYR SER ASN GLY ASN THR TYR LEU GLU SEQRES 4 l 112 TRP TYR LEU GLN ARG PRO GLY GLN SER PRO LYS LEU LEU SEQRES 5 l 112 ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 l 112 ARG VAL SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 l 112 LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY VAL TYR SEQRES 8 l 112 TYR CYS PHE GLN GLY SER HIS VAL PRO TYR THR PHE GLY SEQRES 9 l 112 GLY GLY THR LYS LEU GLU ILE LYS 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 c 601 14 HET NAG c 602 14 HET NAG c 603 14 HET NAG c 604 14 HET BMA c 605 11 HET NAG c 606 14 HET NAG c 607 14 HET BMA c 608 11 HET NAG c 609 14 HET NAG c 610 14 HET NAG c 611 14 HET NAG c 612 14 HET NAG c 613 14 HET NAG c 614 14 HET NAG c 615 14 HET BMA c 616 11 HET MAN c 617 11 HET MAN c 618 11 HET NAG c 619 14 HET NAG c 620 14 HET NAG c 621 14 HET NAG c 622 14 HET NAG c 623 14 HET NAG c 624 14 HET BMA c 625 11 HET NAG c 626 14 HET NAG c 627 14 HET NAG c 628 14 HET NAG c 629 14 HET BMA c 630 11 HET MAN c 631 11 HET MAN c 632 11 HET NAG c 633 14 HET NAG c 634 14 HET NAG c 635 14 HET NAG c 636 14 HET BMA c 637 11 HET MAN c 638 11 HET NAG 2 601 14 HET NAG 2 602 14 HET NAG 2 603 14 HET NAG 2 604 14 HET BMA 2 605 11 HET NAG 2 606 14 HET NAG 2 607 14 HET BMA 2 608 11 HET NAG 2 609 14 HET NAG 2 610 14 HET NAG 2 611 14 HET NAG 2 612 14 HET NAG 2 613 14 HET NAG 2 614 14 HET NAG 2 615 14 HET BMA 2 616 11 HET MAN 2 617 11 HET MAN 2 618 11 HET NAG 2 619 14 HET NAG 2 620 14 HET NAG 2 621 14 HET NAG 2 622 14 HET NAG 2 623 14 HET NAG 2 624 14 HET BMA 2 625 11 HET NAG 2 626 14 HET NAG 2 627 14 HET NAG 2 628 14 HET NAG 2 629 14 HET BMA 2 630 11 HET MAN 2 631 11 HET MAN 2 632 11 HET NAG 2 633 14 HET NAG 2 634 14 HET NAG 2 635 14 HET NAG 2 636 14 HET BMA 2 637 11 HET MAN 2 638 11 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET BMA C 605 11 HET NAG C 606 14 HET NAG C 607 14 HET BMA C 608 11 HET NAG C 609 14 HET NAG C 610 14 HET NAG C 611 14 HET NAG C 612 14 HET NAG C 613 14 HET NAG C 614 14 HET NAG C 615 14 HET BMA C 616 11 HET MAN C 617 11 HET MAN C 618 11 HET NAG C 619 14 HET NAG C 620 14 HET NAG C 621 14 HET NAG C 622 14 HET NAG C 623 14 HET NAG C 624 14 HET BMA C 625 11 HET NAG C 626 14 HET NAG C 627 14 HET NAG C 628 14 HET NAG C 629 14 HET BMA C 630 11 HET MAN C 631 11 HET MAN C 632 11 HET NAG C 633 14 HET NAG C 634 14 HET NAG C 635 14 HET NAG C 636 14 HET BMA C 637 11 HET MAN C 638 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 25 NAG 81(C8 H15 N O6) FORMUL 26 BMA 18(C6 H12 O6) FORMUL 31 MAN 15(C6 H12 O6) HELIX 1 AA1 VAL c 101 SER c 115 1 15 HELIX 2 AA2 LEU c 122 CYS c 126 5 5 HELIX 3 AA3 ASN c 195 THR c 198 5 4 HELIX 4 AA4 LYS c 335 ARG c 350 1 16 HELIX 5 AA5 ASP c 368 THR c 373 1 6 HELIX 6 AA6 ASN c 425 ARG c 429 5 5 HELIX 7 AA7 MET c 475 SER c 481 1 7 HELIX 8 AA8 VAL 2 101 SER 2 115 1 15 HELIX 9 AA9 LEU 2 122 CYS 2 126 5 5 HELIX 10 AB1 ASN 2 195 THR 2 198 5 4 HELIX 11 AB2 LYS 2 335 ARG 2 350 1 16 HELIX 12 AB3 ASP 2 368 THR 2 373 1 6 HELIX 13 AB4 ASN 2 425 ARG 2 429 5 5 HELIX 14 AB5 MET 2 475 ARG 2 480 1 6 HELIX 15 AB6 GLN C 103 SER C 115 1 13 HELIX 16 AB7 LEU C 122 CYS C 126 5 5 HELIX 17 AB8 ASN C 195 THR C 198 5 4 HELIX 18 AB9 LYS C 335 ARG C 350 1 16 HELIX 19 AC1 ASP C 368 THR C 373 1 6 HELIX 20 AC2 ASN C 425 ARG C 429 5 5 HELIX 21 AC3 MET C 475 SER C 481 1 7 HELIX 22 AC4 LEU 1 523 SER 1 528 5 6 HELIX 23 AC5 THR 1 529 ASN 1 543 1 15 HELIX 24 AC6 VAL 1 570 ILE 1 595 1 26 HELIX 25 AC7 ASN 1 611 ASN 1 616 1 6 HELIX 26 AC8 LEU 1 619 TRP 1 623 5 5 HELIX 27 AC9 THR 1 627 ILE 1 635 1 9 HELIX 28 AD1 GLN 1 640 ASP 1 664 1 25 HELIX 29 AD2 THR 3 87 SER 3 91 5 5 HELIX 30 AD3 GLU 4 84 LEU 4 88 5 5 HELIX 31 AD4 THR 5 83 SER 5 87 5 5 HELIX 32 AD5 VAL 5 100D LYS 5 100H 5 5 HELIX 33 AD6 ARG 7 62 GLN 7 65 5 4 HELIX 34 AD7 THR 7 94 THR 7 98 5 5 HELIX 35 AD8 LEU D 523 GLY D 527 5 5 HELIX 36 AD9 THR D 529 SER D 534 1 6 HELIX 37 AE1 THR D 536 ASN D 543 1 8 HELIX 38 AE2 VAL D 570 ILE D 595 1 26 HELIX 39 AE3 ASN D 611 ASN D 616 1 6 HELIX 40 AE4 SER D 620 ASN D 625 1 6 HELIX 41 AE5 THR D 627 ILE D 635 1 9 HELIX 42 AE6 GLN D 640 ASP D 664 1 25 HELIX 43 AE7 THR H 87 SER H 91 5 5 HELIX 44 AE8 THR M 83 SER M 87 5 5 HELIX 45 AE9 VAL M 100D LYS M 100H 5 5 HELIX 46 AF1 ARG Q 62 GLN Q 65 5 4 HELIX 47 AF2 THR Q 94 THR Q 98 5 5 HELIX 48 AF3 ILE d 515 LEU d 520 1 6 HELIX 49 AF4 LEU d 523 SER d 528 5 6 HELIX 50 AF5 THR d 529 SER d 534 1 6 HELIX 51 AF6 THR d 536 LEU d 544 1 9 HELIX 52 AF7 VAL d 570 ILE d 595 1 26 HELIX 53 AF8 ASN d 611 ASN d 616 1 6 HELIX 54 AF9 SER d 620 ASN d 625 1 6 HELIX 55 AG1 THR d 627 ILE d 635 1 9 HELIX 56 AG2 GLN d 640 LEU d 663 1 24 HELIX 57 AG3 THR h 87 SER h 91 5 5 HELIX 58 AG4 GLU l 84 LEU l 88 5 5 HELIX 59 AG5 THR m 83 SER m 87 5 5 HELIX 60 AG6 ARG q 62 GLN q 65 5 4 HELIX 61 AG7 THR q 94 THR q 98 5 5 SHEET 1 AA1 2 TRP c 35 THR c 37 0 SHEET 2 AA1 2 ALA c 497 THR c 499 -1 O THR c 499 N TRP c 35 SHEET 1 AA2 4 TRP c 45 ASP c 47 0 SHEET 2 AA2 4 TYR c 486 ILE c 491 -1 O LYS c 490 N LYS c 46 SHEET 3 AA2 4 PHE c 223 CYS c 228 -1 N ALA c 224 O VAL c 489 SHEET 4 AA2 4 VAL c 242 VAL c 245 -1 O VAL c 245 N ILE c 225 SHEET 1 AA3 3 VAL c 75 PRO c 76 0 SHEET 2 AA3 3 PHE c 53 SER c 56 1 N SER c 56 O VAL c 75 SHEET 3 AA3 3 HIS c 216 CYS c 218 -1 O CYS c 218 N PHE c 53 SHEET 1 AA4 2 GLU c 91 ASN c 94 0 SHEET 2 AA4 2 THR c 236 CYS c 239 -1 O CYS c 239 N GLU c 91 SHEET 1 AA5 5 LYS c 169 TYR c 177 0 SHEET 2 AA5 5 LEU c 154 THR c 162 -1 N MET c 161 O GLN c 170 SHEET 3 AA5 5 LEU c 129 ASN c 133 -1 N GLN c 130 O SER c 158 SHEET 4 AA5 5 GLU c 190 LEU c 193 -1 O TYR c 191 N LEU c 129 SHEET 5 AA5 5 VAL c 181 GLN c 183 -1 N VAL c 182 O ARG c 192 SHEET 1 AA6 6 MET c 271 ARG c 273 0 SHEET 2 AA6 6 ILE c 284 ARG c 298 -1 O GLN c 287 N MET c 271 SHEET 3 AA6 6 HIS c 330 SER c 334 -1 O ASN c 332 N ASN c 295 SHEET 4 AA6 6 SER c 413 ARG c 419 -1 O ILE c 414 N VAL c 333 SHEET 5 AA6 6 PHE c 382 CYS c 385 -1 N TYR c 384 O ARG c 419 SHEET 6 AA6 6 HIS c 374 ASN c 377 -1 N PHE c 376 O PHE c 383 SHEET 1 AA7 4 MET c 271 ARG c 273 0 SHEET 2 AA7 4 ILE c 284 ARG c 298 -1 O GLN c 287 N MET c 271 SHEET 3 AA7 4 ILE c 443 ARG c 456 -1 O ILE c 449 N VAL c 292 SHEET 4 AA7 4 PHE c 468 PRO c 470 -1 O ARG c 469 N THR c 455 SHEET 1 AA8 2 ARG c 304 ARG c 308 0 SHEET 2 AA8 2 ALA c 316 THR c 320 -1 O PHE c 317 N ILE c 307 SHEET 1 AA9 2 ILE c 359 ARG c 360 0 SHEET 2 AA9 2 THR c 394 TRP c 395 -1 O TRP c 395 N ILE c 359 SHEET 1 AB1 2 ILE c 423 ILE c 424 0 SHEET 2 AB1 2 MET c 434 TYR c 435 -1 O MET c 434 N ILE c 424 SHEET 1 AB2 3 GLY 2 495 THR 2 499 0 SHEET 2 AB2 3 TRP 2 35 TYR 2 39 -1 N TRP 2 35 O THR 2 499 SHEET 3 AB2 3 ILE 1 603 PRO 1 609 -1 O THR 1 606 N VAL 2 36 SHEET 1 AB3 4 TRP 2 45 ASP 2 47 0 SHEET 2 AB3 4 TYR 2 486 ILE 2 491 -1 O LYS 2 490 N LYS 2 46 SHEET 3 AB3 4 PHE 2 223 CYS 2 228 -1 N ALA 2 224 O VAL 2 489 SHEET 4 AB3 4 VAL 2 242 VAL 2 245 -1 O SER 2 243 N LYS 2 227 SHEET 1 AB4 3 VAL 2 75 PRO 2 76 0 SHEET 2 AB4 3 PHE 2 53 SER 2 56 1 N SER 2 56 O VAL 2 75 SHEET 3 AB4 3 HIS 2 216 CYS 2 218 -1 O HIS 2 216 N ALA 2 55 SHEET 1 AB5 2 GLU 2 91 ASN 2 94 0 SHEET 2 AB5 2 THR 2 236 CYS 2 239 -1 O CYS 2 239 N GLU 2 91 SHEET 1 AB6 5 LYS 2 169 TYR 2 177 0 SHEET 2 AB6 5 LEU 2 154 THR 2 162 -1 N MET 2 161 O GLN 2 170 SHEET 3 AB6 5 LEU 2 129 ASN 2 133 -1 N GLN 2 130 O SER 2 158 SHEET 4 AB6 5 GLU 2 190 LEU 2 193 -1 O TYR 2 191 N LEU 2 129 SHEET 5 AB6 5 VAL 2 181 GLN 2 183 -1 N VAL 2 182 O ARG 2 192 SHEET 1 AB7 3 THR 2 202 GLN 2 203 0 SHEET 2 AB7 3 MET 2 434 TYR 2 435 1 O TYR 2 435 N THR 2 202 SHEET 3 AB7 3 ILE 2 423 ILE 2 424 -1 N ILE 2 424 O MET 2 434 SHEET 1 AB8 7 LEU 2 260 LEU 2 261 0 SHEET 2 AB8 7 ILE 2 443 ARG 2 456 -1 O THR 2 450 N LEU 2 260 SHEET 3 AB8 7 ILE 2 284 ARG 2 298 -1 N VAL 2 292 O ILE 2 449 SHEET 4 AB8 7 HIS 2 330 SER 2 334 -1 O ASN 2 332 N ASN 2 295 SHEET 5 AB8 7 SER 2 413 ARG 2 419 -1 O ILE 2 414 N VAL 2 333 SHEET 6 AB8 7 PHE 2 382 CYS 2 385 -1 N TYR 2 384 O ARG 2 419 SHEET 7 AB8 7 HIS 2 374 ASN 2 377 -1 N PHE 2 376 O PHE 2 383 SHEET 1 AB9 4 MET 2 271 ARG 2 273 0 SHEET 2 AB9 4 ILE 2 284 ARG 2 298 -1 O GLN 2 287 N MET 2 271 SHEET 3 AB9 4 ILE 2 443 ARG 2 456 -1 O ILE 2 449 N VAL 2 292 SHEET 4 AB9 4 PHE 2 468 PRO 2 470 -1 O ARG 2 469 N THR 2 455 SHEET 1 AC1 2 ARG 2 304 ARG 2 308 0 SHEET 2 AC1 2 ALA 2 316 THR 2 320 -1 O PHE 2 317 N ILE 2 307 SHEET 1 AC2 2 ILE 2 359 PHE 2 361 0 SHEET 2 AC2 2 SER 2 393 TRP 2 395 -1 O TRP 2 395 N ILE 2 359 SHEET 1 AC3 2 TRP C 35 THR C 37 0 SHEET 2 AC3 2 ALA C 497 THR C 499 -1 O THR C 499 N TRP C 35 SHEET 1 AC4 4 TRP C 45 ASP C 47 0 SHEET 2 AC4 4 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AC4 4 PHE C 223 CYS C 228 -1 N ALA C 224 O VAL C 489 SHEET 4 AC4 4 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 1 AC5 3 VAL C 75 PRO C 76 0 SHEET 2 AC5 3 PHE C 53 SER C 56 1 N SER C 56 O VAL C 75 SHEET 3 AC5 3 HIS C 216 CYS C 218 -1 O HIS C 216 N ALA C 55 SHEET 1 AC6 2 GLU C 91 PHE C 93 0 SHEET 2 AC6 2 GLY C 237 CYS C 239 -1 O CYS C 239 N GLU C 91 SHEET 1 AC7 5 LYS C 169 TYR C 177 0 SHEET 2 AC7 5 LEU C 154 THR C 162 -1 N MET C 161 O GLN C 170 SHEET 3 AC7 5 LEU C 129 ASN C 133 -1 N GLN C 130 O SER C 158 SHEET 4 AC7 5 GLU C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AC7 5 VAL C 181 GLN C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AC8 3 THR C 202 GLN C 203 0 SHEET 2 AC8 3 MET C 434 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AC8 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AC9 7 LEU C 260 LEU C 261 0 SHEET 2 AC9 7 ILE C 443 ARG C 456 -1 O THR C 450 N LEU C 260 SHEET 3 AC9 7 ILE C 284 ARG C 298 -1 N ARG C 298 O ILE C 443 SHEET 4 AC9 7 HIS C 330 SER C 334 -1 O HIS C 330 N THR C 297 SHEET 5 AC9 7 SER C 413 ILE C 420 -1 O ILE C 414 N VAL C 333 SHEET 6 AC9 7 PHE C 382 CYS C 385 -1 N TYR C 384 O ARG C 419 SHEET 7 AC9 7 HIS C 374 ASN C 377 -1 N PHE C 376 O PHE C 383 SHEET 1 AD1 4 MET C 271 ARG C 273 0 SHEET 2 AD1 4 ILE C 284 ARG C 298 -1 O GLN C 287 N MET C 271 SHEET 3 AD1 4 ILE C 443 ARG C 456 -1 O ILE C 443 N ARG C 298 SHEET 4 AD1 4 PHE C 468 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 1 AD2 2 ARG C 304 ILE C 307 0 SHEET 2 AD2 2 PHE C 317 THR C 320 -1 O PHE C 317 N ILE C 307 SHEET 1 AD3 2 ILE C 359 PHE C 361 0 SHEET 2 AD3 2 SER C 393 TRP C 395 -1 O TRP C 395 N ILE C 359 SHEET 1 AD4 4 GLN 3 3 GLN 3 5 0 SHEET 2 AD4 4 SER 3 17 SER 3 25 -1 O LYS 3 23 N GLN 3 5 SHEET 3 AD4 4 THR 3 78 ARG 3 84 -1 O LEU 3 83 N VAL 3 18 SHEET 4 AD4 4 MET 3 69 ASP 3 73 -1 N MET 3 69 O GLU 3 82 SHEET 1 AD5 6 GLU 3 10 VAL 3 12 0 SHEET 2 AD5 6 THR 3 112 VAL 3 116 1 O THR 3 113 N GLU 3 10 SHEET 3 AD5 6 ALA 3 92 LEU 3 99 -1 N ALA 3 92 O VAL 3 114 SHEET 4 AD5 6 MET 3 34 THR 3 40 -1 N VAL 3 37 O PHE 3 95 SHEET 5 AD5 6 GLY 3 44 ILE 3 51 -1 O GLY 3 44 N THR 3 40 SHEET 6 AD5 6 THR 3 58 TYR 3 60 -1 O ALA 3 59 N ALA 3 50 SHEET 1 AD6 4 GLU 3 10 VAL 3 12 0 SHEET 2 AD6 4 THR 3 112 VAL 3 116 1 O THR 3 113 N GLU 3 10 SHEET 3 AD6 4 ALA 3 92 LEU 3 99 -1 N ALA 3 92 O VAL 3 114 SHEET 4 AD6 4 PHE 3 105 TRP 3 108 -1 O VAL 3 107 N ARG 3 98 SHEET 1 AD7 4 THR 4 5 SER 4 7 0 SHEET 2 AD7 4 ALA 4 19 ARG 4 24 -1 O SER 4 22 N SER 4 7 SHEET 3 AD7 4 ASP 4 75 ILE 4 80 -1 O LEU 4 78 N ILE 4 21 SHEET 4 AD7 4 VAL 4 67 SER 4 72 -1 N SER 4 68 O LYS 4 79 SHEET 1 AD8 4 SER 4 10 PRO 4 12 0 SHEET 2 AD8 4 THR 4 107 GLU 4 110 1 O GLU 4 110 N LEU 4 11 SHEET 3 AD8 4 GLY 4 89 GLN 4 95 -1 N TYR 4 91 O THR 4 107 SHEET 4 AD8 4 LEU 4 38 TYR 4 41 -1 N TYR 4 41 O TYR 4 92 SHEET 1 AD9 4 GLN 5 5 SER 5 7 0 SHEET 2 AD9 4 LEU 5 18 ASN 5 23 -1 O ASN 5 23 N GLN 5 5 SHEET 3 AD9 4 LEU 5 77 LEU 5 82 -1 O LEU 5 82 N LEU 5 18 SHEET 4 AD9 4 VAL 5 67 ASP 5 72 -1 N HIS 5 68 O ARG 5 81 SHEET 1 AE1 2 LEU 5 11 VAL 5 12 0 SHEET 2 AE1 2 THR 5 108 VAL 5 109 1 O THR 5 108 N VAL 5 12 SHEET 1 AE2 3 GLU 5 46 VAL 5 51 0 SHEET 2 AE2 3 TYR 5 33 GLN 5 39 -1 N ARG 5 38 O GLU 5 46 SHEET 3 AE2 3 ILE 5 89 THR 5 95 -1 O TYR 5 91 N ILE 5 37 SHEET 1 AE3 2 ARG 5 99 ILE 5 100A 0 SHEET 2 AE3 2 TRP 5 100J THR 5 100L-1 O PHE 5 100K N ARG 5 100 SHEET 1 AE4 3 THR 6 18 CYS 6 23 0 SHEET 2 AE4 3 ALA 6 71 THR 6 76 -1 O ILE 6 75 N ALA 6 19 SHEET 3 AE4 3 PHE 6 62 GLY 6 64 -1 N SER 6 63 O THR 6 74 SHEET 1 AE5 3 PRO 6 44 ILE 6 48 0 SHEET 2 AE5 3 VAL 6 33 GLN 6 38 -1 N GLN 6 37 O SER 6 45 SHEET 3 AE5 3 ASP 6 85 ILE 6 90 -1 O TYR 6 87 N TYR 6 36 SHEET 1 AE6 4 GLN 7 3 VAL 7 5 0 SHEET 2 AE6 4 SER 7 17 SER 7 25 -1 O ARG 7 23 N VAL 7 5 SHEET 3 AE6 4 GLY 7 84 SER 7 91 -1 O GLY 7 84 N ALA 7 24 SHEET 4 AE6 4 VAL 7 68 GLN 7 73 -1 N SER 7 69 O GLU 7 89 SHEET 1 AE7 6 VAL 7 10 LYS 7 12 0 SHEET 2 AE7 6 THR 7 124 VAL 7 128 1 O VAL 7 127 N VAL 7 10 SHEET 3 AE7 6 ALA 7 99 ARG 7 106 -1 N ALA 7 99 O VAL 7 126 SHEET 4 AE7 6 ILE 7 34 ILE 7 40 -1 N VAL 7 37 O PHE 7 102 SHEET 5 AE7 6 GLY 7 44 LYS 7 52 -1 O GLY 7 49 N TRP 7 36 SHEET 6 AE7 6 ALA 7 57 TYR 7 60 -1 O SER 7 59 N TRP 7 50 SHEET 1 AE8 4 VAL 7 10 LYS 7 12 0 SHEET 2 AE8 4 THR 7 124 VAL 7 128 1 O VAL 7 127 N VAL 7 10 SHEET 3 AE8 4 ALA 7 99 ARG 7 106 -1 N ALA 7 99 O VAL 7 126 SHEET 4 AE8 4 TRP 7 117 TRP 7 120 -1 O TYR 7 119 N ARG 7 105 SHEET 1 AE9 4 LEU 8 4 SER 8 7 0 SHEET 2 AE9 4 ALA 8 19 ALA 8 25 -1 O PHE 8 22 N SER 8 7 SHEET 3 AE9 4 ASP 8 70 ILE 8 75 -1 O LEU 8 73 N LEU 8 21 SHEET 4 AE9 4 PHE 8 62 SER 8 67 -1 N VAL 8 63 O THR 8 74 SHEET 1 AF1 2 ILE 8 10 LEU 8 13 0 SHEET 2 AF1 2 GLU 8 103 VAL 8 106 1 O GLU 8 103 N LEU 8 11 SHEET 1 AF2 5 ARG 8 53 ARG 8 54 0 SHEET 2 AF2 5 ARG 8 45 TYR 8 49 -1 N TYR 8 49 O ARG 8 53 SHEET 3 AF2 5 THR 8 34 LYS 8 38 -1 N TRP 8 35 O ILE 8 48 SHEET 4 AF2 5 VAL 8 85 GLN 8 90 -1 O TYR 8 87 N TYR 8 36 SHEET 5 AF2 5 PHE 8 97 PHE 8 98 -1 O PHE 8 97 N GLN 8 90 SHEET 1 AF3 2 GLN H 3 GLN H 5 0 SHEET 2 AF3 2 LYS H 23 SER H 25 -1 O LYS H 23 N GLN H 5 SHEET 1 AF4 6 GLU H 10 VAL H 12 0 SHEET 2 AF4 6 THR H 112 VAL H 116 1 O THR H 113 N GLU H 10 SHEET 3 AF4 6 ALA H 92 LEU H 99 -1 N TYR H 94 O THR H 112 SHEET 4 AF4 6 MET H 34 THR H 40 -1 N VAL H 37 O PHE H 95 SHEET 5 AF4 6 GLY H 44 VAL H 52 -1 O ILE H 51 N MET H 34 SHEET 6 AF4 6 PHE H 57 TYR H 60 -1 O ALA H 59 N ALA H 50 SHEET 1 AF5 4 GLU H 10 VAL H 12 0 SHEET 2 AF5 4 THR H 112 VAL H 116 1 O THR H 113 N GLU H 10 SHEET 3 AF5 4 ALA H 92 LEU H 99 -1 N TYR H 94 O THR H 112 SHEET 4 AF5 4 PHE H 105 TRP H 108 -1 O ASP H 106 N ARG H 98 SHEET 1 AF6 2 ALA H 72 ASP H 73 0 SHEET 2 AF6 2 THR H 78 ALA H 79 -1 N THR H 78 O ASP H 73 SHEET 1 AF7 4 THR L 5 SER L 7 0 SHEET 2 AF7 4 ALA L 19 ARG L 24 -1 O SER L 22 N SER L 7 SHEET 3 AF7 4 ASP L 75 ILE L 80 -1 O LEU L 78 N ILE L 21 SHEET 4 AF7 4 VAL L 67 SER L 72 -1 N SER L 68 O LYS L 79 SHEET 1 AF8 3 SER L 10 PRO L 12 0 SHEET 2 AF8 3 THR L 107 GLU L 110 1 O LYS L 108 N LEU L 11 SHEET 3 AF8 3 GLY L 89 TYR L 91 -1 N TYR L 91 O THR L 107 SHEET 1 AF9 2 GLU L 39 TYR L 41 0 SHEET 2 AF9 2 LEU L 51 TYR L 54 -1 O LEU L 52 N TRP L 40 SHEET 1 AG1 4 GLN M 5 SER M 7 0 SHEET 2 AG1 4 LEU M 18 ASN M 23 -1 O ASN M 23 N GLN M 5 SHEET 3 AG1 4 LEU M 77 LEU M 82 -1 O LEU M 82 N LEU M 18 SHEET 4 AG1 4 VAL M 67 ASP M 72 -1 N HIS M 68 O ARG M 81 SHEET 1 AG2 5 LEU M 11 VAL M 12 0 SHEET 2 AG2 5 SER M 106 VAL M 109 1 O THR M 108 N VAL M 12 SHEET 3 AG2 5 ALA M 88 THR M 95 -1 N ALA M 88 O VAL M 107 SHEET 4 AG2 5 TYR M 33 GLN M 39 -1 N ILE M 37 O TYR M 91 SHEET 5 AG2 5 GLU M 46 VAL M 51 -1 O GLU M 46 N ARG M 38 SHEET 1 AG3 2 ARG M 99 ILE M 100A 0 SHEET 2 AG3 2 TRP M 100J THR M 100L-1 O PHE M 100K N ARG M 100 SHEET 1 AG4 3 THR N 18 CYS N 23 0 SHEET 2 AG4 3 ALA N 71 THR N 76 -1 O ILE N 75 N ALA N 19 SHEET 3 AG4 3 PHE N 62 GLY N 64 -1 N SER N 63 O THR N 74 SHEET 1 AG5 4 PRO N 44 ILE N 48 0 SHEET 2 AG5 4 ARG N 31 GLN N 38 -1 N TRP N 35 O ILE N 47 SHEET 3 AG5 4 ASP N 85 ASP N 92 -1 O ASP N 85 N GLN N 38 SHEET 4 AG5 4 THR N 102 THR N 103 -1 O THR N 102 N TYR N 86 SHEET 1 AG6 4 GLN Q 3 VAL Q 5 0 SHEET 2 AG6 4 SER Q 17 SER Q 25 -1 O ARG Q 23 N VAL Q 5 SHEET 3 AG6 4 GLY Q 84 SER Q 91 -1 O GLY Q 84 N ALA Q 24 SHEET 4 AG6 4 VAL Q 68 GLN Q 73 -1 N SER Q 69 O GLU Q 89 SHEET 1 AG7 6 VAL Q 10 LYS Q 12 0 SHEET 2 AG7 6 THR Q 124 VAL Q 128 1 O VAL Q 127 N LYS Q 12 SHEET 3 AG7 6 ALA Q 99 ARG Q 106 -1 N ALA Q 99 O VAL Q 126 SHEET 4 AG7 6 ILE Q 34 ILE Q 40 -1 N LEU Q 39 O GLU Q 100 SHEET 5 AG7 6 GLY Q 44 LYS Q 52 -1 O GLU Q 46 N ARG Q 38 SHEET 6 AG7 6 ALA Q 57 TYR Q 60 -1 O SER Q 59 N TRP Q 50 SHEET 1 AG8 4 VAL Q 10 LYS Q 12 0 SHEET 2 AG8 4 THR Q 124 VAL Q 128 1 O VAL Q 127 N LYS Q 12 SHEET 3 AG8 4 ALA Q 99 ARG Q 106 -1 N ALA Q 99 O VAL Q 126 SHEET 4 AG8 4 TRP Q 117 TRP Q 120 -1 O GLN Q 118 N ARG Q 105 SHEET 1 AG9 4 LEU R 4 SER R 7 0 SHEET 2 AG9 4 ALA R 19 ALA R 25 -1 O PHE R 22 N SER R 7 SHEET 3 AG9 4 ASP R 70 ILE R 75 -1 O LEU R 73 N LEU R 21 SHEET 4 AG9 4 PHE R 62 SER R 67 -1 N VAL R 63 O THR R 74 SHEET 1 AH1 2 ILE R 10 SER R 12 0 SHEET 2 AH1 2 GLU R 103 GLU R 105 1 O GLU R 103 N LEU R 11 SHEET 1 AH2 5 ARG R 53 ARG R 54 0 SHEET 2 AH2 5 LEU R 46 TYR R 49 -1 N TYR R 49 O ARG R 53 SHEET 3 AH2 5 THR R 34 LYS R 38 -1 N TRP R 35 O ILE R 48 SHEET 4 AH2 5 VAL R 85 GLN R 90 -1 O VAL R 85 N LYS R 38 SHEET 5 AH2 5 PHE R 97 PHE R 98 -1 O PHE R 97 N GLN R 90 SHEET 1 AH3 2 GLN h 3 GLN h 5 0 SHEET 2 AH3 2 LYS h 23 SER h 25 -1 O LYS h 23 N GLN h 5 SHEET 1 AH4 6 GLU h 10 VAL h 12 0 SHEET 2 AH4 6 THR h 112 VAL h 116 1 O THR h 115 N GLU h 10 SHEET 3 AH4 6 ALA h 92 LEU h 99 -1 N TYR h 94 O THR h 112 SHEET 4 AH4 6 MET h 34 VAL h 37 -1 N VAL h 37 O PHE h 95 SHEET 5 AH4 6 GLY h 49 VAL h 52 -1 O ILE h 51 N MET h 34 SHEET 6 AH4 6 PHE h 57 ALA h 59 -1 O ALA h 59 N ALA h 50 SHEET 1 AH5 4 GLU h 10 VAL h 12 0 SHEET 2 AH5 4 THR h 112 VAL h 116 1 O THR h 115 N GLU h 10 SHEET 3 AH5 4 ALA h 92 LEU h 99 -1 N TYR h 94 O THR h 112 SHEET 4 AH5 4 PHE h 105 TRP h 108 -1 O VAL h 107 N ARG h 98 SHEET 1 AH6 2 GLN h 39 THR h 40 0 SHEET 2 AH6 2 GLY h 44 LEU h 45 -1 O GLY h 44 N THR h 40 SHEET 1 AH7 2 ALA h 72 ASP h 73 0 SHEET 2 AH7 2 THR h 78 ALA h 79 -1 O THR h 78 N ASP h 73 SHEET 1 AH8 4 THR l 5 SER l 7 0 SHEET 2 AH8 4 ALA l 19 ARG l 24 -1 O SER l 22 N SER l 7 SHEET 3 AH8 4 ASP l 75 ILE l 80 -1 O LEU l 78 N ILE l 21 SHEET 4 AH8 4 VAL l 67 SER l 72 -1 N SER l 68 O LYS l 79 SHEET 1 AH9 3 SER l 10 PRO l 12 0 SHEET 2 AH9 3 THR l 107 GLU l 110 1 O GLU l 110 N LEU l 11 SHEET 3 AH9 3 GLY l 89 TYR l 91 -1 N GLY l 89 O LEU l 109 SHEET 1 AI1 2 TRP l 40 TYR l 41 0 SHEET 2 AI1 2 LEU l 51 ILE l 53 -1 O LEU l 52 N TRP l 40 SHEET 1 AI2 4 GLN m 5 SER m 7 0 SHEET 2 AI2 4 LEU m 18 ASN m 23 -1 O THR m 21 N SER m 7 SHEET 3 AI2 4 LEU m 77 LEU m 82 -1 O LEU m 80 N LEU m 20 SHEET 4 AI2 4 SER m 70 ASP m 72 -1 N SER m 70 O SER m 79 SHEET 1 AI3 5 LEU m 11 VAL m 12 0 SHEET 2 AI3 5 THR m 105 VAL m 109 1 O THR m 108 N VAL m 12 SHEET 3 AI3 5 ALA m 88 THR m 95 -1 N TYR m 90 O THR m 105 SHEET 4 AI3 5 TYR m 33 GLN m 39 -1 N ILE m 37 O TYR m 91 SHEET 5 AI3 5 GLU m 46 VAL m 51 -1 O GLU m 46 N ARG m 38 SHEET 1 AI4 2 ARG m 99 ILE m 100A 0 SHEET 2 AI4 2 TRP m 100J THR m 100L-1 O PHE m 100K N ARG m 100 SHEET 1 AI5 5 VAL n 11 VAL n 13 0 SHEET 2 AI5 5 THR n 102 VAL n 106 1 O ILE n 105 N VAL n 13 SHEET 3 AI5 5 ALA n 84 HIS n 89 -1 N TYR n 86 O THR n 102 SHEET 4 AI5 5 ILE n 34 GLN n 38 -1 N TYR n 36 O TYR n 87 SHEET 5 AI5 5 PRO n 44 ILE n 48 -1 O ILE n 48 N TRP n 35 SHEET 1 AI6 3 THR n 18 CYS n 23 0 SHEET 2 AI6 3 ALA n 71 THR n 76 -1 O ILE n 75 N ALA n 19 SHEET 3 AI6 3 PHE n 62 GLY n 64 -1 N SER n 63 O THR n 74 SHEET 1 AI7 4 GLN q 3 VAL q 5 0 SHEET 2 AI7 4 SER q 17 SER q 25 -1 O ARG q 23 N VAL q 5 SHEET 3 AI7 4 GLY q 84 SER q 91 -1 O ALA q 86 N CYS q 22 SHEET 4 AI7 4 VAL q 68 GLN q 73 -1 N SER q 69 O GLU q 89 SHEET 1 AI8 6 VAL q 10 LYS q 12 0 SHEET 2 AI8 6 THR q 124 VAL q 128 1 O VAL q 127 N LYS q 12 SHEET 3 AI8 6 ALA q 99 ARG q 106 -1 N ALA q 99 O VAL q 126 SHEET 4 AI8 6 ILE q 34 ILE q 40 -1 N VAL q 37 O PHE q 102 SHEET 5 AI8 6 GLY q 44 LYS q 52 -1 O GLY q 49 N TRP q 36 SHEET 6 AI8 6 ALA q 57 TYR q 60 -1 O SER q 59 N TRP q 50 SHEET 1 AI9 4 VAL q 10 LYS q 12 0 SHEET 2 AI9 4 THR q 124 VAL q 128 1 O VAL q 127 N LYS q 12 SHEET 3 AI9 4 ALA q 99 ARG q 106 -1 N ALA q 99 O VAL q 126 SHEET 4 AI9 4 TRP q 117 TRP q 120 -1 O GLN q 118 N ARG q 105 SHEET 1 AJ1 4 LEU r 4 SER r 7 0 SHEET 2 AJ1 4 ALA r 19 ALA r 25 -1 O LYS r 24 N THR r 5 SHEET 3 AJ1 4 ASP r 70 ILE r 75 -1 O LEU r 73 N LEU r 21 SHEET 4 AJ1 4 PHE r 62 SER r 67 -1 N VAL r 63 O THR r 74 SHEET 1 AJ2 2 ILE r 10 LEU r 13 0 SHEET 2 AJ2 2 GLU r 103 VAL r 106 1 O GLU r 103 N LEU r 11 SHEET 1 AJ3 5 ARG r 53 ARG r 54 0 SHEET 2 AJ3 5 LEU r 46 TYR r 49 -1 N TYR r 49 O ARG r 53 SHEET 3 AJ3 5 THR r 34 LYS r 38 -1 N TRP r 35 O ILE r 48 SHEET 4 AJ3 5 VAL r 85 GLN r 90 -1 O TYR r 87 N TYR r 36 SHEET 5 AJ3 5 PHE r 97 PHE r 98 -1 O PHE r 97 N GLN r 90 SSBOND 1 CYS c 54 CYS c 74 1555 1555 2.03 SSBOND 2 CYS c 119 CYS c 205 1555 1555 2.03 SSBOND 3 CYS c 126 CYS c 196 1555 1555 2.03 SSBOND 4 CYS c 131 CYS c 157 1555 1555 2.03 SSBOND 5 CYS c 201 CYS c 433 1555 1555 2.03 SSBOND 6 CYS c 218 CYS c 247 1555 1555 2.03 SSBOND 7 CYS c 228 CYS c 239 1555 1555 2.03 SSBOND 8 CYS c 296 CYS c 331 1555 1555 2.03 SSBOND 9 CYS c 378 CYS c 445 1555 1555 2.02 SSBOND 10 CYS c 385 CYS c 418 1555 1555 2.03 SSBOND 11 CYS c 501 CYS d 605 1555 1555 2.04 SSBOND 12 CYS 2 54 CYS 2 74 1555 1555 2.03 SSBOND 13 CYS 2 119 CYS 2 205 1555 1555 2.03 SSBOND 14 CYS 2 126 CYS 2 196 1555 1555 2.03 SSBOND 15 CYS 2 131 CYS 2 157 1555 1555 2.03 SSBOND 16 CYS 2 201 CYS 2 433 1555 1555 2.03 SSBOND 17 CYS 2 218 CYS 2 247 1555 1555 2.03 SSBOND 18 CYS 2 228 CYS 2 239 1555 1555 2.03 SSBOND 19 CYS 2 296 CYS 2 331 1555 1555 2.03 SSBOND 20 CYS 2 378 CYS 2 445 1555 1555 2.02 SSBOND 21 CYS 2 385 CYS 2 418 1555 1555 2.03 SSBOND 22 CYS 2 501 CYS 1 605 1555 1555 2.04 SSBOND 23 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 24 CYS C 119 CYS C 205 1555 1555 2.03 SSBOND 25 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 26 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 27 CYS C 201 CYS C 433 1555 1555 2.03 SSBOND 28 CYS C 218 CYS C 247 1555 1555 2.03 SSBOND 29 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 30 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 31 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 32 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 33 CYS C 501 CYS D 605 1555 1555 2.10 SSBOND 34 CYS 1 598 CYS 1 604 1555 1555 1.92 SSBOND 35 CYS 3 22 CYS 3 96 1555 1555 2.03 SSBOND 36 CYS 4 23 CYS 4 93 1555 1555 2.03 SSBOND 37 CYS 5 22 CYS 5 92 1555 1555 2.03 SSBOND 38 CYS 6 23 CYS 6 88 1555 1555 2.04 SSBOND 39 CYS 7 22 CYS 7 103 1555 1555 2.03 SSBOND 40 CYS 7 109 CYS 7 112 1555 1555 2.00 SSBOND 41 CYS 8 23 CYS 8 88 1555 1555 2.04 SSBOND 42 CYS D 598 CYS D 604 1555 1555 1.94 SSBOND 43 CYS H 22 CYS H 96 1555 1555 2.03 SSBOND 44 CYS L 23 CYS L 93 1555 1555 2.03 SSBOND 45 CYS M 22 CYS M 92 1555 1555 2.03 SSBOND 46 CYS N 23 CYS N 88 1555 1555 2.04 SSBOND 47 CYS Q 22 CYS Q 103 1555 1555 2.03 SSBOND 48 CYS Q 109 CYS Q 112 1555 1555 2.00 SSBOND 49 CYS R 23 CYS R 88 1555 1555 2.04 SSBOND 50 CYS d 598 CYS d 604 1555 1555 2.00 SSBOND 51 CYS h 22 CYS h 96 1555 1555 2.03 SSBOND 52 CYS l 23 CYS l 93 1555 1555 2.03 SSBOND 53 CYS m 22 CYS m 92 1555 1555 2.03 SSBOND 54 CYS n 23 CYS n 88 1555 1555 2.03 SSBOND 55 CYS q 22 CYS q 103 1555 1555 2.03 SSBOND 56 CYS q 109 CYS q 112 1555 1555 1.98 SSBOND 57 CYS r 23 CYS r 88 1555 1555 2.05 LINK ND2 ASN c 133 C1 NAG c 601 1555 1555 1.44 LINK ND2 ASN c 137 C1 NAG c 603 1555 1555 1.44 LINK ND2 ASN c 156 C1 NAG c 606 1555 1555 1.43 LINK ND2 ASN c 160 C1 NAG c 609 1555 1555 1.47 LINK ND2 ASN c 197 C1 NAG c 611 1555 1555 1.43 LINK ND2 ASN c 234 C1 NAG c 612 1555 1555 1.44 LINK ND2 ASN c 262 C1 NAG c 614 1555 1555 1.44 LINK ND2 ASN c 276 C1 NAG c 635 1555 1555 1.43 LINK ND2 ASN c 295 C1 NAG c 619 1555 1555 1.43 LINK ND2 ASN c 301 C1 NAG c 621 1555 1555 1.44 LINK ND2 ASN c 332 C1 NAG c 628 1555 1555 1.43 LINK ND2 ASN c 363 C1 NAG c 623 1555 1555 1.37 LINK ND2 ASN c 386 C1 NAG c 626 1555 1555 1.40 LINK ND2 ASN c 448 C1 NAG c 633 1555 1555 1.44 LINK ND2 ASN 2 133 C1 NAG 2 601 1555 1555 1.43 LINK ND2 ASN 2 137 C1 NAG 2 603 1555 1555 1.45 LINK ND2 ASN 2 156 C1 NAG 2 606 1555 1555 1.43 LINK ND2 ASN 2 160 C1 NAG 2 609 1555 1555 1.46 LINK ND2 ASN 2 197 C1 NAG 2 611 1555 1555 1.43 LINK ND2 ASN 2 234 C1 NAG 2 612 1555 1555 1.44 LINK ND2 ASN 2 262 C1 NAG 2 614 1555 1555 1.44 LINK ND2 ASN 2 276 C1 NAG 2 635 1555 1555 1.43 LINK ND2 ASN 2 295 C1 NAG 2 619 1555 1555 1.44 LINK ND2 ASN 2 301 C1 NAG 2 621 1555 1555 1.44 LINK ND2 ASN 2 332 C1 NAG 2 628 1555 1555 1.43 LINK ND2 ASN 2 363 C1 NAG 2 623 1555 1555 1.35 LINK ND2 ASN 2 386 C1 NAG 2 626 1555 1555 1.42 LINK ND2 ASN 2 448 C1 NAG 2 633 1555 1555 1.43 LINK ND2 ASN C 133 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 137 C1 NAG C 603 1555 1555 1.45 LINK ND2 ASN C 156 C1 NAG C 606 1555 1555 1.43 LINK ND2 ASN C 160 C1 NAG C 609 1555 1555 1.47 LINK ND2 ASN C 197 C1 NAG C 611 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG C 612 1555 1555 1.44 LINK ND2 ASN C 262 C1 NAG C 614 1555 1555 1.43 LINK ND2 ASN C 276 C1 NAG C 635 1555 1555 1.43 LINK ND2 ASN C 295 C1 NAG C 619 1555 1555 1.43 LINK ND2 ASN C 301 C1 NAG C 621 1555 1555 1.43 LINK ND2 ASN C 332 C1 NAG C 628 1555 1555 1.43 LINK ND2 ASN C 363 C1 NAG C 623 1555 1555 1.38 LINK ND2 ASN C 386 C1 NAG C 626 1555 1555 1.43 LINK ND2 ASN C 448 C1 NAG C 633 1555 1555 1.43 LINK O4 NAG c 601 C1 NAG c 602 1555 1555 1.46 LINK O4 NAG c 603 C1 NAG c 604 1555 1555 1.44 LINK O4 NAG c 604 C1 BMA c 605 1555 1555 1.44 LINK O4 NAG c 606 C1 NAG c 607 1555 1555 1.44 LINK O4 NAG c 607 C1 BMA c 608 1555 1555 1.44 LINK O4 NAG c 609 C1 NAG c 610 1555 1555 1.45 LINK O4 NAG c 612 C1 NAG c 613 1555 1555 1.44 LINK O4 NAG c 614 C1 NAG c 615 1555 1555 1.45 LINK O4 NAG c 615 C1 BMA c 616 1555 1555 1.45 LINK O3 BMA c 616 C1 MAN c 617 1555 1555 1.44 LINK O6 BMA c 616 C1 MAN c 618 1555 1555 1.44 LINK O4 NAG c 619 C1 NAG c 620 1555 1555 1.45 LINK O4 NAG c 621 C1 NAG c 622 1555 1555 1.44 LINK O4 NAG c 623 C1 NAG c 624 1555 1555 1.44 LINK O4 NAG c 624 C1 BMA c 625 1555 1555 1.46 LINK O4 NAG c 626 C1 NAG c 627 1555 1555 1.45 LINK O4 NAG c 628 C1 NAG c 629 1555 1555 1.45 LINK O4 NAG c 629 C1 BMA c 630 1555 1555 1.44 LINK O3 BMA c 630 C1 MAN c 631 1555 1555 1.45 LINK O2 MAN c 631 C1 MAN c 632 1555 1555 1.44 LINK O4 NAG c 633 C1 NAG c 634 1555 1555 1.44 LINK O4 NAG c 635 C1 NAG c 636 1555 1555 1.42 LINK O4 NAG c 636 C1 BMA c 637 1555 1555 1.44 LINK O3 BMA c 637 C1 MAN c 638 1555 1555 1.45 LINK O4 NAG 2 601 C1 NAG 2 602 1555 1555 1.46 LINK O4 NAG 2 603 C1 NAG 2 604 1555 1555 1.45 LINK O4 NAG 2 604 C1 BMA 2 605 1555 1555 1.44 LINK O4 NAG 2 606 C1 NAG 2 607 1555 1555 1.44 LINK O4 NAG 2 607 C1 BMA 2 608 1555 1555 1.44 LINK O4 NAG 2 609 C1 NAG 2 610 1555 1555 1.45 LINK O4 NAG 2 612 C1 NAG 2 613 1555 1555 1.45 LINK O4 NAG 2 614 C1 NAG 2 615 1555 1555 1.45 LINK O4 NAG 2 615 C1 BMA 2 616 1555 1555 1.45 LINK O3 BMA 2 616 C1 MAN 2 617 1555 1555 1.44 LINK O6 BMA 2 616 C1 MAN 2 618 1555 1555 1.44 LINK O4 NAG 2 619 C1 NAG 2 620 1555 1555 1.45 LINK O4 NAG 2 621 C1 NAG 2 622 1555 1555 1.45 LINK O4 NAG 2 623 C1 NAG 2 624 1555 1555 1.44 LINK O4 NAG 2 624 C1 BMA 2 625 1555 1555 1.46 LINK O4 NAG 2 626 C1 NAG 2 627 1555 1555 1.44 LINK O4 NAG 2 628 C1 NAG 2 629 1555 1555 1.45 LINK O4 NAG 2 629 C1 BMA 2 630 1555 1555 1.44 LINK O3 BMA 2 630 C1 MAN 2 631 1555 1555 1.45 LINK O2 MAN 2 631 C1 MAN 2 632 1555 1555 1.44 LINK O4 NAG 2 633 C1 NAG 2 634 1555 1555 1.44 LINK O4 NAG 2 635 C1 NAG 2 636 1555 1555 1.42 LINK O4 NAG 2 636 C1 BMA 2 637 1555 1555 1.44 LINK O3 BMA 2 637 C1 MAN 2 638 1555 1555 1.45 LINK O4 NAG C 601 C1 NAG C 602 1555 1555 1.46 LINK O4 NAG C 603 C1 NAG C 604 1555 1555 1.44 LINK O4 NAG C 604 C1 BMA C 605 1555 1555 1.44 LINK O4 NAG C 606 C1 NAG C 607 1555 1555 1.45 LINK O4 NAG C 607 C1 BMA C 608 1555 1555 1.44 LINK O4 NAG C 609 C1 NAG C 610 1555 1555 1.45 LINK O4 NAG C 612 C1 NAG C 613 1555 1555 1.45 LINK O4 NAG C 614 C1 NAG C 615 1555 1555 1.45 LINK O4 NAG C 615 C1 BMA C 616 1555 1555 1.45 LINK O3 BMA C 616 C1 MAN C 617 1555 1555 1.45 LINK O6 BMA C 616 C1 MAN C 618 1555 1555 1.44 LINK O4 NAG C 619 C1 NAG C 620 1555 1555 1.45 LINK O4 NAG C 621 C1 NAG C 622 1555 1555 1.44 LINK O4 NAG C 623 C1 NAG C 624 1555 1555 1.44 LINK O4 NAG C 624 C1 BMA C 625 1555 1555 1.46 LINK O4 NAG C 626 C1 NAG C 627 1555 1555 1.45 LINK O4 NAG C 628 C1 NAG C 629 1555 1555 1.45 LINK O4 NAG C 629 C1 BMA C 630 1555 1555 1.44 LINK O3 BMA C 630 C1 MAN C 631 1555 1555 1.45 LINK O2 MAN C 631 C1 MAN C 632 1555 1555 1.44 LINK O4 NAG C 633 C1 NAG C 634 1555 1555 1.44 LINK O4 NAG C 635 C1 NAG C 636 1555 1555 1.43 LINK O4 NAG C 636 C1 BMA C 637 1555 1555 1.44 LINK O3 BMA C 637 C1 MAN C 638 1555 1555 1.45 CISPEP 1 SER 4 7 PRO 4 8 0 -9.42 CISPEP 2 VAL 4 99 PRO 4 100 0 -3.40 CISPEP 3 SER 8 7 PRO 8 8 0 0.09 CISPEP 4 SER L 7 PRO L 8 0 -7.98 CISPEP 5 VAL L 99 PRO L 100 0 -8.37 CISPEP 6 SER R 7 PRO R 8 0 2.55 CISPEP 7 SER l 7 PRO l 8 0 -5.60 CISPEP 8 VAL l 99 PRO l 100 0 -5.54 CISPEP 9 SER r 7 PRO r 8 0 0.53 SITE 1 AC1 2 ASN 2 133 ASP 2 140 SITE 1 AC2 4 ASN 2 137 ASN 5 58 THR 5 100L THR 6 95B SITE 1 AC3 3 ASN 2 156 TYR 2 173 ASP 2 321A SITE 1 AC4 3 ASN 2 160 LYS 2 169 LYS 2 171 SITE 1 AC5 2 ARG 2 192 ASN 2 197 SITE 1 AC6 3 ASN 2 234 SER 2 274 HIS 2 352 SITE 1 AC7 5 ASN 2 262 ASN 2 377 GLY 2 379 VAL 2 446 SITE 2 AC7 5 SER 2 447 SITE 1 AC8 4 ASN 2 276 TYR 7 111 SER 8 52 PHE 8 91 SITE 1 AC9 3 GLN 2 293 ASN 2 295 SER 2 334 SITE 1 AD1 1 ASN 2 301 SITE 1 AD2 9 HIS 2 330 ASN 2 332 ARG 5 100 GLY 5 100C SITE 2 AD2 9 SER 6 30 ASN 6 50 ASN 6 51 PRO 6 66 SITE 3 AD2 9 GLY 6 67 SITE 1 AD3 4 ASN 2 363 SER 2 364 NAG 2 626 NAG 2 627 SITE 1 AD4 3 ASN 2 386 SER 2 388 NAG 2 623 SITE 1 AD5 4 PRO 2 291 ASN 2 448 ARG 4 24 ASP 4 75 SITE 1 AD6 2 ASN C 133 ASP C 140 SITE 1 AD7 3 ASN C 137 THR M 100L THR N 95B SITE 1 AD8 3 ASN C 156 TYR C 173 ASP C 321A SITE 1 AD9 3 ASN C 160 LYS C 169 LYS C 171 SITE 1 AE1 2 ARG C 192 ASN C 197 SITE 1 AE2 3 ASN C 234 THR C 236 SER C 274 SITE 1 AE3 4 ASN C 262 ASN C 377 GLY C 379 SER C 447 SITE 1 AE4 4 ASN C 276 TYR Q 111 SER R 52 PHE R 91 SITE 1 AE5 2 GLN C 293 ASN C 295 SITE 1 AE6 1 ASN C 301 SITE 1 AE7 10 HIS C 330 ASN C 332 ARG M 100 GLY M 100C SITE 2 AE7 10 VAL M 100D SER N 30 ASN N 50 ASN N 51 SITE 3 AE7 10 PRO N 66 GLY N 67 SITE 1 AE8 4 ASN C 363 SER C 364 NAG C 626 NAG C 627 SITE 1 AE9 3 ASN C 386 SER C 388 NAG C 623 SITE 1 AF1 3 PRO C 291 ASN C 448 ASP L 75 SITE 1 AF2 2 ASN c 133 ASP c 140 SITE 1 AF3 5 ASN c 137 THR c 139 ASN m 58 THR m 100L SITE 2 AF3 5 THR n 95B SITE 1 AF4 4 THR c 135 ASN c 156 TYR c 173 ASP c 321A SITE 1 AF5 3 ASN c 160 LYS c 169 LYS c 171 SITE 1 AF6 2 ARG c 192 ASN c 197 SITE 1 AF7 2 ASN c 234 ILE c 277 SITE 1 AF8 5 ASN c 262 ASN c 377 GLY c 379 VAL c 446 SITE 2 AF8 5 SER c 447 SITE 1 AF9 4 ASN c 276 TYR q 111 SER r 52 PHE r 91 SITE 1 AG1 2 GLN c 293 ASN c 295 SITE 1 AG2 2 ASN c 301 ILE c 323 SITE 1 AG3 11 HIS c 330 ASN c 332 ARG m 100 ILE m 100A SITE 2 AG3 11 GLY m 100C VAL m 100D SER n 30 ASN n 50 SITE 3 AG3 11 ASN n 51 PRO n 66 GLY n 67 SITE 1 AG4 5 ASN c 363 SER c 364 SER c 388 NAG c 626 SITE 2 AG4 5 NAG c 627 SITE 1 AG5 3 ASN c 386 SER c 388 NAG c 623 SITE 1 AG6 5 PRO c 291 VAL c 446 ASN c 448 ARG l 24 SITE 2 AG6 5 ASP l 75 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.002376 0.000000 0.000000 0.00000 SCALE2 0.000000 0.002376 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002376 0.00000