HEADER VIRAL PROTEIN 02-MAR-22 7Z3A TITLE AMC009 SOSIPV5.2 IN COMPLEX WITH FABS ACS101 AND ACS124 COMPND MOL_ID: 1; COMPND 2 MOLECULE: AMC009 SOSIPV5.2 ENVELOPE GLYCOPROTEIN GP120; COMPND 3 CHAIN: A, C, D; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: AMC009 SOSIP.V5.2 ENVELOPE GLYCOPROTEIN GP41; COMPND 7 CHAIN: B, E, F; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ACS124 HEAVY CHAIN; COMPND 11 CHAIN: G, M; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 4; COMPND 14 MOLECULE: ACS124 LIGHT CHAIN; COMPND 15 CHAIN: I, O; COMPND 16 ENGINEERED: YES; COMPND 17 MOL_ID: 5; COMPND 18 MOLECULE: ACS101 HEAVY CHAIN; COMPND 19 CHAIN: H, J, K; COMPND 20 ENGINEERED: YES; COMPND 21 MOL_ID: 6; COMPND 22 MOLECULE: ACS101 LIGHT CHAIN; COMPND 23 CHAIN: L, N, P; COMPND 24 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 3 ORGANISM_TAXID: 11676; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 8 ORGANISM_TAXID: 11676; SOURCE 9 GENE: ENV; SOURCE 10 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 12 MOL_ID: 3; SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 4; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 23 MOL_ID: 5; SOURCE 24 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 28 MOL_ID: 6; SOURCE 29 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 30 ORGANISM_TAXID: 9606; SOURCE 31 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 32 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1, ANTIBODIES, CD4-BINDING SITE, GP41-GP120 INTERFACE, VIRAL KEYWDS 2 PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.VAN SCHOOTEN,A.WARD JRNL AUTH J.VAN SCHOOTEN,A.WARD JRNL TITL IDENTIFICATION OF IOMA-CLASS NEUTRALIZING ANTIBODIES JRNL TITL 2 TARGETING THE CD4-BINDING SITE ON THE HIV-1 ENVELOPE JRNL TITL 3 GLYCOPROTEIN JRNL REF TO BE PUBLISHED JRNL REFN JRNL DOI 10.1038/S41467-022-32208-0 REMARK 2 REMARK 2 RESOLUTION. 3.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LEGINON, 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 : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.950 REMARK 3 NUMBER OF PARTICLES : 95062 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 7Z3A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292121235. 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 : AMC009 SOSIPV5.2 IN COMPLEX REMARK 245 WITH FABS ACS101 AND ACS124; REMARK 245 AMC009 SOSIPV5.2 IN COMPLEX REMARK 245 WITH FABS ACS101 AND ACS124; REMARK 245 AMC009 SOSIPV5.2 IN COMPLEX REMARK 245 WITH FABS ACS101 AND ACS124 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TALOS ARCTICA REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1700.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 49.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 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: HEXADECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, D, F, G, I, H, L, REMARK 350 AND CHAINS: M, O, J, N, K, P, Q, R, S, REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, a, b, c, REMARK 350 AND CHAINS: d, e, f, g, h, i, j, k, l, REMARK 350 AND CHAINS: m, n, o, p, q, r, s, t, u, v, REMARK 350 AND CHAINS: w, x, y, z, 0, 1, 2, 3, 4, REMARK 350 AND CHAINS: 5, 6, 7, 8, 9, AA REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA A 29 REMARK 465 ARG A 30 REMARK 465 ALA A 31 REMARK 465 ASP A 32 REMARK 465 LYS A 33 REMARK 465 LEU A 34 REMARK 465 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 ASP A 62 REMARK 465 THR A 63 REMARK 465 GLU A 64 REMARK 465 VAL A 65 REMARK 465 VAL A 134A REMARK 465 GLY A 134B REMARK 465 ASN A 134C REMARK 465 ALA A 134D REMARK 465 THR A 134E REMARK 465 ASN A 134F REMARK 465 ALA A 134G REMARK 465 SER A 134H REMARK 465 THR A 134I REMARK 465 THR A 134J REMARK 465 ASN A 134K REMARK 465 ALA A 134L REMARK 465 THR A 134M REMARK 465 GLY A 134N REMARK 465 GLY A 134O REMARK 465 ILE A 134P REMARK 465 GLY A 134Q REMARK 465 GLY A 134R REMARK 465 THR A 134S REMARK 465 VAL A 134T REMARK 465 ASP A 184A REMARK 465 ASN A 184B REMARK 465 ASP A 184C REMARK 465 ASN A 184D REMARK 465 THR A 184E REMARK 465 THR A 403 REMARK 465 GLU A 404 REMARK 465 VAL A 405 REMARK 465 SER A 406 REMARK 465 ASN A 407 REMARK 465 TYR A 408 REMARK 465 ASN A 409 REMARK 465 ASP A 410 REMARK 465 ILE A 411 REMARK 465 THR A 412 REMARK 465 ARG A 503 REMARK 465 ARG A 504 REMARK 465 VAL A 505 REMARK 465 VAL A 506 REMARK 465 GLN A 507 REMARK 465 ALA B 511 REMARK 465 VAL B 512 REMARK 465 GLY B 513 REMARK 465 ALA B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 VAL B 518 REMARK 465 PHE B 519 REMARK 465 LEU B 520 REMARK 465 GLY B 521 REMARK 465 PHE B 522 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 ASN B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 CYS B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 MET B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 LEU B 568 REMARK 465 ALA C 29 REMARK 465 ARG C 30 REMARK 465 ALA C 31 REMARK 465 ASP C 32 REMARK 465 LYS C 33 REMARK 465 LEU C 34 REMARK 465 LYS C 59 REMARK 465 ALA C 60 REMARK 465 TYR C 61 REMARK 465 ASP C 62 REMARK 465 THR C 63 REMARK 465 GLU C 64 REMARK 465 VAL C 65 REMARK 465 VAL C 134A REMARK 465 GLY C 134B REMARK 465 ASN C 134C REMARK 465 ALA C 134D REMARK 465 THR C 134E REMARK 465 ASN C 134F REMARK 465 ALA C 134G REMARK 465 SER C 134H REMARK 465 THR C 134I REMARK 465 THR C 134J REMARK 465 ASN C 134K REMARK 465 ALA C 134L REMARK 465 THR C 134M REMARK 465 GLY C 134N REMARK 465 GLY C 134O REMARK 465 ILE C 134P REMARK 465 GLY C 134Q REMARK 465 GLY C 134R REMARK 465 THR C 134S REMARK 465 VAL C 134T REMARK 465 ASP C 184A REMARK 465 ASN C 184B REMARK 465 ASP C 184C REMARK 465 ASN C 184D REMARK 465 THR C 184E REMARK 465 THR C 403 REMARK 465 GLU C 404 REMARK 465 VAL C 405 REMARK 465 SER C 406 REMARK 465 ASN C 407 REMARK 465 TYR C 408 REMARK 465 ASN C 409 REMARK 465 ASP C 410 REMARK 465 ILE C 411 REMARK 465 THR C 412 REMARK 465 ARG C 503 REMARK 465 ARG C 504 REMARK 465 VAL C 505 REMARK 465 VAL C 506 REMARK 465 GLN C 507 REMARK 465 ALA E 511 REMARK 465 VAL E 512 REMARK 465 GLY E 513 REMARK 465 ALA E 514 REMARK 465 ILE E 515 REMARK 465 GLY E 516 REMARK 465 ALA E 517 REMARK 465 VAL E 518 REMARK 465 PHE E 519 REMARK 465 LEU E 520 REMARK 465 GLY E 521 REMARK 465 PHE E 522 REMARK 465 GLN E 551 REMARK 465 GLN E 552 REMARK 465 ASN 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 PRO E 559 REMARK 465 GLU E 560 REMARK 465 CYS E 561 REMARK 465 GLN E 562 REMARK 465 GLN E 563 REMARK 465 HIS E 564 REMARK 465 MET E 565 REMARK 465 LEU E 566 REMARK 465 LYS E 567 REMARK 465 LEU E 568 REMARK 465 GLU E 654 REMARK 465 LYS E 655 REMARK 465 ASN E 656 REMARK 465 GLU E 657 REMARK 465 GLN E 658 REMARK 465 GLU E 659 REMARK 465 LEU E 660 REMARK 465 LEU E 661 REMARK 465 GLU E 662 REMARK 465 LEU E 663 REMARK 465 ASP E 664 REMARK 465 ALA D 29 REMARK 465 ARG D 30 REMARK 465 ALA D 31 REMARK 465 ASP D 32 REMARK 465 LYS D 33 REMARK 465 LEU D 34 REMARK 465 LYS D 59 REMARK 465 ALA D 60 REMARK 465 TYR D 61 REMARK 465 ASP D 62 REMARK 465 THR D 63 REMARK 465 GLU D 64 REMARK 465 VAL D 65 REMARK 465 VAL D 134A REMARK 465 GLY D 134B REMARK 465 ASN D 134C REMARK 465 ALA D 134D REMARK 465 THR D 134E REMARK 465 ASN D 134F REMARK 465 ALA D 134G REMARK 465 SER D 134H REMARK 465 THR D 134I REMARK 465 THR D 134J REMARK 465 ASN D 134K REMARK 465 ALA D 134L REMARK 465 THR D 134M REMARK 465 GLY D 134N REMARK 465 GLY D 134O REMARK 465 ILE D 134P REMARK 465 GLY D 134Q REMARK 465 GLY D 134R REMARK 465 THR D 134S REMARK 465 VAL D 134T REMARK 465 ASP D 184A REMARK 465 ASN D 184B REMARK 465 ASP D 184C REMARK 465 ASN D 184D REMARK 465 THR D 184E REMARK 465 THR D 403 REMARK 465 GLU D 404 REMARK 465 VAL D 405 REMARK 465 SER D 406 REMARK 465 ASN D 407 REMARK 465 TYR D 408 REMARK 465 ASN D 409 REMARK 465 ASP D 410 REMARK 465 ILE D 411 REMARK 465 THR D 412 REMARK 465 ARG D 503 REMARK 465 ARG D 504 REMARK 465 VAL D 505 REMARK 465 VAL D 506 REMARK 465 GLN D 507 REMARK 465 ALA F 511 REMARK 465 VAL F 512 REMARK 465 GLY F 513 REMARK 465 ALA F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 REMARK 465 VAL F 518 REMARK 465 PHE F 519 REMARK 465 LEU F 520 REMARK 465 GLY F 521 REMARK 465 PHE F 522 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 ASN F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 CYS F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 MET F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 LEU F 568 REMARK 465 LYS F 655 REMARK 465 ASN F 656 REMARK 465 GLU F 657 REMARK 465 GLN F 658 REMARK 465 GLU F 659 REMARK 465 LEU F 660 REMARK 465 LEU F 661 REMARK 465 GLU F 662 REMARK 465 LEU F 663 REMARK 465 ASP F 664 REMARK 465 GLU G 1 REMARK 465 GLU H 1 REMARK 465 VAL L -1 REMARK 465 THR L 0 REMARK 465 GLU M 1 REMARK 465 GLU J 1 REMARK 465 VAL N -1 REMARK 465 THR N 0 REMARK 465 GLU K 1 REMARK 465 VAL P -1 REMARK 465 THR P 0 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 OD1 ASP K 101 CG2 VAL P 46 1.98 REMARK 500 NE1 TRP K 100H OD2 ASP K 101 2.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 TRP A 35 CH2 TRP A 35 CZ2 0.116 REMARK 500 TYR A 134 CG TYR A 134 CD2 0.102 REMARK 500 TYR A 134 CG TYR A 134 CD1 0.104 REMARK 500 TYR A 134 CE1 TYR A 134 CZ 0.093 REMARK 500 TYR A 134 CZ TYR A 134 CE2 0.094 REMARK 500 PHE A 376 CB PHE A 376 CG -0.149 REMARK 500 GLU A 466 CD GLU A 466 OE2 -0.067 REMARK 500 TRP B 596 CB TRP B 596 CG -0.115 REMARK 500 TYR C 134 CB TYR C 134 CG 0.091 REMARK 500 TYR C 134 CG TYR C 134 CD2 0.091 REMARK 500 TYR C 134 CG TYR C 134 CD1 0.103 REMARK 500 TYR C 134 CD1 TYR C 134 CE1 0.097 REMARK 500 TYR C 134 CE1 TYR C 134 CZ 0.100 REMARK 500 TYR C 134 CZ TYR C 134 CE2 0.090 REMARK 500 TYR C 217 CB TYR C 217 CG -0.091 REMARK 500 TYR C 384 CB TYR C 384 CG -0.099 REMARK 500 TYR D 134 CG TYR D 134 CD2 0.100 REMARK 500 TYR D 134 CG TYR D 134 CD1 0.092 REMARK 500 TYR D 134 CE1 TYR D 134 CZ 0.104 REMARK 500 TYR D 134 CZ TYR D 134 CE2 0.084 REMARK 500 GLU D 150 CB GLU D 150 CG 0.121 REMARK 500 TRP D 427 CB TRP D 427 CG -0.141 REMARK 500 TYR D 435 CG TYR D 435 CD1 -0.079 REMARK 500 TRP G 34 CZ3 TRP G 34 CH2 -0.100 REMARK 500 PHE G 53 CB PHE G 53 CG -0.137 REMARK 500 PHE G 78 CB PHE G 78 CG -0.103 REMARK 500 CYS G 92 CB CYS G 92 SG -0.178 REMARK 500 TYR I 48 CB TYR I 48 CG -0.119 REMARK 500 TYR I 86 CB TYR I 86 CG -0.090 REMARK 500 GLU H 6 CD GLU H 6 OE1 -0.069 REMARK 500 PHE L 49 CB PHE L 49 CG -0.137 REMARK 500 TRP M 34 CB TRP M 34 CG -0.116 REMARK 500 PHE M 53 CB PHE M 53 CG -0.141 REMARK 500 PHE M 78 CB PHE M 78 CG -0.152 REMARK 500 TRP M 103 NE1 TRP M 103 CE2 -0.078 REMARK 500 TYR O 48 CB TYR O 48 CG -0.172 REMARK 500 TYR J 59 CB TYR J 59 CG -0.112 REMARK 500 TRP J 100H CB TRP J 100H CG -0.108 REMARK 500 GLU N 3 CG GLU N 3 CD -0.103 REMARK 500 CYS N 88 CB CYS N 88 SG -0.105 REMARK 500 TYR K 79 CB TYR K 79 CG -0.094 REMARK 500 TYR K 99 CD1 TYR K 99 CE1 -0.094 REMARK 500 TRP K 100H CB TRP K 100H CG -0.112 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 TYR A 40 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES REMARK 500 TYR A 217 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 ARG A 273 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES REMARK 500 ARG A 456 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 ARG A 469 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES REMARK 500 ARG B 617 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 ARG C 166 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG C 166 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 TYR C 217 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES REMARK 500 PRO C 299 C - N - CA ANGL. DEV. = 9.2 DEGREES REMARK 500 ARG C 419 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 ARG D 273 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES REMARK 500 ARG D 304 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES REMARK 500 ARG G 100F NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 TYR I 48 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 ARG H 66 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES REMARK 500 PHE L 49 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES REMARK 500 TYR O 2 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES REMARK 500 ARG N 54 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 ARG K 97 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 ARG P 54 NE - CZ - NH2 ANGL. DEV. = -3.6 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 THR A 71 64.78 37.04 REMARK 500 THR A 198 -10.34 72.42 REMARK 500 THR A 257 -85.96 -114.85 REMARK 500 LYS A 354 74.82 53.04 REMARK 500 ASN A 356 -100.65 63.53 REMARK 500 LYS A 357 -140.56 45.23 REMARK 500 THR A 463B 57.21 36.38 REMARK 500 GLN B 543 -58.43 71.47 REMARK 500 VAL B 549 50.72 39.50 REMARK 500 TRP C 69 45.88 71.31 REMARK 500 THR C 132 -88.20 -123.27 REMARK 500 ARG C 151 -136.10 57.20 REMARK 500 ASP C 167 15.06 -143.57 REMARK 500 THR C 257 -88.52 -110.91 REMARK 500 LYS C 268 -53.68 68.80 REMARK 500 ASN C 276 114.28 -162.57 REMARK 500 LYS C 354 78.53 -69.10 REMARK 500 ASN C 356 40.83 39.81 REMARK 500 GLN C 363 -125.88 48.39 REMARK 500 TRP C 427 12.96 57.34 REMARK 500 ARG E 617 -115.31 54.45 REMARK 500 ASN E 625 -68.99 -143.16 REMARK 500 THR D 132 -91.37 -120.75 REMARK 500 ARG D 151 -132.13 54.64 REMARK 500 THR D 163 -76.15 -121.41 REMARK 500 SER D 164 -129.52 57.09 REMARK 500 THR D 198 -9.82 73.72 REMARK 500 GLN D 258 -60.29 79.38 REMARK 500 ASN D 276 119.73 -163.70 REMARK 500 ASN D 396 -146.90 -104.84 REMARK 500 ARG D 440 -0.39 76.99 REMARK 500 ASN F 625 -64.66 -129.23 REMARK 500 ASN F 651 -46.54 -135.27 REMARK 500 THR H 52A -20.16 75.46 REMARK 500 ARG H 97 -155.91 -125.40 REMARK 500 THR H 100G 6.45 81.32 REMARK 500 TRP H 100H -90.43 -115.98 REMARK 500 TYR L 2 -121.24 54.85 REMARK 500 THR L 23 55.58 34.07 REMARK 500 GLU L 50 -126.77 46.06 REMARK 500 SER L 67 116.33 -164.83 REMARK 500 ASN M 100C -37.80 64.79 REMARK 500 PHE M 100H 72.59 77.63 REMARK 500 THR J 52A -18.68 73.10 REMARK 500 ALA J 93 52.91 -143.03 REMARK 500 ARG J 94 -34.87 63.47 REMARK 500 THR J 100G -3.72 75.79 REMARK 500 TRP J 100H -90.70 -112.41 REMARK 500 CYS N 22 -18.67 -140.88 REMARK 500 THR N 23 56.94 27.15 REMARK 500 REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-14474 RELATED DB: EMDB REMARK 900 AMC009 SOSIPV5.2 IN COMPLEX WITH FABS ACS101 AND ACS124 DBREF 7Z3A A 29 507 PDB 7Z3A 7Z3A 29 507 DBREF 7Z3A B 511 664 PDB 7Z3A 7Z3A 511 664 DBREF 7Z3A C 29 507 PDB 7Z3A 7Z3A 29 507 DBREF 7Z3A E 511 664 PDB 7Z3A 7Z3A 511 664 DBREF 7Z3A D 29 507 PDB 7Z3A 7Z3A 29 507 DBREF 7Z3A F 511 664 PDB 7Z3A 7Z3A 511 664 DBREF 7Z3A G 1 113 PDB 7Z3A 7Z3A 1 113 DBREF 7Z3A I 1 108 PDB 7Z3A 7Z3A 1 108 DBREF 7Z3A H 1 113 PDB 7Z3A 7Z3A 1 113 DBREF 7Z3A L -1 106 PDB 7Z3A 7Z3A -1 106 DBREF 7Z3A M 1 113 PDB 7Z3A 7Z3A 1 113 DBREF 7Z3A O 1 108 PDB 7Z3A 7Z3A 1 108 DBREF 7Z3A J 1 113 PDB 7Z3A 7Z3A 1 113 DBREF 7Z3A N -1 106 PDB 7Z3A 7Z3A -1 106 DBREF 7Z3A K 1 113 PDB 7Z3A 7Z3A 1 113 DBREF 7Z3A P -1 106 PDB 7Z3A 7Z3A -1 106 SEQRES 1 A 482 ALA ARG ALA ASP LYS LEU TRP VAL THR VAL TYR TYR GLY SEQRES 2 A 482 VAL PRO VAL TRP LYS GLU ALA THR THR THR LEU PHE CYS SEQRES 3 A 482 ALA SER ASP ALA LYS ALA TYR ASP THR GLU VAL ARG ASN SEQRES 4 A 482 VAL TRP ALA THR HIS CYS CYS VAL PRO THR ASP PRO ASN SEQRES 5 A 482 PRO GLN GLU VAL VAL LEU GLU ASN VAL THR GLU ASN PHE SEQRES 6 A 482 ASN MET TRP LYS ASN ASP MET VAL GLU GLN MET HIS GLU SEQRES 7 A 482 ASP ILE ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS SEQRES 8 A 482 VAL LYS LEU THR PRO LEU CYS VAL THR LEU ASN CYS THR SEQRES 9 A 482 ASP TYR VAL GLY ASN ALA THR ASN ALA SER THR THR ASN SEQRES 10 A 482 ALA THR GLY GLY ILE GLY GLY THR VAL GLU ARG GLY GLU SEQRES 11 A 482 ILE LYS ASN CYS SER PHE ASN ILE THR THR SER ILE ARG SEQRES 12 A 482 ASP LYS VAL GLN LYS GLU TYR ALA LEU PHE TYR LYS LEU SEQRES 13 A 482 ASP ILE VAL PRO ILE ASP ASN ASP ASN THR ASN ASN SER SEQRES 14 A 482 TYR ARG LEU ILE ASN CYS ASN THR SER VAL ILE LYS GLN SEQRES 15 A 482 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 16 A 482 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS ASN SEQRES 17 A 482 ASP LYS LYS PHE ASN GLY THR GLY PRO CYS THR ASN VAL SEQRES 18 A 482 SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO VAL VAL SEQRES 19 A 482 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU LYS SEQRES 20 A 482 GLU VAL VAL ILE ARG SER GLN ASN PHE THR ASN ASN ALA SEQRES 21 A 482 LYS VAL ILE ILE VAL GLN LEU ASN GLU SER VAL VAL ILE SEQRES 22 A 482 ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SER ILE SEQRES 23 A 482 HIS ILE ALA PRO GLY ARG TRP PHE TYR THR THR GLY ALA SEQRES 24 A 482 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN ILE SER SEQRES 25 A 482 ARG VAL LYS TRP ASN ASN THR LEU LYS GLN ILE ALA THR SEQRES 26 A 482 LYS LEU ARG GLU GLN PHE LYS ASN LYS THR ILE ALA PHE SEQRES 27 A 482 ASN GLN SER SER GLY GLY ASP PRO GLU ILE VAL MET HIS SEQRES 28 A 482 SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SEQRES 29 A 482 THR GLN LEU PHE ASN SER THR TRP ASN ASP THR GLU VAL SEQRES 30 A 482 SER ASN TYR ASN ASP ILE THR HIS ILE THR LEU PRO CYS SEQRES 31 A 482 ARG ILE LYS GLN ILE ILE ASN MET TRP GLN LYS VAL GLY SEQRES 32 A 482 LYS ALA MET TYR ALA PRO PRO ILE ARG GLY GLN ILE ARG SEQRES 33 A 482 CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP SEQRES 34 A 482 GLY GLY SER ASN GLU ASN LYS THR SER GLU THR GLU THR SEQRES 35 A 482 PHE ARG PRO ALA GLY GLY ASP MET ARG ASP ASN TRP ARG SEQRES 36 A 482 SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO SEQRES 37 A 482 LEU GLY VAL ALA PRO THR LYS CYS LYS ARG ARG VAL VAL SEQRES 38 A 482 GLN SEQRES 1 B 154 ALA VAL GLY ALA ILE GLY ALA VAL PHE LEU GLY PHE LEU SEQRES 2 B 154 GLY ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR SEQRES 3 B 154 LEU THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL SEQRES 4 B 154 GLN GLN GLN ASN ASN LEU LEU ARG ALA PRO GLU CYS GLN SEQRES 5 B 154 GLN HIS MET LEU LYS LEU THR VAL TRP GLY ILE LYS GLN SEQRES 6 B 154 LEU GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG SEQRES 7 B 154 ASP GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS SEQRES 8 B 154 LEU ILE CYS CYS THR ALA VAL PRO TRP ASN ASN SER TRP SEQRES 9 B 154 SER ASN ARG SER LEU ASP MET ILE TRP ASN ASN MET THR SEQRES 10 B 154 TRP ILE GLU TRP GLU ARG GLU ILE ASP ASN TYR THR GLY SEQRES 11 B 154 LEU ILE TYR ASN LEU LEU GLU GLU SER GLN ASN GLN GLN SEQRES 12 B 154 GLU LYS ASN GLU GLN GLU LEU LEU GLU LEU ASP SEQRES 1 C 482 ALA ARG ALA ASP LYS LEU TRP VAL THR VAL TYR TYR GLY SEQRES 2 C 482 VAL PRO VAL TRP LYS GLU ALA THR THR THR LEU PHE CYS SEQRES 3 C 482 ALA SER ASP ALA LYS ALA TYR ASP THR GLU VAL ARG ASN SEQRES 4 C 482 VAL TRP ALA THR HIS CYS CYS VAL PRO THR ASP PRO ASN SEQRES 5 C 482 PRO GLN GLU VAL VAL LEU GLU ASN VAL THR GLU ASN PHE SEQRES 6 C 482 ASN MET TRP LYS ASN ASP MET VAL GLU GLN MET HIS GLU SEQRES 7 C 482 ASP ILE ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS SEQRES 8 C 482 VAL LYS LEU THR PRO LEU CYS VAL THR LEU ASN CYS THR SEQRES 9 C 482 ASP TYR VAL GLY ASN ALA THR ASN ALA SER THR THR ASN SEQRES 10 C 482 ALA THR GLY GLY ILE GLY GLY THR VAL GLU ARG GLY GLU SEQRES 11 C 482 ILE LYS ASN CYS SER PHE ASN ILE THR THR SER ILE ARG SEQRES 12 C 482 ASP LYS VAL GLN LYS GLU TYR ALA LEU PHE TYR LYS LEU SEQRES 13 C 482 ASP ILE VAL PRO ILE ASP ASN ASP ASN THR ASN ASN SER SEQRES 14 C 482 TYR ARG LEU ILE ASN CYS ASN THR SER VAL ILE LYS GLN SEQRES 15 C 482 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 16 C 482 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS ASN SEQRES 17 C 482 ASP LYS LYS PHE ASN GLY THR GLY PRO CYS THR ASN VAL SEQRES 18 C 482 SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO VAL VAL SEQRES 19 C 482 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU LYS SEQRES 20 C 482 GLU VAL VAL ILE ARG SER GLN ASN PHE THR ASN ASN ALA SEQRES 21 C 482 LYS VAL ILE ILE VAL GLN LEU ASN GLU SER VAL VAL ILE SEQRES 22 C 482 ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SER ILE SEQRES 23 C 482 HIS ILE ALA PRO GLY ARG TRP PHE TYR THR THR GLY ALA SEQRES 24 C 482 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN ILE SER SEQRES 25 C 482 ARG VAL LYS TRP ASN ASN THR LEU LYS GLN ILE ALA THR SEQRES 26 C 482 LYS LEU ARG GLU GLN PHE LYS ASN LYS THR ILE ALA PHE SEQRES 27 C 482 ASN GLN SER SER GLY GLY ASP PRO GLU ILE VAL MET HIS SEQRES 28 C 482 SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SEQRES 29 C 482 THR GLN LEU PHE ASN SER THR TRP ASN ASP THR GLU VAL SEQRES 30 C 482 SER ASN TYR ASN ASP ILE THR HIS ILE THR LEU PRO CYS SEQRES 31 C 482 ARG ILE LYS GLN ILE ILE ASN MET TRP GLN LYS VAL GLY SEQRES 32 C 482 LYS ALA MET TYR ALA PRO PRO ILE ARG GLY GLN ILE ARG SEQRES 33 C 482 CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP SEQRES 34 C 482 GLY GLY SER ASN GLU ASN LYS THR SER GLU THR GLU THR SEQRES 35 C 482 PHE ARG PRO ALA GLY GLY ASP MET ARG ASP ASN TRP ARG SEQRES 36 C 482 SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO SEQRES 37 C 482 LEU GLY VAL ALA PRO THR LYS CYS LYS ARG ARG VAL VAL SEQRES 38 C 482 GLN SEQRES 1 E 154 ALA VAL GLY ALA ILE GLY ALA VAL PHE LEU GLY PHE LEU SEQRES 2 E 154 GLY ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR SEQRES 3 E 154 LEU THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL SEQRES 4 E 154 GLN GLN GLN ASN ASN LEU LEU ARG ALA PRO GLU CYS GLN SEQRES 5 E 154 GLN HIS MET LEU LYS LEU THR VAL TRP GLY ILE LYS GLN SEQRES 6 E 154 LEU GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG SEQRES 7 E 154 ASP GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS SEQRES 8 E 154 LEU ILE CYS CYS THR ALA VAL PRO TRP ASN ASN SER TRP SEQRES 9 E 154 SER ASN ARG SER LEU ASP MET ILE TRP ASN ASN MET THR SEQRES 10 E 154 TRP ILE GLU TRP GLU ARG GLU ILE ASP ASN TYR THR GLY SEQRES 11 E 154 LEU ILE TYR ASN LEU LEU GLU GLU SER GLN ASN GLN GLN SEQRES 12 E 154 GLU LYS ASN GLU GLN GLU LEU LEU GLU LEU ASP SEQRES 1 D 482 ALA ARG ALA ASP LYS LEU TRP VAL THR VAL TYR TYR GLY SEQRES 2 D 482 VAL PRO VAL TRP LYS GLU ALA THR THR THR LEU PHE CYS SEQRES 3 D 482 ALA SER ASP ALA LYS ALA TYR ASP THR GLU VAL ARG ASN SEQRES 4 D 482 VAL TRP ALA THR HIS CYS CYS VAL PRO THR ASP PRO ASN SEQRES 5 D 482 PRO GLN GLU VAL VAL LEU GLU ASN VAL THR GLU ASN PHE SEQRES 6 D 482 ASN MET TRP LYS ASN ASP MET VAL GLU GLN MET HIS GLU SEQRES 7 D 482 ASP ILE ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS SEQRES 8 D 482 VAL LYS LEU THR PRO LEU CYS VAL THR LEU ASN CYS THR SEQRES 9 D 482 ASP TYR VAL GLY ASN ALA THR ASN ALA SER THR THR ASN SEQRES 10 D 482 ALA THR GLY GLY ILE GLY GLY THR VAL GLU ARG GLY GLU SEQRES 11 D 482 ILE LYS ASN CYS SER PHE ASN ILE THR THR SER ILE ARG SEQRES 12 D 482 ASP LYS VAL GLN LYS GLU TYR ALA LEU PHE TYR LYS LEU SEQRES 13 D 482 ASP ILE VAL PRO ILE ASP ASN ASP ASN THR ASN ASN SER SEQRES 14 D 482 TYR ARG LEU ILE ASN CYS ASN THR SER VAL ILE LYS GLN SEQRES 15 D 482 ALA CYS PRO LYS VAL SER PHE GLU PRO ILE PRO ILE HIS SEQRES 16 D 482 TYR CYS ALA PRO ALA GLY PHE ALA ILE LEU LYS CYS ASN SEQRES 17 D 482 ASP LYS LYS PHE ASN GLY THR GLY PRO CYS THR ASN VAL SEQRES 18 D 482 SER THR VAL GLN CYS THR HIS GLY ILE ARG PRO VAL VAL SEQRES 19 D 482 SER THR GLN LEU LEU LEU ASN GLY SER LEU ALA GLU LYS SEQRES 20 D 482 GLU VAL VAL ILE ARG SER GLN ASN PHE THR ASN ASN ALA SEQRES 21 D 482 LYS VAL ILE ILE VAL GLN LEU ASN GLU SER VAL VAL ILE SEQRES 22 D 482 ASN CYS THR ARG PRO ASN ASN ASN THR ARG LYS SER ILE SEQRES 23 D 482 HIS ILE ALA PRO GLY ARG TRP PHE TYR THR THR GLY ALA SEQRES 24 D 482 ILE ILE GLY ASP ILE ARG GLN ALA HIS CYS ASN ILE SER SEQRES 25 D 482 ARG VAL LYS TRP ASN ASN THR LEU LYS GLN ILE ALA THR SEQRES 26 D 482 LYS LEU ARG GLU GLN PHE LYS ASN LYS THR ILE ALA PHE SEQRES 27 D 482 ASN GLN SER SER GLY GLY ASP PRO GLU ILE VAL MET HIS SEQRES 28 D 482 SER PHE ASN CYS GLY GLY GLU PHE PHE TYR CYS ASN THR SEQRES 29 D 482 THR GLN LEU PHE ASN SER THR TRP ASN ASP THR GLU VAL SEQRES 30 D 482 SER ASN TYR ASN ASP ILE THR HIS ILE THR LEU PRO CYS SEQRES 31 D 482 ARG ILE LYS GLN ILE ILE ASN MET TRP GLN LYS VAL GLY SEQRES 32 D 482 LYS ALA MET TYR ALA PRO PRO ILE ARG GLY GLN ILE ARG SEQRES 33 D 482 CYS SER SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP SEQRES 34 D 482 GLY GLY SER ASN GLU ASN LYS THR SER GLU THR GLU THR SEQRES 35 D 482 PHE ARG PRO ALA GLY GLY ASP MET ARG ASP ASN TRP ARG SEQRES 36 D 482 SER GLU LEU TYR LYS TYR LYS VAL VAL LYS ILE GLU PRO SEQRES 37 D 482 LEU GLY VAL ALA PRO THR LYS CYS LYS ARG ARG VAL VAL SEQRES 38 D 482 GLN SEQRES 1 F 154 ALA VAL GLY ALA ILE GLY ALA VAL PHE LEU GLY PHE LEU SEQRES 2 F 154 GLY ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR SEQRES 3 F 154 LEU THR VAL GLN ALA ARG GLN LEU LEU SER GLY ILE VAL SEQRES 4 F 154 GLN GLN GLN ASN ASN LEU LEU ARG ALA PRO GLU CYS GLN SEQRES 5 F 154 GLN HIS MET LEU LYS LEU THR VAL TRP GLY ILE LYS GLN SEQRES 6 F 154 LEU GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG SEQRES 7 F 154 ASP GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS SEQRES 8 F 154 LEU ILE CYS CYS THR ALA VAL PRO TRP ASN ASN SER TRP SEQRES 9 F 154 SER ASN ARG SER LEU ASP MET ILE TRP ASN ASN MET THR SEQRES 10 F 154 TRP ILE GLU TRP GLU ARG GLU ILE ASP ASN TYR THR GLY SEQRES 11 F 154 LEU ILE TYR ASN LEU LEU GLU GLU SER GLN ASN GLN GLN SEQRES 12 F 154 GLU LYS ASN GLU GLN GLU LEU LEU GLU LEU ASP SEQRES 1 G 124 GLU VAL GLN LEU LEU GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 G 124 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 G 124 VAL PRO ILE SER ARG HIS TYR TRP ASN TRP ILE ARG GLN SEQRES 4 G 124 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE PHE SEQRES 5 G 124 PHE ASN GLY ASN ALA ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 G 124 ARG VAL THR ILE SER VAL ASP MET SER LYS ASN GLN PHE SEQRES 7 G 124 SER LEU THR LEU ARG SER VAL THR ALA ALA ASP THR ALA SEQRES 8 G 124 VAL TYR TYR CYS VAL ARG GLU LYS SER ILE ALA GLU GLU SEQRES 9 G 124 ASP ASN MET VAL ARG TRP PHE ASP PRO TRP GLY GLN GLY SEQRES 10 G 124 THR LEU VAL THR VAL SER SER SEQRES 1 I 108 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL ALA SEQRES 2 I 108 PRO GLY LYS THR ALA ARG ILE THR CYS GLY GLY ASN ASN SEQRES 3 I 108 LEU GLY THR LYS SER VAL HIS TRP TYR GLN GLN LYS PRO SEQRES 4 I 108 GLY GLN ALA PRO VAL ASN VAL ILE TYR TYR ASP SER ASP SEQRES 5 I 108 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER LYS SEQRES 6 I 108 SER GLY ASN THR ALA THR LEU THR ILE SER ARG VAL GLU SEQRES 7 I 108 ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN VAL TRP ASP SEQRES 8 I 108 SER SER ARG ASP GLN CYS VAL PHE GLY ILE GLY THR LYS SEQRES 9 I 108 VAL THR VAL LEU SEQRES 1 H 126 GLU VAL GLN LEU LEU GLU SER GLY ALA GLU VAL LYS LYS SEQRES 2 H 126 PRO GLY ALA SER VAL ARG VAL SER CYS GLU ALA SER GLY SEQRES 3 H 126 TYR THR PHE THR LYS TYR PHE ILE HIS TRP VAL ARG GLN SEQRES 4 H 126 ALA PRO GLY HIS GLY LEU GLU TRP ILE GLY TRP ILE ASN SEQRES 5 H 126 THR LEU THR SER GLY VAL ASN TYR ALA ARG ASN PHE GLN SEQRES 6 H 126 GLY ARG LEU THR LEU THR ARG ASP LEU SER THR GLU THR SEQRES 7 H 126 VAL TYR MET ASP LEU ARG ASN LEU LYS SER ASP ASP THR SEQRES 8 H 126 ALA VAL TYR TYR CYS ALA ARG GLY GLY ARG GLY TYR ASP SEQRES 9 H 126 GLU PRO TRP GLY ALA TYR THR TRP LEU ASP PRO TRP GLY SEQRES 10 H 126 GLN GLY SER LEU VAL THR VAL SER SER SEQRES 1 L 108 VAL THR SER TYR GLU LEU THR GLN PRO ALA SER VAL SER SEQRES 2 L 108 GLY SER PRO GLY GLN SER ILE THR ILE SER CYS THR GLY SEQRES 3 L 108 SER SER ILE GLY SER TYR ASP LEU VAL SER TRP TYR GLN SEQRES 4 L 108 GLN TYR PRO GLY LYS ALA PRO LYS VAL ILE ILE PHE GLU SEQRES 5 L 108 VAL SER LYS ARG PRO SER GLY VAL SER HIS ARG PHE SER SEQRES 6 L 108 GLY SER LYS SER GLY ASN THR ALA ALA LEU THR ILE SER SEQRES 7 L 108 GLY LEU GLN VAL GLU ASP GLU ALA ILE TYR HIS CYS TYR SEQRES 8 L 108 SER TYR ASP ASP MET ILE ILE PHE GLY GLY GLY THR ARG SEQRES 9 L 108 LEU THR VAL LEU SEQRES 1 M 124 GLU VAL GLN LEU LEU GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 M 124 PRO SER GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 M 124 VAL PRO ILE SER ARG HIS TYR TRP ASN TRP ILE ARG GLN SEQRES 4 M 124 SER PRO GLY LYS GLY LEU GLU TRP ILE GLY TYR ILE PHE SEQRES 5 M 124 PHE ASN GLY ASN ALA ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 M 124 ARG VAL THR ILE SER VAL ASP MET SER LYS ASN GLN PHE SEQRES 7 M 124 SER LEU THR LEU ARG SER VAL THR ALA ALA ASP THR ALA SEQRES 8 M 124 VAL TYR TYR CYS VAL ARG GLU LYS SER ILE ALA GLU GLU SEQRES 9 M 124 ASP ASN MET VAL ARG TRP PHE ASP PRO TRP GLY GLN GLY SEQRES 10 M 124 THR LEU VAL THR VAL SER SER SEQRES 1 O 108 SER TYR GLU LEU THR GLN PRO PRO SER VAL SER VAL ALA SEQRES 2 O 108 PRO GLY LYS THR ALA ARG ILE THR CYS GLY GLY ASN ASN SEQRES 3 O 108 LEU GLY THR LYS SER VAL HIS TRP TYR GLN GLN LYS PRO SEQRES 4 O 108 GLY GLN ALA PRO VAL ASN VAL ILE TYR TYR ASP SER ASP SEQRES 5 O 108 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER LYS SEQRES 6 O 108 SER GLY ASN THR ALA THR LEU THR ILE SER ARG VAL GLU SEQRES 7 O 108 ALA GLY ASP GLU ALA ASP TYR TYR CYS GLN VAL TRP ASP SEQRES 8 O 108 SER SER ARG ASP GLN CYS VAL PHE GLY ILE GLY THR LYS SEQRES 9 O 108 VAL THR VAL LEU SEQRES 1 J 126 GLU VAL GLN LEU LEU GLU SER GLY ALA GLU VAL LYS LYS SEQRES 2 J 126 PRO GLY ALA SER VAL ARG VAL SER CYS GLU ALA SER GLY SEQRES 3 J 126 TYR THR PHE THR LYS TYR PHE ILE HIS TRP VAL ARG GLN SEQRES 4 J 126 ALA PRO GLY HIS GLY LEU GLU TRP ILE GLY TRP ILE ASN SEQRES 5 J 126 THR LEU THR SER GLY VAL ASN TYR ALA ARG ASN PHE GLN SEQRES 6 J 126 GLY ARG LEU THR LEU THR ARG ASP LEU SER THR GLU THR SEQRES 7 J 126 VAL TYR MET ASP LEU ARG ASN LEU LYS SER ASP ASP THR SEQRES 8 J 126 ALA VAL TYR TYR CYS ALA ARG GLY GLY ARG GLY TYR ASP SEQRES 9 J 126 GLU PRO TRP GLY ALA TYR THR TRP LEU ASP PRO TRP GLY SEQRES 10 J 126 GLN GLY SER LEU VAL THR VAL SER SER SEQRES 1 N 108 VAL THR SER TYR GLU LEU THR GLN PRO ALA SER VAL SER SEQRES 2 N 108 GLY SER PRO GLY GLN SER ILE THR ILE SER CYS THR GLY SEQRES 3 N 108 SER SER ILE GLY SER TYR ASP LEU VAL SER TRP TYR GLN SEQRES 4 N 108 GLN TYR PRO GLY LYS ALA PRO LYS VAL ILE ILE PHE GLU SEQRES 5 N 108 VAL SER LYS ARG PRO SER GLY VAL SER HIS ARG PHE SER SEQRES 6 N 108 GLY SER LYS SER GLY ASN THR ALA ALA LEU THR ILE SER SEQRES 7 N 108 GLY LEU GLN VAL GLU ASP GLU ALA ILE TYR HIS CYS TYR SEQRES 8 N 108 SER TYR ASP ASP MET ILE ILE PHE GLY GLY GLY THR ARG SEQRES 9 N 108 LEU THR VAL LEU SEQRES 1 K 126 GLU VAL GLN LEU LEU GLU SER GLY ALA GLU VAL LYS LYS SEQRES 2 K 126 PRO GLY ALA SER VAL ARG VAL SER CYS GLU ALA SER GLY SEQRES 3 K 126 TYR THR PHE THR LYS TYR PHE ILE HIS TRP VAL ARG GLN SEQRES 4 K 126 ALA PRO GLY HIS GLY LEU GLU TRP ILE GLY TRP ILE ASN SEQRES 5 K 126 THR LEU THR SER GLY VAL ASN TYR ALA ARG ASN PHE GLN SEQRES 6 K 126 GLY ARG LEU THR LEU THR ARG ASP LEU SER THR GLU THR SEQRES 7 K 126 VAL TYR MET ASP LEU ARG ASN LEU LYS SER ASP ASP THR SEQRES 8 K 126 ALA VAL TYR TYR CYS ALA ARG GLY GLY ARG GLY TYR ASP SEQRES 9 K 126 GLU PRO TRP GLY ALA TYR THR TRP LEU ASP PRO TRP GLY SEQRES 10 K 126 GLN GLY SER LEU VAL THR VAL SER SER SEQRES 1 P 108 VAL THR SER TYR GLU LEU THR GLN PRO ALA SER VAL SER SEQRES 2 P 108 GLY SER PRO GLY GLN SER ILE THR ILE SER CYS THR GLY SEQRES 3 P 108 SER SER ILE GLY SER TYR ASP LEU VAL SER TRP TYR GLN SEQRES 4 P 108 GLN TYR PRO GLY LYS ALA PRO LYS VAL ILE ILE PHE GLU SEQRES 5 P 108 VAL SER LYS ARG PRO SER GLY VAL SER HIS ARG PHE SER SEQRES 6 P 108 GLY SER LYS SER GLY ASN THR ALA ALA LEU THR ILE SER SEQRES 7 P 108 GLY LEU GLN VAL GLU ASP GLU ALA ILE TYR HIS CYS TYR SEQRES 8 P 108 SER TYR ASP ASP MET ILE ILE PHE GLY GLY GLY THR ARG SEQRES 9 P 108 LEU THR VAL LEU HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG A 604 14 HET NAG A 605 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG E 701 14 HET NAG E 702 14 HET NAG D 601 14 HET NAG D 602 14 HET NAG D 603 14 HET NAG D 604 14 HET NAG D 605 14 HET NAG D 606 14 HET NAG F 701 14 HET NAG F 702 14 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG R 1 14 HET NAG R 2 14 HET BMA R 3 11 HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 11 HET MAN S 4 11 HET MAN S 5 11 HET NAG T 1 14 HET NAG T 2 14 HET BMA T 3 11 HET NAG U 1 14 HET NAG U 2 14 HET BMA U 3 11 HET NAG V 1 14 HET NAG V 2 14 HET BMA V 3 11 HET NAG W 1 14 HET NAG W 2 14 HET NAG X 1 14 HET NAG X 2 14 HET BMA X 3 11 HET NAG Y 1 14 HET NAG Y 2 14 HET BMA Y 3 11 HET NAG Z 1 14 HET NAG Z 2 14 HET BMA Z 3 11 HET NAG a 1 14 HET NAG a 2 14 HET BMA a 3 11 HET NAG b 1 14 HET NAG b 2 14 HET BMA b 3 11 HET NAG c 1 14 HET NAG c 2 14 HET BMA c 3 11 HET NAG d 1 14 HET NAG d 2 14 HET BMA d 3 11 HET NAG e 1 14 HET NAG e 2 14 HET BMA e 3 11 HET NAG f 1 14 HET NAG f 2 14 HET BMA f 3 11 HET NAG g 1 14 HET NAG g 2 14 HET NAG h 1 14 HET NAG h 2 14 HET BMA h 3 11 HET NAG i 1 14 HET NAG i 2 14 HET BMA i 3 11 HET NAG j 1 14 HET NAG j 2 14 HET BMA j 3 11 HET NAG k 1 14 HET NAG k 2 14 HET BMA k 3 11 HET NAG l 1 14 HET NAG l 2 14 HET NAG m 1 14 HET NAG m 2 14 HET BMA m 3 11 HET NAG n 1 14 HET NAG n 2 14 HET BMA n 3 11 HET NAG o 1 14 HET NAG o 2 14 HET BMA o 3 11 HET NAG p 1 14 HET NAG p 2 14 HET BMA p 3 11 HET NAG q 1 14 HET NAG q 2 14 HET BMA q 3 11 HET NAG r 1 14 HET NAG r 2 14 HET BMA r 3 11 HET NAG s 1 14 HET NAG s 2 14 HET NAG t 1 14 HET NAG t 2 14 HET BMA t 3 11 HET NAG u 1 14 HET NAG u 2 14 HET NAG v 1 14 HET NAG v 2 14 HET NAG w 1 14 HET NAG w 2 14 HET BMA w 3 11 HET NAG x 1 14 HET NAG x 2 14 HET BMA x 3 11 HET NAG y 1 14 HET NAG y 2 14 HET BMA y 3 11 HET MAN y 4 11 HET MAN y 5 11 HET NAG z 1 14 HET NAG z 2 14 HET BMA z 3 11 HET NAG 0 1 14 HET NAG 0 2 14 HET BMA 0 3 11 HET NAG 1 1 14 HET NAG 1 2 14 HET BMA 1 3 11 HET NAG 2 1 14 HET NAG 2 2 14 HET NAG 3 1 14 HET NAG 3 2 14 HET BMA 3 3 11 HET NAG 4 1 14 HET NAG 4 2 14 HET BMA 4 3 11 HET NAG 5 1 14 HET NAG 5 2 14 HET BMA 5 3 11 HET NAG 6 1 14 HET NAG 6 2 14 HET BMA 6 3 11 HET NAG 7 1 14 HET NAG 7 2 14 HET BMA 7 3 11 HET NAG 8 1 14 HET NAG 8 2 14 HET BMA 8 3 11 HET NAG 9 1 14 HET NAG 9 2 14 HET NAG AA 1 14 HET NAG AA 2 14 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 17 NAG 115(C8 H15 N O6) FORMUL 39 BMA 37(C6 H12 O6) FORMUL 40 MAN 4(C6 H12 O6) HELIX 1 AA1 ASN A 98 LYS A 117 1 20 HELIX 2 AA2 LEU A 122 CYS A 126 5 5 HELIX 3 AA3 SER A 334 PHE A 353 1 20 HELIX 4 AA4 ASP A 368 MET A 373 1 6 HELIX 5 AA5 TRP A 427 LYS A 429 5 3 HELIX 6 AA6 MET A 475 TYR A 484 1 10 HELIX 7 AA7 LEU B 523 SER B 528 5 6 HELIX 8 AA8 THR B 529 MET B 535 1 7 HELIX 9 AA9 THR B 536 ALA B 541 1 6 HELIX 10 AB1 VAL B 570 TRP B 596 1 27 HELIX 11 AB2 SER B 618 ASN B 624 1 7 HELIX 12 AB3 THR B 627 ILE B 635 1 9 HELIX 13 AB4 TYR B 638 ASN B 651 1 14 HELIX 14 AB5 ASN B 651 ASP B 664 1 14 HELIX 15 AB6 ALA C 70 CYS C 74 5 5 HELIX 16 AB7 ASN C 98 LYS C 117 1 20 HELIX 17 AB8 LEU C 122 CYS C 126 5 5 HELIX 18 AB9 SER C 334 PHE C 353 1 20 HELIX 19 AC1 ASP C 368 MET C 373 1 6 HELIX 20 AC2 THR C 387 LEU C 390 5 4 HELIX 21 AC3 ASN C 425 LYS C 429 5 5 HELIX 22 AC4 MET C 475 TYR C 484 1 10 HELIX 23 AC5 ALA E 532 GLN E 540 1 9 HELIX 24 AC6 VAL E 570 TRP E 596 1 27 HELIX 25 AC7 LEU E 619 ASN E 624 1 6 HELIX 26 AC8 THR E 627 ASP E 636 1 10 HELIX 27 AC9 TYR E 638 ASN E 651 1 14 HELIX 28 AD1 ASN D 98 LYS D 117 1 20 HELIX 29 AD2 LEU D 122 CYS D 126 5 5 HELIX 30 AD3 SER D 334 PHE D 353 1 20 HELIX 31 AD4 ASP D 368 MET D 373 1 6 HELIX 32 AD5 ASN D 425 LYS D 429 5 5 HELIX 33 AD6 ASP D 474 TYR D 484 1 11 HELIX 34 AD7 THR F 529 MET F 535 1 7 HELIX 35 AD8 THR F 536 ALA F 541 1 6 HELIX 36 AD9 VAL F 570 TRP F 596 1 27 HELIX 37 AE1 ASN F 611 SER F 615 5 5 HELIX 38 AE2 SER F 618 ASN F 625 1 8 HELIX 39 AE3 THR F 627 ILE F 635 1 9 HELIX 40 AE4 TYR F 638 GLN F 652 1 15 HELIX 41 AE5 PRO G 28 HIS G 32 5 5 HELIX 42 AE6 LEU G 63 SER G 65 5 3 HELIX 43 AE7 THR G 83 THR G 87 5 5 HELIX 44 AE8 ASN I 26 LYS I 30 5 5 HELIX 45 AE9 GLU I 78 GLU I 82 5 5 HELIX 46 AF1 THR H 28 TYR H 32 5 5 HELIX 47 AF2 ARG H 61 GLN H 64 5 4 HELIX 48 AF3 LEU H 73 THR H 75 5 3 HELIX 49 AF4 LYS H 83 THR H 87 5 5 HELIX 50 AF5 GLN L 79 GLU L 83 5 5 HELIX 51 AF6 PRO M 28 HIS M 32 5 5 HELIX 52 AF7 LEU M 63 SER M 65 5 3 HELIX 53 AF8 THR M 83 THR M 87 5 5 HELIX 54 AF9 ASN O 26 LYS O 30 5 5 HELIX 55 AG1 GLU O 78 GLU O 82 5 5 HELIX 56 AG2 THR J 28 TYR J 32 5 5 HELIX 57 AG3 ARG J 61 GLN J 64 5 4 HELIX 58 AG4 LEU J 73 THR J 75 5 3 HELIX 59 AG5 LYS J 83 THR J 87 5 5 HELIX 60 AG6 GLN N 79 GLU N 83 5 5 HELIX 61 AG7 ARG K 61 GLN K 64 5 4 HELIX 62 AG8 LEU K 73 THR K 75 5 3 HELIX 63 AG9 LYS K 83 THR K 87 5 5 HELIX 64 AH1 GLN P 79 GLU P 83 5 5 SHEET 1 AA1 3 LEU A 494 PRO A 498 0 SHEET 2 AA1 3 VAL A 36 TYR A 40 -1 N TYR A 39 O GLY A 495 SHEET 3 AA1 3 ILE B 603 CYS B 604 -1 O CYS B 604 N VAL A 38 SHEET 1 AA2 5 TRP A 45 GLU A 47 0 SHEET 2 AA2 5 TYR A 486 ILE A 491 -1 O LYS A 490 N LYS A 46 SHEET 3 AA2 5 PHE A 223 CYS A 228 -1 N LEU A 226 O LYS A 487 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 VAL A 84 LEU A 86 -1 N VAL A 84 O THR A 244 SHEET 1 AA3 2 PHE A 53 ALA A 55 0 SHEET 2 AA3 2 HIS A 216 CYS A 218 -1 O HIS A 216 N ALA A 55 SHEET 1 AA4 2 GLU A 91 ASN A 94 0 SHEET 2 AA4 2 THR A 236 CYS A 239 -1 O CYS A 239 N GLU A 91 SHEET 1 AA5 5 GLN A 170 TYR A 177 0 SHEET 2 AA5 5 ILE A 154 ILE A 161 -1 N LYS A 155 O PHE A 176 SHEET 3 AA5 5 LEU A 129 THR A 132 -1 N ASN A 130 O SER A 158 SHEET 4 AA5 5 SER A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA5 5 ILE A 181 PRO A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA6 3 ILE A 201 GLN A 203 0 SHEET 2 AA6 3 ALA A 433 TYR A 435 1 O TYR A 435 N LYS A 202 SHEET 3 AA6 3 ILE A 423 ASN A 425 -1 N ILE A 424 O MET A 434 SHEET 1 AA711 LEU A 259 LEU A 261 0 SHEET 2 AA711 VAL A 271 ARG A 273 0 SHEET 3 AA711 VAL A 283 ARG A 298 -1 O GLN A 287 N VAL A 271 SHEET 4 AA711 ALA A 329 ILE A 333 -1 O ASN A 332 N ASN A 295 SHEET 5 AA711 ILE A 359 PHE A 361 0 SHEET 6 AA711 HIS A 374 CYS A 378 0 SHEET 7 AA711 GLU A 381 CYS A 385 -1 O PHE A 383 N PHE A 376 SHEET 8 AA711 SER A 393 TRP A 395 -1 O TRP A 395 N ILE A 359 SHEET 9 AA711 ILE A 414 LYS A 421 -1 O ARG A 419 N TYR A 384 SHEET 10 AA711 ILE A 443 ASP A 457 -1 O LEU A 454 N ILE A 284 SHEET 11 AA711 GLU A 466 PRO A 470 -1 O ARG A 469 N THR A 455 SHEET 1 AA8 2 ASN A 301 ALA A 312 0 SHEET 2 AA8 2 ARG A 315 ILE A 323A-1 O PHE A 317 N ILE A 307 SHEET 1 AA9 3 LEU C 494 PRO C 498 0 SHEET 2 AA9 3 VAL C 36 TYR C 40 -1 N TYR C 39 O GLY C 495 SHEET 3 AA9 3 ILE E 603 CYS E 604 -1 O CYS E 604 N VAL C 38 SHEET 1 AB1 5 TRP C 45 GLU C 47 0 SHEET 2 AB1 5 TYR C 486 ILE C 491 -1 O LYS C 490 N LYS C 46 SHEET 3 AB1 5 PHE C 223 CYS C 228 -1 N LEU C 226 O LYS C 487 SHEET 4 AB1 5 VAL C 242 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AB1 5 VAL C 84 LEU C 86 -1 N VAL C 84 O THR C 244 SHEET 1 AB2 2 ALA C 55 SER C 56 0 SHEET 2 AB2 2 VAL C 75 PRO C 76 1 O VAL C 75 N SER C 56 SHEET 1 AB3 2 GLU C 91 ASN C 94 0 SHEET 2 AB3 2 THR C 236 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AB4 5 GLN C 170 TYR C 177 0 SHEET 2 AB4 5 ILE C 154 ILE C 161 -1 N PHE C 159 O GLU C 172 SHEET 3 AB4 5 LEU C 129 CYS C 131 -1 N ASN C 130 O SER C 158 SHEET 4 AB4 5 SER C 190 LEU C 193 -1 O TYR C 191 N LEU C 129 SHEET 5 AB4 5 ILE C 181 PRO C 183 -1 N VAL C 182 O ARG C 192 SHEET 1 AB5 3 VAL C 200 GLN C 203 0 SHEET 2 AB5 3 LYS C 432 TYR C 435 1 O TYR C 435 N LYS C 202 SHEET 3 AB5 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AB612 LEU C 259 LEU C 261 0 SHEET 2 AB612 VAL C 271 ARG C 273 0 SHEET 3 AB612 ILE C 284 ALA C 312 -1 O ILE C 285 N ARG C 273 SHEET 4 AB612 ARG C 315 ILE C 323 -1 O PHE C 317 N ILE C 307 SHEET 5 AB612 ALA C 329 ILE C 333 -1 O HIS C 330 N THR C 297 SHEET 6 AB612 THR C 358 ASN C 362 0 SHEET 7 AB612 HIS C 374 CYS C 378 0 SHEET 8 AB612 GLU C 381 CYS C 385 -1 O CYS C 385 N HIS C 374 SHEET 9 AB612 ASN C 392 TRP C 395 -1 O TRP C 395 N ILE C 359 SHEET 10 AB612 ILE C 414 LYS C 421 -1 O ARG C 419 N TYR C 384 SHEET 11 AB612 GLY C 441 ARG C 456 -1 O LEU C 454 N ILE C 284 SHEET 12 AB612 THR C 465 PRO C 470 -1 O ARG C 469 N THR C 455 SHEET 1 AB7 3 LEU D 494 PRO D 498 0 SHEET 2 AB7 3 VAL D 36 TYR D 40 -1 N THR D 37 O ALA D 497 SHEET 3 AB7 3 ILE F 603 CYS F 604 -1 O CYS F 604 N VAL D 38 SHEET 1 AB8 5 TRP D 45 GLU D 47 0 SHEET 2 AB8 5 TYR D 486 ILE D 491 -1 O LYS D 490 N LYS D 46 SHEET 3 AB8 5 PHE D 223 CYS D 228 -1 N LEU D 226 O LYS D 487 SHEET 4 AB8 5 VAL D 242 VAL D 245 -1 O SER D 243 N LYS D 227 SHEET 5 AB8 5 VAL D 84 VAL D 85 -1 N VAL D 84 O THR D 244 SHEET 1 AB9 3 CYS D 74 PRO D 76 0 SHEET 2 AB9 3 PHE D 53 SER D 56 1 N SER D 56 O VAL D 75 SHEET 3 AB9 3 HIS D 216 CYS D 218 -1 O HIS D 216 N ALA D 55 SHEET 1 AC1 2 GLU D 91 ASN D 94 0 SHEET 2 AC1 2 THR D 236 CYS D 239 -1 O GLY D 237 N PHE D 93 SHEET 1 AC2 5 GLN D 170 TYR D 177 0 SHEET 2 AC2 5 ILE D 154 ILE D 161 -1 N LYS D 155 O PHE D 176 SHEET 3 AC2 5 LEU D 129 CYS D 131 -1 N ASN D 130 O SER D 158 SHEET 4 AC2 5 SER D 190 LEU D 193 -1 O TYR D 191 N LEU D 129 SHEET 5 AC2 5 ILE D 181 PRO D 183 -1 N VAL D 182 O ARG D 192 SHEET 1 AC3 3 VAL D 200 GLN D 203 0 SHEET 2 AC3 3 LYS D 432 TYR D 435 1 O TYR D 435 N LYS D 202 SHEET 3 AC3 3 ILE D 423 ILE D 424 -1 N ILE D 424 O MET D 434 SHEET 1 AC411 LEU D 259 LEU D 261 0 SHEET 2 AC411 VAL D 271 ARG D 273 0 SHEET 3 AC411 ILE D 284 ARG D 298 -1 O ILE D 285 N ARG D 273 SHEET 4 AC411 ALA D 329 ILE D 333 -1 O ASN D 332 N ASN D 295 SHEET 5 AC411 THR D 358 PHE D 361 0 SHEET 6 AC411 HIS D 374 CYS D 378 0 SHEET 7 AC411 GLU D 381 CYS D 385 -1 O CYS D 385 N HIS D 374 SHEET 8 AC411 SER D 393 TRP D 395 -1 O TRP D 395 N ILE D 359 SHEET 9 AC411 ILE D 414 LYS D 421 -1 O ARG D 419 N TYR D 384 SHEET 10 AC411 ILE D 443 ARG D 456 -1 O SER D 447 N ILE D 294 SHEET 11 AC411 THR D 465 PRO D 470 -1 O ARG D 469 N THR D 455 SHEET 1 AC5 2 ASN D 302 ILE D 307 0 SHEET 2 AC5 2 PHE D 317 ILE D 323 -1 O PHE D 317 N ILE D 307 SHEET 1 AC6 4 LEU G 4 LEU G 5 0 SHEET 2 AC6 4 LEU G 18 VAL G 24 -1 O THR G 23 N LEU G 5 SHEET 3 AC6 4 GLN G 77 LEU G 82 -1 O PHE G 78 N CYS G 22 SHEET 4 AC6 4 VAL G 67 ASP G 72 -1 N ASP G 72 O GLN G 77 SHEET 1 AC7 6 LEU G 11 VAL G 12 0 SHEET 2 AC7 6 THR G 107 VAL G 111 1 O THR G 110 N VAL G 12 SHEET 3 AC7 6 ALA G 88 GLU G 95 -1 N TYR G 90 O THR G 107 SHEET 4 AC7 6 TYR G 33 GLN G 39 -1 N ILE G 37 O TYR G 91 SHEET 5 AC7 6 GLU G 46 ILE G 51 -1 O GLU G 46 N ARG G 38 SHEET 6 AC7 6 ASN G 58 TYR G 59 -1 O ASN G 58 N TYR G 50 SHEET 1 AC8 2 SER G 97 ILE G 98 0 SHEET 2 AC8 2 MET G 100D VAL G 100E-1 O MET G 100D N ILE G 98 SHEET 1 AC9 6 SER I 9 VAL I 12 0 SHEET 2 AC9 6 HIS I 33 GLN I 37 0 SHEET 3 AC9 6 VAL I 44 ILE I 47 -1 O ILE I 47 N TRP I 34 SHEET 4 AC9 6 ALA I 83 TRP I 90 -1 O GLN I 88 N HIS I 33 SHEET 5 AC9 6 CYS I 97 PHE I 99 -1 O VAL I 98 N VAL I 89 SHEET 6 AC9 6 THR I 103 VAL I 107 -1 O THR I 103 N TYR I 85 SHEET 1 AD1 3 ALA I 18 GLY I 23 0 SHEET 2 AD1 3 THR I 69 ILE I 74 -1 O ALA I 70 N CYS I 22 SHEET 3 AD1 3 PHE I 61 SER I 66 -1 N SER I 64 O THR I 71 SHEET 1 AD2 4 GLN H 3 GLU H 6 0 SHEET 2 AD2 4 ALA H 16 SER H 25 -1 O GLU H 23 N LEU H 5 SHEET 3 AD2 4 THR H 77 LEU H 82C-1 O LEU H 82C N ALA H 16 SHEET 4 AD2 4 LEU H 67 ASP H 72 -1 N THR H 70 O TYR H 79 SHEET 1 AD3 6 GLU H 10 LYS H 12 0 SHEET 2 AD3 6 SER H 107 VAL H 111 1 O THR H 110 N LYS H 12 SHEET 3 AD3 6 ALA H 88 GLY H 95 -1 N TYR H 90 O SER H 107 SHEET 4 AD3 6 PHE H 33 ALA H 40 -1 N VAL H 37 O TYR H 91 SHEET 5 AD3 6 GLY H 44 ILE H 51 -1 O GLY H 49 N TRP H 36 SHEET 6 AD3 6 VAL H 57 TYR H 59 -1 O ASN H 58 N TRP H 50 SHEET 1 AD4 6 SER L 9 GLY L 12 0 SHEET 2 AD4 6 SER L 34 GLN L 38 0 SHEET 3 AD4 6 LYS L 45 ILE L 48 -1 O ILE L 47 N TRP L 35 SHEET 4 AD4 6 ALA L 84 TYR L 91 -1 O HIS L 87 N TYR L 36 SHEET 5 AD4 6 ILE L 95 PHE L 97 -1 O ILE L 96 N SER L 90 SHEET 6 AD4 6 THR L 101 VAL L 105 -1 O LEU L 103 N ALA L 84 SHEET 1 AD5 3 ILE L 18 SER L 21 0 SHEET 2 AD5 3 THR L 70 ILE L 75 -1 O LEU L 73 N ILE L 20 SHEET 3 AD5 3 PHE L 62 SER L 67 -1 N SER L 67 O THR L 70 SHEET 1 AD6 4 LEU M 4 LEU M 5 0 SHEET 2 AD6 4 LEU M 18 VAL M 24 -1 O THR M 23 N LEU M 5 SHEET 3 AD6 4 GLN M 77 LEU M 82 -1 O LEU M 80 N LEU M 20 SHEET 4 AD6 4 VAL M 67 ASP M 72 -1 N ASP M 72 O GLN M 77 SHEET 1 AD7 6 LEU M 11 VAL M 12 0 SHEET 2 AD7 6 THR M 107 VAL M 111 1 O THR M 110 N VAL M 12 SHEET 3 AD7 6 ALA M 88 GLU M 95 -1 N TYR M 90 O THR M 107 SHEET 4 AD7 6 TYR M 33 GLN M 39 -1 N TYR M 33 O GLU M 95 SHEET 5 AD7 6 GLU M 46 ILE M 51 -1 O GLU M 46 N ARG M 38 SHEET 6 AD7 6 ASN M 58 TYR M 59 -1 O ASN M 58 N TYR M 50 SHEET 1 AD8 6 SER O 9 VAL O 12 0 SHEET 2 AD8 6 HIS O 33 GLN O 37 0 SHEET 3 AD8 6 VAL O 44 ILE O 47 -1 O ILE O 47 N TRP O 34 SHEET 4 AD8 6 ALA O 83 TRP O 90 -1 O GLN O 88 N HIS O 33 SHEET 5 AD8 6 CYS O 97 PHE O 99 -1 O VAL O 98 N VAL O 89 SHEET 6 AD8 6 THR O 103 VAL O 107 -1 O THR O 103 N TYR O 85 SHEET 1 AD9 3 ALA O 18 GLY O 23 0 SHEET 2 AD9 3 THR O 69 ILE O 74 -1 O LEU O 72 N ILE O 20 SHEET 3 AD9 3 PHE O 61 SER O 66 -1 N SER O 64 O THR O 71 SHEET 1 AE1 4 GLN J 3 GLU J 6 0 SHEET 2 AE1 4 ALA J 16 SER J 25 -1 O GLU J 23 N LEU J 5 SHEET 3 AE1 4 THR J 77 LEU J 82C-1 O LEU J 82C N ALA J 16 SHEET 4 AE1 4 LEU J 67 ASP J 72 -1 N THR J 68 O ASP J 81 SHEET 1 AE2 6 GLU J 10 LYS J 12 0 SHEET 2 AE2 6 SER J 107 VAL J 111 1 O THR J 110 N LYS J 12 SHEET 3 AE2 6 ALA J 88 CYS J 92 -1 N TYR J 90 O SER J 107 SHEET 4 AE2 6 ILE J 34 ALA J 40 -1 N VAL J 37 O TYR J 91 SHEET 5 AE2 6 GLY J 44 ILE J 51 -1 O GLY J 49 N TRP J 36 SHEET 6 AE2 6 VAL J 57 TYR J 59 -1 O ASN J 58 N TRP J 50 SHEET 1 AE3 6 SER N 9 GLY N 12 0 SHEET 2 AE3 6 VAL N 33 GLN N 38 0 SHEET 3 AE3 6 PRO N 44 ILE N 48 -1 O ILE N 47 N TRP N 35 SHEET 4 AE3 6 ALA N 84 TYR N 91 -1 O ILE N 85 N GLN N 38 SHEET 5 AE3 6 ILE N 95 PHE N 97 -1 O ILE N 96 N SER N 90 SHEET 6 AE3 6 THR N 101 VAL N 105 -1 O THR N 101 N TYR N 86 SHEET 1 AE4 3 ILE N 18 SER N 21 0 SHEET 2 AE4 3 THR N 70 ILE N 75 -1 O LEU N 73 N ILE N 20 SHEET 3 AE4 3 PHE N 62 SER N 67 -1 N SER N 63 O THR N 74 SHEET 1 AE5 4 GLN K 3 GLU K 6 0 SHEET 2 AE5 4 ALA K 16 SER K 25 -1 O GLU K 23 N LEU K 5 SHEET 3 AE5 4 THR K 77 LEU K 82C-1 O MET K 80 N VAL K 20 SHEET 4 AE5 4 LEU K 67 ASP K 72 -1 N THR K 70 O TYR K 79 SHEET 1 AE6 6 GLU K 10 LYS K 12 0 SHEET 2 AE6 6 SER K 107 VAL K 111 1 O THR K 110 N LYS K 12 SHEET 3 AE6 6 ALA K 88 ALA K 93 -1 N TYR K 90 O SER K 107 SHEET 4 AE6 6 PHE K 33 ALA K 40 -1 N VAL K 37 O TYR K 91 SHEET 5 AE6 6 GLY K 44 ASN K 52 -1 O GLY K 49 N TRP K 36 SHEET 6 AE6 6 VAL K 57 TYR K 59 -1 O ASN K 58 N TRP K 50 SHEET 1 AE7 6 SER P 9 GLY P 12 0 SHEET 2 AE7 6 SER P 34 GLN P 38 0 SHEET 3 AE7 6 LYS P 45 ILE P 48 -1 O ILE P 47 N TRP P 35 SHEET 4 AE7 6 ALA P 84 TYR P 91 -1 O HIS P 87 N TYR P 36 SHEET 5 AE7 6 ILE P 95 PHE P 97 -1 O ILE P 96 N SER P 90 SHEET 6 AE7 6 THR P 101 VAL P 105 -1 O THR P 101 N TYR P 86 SHEET 1 AE8 3 ILE P 18 CYS P 22 0 SHEET 2 AE8 3 ALA P 71 ILE P 75 -1 O LEU P 73 N ILE P 20 SHEET 3 AE8 3 PHE P 62 LYS P 66 -1 N SER P 63 O THR P 74 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.03 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.05 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.02 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.03 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.04 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.04 SSBOND 9 CYS A 385 CYS A 418 1555 1555 2.03 SSBOND 10 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 11 CYS C 54 CYS C 74 1555 1555 2.03 SSBOND 12 CYS C 119 CYS C 205 1555 1555 2.04 SSBOND 13 CYS C 126 CYS C 196 1555 1555 2.07 SSBOND 14 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 15 CYS C 218 CYS C 247 1555 1555 2.02 SSBOND 16 CYS C 228 CYS C 239 1555 1555 2.03 SSBOND 17 CYS C 296 CYS C 331 1555 1555 2.03 SSBOND 18 CYS C 378 CYS C 445 1555 1555 2.03 SSBOND 19 CYS C 385 CYS C 418 1555 1555 2.03 SSBOND 20 CYS E 598 CYS E 604 1555 1555 2.02 SSBOND 21 CYS D 54 CYS D 74 1555 1555 2.03 SSBOND 22 CYS D 119 CYS D 205 1555 1555 2.04 SSBOND 23 CYS D 126 CYS D 196 1555 1555 2.03 SSBOND 24 CYS D 131 CYS D 157 1555 1555 2.03 SSBOND 25 CYS D 218 CYS D 247 1555 1555 2.03 SSBOND 26 CYS D 228 CYS D 239 1555 1555 2.03 SSBOND 27 CYS D 296 CYS D 331 1555 1555 2.03 SSBOND 28 CYS D 378 CYS D 445 1555 1555 2.03 SSBOND 29 CYS D 385 CYS D 418 1555 1555 2.03 SSBOND 30 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 31 CYS G 22 CYS G 92 1555 1555 2.03 SSBOND 32 CYS I 22 CYS I 87 1555 1555 2.04 SSBOND 33 CYS H 22 CYS H 92 1555 1555 2.02 SSBOND 34 CYS L 22 CYS L 88 1555 1555 2.03 SSBOND 35 CYS M 22 CYS M 92 1555 1555 2.05 SSBOND 36 CYS O 22 CYS O 87 1555 1555 2.04 SSBOND 37 CYS J 22 CYS J 92 1555 1555 2.03 SSBOND 38 CYS N 22 CYS N 88 1555 1555 2.03 SSBOND 39 CYS K 22 CYS K 92 1555 1555 2.02 SSBOND 40 CYS P 22 CYS P 88 1555 1555 2.03 LINK ND2 ASN A 88 C1 NAG d 1 1555 1555 1.53 LINK ND2 ASN A 130 C1 NAG Q 1 1555 1555 1.52 LINK ND2 ASN A 156 C1 NAG A 601 1555 1555 1.53 LINK ND2 ASN A 160 C1 NAG A 602 1555 1555 1.53 LINK ND2 ASN A 197 C1 NAG R 1 1555 1555 1.52 LINK ND2 ASN A 234 C1 NAG S 1 1555 1555 1.53 LINK ND2 ASN A 241 C1 NAG T 1 1555 1555 1.51 LINK ND2 ASN A 262 C1 NAG U 1 1555 1555 1.53 LINK ND2 ASN A 276 C1 NAG V 1 1555 1555 1.52 LINK ND2 ASN A 289 C1 NAG W 1 1555 1555 1.51 LINK ND2 ASN A 295 C1 NAG X 1 1555 1555 1.51 LINK ND2 ASN A 301 C1 NAG c 1 1555 1555 1.52 LINK ND2 ASN A 332 C1 NAG A 603 1555 1555 1.51 LINK ND2 ASN A 339 C1 NAG A 604 1555 1555 1.53 LINK ND2 ASN A 362 C1 NAG Y 1 1555 1555 1.51 LINK ND2 ASN A 386 C1 NAG Z 1 1555 1555 1.52 LINK ND2 ASN A 392 C1 NAG a 1 1555 1555 1.52 LINK ND2 ASN A 396 C1 NAG A 605 1555 1555 1.52 LINK ND2 ASN A 448 C1 NAG b 1 1555 1555 1.52 LINK ND2 ASN B 611 C1 NAG B 703 1555 1555 1.52 LINK ND2 ASN B 616 C1 NAG B 701 1555 1555 1.53 LINK ND2 ASN B 625 C1 NAG e 1 1555 1555 1.49 LINK ND2 ASN B 637 C1 NAG B 702 1555 1555 1.52 LINK ND2 ASN C 88 C1 NAG f 1 1555 1555 1.52 LINK ND2 ASN C 130 C1 NAG g 1 1555 1555 1.53 LINK ND2 ASN C 156 C1 NAG C 601 1555 1555 1.53 LINK ND2 ASN C 160 C1 NAG s 1 1555 1555 1.52 LINK ND2 ASN C 197 C1 NAG h 1 1555 1555 1.52 LINK ND2 ASN C 234 C1 NAG t 1 1555 1555 1.51 LINK ND2 ASN C 241 C1 NAG i 1 1555 1555 1.52 LINK ND2 ASN C 262 C1 NAG j 1 1555 1555 1.51 LINK ND2 ASN C 276 C1 NAG k 1 1555 1555 1.52 LINK ND2 ASN C 289 C1 NAG l 1 1555 1555 1.51 LINK ND2 ASN C 295 C1 NAG m 1 1555 1555 1.50 LINK ND2 ASN C 301 C1 NAG n 1 1555 1555 1.51 LINK ND2 ASN C 362 C1 NAG o 1 1555 1555 1.51 LINK ND2 ASN C 386 C1 NAG p 1 1555 1555 1.53 LINK ND2 ASN C 392 C1 NAG q 1 1555 1555 1.51 LINK ND2 ASN C 396 C1 NAG C 602 1555 1555 1.51 LINK OG1 THR C 415 C1 NAG C 603 1555 1555 1.51 LINK ND2 ASN C 448 C1 NAG r 1 1555 1555 1.52 LINK ND2 ASN E 611 C1 NAG u 1 1555 1555 1.51 LINK ND2 ASN E 616 C1 NAG E 701 1555 1555 1.52 LINK ND2 ASN E 625 C1 NAG v 1 1555 1555 1.52 LINK ND2 ASN E 637 C1 NAG E 702 1555 1555 1.51 LINK ND2 ASN D 88 C1 NAG w 1 1555 1555 1.52 LINK ND2 ASN D 130 C1 NAG D 605 1555 1555 1.53 LINK ND2 ASN D 156 C1 NAG D 601 1555 1555 1.52 LINK ND2 ASN D 160 C1 NAG D 602 1555 1555 1.52 LINK ND2 ASN D 197 C1 NAG x 1 1555 1555 1.53 LINK ND2 ASN D 234 C1 NAG y 1 1555 1555 1.53 LINK ND2 ASN D 241 C1 NAG z 1 1555 1555 1.52 LINK ND2 ASN D 262 C1 NAG 0 1 1555 1555 1.51 LINK ND2 ASN D 276 C1 NAG 1 1 1555 1555 1.52 LINK ND2 ASN D 289 C1 NAG 2 1 1555 1555 1.51 LINK ND2 ASN D 295 C1 NAG 8 1 1555 1555 1.42 LINK ND2 ASN D 301 C1 NAG 3 1 1555 1555 1.51 LINK ND2 ASN D 332 C1 NAG D 603 1555 1555 1.52 LINK ND2 ASN D 339 C1 NAG D 604 1555 1555 1.52 LINK ND2 ASN D 362 C1 NAG 4 1 1555 1555 1.52 LINK ND2 ASN D 386 C1 NAG 5 1 1555 1555 1.51 LINK ND2 ASN D 392 C1 NAG 6 1 1555 1555 1.52 LINK ND2 ASN D 396 C1 NAG D 606 1555 1555 1.44 LINK ND2 ASN D 448 C1 NAG 7 1 1555 1555 1.52 LINK ND2 ASN F 611 C1 NAG 9 1 1555 1555 1.52 LINK ND2 ASN F 616 C1 NAG F 701 1555 1555 1.52 LINK ND2 ASN F 625 C1 NAGAA 1 1555 1555 1.52 LINK ND2 ASN F 637 C1 NAG F 702 1555 1555 1.52 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.50 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.52 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.52 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.51 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.53 LINK O3 BMA S 3 C1 MAN S 4 1555 1555 1.53 LINK O6 BMA S 3 C1 MAN S 5 1555 1555 1.49 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.51 LINK O4 NAG T 2 C1 BMA T 3 1555 1555 1.51 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.52 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.53 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.52 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.52 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.52 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.52 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.52 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.51 LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.52 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.51 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.51 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.54 LINK O4 NAG a 2 C1 BMA a 3 1555 1555 1.53 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.52 LINK O4 NAG b 2 C1 BMA b 3 1555 1555 1.52 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.53 LINK O4 NAG c 2 C1 BMA c 3 1555 1555 1.52 LINK O6 NAG d 1 C1 NAG d 2 1555 1555 1.52 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.52 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.51 LINK O4 NAG e 2 C1 BMA e 3 1555 1555 1.51 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.51 LINK O4 NAG f 2 C1 BMA f 3 1555 1555 1.52 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.51 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.51 LINK O4 NAG h 2 C1 BMA h 3 1555 1555 1.52 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.53 LINK O4 NAG i 2 C1 BMA i 3 1555 1555 1.53 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.53 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.52 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.51 LINK O4 NAG k 2 C1 BMA k 3 1555 1555 1.52 LINK O4 NAG l 1 C1 NAG l 2 1555 1555 1.51 LINK O4 NAG m 1 C1 NAG m 2 1555 1555 1.52 LINK O4 NAG m 2 C1 BMA m 3 1555 1555 1.52 LINK O4 NAG n 1 C1 NAG n 2 1555 1555 1.53 LINK O4 NAG n 2 C1 BMA n 3 1555 1555 1.53 LINK O4 NAG o 1 C1 NAG o 2 1555 1555 1.51 LINK O4 NAG o 2 C1 BMA o 3 1555 1555 1.53 LINK O4 NAG p 1 C1 NAG p 2 1555 1555 1.54 LINK O4 NAG p 2 C1 BMA p 3 1555 1555 1.53 LINK O4 NAG q 1 C1 NAG q 2 1555 1555 1.52 LINK O4 NAG q 2 C1 BMA q 3 1555 1555 1.53 LINK O4 NAG r 1 C1 NAG r 2 1555 1555 1.51 LINK O4 NAG r 2 C1 BMA r 3 1555 1555 1.52 LINK O4 NAG s 1 C1 NAG s 2 1555 1555 1.52 LINK O4 NAG t 1 C1 NAG t 2 1555 1555 1.52 LINK O4 NAG t 2 C1 BMA t 3 1555 1555 1.53 LINK O4 NAG u 1 C1 NAG u 2 1555 1555 1.51 LINK O4 NAG v 1 C1 NAG v 2 1555 1555 1.53 LINK O4 NAG w 1 C1 NAG w 2 1555 1555 1.51 LINK O4 NAG w 2 C1 BMA w 3 1555 1555 1.52 LINK O4 NAG x 1 C1 NAG x 2 1555 1555 1.53 LINK O4 NAG x 2 C1 BMA x 3 1555 1555 1.52 LINK O4 NAG y 1 C1 NAG y 2 1555 1555 1.52 LINK O4 NAG y 2 C1 BMA y 3 1555 1555 1.53 LINK O3 BMA y 3 C1 MAN y 4 1555 1555 1.52 LINK O6 BMA y 3 C1 MAN y 5 1555 1555 1.50 LINK O4 NAG z 1 C1 NAG z 2 1555 1555 1.53 LINK O4 NAG z 2 C1 BMA z 3 1555 1555 1.53 LINK O4 NAG 0 1 C1 NAG 0 2 1555 1555 1.53 LINK O4 NAG 0 2 C1 BMA 0 3 1555 1555 1.52 LINK O4 NAG 1 1 C1 NAG 1 2 1555 1555 1.51 LINK O4 NAG 1 2 C1 BMA 1 3 1555 1555 1.51 LINK O4 NAG 2 1 C1 NAG 2 2 1555 1555 1.53 LINK O4 NAG 3 1 C1 NAG 3 2 1555 1555 1.51 LINK O4 NAG 3 2 C1 BMA 3 3 1555 1555 1.52 LINK O4 NAG 4 1 C1 NAG 4 2 1555 1555 1.52 LINK O4 NAG 4 2 C1 BMA 4 3 1555 1555 1.51 LINK O4 NAG 5 1 C1 NAG 5 2 1555 1555 1.51 LINK O4 NAG 5 2 C1 BMA 5 3 1555 1555 1.52 LINK O4 NAG 6 1 C1 NAG 6 2 1555 1555 1.54 LINK O4 NAG 6 2 C1 BMA 6 3 1555 1555 1.52 LINK O4 NAG 7 1 C1 NAG 7 2 1555 1555 1.52 LINK O4 NAG 7 2 C1 BMA 7 3 1555 1555 1.51 LINK O4 NAG 8 1 C1 NAG 8 2 1555 1555 1.44 LINK O4 NAG 8 2 C1 BMA 8 3 1555 1555 1.44 LINK O4 NAG 9 1 C1 NAG 9 2 1555 1555 1.51 LINK O4 NAGAA 1 C1 NAGAA 2 1555 1555 1.53 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000