HEADER VIRAL PROTEIN/IMMUNE SYSTEM 02-MAY-24 9BNL TITLE CRYO-EM STRUCTURE OF RHESUS ANTIBODY 6070-A.01 IN COMPLEX WITH HIV-1 TITLE 2 ENV TRIMER Q23.17 MD39 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 3 CHAIN: A, C, E; COMPND 4 SYNONYM: ENV POLYPROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 8 CHAIN: B, F, G; COMPND 9 SYNONYM: ENV POLYPROTEIN; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: 6070-A.01 HEAVY CHAIN; COMPND 13 CHAIN: H; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: 6070-A.01 LIGHT CHAIN; COMPND 17 CHAIN: L; COMPND 18 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: MACACA MULATTA; SOURCE 17 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 18 ORGANISM_TAXID: 9544; 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: MACACA MULATTA; SOURCE 24 ORGANISM_COMMON: RHESUS MONKEY; SOURCE 25 ORGANISM_TAXID: 9544; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS NEUTRALIZING ANTIBODY, HIV-1 V2 APEX, SHIV-ELICITED, VIRAL PROTEIN, KEYWDS 2 IMMUNE SYSTEM, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR R.S.ROARK,L.SHAPIRO,P.D.KWONG REVDAT 1 07-MAY-25 9BNL 0 JRNL AUTH R.S.ROARK,L.SHAPIRO,P.D.KWONG JRNL TITL HIV-1 NEUTRALIZING ANTIBODIES IN SHIV-INFECTED MACAQUES JRNL TITL 2 RECAPITULATE STRUCTURALLY DIVERGENT MODES OF HUMAN V2 APEX JRNL TITL 3 RECOGNITION WITH A SINGLE D GENE JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.600 REMARK 3 NUMBER OF PARTICLES : 62547 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9BNL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1000283692. 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 : COMPLEX OF 6070-A.01 WITH HIV-1 REMARK 245 Q23.17 ENVELOPE TRIMER REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5800.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, F, G, H, L, D, I, REMARK 350 AND CHAINS: J, K, M, N, O, 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 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 LYS A 59 REMARK 465 ALA A 60 REMARK 465 TYR A 61 REMARK 465 GLU A 62 REMARK 465 THR A 63 REMARK 465 GLU A 64 REMARK 465 SER A 144 REMARK 465 VAL A 145 REMARK 465 ASN A 146 REMARK 465 THR A 147 REMARK 465 THR A 148 REMARK 465 GLY A 149 REMARK 465 ASP A 150 REMARK 465 ARG A 151 REMARK 465 THR A 405A REMARK 465 TRP A 405B REMARK 465 ASN A 405C REMARK 465 ASP A 405D REMARK 465 THR A 405E REMARK 465 ASP A 405F REMARK 465 SER A 405G REMARK 465 THR A 405H REMARK 465 GLN A 405I REMARK 465 GLU A 405J REMARK 465 SER A 405K REMARK 465 SER B 546 REMARK 465 GLY B 547 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 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 ILE B 559 REMARK 465 GLU B 560 REMARK 465 ALA B 561 REMARK 465 GLN B 562 REMARK 465 GLN B 563 REMARK 465 HIS B 564 REMARK 465 LEU B 565 REMARK 465 LEU B 566 REMARK 465 LYS B 567 REMARK 465 LYS C 59 REMARK 465 ALA C 60 REMARK 465 TYR C 61 REMARK 465 GLU C 62 REMARK 465 THR C 63 REMARK 465 GLU C 64 REMARK 465 VAL C 145 REMARK 465 ASN C 146 REMARK 465 THR C 147 REMARK 465 THR C 148 REMARK 465 GLY C 149 REMARK 465 ASP C 150 REMARK 465 ARG C 151 REMARK 465 GLU C 185A REMARK 465 ASN C 185B REMARK 465 GLN C 185C REMARK 465 THR C 405A REMARK 465 TRP C 405B REMARK 465 ASN C 405C REMARK 465 ASP C 405D REMARK 465 THR C 405E REMARK 465 ASP C 405F REMARK 465 SER C 405G REMARK 465 THR C 405H REMARK 465 GLN C 405I REMARK 465 GLU C 405J REMARK 465 SER C 405K REMARK 465 LYS E 59 REMARK 465 ALA E 60 REMARK 465 TYR E 61 REMARK 465 GLU E 62 REMARK 465 THR E 63 REMARK 465 GLU E 64 REMARK 465 VAL E 145 REMARK 465 ASN E 146 REMARK 465 THR E 147 REMARK 465 THR E 148 REMARK 465 GLY E 149 REMARK 465 ASP E 150 REMARK 465 ARG E 151 REMARK 465 GLU E 185A REMARK 465 ASN E 185B REMARK 465 GLN E 185C REMARK 465 THR E 405A REMARK 465 TRP E 405B REMARK 465 ASN E 405C REMARK 465 ASP E 405D REMARK 465 THR E 405E REMARK 465 ASP E 405F REMARK 465 SER E 405G REMARK 465 THR E 405H REMARK 465 GLN E 405I REMARK 465 GLU E 405J REMARK 465 SER E 405K REMARK 465 SER F 546 REMARK 465 GLY F 547 REMARK 465 ILE F 548 REMARK 465 VAL F 549 REMARK 465 GLN F 550 REMARK 465 GLN F 551 REMARK 465 GLN F 552 REMARK 465 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 ILE F 559 REMARK 465 GLU F 560 REMARK 465 ALA F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 SER G 546 REMARK 465 GLY G 547 REMARK 465 ILE G 548 REMARK 465 VAL G 549 REMARK 465 GLN G 550 REMARK 465 GLN G 551 REMARK 465 GLN G 552 REMARK 465 ASN G 553 REMARK 465 ASN G 554 REMARK 465 LEU G 555 REMARK 465 LEU G 556 REMARK 465 ARG G 557 REMARK 465 ALA G 558 REMARK 465 ILE G 559 REMARK 465 GLU G 560 REMARK 465 ALA G 561 REMARK 465 GLN G 562 REMARK 465 GLN G 563 REMARK 465 HIS G 564 REMARK 465 LEU G 565 REMARK 465 LEU G 566 REMARK 465 LYS G 567 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 H 22 SG CYS H 92 1.79 REMARK 500 O LEU E 369 OG1 THR E 373 2.19 REMARK 500 O ILE F 535 ND2 ASN G 651 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 E 205 CA - CB - SG ANGL. DEV. = 8.0 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 ALA A 73 35.26 -93.11 REMARK 500 ASN A 88 -0.11 67.90 REMARK 500 THR A 163 -167.88 -78.96 REMARK 500 PHE A 210 31.49 -96.28 REMARK 500 GLN A 258 -6.78 72.15 REMARK 500 GLU A 267 -72.08 -75.41 REMARK 500 SER A 364 -177.26 57.43 REMARK 500 ASP A 412 54.04 -91.37 REMARK 500 ASN A 425 -41.64 -130.98 REMARK 500 MET A 426 10.16 55.10 REMARK 500 ASN A 463 -119.36 38.36 REMARK 500 PRO A 493 2.53 -69.19 REMARK 500 ARG A 500 40.36 -107.37 REMARK 500 SER B 615 129.69 -170.31 REMARK 500 ASN C 88 13.06 59.70 REMARK 500 LEU C 122 38.61 -99.60 REMARK 500 ARG C 166 43.63 -87.91 REMARK 500 ASP C 167 -38.40 -137.80 REMARK 500 ASN C 195 -0.33 69.32 REMARK 500 PRO C 212 71.42 -68.86 REMARK 500 GLN C 258 18.87 47.91 REMARK 500 LEU C 259 115.11 -164.73 REMARK 500 SER C 274 149.25 -173.78 REMARK 500 LYS C 356 -168.18 70.16 REMARK 500 SER C 364 -172.70 56.87 REMARK 500 SER C 473 19.43 55.09 REMARK 500 LYS C 485 37.69 -99.51 REMARK 500 PRO C 493 8.52 -69.73 REMARK 500 ALA E 48 142.82 -171.35 REMARK 500 ASN E 88 -1.25 67.90 REMARK 500 VAL E 120 140.12 -39.57 REMARK 500 ASN E 195 -2.02 80.09 REMARK 500 THR E 198 -25.51 -146.60 REMARK 500 PRO E 212 75.06 -69.85 REMARK 500 GLN E 258 -7.89 75.28 REMARK 500 SER E 364 -178.26 57.90 REMARK 500 MET E 426 4.46 55.83 REMARK 500 THR F 606 -169.17 -129.74 REMARK 500 TYR G 638 -1.21 64.53 REMARK 500 SER H 25 -34.20 -130.29 REMARK 500 THR H 31 52.12 -91.55 REMARK 500 SER H 32 66.22 38.14 REMARK 500 ARG H 66 32.48 -141.75 REMARK 500 ASP H 100B 32.26 -95.51 REMARK 500 ASP H 100C -52.81 74.72 REMARK 500 SER L 30 -143.58 56.33 REMARK 500 ALA L 51 -3.85 68.01 REMARK 500 SER L 52 -36.63 -134.27 REMARK 500 PHE L 83 97.20 -66.44 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-44729 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF RHESUS ANTIBODY 6070-A.01 IN COMPLEX WITH HIV- REMARK 900 1 ENV Q23.17 MD39 SOSIP DBREF 9BNL A 33 505 UNP O55774 O55774_9HIV1 32 495 DBREF 9BNL B 520 661 UNP O55774 O55774_9HIV1 510 651 DBREF 9BNL C 33 505 UNP O55774 O55774_9HIV1 32 495 DBREF 9BNL E 33 505 UNP O55774 O55774_9HIV1 32 495 DBREF 9BNL F 520 661 UNP O55774 O55774_9HIV1 510 651 DBREF 9BNL G 520 661 UNP O55774 O55774_9HIV1 510 651 DBREF 9BNL H 1 113 PDB 9BNL 9BNL 1 113 DBREF 9BNL L 1 107 PDB 9BNL 9BNL 1 107 SEQADV 9BNL GLU A 106 UNP O55774 THR 105 CONFLICT SEQADV 9BNL ILE A 271 UNP O55774 THR 263 CONFLICT SEQADV 9BNL VAL A 304 UNP O55774 ARG 296 CONFLICT SEQADV 9BNL TYR A 319 UNP O55774 ALA 309 CONFLICT SEQADV 9BNL SER A 473 UNP O55774 GLY 463 CONFLICT SEQADV 9BNL CYS A 501 UNP O55774 ALA 491 CONFLICT SEQADV 9BNL ALA B 533 UNP O55774 THR 523 CONFLICT SEQADV 9BNL ASN B 543 UNP O55774 GLN 533 CONFLICT SEQADV 9BNL HIS B 570 UNP O55774 VAL 560 CONFLICT SEQADV 9BNL HIS B 585 UNP O55774 ARG 575 CONFLICT SEQADV 9BNL CYS B 605 UNP O55774 THR 595 CONFLICT SEQADV 9BNL GLU C 106 UNP O55774 THR 105 CONFLICT SEQADV 9BNL ILE C 271 UNP O55774 THR 263 CONFLICT SEQADV 9BNL VAL C 304 UNP O55774 ARG 296 CONFLICT SEQADV 9BNL TYR C 319 UNP O55774 ALA 309 CONFLICT SEQADV 9BNL SER C 473 UNP O55774 GLY 463 CONFLICT SEQADV 9BNL CYS C 501 UNP O55774 ALA 491 CONFLICT SEQADV 9BNL GLU E 106 UNP O55774 THR 105 CONFLICT SEQADV 9BNL ILE E 271 UNP O55774 THR 263 CONFLICT SEQADV 9BNL VAL E 304 UNP O55774 ARG 296 CONFLICT SEQADV 9BNL TYR E 319 UNP O55774 ALA 309 CONFLICT SEQADV 9BNL SER E 473 UNP O55774 GLY 463 CONFLICT SEQADV 9BNL CYS E 501 UNP O55774 ALA 491 CONFLICT SEQADV 9BNL ALA F 533 UNP O55774 THR 523 CONFLICT SEQADV 9BNL ASN F 543 UNP O55774 GLN 533 CONFLICT SEQADV 9BNL HIS F 570 UNP O55774 VAL 560 CONFLICT SEQADV 9BNL HIS F 585 UNP O55774 ARG 575 CONFLICT SEQADV 9BNL CYS F 605 UNP O55774 THR 595 CONFLICT SEQADV 9BNL ALA G 533 UNP O55774 THR 523 CONFLICT SEQADV 9BNL ASN G 543 UNP O55774 GLN 533 CONFLICT SEQADV 9BNL HIS G 570 UNP O55774 VAL 560 CONFLICT SEQADV 9BNL HIS G 585 UNP O55774 ARG 575 CONFLICT SEQADV 9BNL CYS G 605 UNP O55774 THR 595 CONFLICT SEQRES 1 A 464 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 A 464 ARG ASP ALA ASP THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 A 464 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 4 A 464 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 5 A 464 HIS LEU ASP ASN VAL THR GLU LYS PHE ASN MET TRP LYS SEQRES 6 A 464 ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE ILE SER SEQRES 7 A 464 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 A 464 PRO LEU CYS VAL THR LEU HIS CYS THR ASN VAL THR SER SEQRES 9 A 464 VAL ASN THR THR GLY ASP ARG GLU GLY LEU LYS ASN CYS SEQRES 10 A 464 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS ARG GLN SEQRES 11 A 464 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE VAL PRO SEQRES 12 A 464 ILE ASN GLU ASN GLN GLY SER GLU TYR ARG LEU ILE ASN SEQRES 13 A 464 CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO LYS VAL SEQRES 14 A 464 SER PHE GLU PRO ILE PRO ILE HIS TYR CYS THR PRO ALA SEQRES 15 A 464 GLY PHE ALA ILE LEU LYS CYS LYS ASP GLU GLY PHE ASN SEQRES 16 A 464 GLY THR GLY LEU CYS LYS ASN VAL SER THR VAL GLN CYS SEQRES 17 A 464 THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU SEQRES 18 A 464 LEU ASN GLY SER LEU ALA GLU LYS ASN ILE ILE ILE ARG SEQRES 19 A 464 SER GLU ASN ILE THR ASN ASN ALA LYS ILE ILE ILE VAL SEQRES 20 A 464 GLN LEU VAL GLN PRO VAL THR ILE LYS CYS ILE ARG PRO SEQRES 21 A 464 ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY PRO GLY SEQRES 22 A 464 GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY ASP ILE SEQRES 23 A 464 ARG GLN ALA HIS CYS ASN VAL THR ARG SER ARG TRP ASN SEQRES 24 A 464 LYS THR LEU GLN GLU VAL ALA GLU LYS LEU ARG THR TYR SEQRES 25 A 464 PHE GLY ASN LYS THR ILE ILE PHE ALA ASN SER SER GLY SEQRES 26 A 464 GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY SEQRES 27 A 464 GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU PHE ASN SEQRES 28 A 464 SER THR TRP TYR VAL ASN SER THR TRP ASN ASP THR ASP SEQRES 29 A 464 SER THR GLN GLU SER ASN ASP THR ILE THR LEU PRO CYS SEQRES 30 A 464 ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG ALA GLY SEQRES 31 A 464 GLN ALA MET TYR ALA PRO PRO ILE PRO GLY VAL ILE LYS SEQRES 32 A 464 CYS GLU SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP SEQRES 33 A 464 GLY GLY LYS ASP ASN ASN VAL ASN GLU THR PHE ARG PRO SEQRES 34 A 464 GLY GLY SER ASP MET ARG ASP ASN TRP ARG SER GLU LEU SEQRES 35 A 464 TYR LYS TYR LYS VAL VAL GLU ILE GLU PRO LEU GLY VAL SEQRES 36 A 464 ALA PRO THR ARG CYS LYS ARG ARG VAL SEQRES 1 B 142 LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET GLY ALA SEQRES 2 B 142 ALA SER ILE THR LEU THR VAL GLN ALA ARG ASN LEU LEU SEQRES 3 B 142 SER GLY ILE VAL GLN GLN GLN ASN ASN LEU LEU ARG ALA SEQRES 4 B 142 ILE GLU ALA GLN GLN HIS LEU LEU LYS LEU THR HIS TRP SEQRES 5 B 142 GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU SEQRES 6 B 142 HIS TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY SEQRES 7 B 142 CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL PRO TRP SEQRES 8 B 142 ASN SER SER TRP SER ASN LYS SER LEU ASP GLU ILE TRP SEQRES 9 B 142 ASN ASN MET THR TRP LEU GLN TRP ASP LYS GLU ILE ASN SEQRES 10 B 142 ASN TYR THR GLN LEU ILE TYR ARG LEU ILE GLU GLU SER SEQRES 11 B 142 GLN ASN GLN GLN GLU LYS ASN GLU LYS GLU LEU LEU SEQRES 1 C 464 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 C 464 ARG ASP ALA ASP THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 C 464 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 4 C 464 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 5 C 464 HIS LEU ASP ASN VAL THR GLU LYS PHE ASN MET TRP LYS SEQRES 6 C 464 ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE ILE SER SEQRES 7 C 464 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 C 464 PRO LEU CYS VAL THR LEU HIS CYS THR ASN VAL THR SER SEQRES 9 C 464 VAL ASN THR THR GLY ASP ARG GLU GLY LEU LYS ASN CYS SEQRES 10 C 464 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS ARG GLN SEQRES 11 C 464 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE VAL PRO SEQRES 12 C 464 ILE ASN GLU ASN GLN GLY SER GLU TYR ARG LEU ILE ASN SEQRES 13 C 464 CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO LYS VAL SEQRES 14 C 464 SER PHE GLU PRO ILE PRO ILE HIS TYR CYS THR PRO ALA SEQRES 15 C 464 GLY PHE ALA ILE LEU LYS CYS LYS ASP GLU GLY PHE ASN SEQRES 16 C 464 GLY THR GLY LEU CYS LYS ASN VAL SER THR VAL GLN CYS SEQRES 17 C 464 THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU SEQRES 18 C 464 LEU ASN GLY SER LEU ALA GLU LYS ASN ILE ILE ILE ARG SEQRES 19 C 464 SER GLU ASN ILE THR ASN ASN ALA LYS ILE ILE ILE VAL SEQRES 20 C 464 GLN LEU VAL GLN PRO VAL THR ILE LYS CYS ILE ARG PRO SEQRES 21 C 464 ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY PRO GLY SEQRES 22 C 464 GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY ASP ILE SEQRES 23 C 464 ARG GLN ALA HIS CYS ASN VAL THR ARG SER ARG TRP ASN SEQRES 24 C 464 LYS THR LEU GLN GLU VAL ALA GLU LYS LEU ARG THR TYR SEQRES 25 C 464 PHE GLY ASN LYS THR ILE ILE PHE ALA ASN SER SER GLY SEQRES 26 C 464 GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY SEQRES 27 C 464 GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU PHE ASN SEQRES 28 C 464 SER THR TRP TYR VAL ASN SER THR TRP ASN ASP THR ASP SEQRES 29 C 464 SER THR GLN GLU SER ASN ASP THR ILE THR LEU PRO CYS SEQRES 30 C 464 ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG ALA GLY SEQRES 31 C 464 GLN ALA MET TYR ALA PRO PRO ILE PRO GLY VAL ILE LYS SEQRES 32 C 464 CYS GLU SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP SEQRES 33 C 464 GLY GLY LYS ASP ASN ASN VAL ASN GLU THR PHE ARG PRO SEQRES 34 C 464 GLY GLY SER ASP MET ARG ASP ASN TRP ARG SER GLU LEU SEQRES 35 C 464 TYR LYS TYR LYS VAL VAL GLU ILE GLU PRO LEU GLY VAL SEQRES 36 C 464 ALA PRO THR ARG CYS LYS ARG ARG VAL SEQRES 1 E 464 ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL TRP SEQRES 2 E 464 ARG ASP ALA ASP THR THR LEU PHE CYS ALA SER ASP ALA SEQRES 3 E 464 LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP ALA THR SEQRES 4 E 464 HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU ILE SEQRES 5 E 464 HIS LEU ASP ASN VAL THR GLU LYS PHE ASN MET TRP LYS SEQRES 6 E 464 ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE ILE SER SEQRES 7 E 464 LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU THR SEQRES 8 E 464 PRO LEU CYS VAL THR LEU HIS CYS THR ASN VAL THR SER SEQRES 9 E 464 VAL ASN THR THR GLY ASP ARG GLU GLY LEU LYS ASN CYS SEQRES 10 E 464 SER PHE ASN MET THR THR GLU LEU ARG ASP LYS ARG GLN SEQRES 11 E 464 LYS VAL TYR SER LEU PHE TYR ARG LEU ASP ILE VAL PRO SEQRES 12 E 464 ILE ASN GLU ASN GLN GLY SER GLU TYR ARG LEU ILE ASN SEQRES 13 E 464 CYS ASN THR SER ALA ILE THR GLN ALA CYS PRO LYS VAL SEQRES 14 E 464 SER PHE GLU PRO ILE PRO ILE HIS TYR CYS THR PRO ALA SEQRES 15 E 464 GLY PHE ALA ILE LEU LYS CYS LYS ASP GLU GLY PHE ASN SEQRES 16 E 464 GLY THR GLY LEU CYS LYS ASN VAL SER THR VAL GLN CYS SEQRES 17 E 464 THR HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU SEQRES 18 E 464 LEU ASN GLY SER LEU ALA GLU LYS ASN ILE ILE ILE ARG SEQRES 19 E 464 SER GLU ASN ILE THR ASN ASN ALA LYS ILE ILE ILE VAL SEQRES 20 E 464 GLN LEU VAL GLN PRO VAL THR ILE LYS CYS ILE ARG PRO SEQRES 21 E 464 ASN ASN ASN THR VAL LYS SER ILE ARG ILE GLY PRO GLY SEQRES 22 E 464 GLN ALA PHE TYR TYR THR GLY ASP ILE ILE GLY ASP ILE SEQRES 23 E 464 ARG GLN ALA HIS CYS ASN VAL THR ARG SER ARG TRP ASN SEQRES 24 E 464 LYS THR LEU GLN GLU VAL ALA GLU LYS LEU ARG THR TYR SEQRES 25 E 464 PHE GLY ASN LYS THR ILE ILE PHE ALA ASN SER SER GLY SEQRES 26 E 464 GLY ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY SEQRES 27 E 464 GLY GLU PHE PHE TYR CYS ASN THR SER GLY LEU PHE ASN SEQRES 28 E 464 SER THR TRP TYR VAL ASN SER THR TRP ASN ASP THR ASP SEQRES 29 E 464 SER THR GLN GLU SER ASN ASP THR ILE THR LEU PRO CYS SEQRES 30 E 464 ARG ILE LYS GLN ILE ILE ASN MET TRP GLN ARG ALA GLY SEQRES 31 E 464 GLN ALA MET TYR ALA PRO PRO ILE PRO GLY VAL ILE LYS SEQRES 32 E 464 CYS GLU SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP SEQRES 33 E 464 GLY GLY LYS ASP ASN ASN VAL ASN GLU THR PHE ARG PRO SEQRES 34 E 464 GLY GLY SER ASP MET ARG ASP ASN TRP ARG SER GLU LEU SEQRES 35 E 464 TYR LYS TYR LYS VAL VAL GLU ILE GLU PRO LEU GLY VAL SEQRES 36 E 464 ALA PRO THR ARG CYS LYS ARG ARG VAL SEQRES 1 F 142 LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET GLY ALA SEQRES 2 F 142 ALA SER ILE THR LEU THR VAL GLN ALA ARG ASN LEU LEU SEQRES 3 F 142 SER GLY ILE VAL GLN GLN GLN ASN ASN LEU LEU ARG ALA SEQRES 4 F 142 ILE GLU ALA GLN GLN HIS LEU LEU LYS LEU THR HIS TRP SEQRES 5 F 142 GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU SEQRES 6 F 142 HIS TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY SEQRES 7 F 142 CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL PRO TRP SEQRES 8 F 142 ASN SER SER TRP SER ASN LYS SER LEU ASP GLU ILE TRP SEQRES 9 F 142 ASN ASN MET THR TRP LEU GLN TRP ASP LYS GLU ILE ASN SEQRES 10 F 142 ASN TYR THR GLN LEU ILE TYR ARG LEU ILE GLU GLU SER SEQRES 11 F 142 GLN ASN GLN GLN GLU LYS ASN GLU LYS GLU LEU LEU SEQRES 1 G 142 LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET GLY ALA SEQRES 2 G 142 ALA SER ILE THR LEU THR VAL GLN ALA ARG ASN LEU LEU SEQRES 3 G 142 SER GLY ILE VAL GLN GLN GLN ASN ASN LEU LEU ARG ALA SEQRES 4 G 142 ILE GLU ALA GLN GLN HIS LEU LEU LYS LEU THR HIS TRP SEQRES 5 G 142 GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA VAL GLU SEQRES 6 G 142 HIS TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE TRP GLY SEQRES 7 G 142 CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL PRO TRP SEQRES 8 G 142 ASN SER SER TRP SER ASN LYS SER LEU ASP GLU ILE TRP SEQRES 9 G 142 ASN ASN MET THR TRP LEU GLN TRP ASP LYS GLU ILE ASN SEQRES 10 G 142 ASN TYR THR GLN LEU ILE TYR ARG LEU ILE GLU GLU SER SEQRES 11 G 142 GLN ASN GLN GLN GLU LYS ASN GLU LYS GLU LEU LEU SEQRES 1 H 131 GLN VAL THR LEU LYS GLU SER GLY PRO ALA LEU VAL LYS SEQRES 2 H 131 PRO THR GLN THR LEU THR LEU THR CYS THR PHE SER GLY SEQRES 3 H 131 PHE SER LEU SER THR SER GLY MET ALA VAL GLY TRP ILE SEQRES 4 H 131 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP LEU ALA ASN SEQRES 5 H 131 ILE TYR TRP ASP GLY ASP THR TYR TYR SER THR SER LEU SEQRES 6 H 131 LYS SER ARG LEU THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 H 131 GLN VAL ALA LEU LYS MET THR ASN MET ASP PRO VAL ASP SEQRES 8 H 131 THR ALA THR TYR PHE CYS ALA ARG GLY GLU GLU SER PHE SEQRES 9 H 131 TYR GLU ASP ASP TYS GLY GLN MET GLU TRP LEU HIS SER SEQRES 10 H 131 PHE ASP ALA TRP GLY GLN GLY LEU ARG VAL THR VAL SER SEQRES 11 H 131 SER SEQRES 1 L 107 ASP ILE GLN MET THR GLN SER PRO PRO SER LEU SER ALA SEQRES 2 L 107 SER ILE GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 107 GLN GLY ILE SER ASN TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 107 PRO GLY LYS ALA PRO LYS ARG LEU VAL TYR ASP ALA SER SEQRES 5 L 107 THR LEU GLN GLY GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 107 GLY SER GLY THR TYR PHE SER LEU THR ILE SER SER LEU SEQRES 7 L 107 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS LEU GLN HIS SEQRES 8 L 107 ASN SER HIS PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 L 107 ASP ILE LYS HET TYS H 100D 16 HET NAG D 1 14 HET NAG D 2 14 HET BMA D 3 11 HET MAN D 4 11 HET NAG I 1 14 HET NAG I 2 14 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 NAG M 1 14 HET NAG M 2 14 HET NAG N 1 14 HET NAG N 2 14 HET NAG O 1 14 HET NAG O 2 14 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 NAG R 1 14 HET NAG R 2 14 HET NAG S 1 14 HET NAG S 2 14 HET BMA S 3 11 HET NAG T 1 14 HET NAG T 2 14 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 NAG X 1 14 HET NAG X 2 14 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 NAG b 1 14 HET NAG b 2 14 HET NAG c 1 14 HET NAG c 2 14 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 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 MAN h 4 11 HET MAN h 5 11 HET NAG i 1 14 HET NAG i 2 14 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 NAG l 1 14 HET NAG l 2 14 HET BMA l 3 11 HET NAG m 1 14 HET NAG m 2 14 HET NAG n 1 14 HET NAG n 2 14 HET NAG o 1 14 HET NAG o 2 14 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 NAG r 1 14 HET NAG r 2 14 HET NAG s 1 14 HET NAG s 2 14 HET BMA s 3 11 HET NAG t 1 14 HET NAG t 2 14 HET NAG u 1 14 HET NAG u 2 14 HET BMA u 3 11 HET MAN u 4 11 HET MAN u 5 11 HET MAN u 6 11 HET NAG v 1 14 HET NAG v 2 14 HET NAG A 601 14 HET NAG A 602 14 HET NAG A 603 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG C 601 14 HET NAG C 602 14 HET NAG C 603 14 HET NAG C 604 14 HET NAG C 605 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG E 603 14 HET NAG E 604 14 HET NAG F 701 14 HET NAG F 702 14 HET NAG F 703 14 HET NAG G 701 14 HET NAG G 702 14 HET NAG G 703 14 HETNAM TYS O-SULFO-L-TYROSINE HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 7 TYS C9 H11 N O6 S FORMUL 9 NAG 100(C8 H15 N O6) FORMUL 9 BMA 14(C6 H12 O6) FORMUL 9 MAN 6(C6 H12 O6) HELIX 1 AA1 ALA A 70 CYS A 74 5 5 HELIX 2 AA2 ASN A 98 LYS A 117 1 20 HELIX 3 AA3 LEU A 122 CYS A 126 5 5 HELIX 4 AA4 ARG A 335 THR A 351 1 17 HELIX 5 AA5 ASP A 368 THR A 373 1 6 HELIX 6 AA6 THR A 387 LEU A 390 5 4 HELIX 7 AA7 MET A 475 TYR A 484 1 10 HELIX 8 AA8 THR B 529 SER B 534 1 6 HELIX 9 AA9 THR B 536 ASN B 543 1 8 HELIX 10 AB1 THR B 569 TRP B 596 1 28 HELIX 11 AB2 SER B 618 ASN B 625 1 8 HELIX 12 AB3 THR B 627 ILE B 635 1 9 HELIX 13 AB4 ILE B 635 LEU B 661 1 27 HELIX 14 AB5 ASN C 99 SER C 115 1 17 HELIX 15 AB6 LEU C 122 VAL C 127 5 6 HELIX 16 AB7 ARG C 335 PHE C 353 1 19 HELIX 17 AB8 ASP C 368 THR C 373 1 6 HELIX 18 AB9 ASN C 386 LEU C 390 5 5 HELIX 19 AC1 ASN C 425 ARG C 429 5 5 HELIX 20 AC2 MET C 475 SER C 481 1 7 HELIX 21 AC3 GLU C 482 TYR C 486 5 5 HELIX 22 AC4 ASN E 99 LYS E 117 1 19 HELIX 23 AC5 LEU E 122 VAL E 127 5 6 HELIX 24 AC6 ARG E 335 PHE E 353 1 19 HELIX 25 AC7 THR E 387 LEU E 390 5 4 HELIX 26 AC8 MET E 475 SER E 481 1 7 HELIX 27 AC9 THR F 529 SER F 534 1 6 HELIX 28 AD1 THR F 536 ASN F 543 1 8 HELIX 29 AD2 THR F 569 TRP F 596 1 28 HELIX 30 AD3 SER F 618 ASN F 625 1 8 HELIX 31 AD4 THR F 627 ILE F 635 1 9 HELIX 32 AD5 ILE F 635 LEU F 661 1 27 HELIX 33 AD6 THR G 529 SER G 534 1 6 HELIX 34 AD7 LEU G 537 LEU G 544 1 8 HELIX 35 AD8 THR G 569 TRP G 596 1 28 HELIX 36 AD9 SER G 618 ASN G 625 1 8 HELIX 37 AE1 THR G 627 ILE G 635 1 9 HELIX 38 AE2 TYR G 638 LEU G 661 1 24 HELIX 39 AE3 ASP H 83 THR H 87 5 5 HELIX 40 AE4 GLN L 79 PHE L 83 5 5 SHEET 1 AA1 3 GLY A 495 THR A 499 0 SHEET 2 AA1 3 TRP A 35 TYR A 39 -1 N TYR A 39 O GLY A 495 SHEET 3 AA1 3 ILE B 603 PRO B 609 -1 O VAL B 608 N VAL A 36 SHEET 1 AA2 5 TRP A 45 ASP A 47 0 SHEET 2 AA2 5 TYR A 486 ILE A 491 -1 O GLU A 490 N ARG 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 ILE A 84 LEU A 86 -1 N ILE A 84 O THR A 244 SHEET 1 AA3 2 GLU A 91 ASN A 94 0 SHEET 2 AA3 2 THR A 236 CYS A 239 -1 O GLY A 237 N PHE A 93 SHEET 1 AA4 5 ARG A 169 TYR A 177 0 SHEET 2 AA4 5 LEU A 154 THR A 162 -1 N MET A 161 O GLN A 170 SHEET 3 AA4 5 LEU A 129 ASN A 133 -1 N HIS A 130 O SER A 158 SHEET 4 AA4 5 GLU A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 5 AA4 5 ILE A 181 PRO A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA5 3 ALA A 200 GLN A 203 0 SHEET 2 AA5 3 GLN A 432 TYR A 435 1 O TYR A 435 N THR A 202 SHEET 3 AA5 3 ILE A 423 ILE A 424 -1 N ILE A 424 O MET A 434 SHEET 1 AA6 6 LEU A 260 LEU A 261 0 SHEET 2 AA6 6 ILE A 443 ASP A 457 -1 O GLY A 451 N LEU A 260 SHEET 3 AA6 6 ILE A 284 ARG A 298 -1 N ILE A 284 O LEU A 454 SHEET 4 AA6 6 ALA A 329 THR A 334 -1 O ASN A 332 N LYS A 295 SHEET 5 AA6 6 THR A 413 ILE A 420 -1 O ILE A 414 N VAL A 333 SHEET 6 AA6 6 PHE A 383 CYS A 385 -1 N TYR A 384 O ARG A 419 SHEET 1 AA7 6 ILE A 271 ARG A 273 0 SHEET 2 AA7 6 ILE A 284 ARG A 298 -1 O ILE A 285 N ARG A 273 SHEET 3 AA7 6 ILE A 443 ASP A 457 -1 O LEU A 454 N ILE A 284 SHEET 4 AA7 6 ASN A 465 PRO A 470 -1 O THR A 467 N ASP A 457 SHEET 5 AA7 6 THR A 358 PHE A 361 1 N ILE A 360 O PHE A 468 SHEET 6 AA7 6 SER A 393 TRP A 395 -1 O TRP A 395 N ILE A 359 SHEET 1 AA8 2 VAL A 304 ILE A 309 0 SHEET 2 AA8 2 GLN A 315 THR A 320 -1 O GLN A 315 N ILE A 309 SHEET 1 AA9 3 GLY C 495 THR C 499 0 SHEET 2 AA9 3 TRP C 35 TYR C 39 -1 N TRP C 35 O THR C 499 SHEET 3 AA9 3 ILE F 603 CYS F 604 -1 O CYS F 604 N VAL C 38 SHEET 1 AB1 5 TRP C 45 ARG C 46 0 SHEET 2 AB1 5 LYS C 487 ILE C 491 -1 O GLU C 490 N ARG C 46 SHEET 3 AB1 5 PHE C 223 LYS C 227 -1 N LEU C 226 O LYS C 487 SHEET 4 AB1 5 SER C 243 VAL C 245 -1 O SER C 243 N LYS C 227 SHEET 5 AB1 5 ILE C 84 HIS C 85 -1 N ILE C 84 O THR C 244 SHEET 1 AB2 2 PHE C 53 CYS C 54 0 SHEET 2 AB2 2 TYR C 217 CYS C 218 -1 O CYS C 218 N PHE C 53 SHEET 1 AB3 2 GLU C 91 PHE C 93 0 SHEET 2 AB3 2 GLY C 237 CYS C 239 -1 O GLY C 237 N PHE C 93 SHEET 1 AB4 5 ARG C 169 TYR C 177 0 SHEET 2 AB4 5 LEU C 154 THR C 162 -1 N MET C 161 O GLN C 170 SHEET 3 AB4 5 LEU C 129 ASN C 133 -1 N THR C 132 O ASN C 156 SHEET 4 AB4 5 GLU 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 ILE C 201 GLN C 203 0 SHEET 2 AB5 3 ALA C 433 TYR C 435 1 O TYR C 435 N THR C 202 SHEET 3 AB5 3 ILE C 423 ILE C 424 -1 N ILE C 424 O MET C 434 SHEET 1 AB6 6 LEU C 260 LEU C 261 0 SHEET 2 AB6 6 ILE C 443 ARG C 456 -1 O GLY C 451 N LEU C 260 SHEET 3 AB6 6 ILE C 284 ARG C 298 -1 N ILE C 284 O LEU C 454 SHEET 4 AB6 6 GLU C 466 PRO C 470 0 SHEET 5 AB6 6 ILE C 358 PHE C 361 1 N ILE C 359 O PHE C 468 SHEET 6 AB6 6 SER C 393 TRP C 395 -1 O SER C 393 N PHE C 361 SHEET 1 AB7 5 ILE C 271 ARG C 273 0 SHEET 2 AB7 5 ILE C 284 ARG C 298 -1 O GLN C 287 N ILE C 271 SHEET 3 AB7 5 ILE C 443 ARG C 456 -1 O LEU C 454 N ILE C 284 SHEET 4 AB7 5 ALA C 329 THR C 334 0 SHEET 5 AB7 5 THR C 413 CYS C 418 -1 O ILE C 414 N VAL C 333 SHEET 1 AB8 2 ASN C 301 GLY C 312 0 SHEET 2 AB8 2 GLN C 315 ILE C 323A-1 O PHE C 317 N ILE C 307 SHEET 1 AB9 2 HIS C 374 CYS C 378 0 SHEET 2 AB9 2 GLU C 381 CYS C 385 -1 O PHE C 383 N PHE C 376 SHEET 1 AC1 3 LEU E 494 THR E 499 0 SHEET 2 AC1 3 TRP E 35 TYR E 40 -1 N TYR E 39 O GLY E 495 SHEET 3 AC1 3 ILE G 603 PRO G 609 -1 O VAL G 608 N VAL E 36 SHEET 1 AC2 5 TRP E 45 ASP E 47 0 SHEET 2 AC2 5 TYR E 486 ILE E 491 -1 O GLU E 490 N ARG E 46 SHEET 3 AC2 5 PHE E 223 CYS E 228 -1 N LEU E 226 O LYS E 487 SHEET 4 AC2 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AC2 5 ILE E 84 HIS E 85 -1 N ILE E 84 O THR E 244 SHEET 1 AC3 2 PHE E 53 ALA E 55 0 SHEET 2 AC3 2 HIS E 216 CYS E 218 -1 O HIS E 216 N ALA E 55 SHEET 1 AC4 2 GLU E 91 ASN E 94 0 SHEET 2 AC4 2 THR E 236 CYS E 239 -1 O CYS E 239 N GLU E 91 SHEET 1 AC5 3 LEU E 129 HIS E 130 0 SHEET 2 AC5 3 GLU E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 3 AC5 3 ILE E 181 PRO E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC6 2 LEU E 154 THR E 162 0 SHEET 2 AC6 2 ARG E 169 TYR E 177 -1 O SER E 174 N CYS E 157 SHEET 1 AC7 3 ILE E 201 GLN E 203 0 SHEET 2 AC7 3 ALA E 433 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AC7 3 ILE E 423 ILE E 424 -1 N ILE E 424 O MET E 434 SHEET 1 AC8 7 LEU E 259 LEU E 261 0 SHEET 2 AC8 7 ILE E 443 ASP E 457 -1 O THR E 450 N LEU E 260 SHEET 3 AC8 7 ILE E 284 ARG E 298 -1 N ILE E 284 O LEU E 454 SHEET 4 AC8 7 ALA E 329 THR E 334 -1 O ASN E 332 N LYS E 295 SHEET 5 AC8 7 THR E 413 ILE E 420 -1 O ILE E 414 N VAL E 333 SHEET 6 AC8 7 PHE E 383 CYS E 385 -1 N TYR E 384 O ARG E 419 SHEET 7 AC8 7 HIS E 374 PHE E 376 -1 N HIS E 374 O CYS E 385 SHEET 1 AC9 6 ILE E 271 ARG E 273 0 SHEET 2 AC9 6 ILE E 284 ARG E 298 -1 O ILE E 285 N ARG E 273 SHEET 3 AC9 6 ILE E 443 ASP E 457 -1 O LEU E 454 N ILE E 284 SHEET 4 AC9 6 ASN E 465 ARG E 469 -1 O THR E 467 N ASP E 457 SHEET 5 AC9 6 THR E 358 PHE E 361 1 N ILE E 360 O GLU E 466 SHEET 6 AC9 6 SER E 393 TRP E 395 -1 O TRP E 395 N ILE E 359 SHEET 1 AD1 2 VAL E 304 ARG E 308 0 SHEET 2 AD1 2 ALA E 316 THR E 320 -1 O TYR E 319 N LYS E 305 SHEET 1 AD2 4 LEU H 4 SER H 7 0 SHEET 2 AD2 4 LEU H 18 PHE H 24 -1 O THR H 23 N LYS H 5 SHEET 3 AD2 4 GLN H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AD2 4 LEU H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AD3 4 LEU H 11 VAL H 12 0 SHEET 2 AD3 4 LEU H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AD3 4 ALA H 88 GLU H 100A-1 N TYR H 90 O LEU H 107 SHEET 4 AD3 4 GLN H 100F LEU H 100J-1 O MET H 100G N TYR H 100 SHEET 1 AD4 5 THR H 57 TYR H 59 0 SHEET 2 AD4 5 GLU H 46 ILE H 51 -1 N ASN H 50 O TYR H 58 SHEET 3 AD4 5 MET H 34 GLN H 39 -1 N VAL H 35A O ILE H 51 SHEET 4 AD4 5 ALA H 88 GLU H 100A-1 O ALA H 93 N GLY H 35B SHEET 5 AD4 5 ALA H 102 TRP H 103 -1 O ALA H 102 N ARG H 94 SHEET 1 AD5 4 MET L 4 SER L 7 0 SHEET 2 AD5 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AD5 4 TYR L 70 ILE L 75 -1 O PHE L 71 N CYS L 23 SHEET 4 AD5 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AD6 6 SER L 10 ALA L 13 0 SHEET 2 AD6 6 THR L 102 ILE L 106 1 O ASP L 105 N ALA L 13 SHEET 3 AD6 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AD6 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AD6 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AD6 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AD7 4 SER L 10 ALA L 13 0 SHEET 2 AD7 4 THR L 102 ILE L 106 1 O ASP L 105 N ALA L 13 SHEET 3 AD7 4 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AD7 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SSBOND 1 CYS A 54 CYS A 74 1555 1555 1.98 SSBOND 2 CYS A 119 CYS A 205 1555 1555 2.03 SSBOND 3 CYS A 126 CYS A 196 1555 1555 2.03 SSBOND 4 CYS A 131 CYS A 157 1555 1555 2.03 SSBOND 5 CYS A 218 CYS A 247 1555 1555 2.04 SSBOND 6 CYS A 228 CYS A 239 1555 1555 2.03 SSBOND 7 CYS A 296 CYS A 331 1555 1555 2.03 SSBOND 8 CYS A 378 CYS A 445 1555 1555 2.03 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 2.00 SSBOND 12 CYS C 119 CYS C 205 1555 1555 2.04 SSBOND 13 CYS C 126 CYS C 196 1555 1555 2.03 SSBOND 14 CYS C 131 CYS C 157 1555 1555 2.03 SSBOND 15 CYS C 218 CYS C 247 1555 1555 2.03 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 C 501 CYS F 605 1555 1555 2.03 SSBOND 21 CYS E 54 CYS E 74 1555 1555 2.04 SSBOND 22 CYS E 119 CYS E 205 1555 1555 2.02 SSBOND 23 CYS E 126 CYS E 196 1555 1555 2.02 SSBOND 24 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 25 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 26 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 27 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 28 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 29 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 30 CYS E 501 CYS G 605 1555 1555 2.03 SSBOND 31 CYS F 598 CYS F 604 1555 1555 2.03 SSBOND 32 CYS G 598 CYS G 604 1555 1555 2.03 SSBOND 33 CYS L 23 CYS L 88 1555 1555 2.04 LINK ND2 ASN A 88 C1 NAG A 603 1555 1555 1.44 LINK ND2 ASN A 133 C1 NAG R 1 1555 1555 1.44 LINK ND2 ASN A 156 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 160 C1 NAG U 1 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG J 1 1555 1555 1.43 LINK ND2 ASN A 241 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG S 1 1555 1555 1.44 LINK ND2 ASN A 276 C1 NAG K 1 1555 1555 1.44 LINK ND2 ASN A 301 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN A 332 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN A 339 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 363 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 392 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN A 448 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN A 465 C1 NAG M 1 1555 1555 1.44 LINK ND2 ASN B 611 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN B 625 C1 NAG B 702 1555 1555 1.45 LINK ND2 ASN B 637 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN C 88 C1 NAG C 604 1555 1555 1.44 LINK ND2 ASN C 133 C1 NAG C 605 1555 1555 1.44 LINK ND2 ASN C 156 C1 NAG X 1 1555 1555 1.44 LINK ND2 ASN C 160 C1 NAG h 1 1555 1555 1.44 LINK ND2 ASN C 197 C1 NAG g 1 1555 1555 1.44 LINK ND2 ASN C 234 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN C 241 C1 NAG Y 1 1555 1555 1.45 LINK ND2 ASN C 262 C1 NAG f 1 1555 1555 1.44 LINK ND2 ASN C 276 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN C 301 C1 NAG e 1 1555 1555 1.44 LINK ND2 ASN C 332 C1 NAG d 1 1555 1555 1.44 LINK ND2 ASN C 339 C1 NAG C 601 1555 1555 1.44 LINK ND2 ASN C 363 C1 NAG c 1 1555 1555 1.44 LINK ND2 ASN C 386 C1 NAG C 602 1555 1555 1.44 LINK ND2 ASN C 392 C1 NAG i 1 1555 1555 1.44 LINK ND2 ASN C 448 C1 NAG C 603 1555 1555 1.44 LINK ND2 ASN C 465 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN E 88 C1 NAG k 1 1555 1555 1.45 LINK ND2 ASN E 133 C1 NAG r 1 1555 1555 1.44 LINK ND2 ASN E 156 C1 NAG j 1 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG u 1 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG t 1 1555 1555 1.43 LINK ND2 ASN E 234 C1 NAG v 1 1555 1555 1.44 LINK ND2 ASN E 241 C1 NAG l 1 1555 1555 1.45 LINK ND2 ASN E 262 C1 NAG s 1 1555 1555 1.44 LINK ND2 ASN E 276 C1 NAG m 1 1555 1555 1.43 LINK ND2 ASN E 301 C1 NAG q 1 1555 1555 1.44 LINK ND2 ASN E 332 C1 NAG p 1 1555 1555 1.44 LINK ND2 ASN E 339 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 363 C1 NAG o 1 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 392 C1 NAG n 1 1555 1555 1.44 LINK ND2 ASN E 448 C1 NAG E 603 1555 1555 1.44 LINK ND2 ASN E 465 C1 NAG E 604 1555 1555 1.44 LINK ND2 ASN F 611 C1 NAG F 701 1555 1555 1.44 LINK ND2 ASN F 625 C1 NAG F 702 1555 1555 1.44 LINK ND2 ASN F 637 C1 NAG F 703 1555 1555 1.44 LINK ND2 ASN G 611 C1 NAG G 703 1555 1555 1.44 LINK ND2 ASN G 625 C1 NAG G 702 1555 1555 1.44 LINK ND2 ASN G 637 C1 NAG G 701 1555 1555 1.45 LINK C ASP H 100C N TYS H 100D 1555 1555 1.33 LINK C TYS H 100D N GLY H 100E 1555 1555 1.33 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.47 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.45 LINK O3 BMA D 3 C1 MAN D 4 1555 1555 1.46 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.39 LINK O4 NAG J 2 C1 BMA J 3 1555 1555 1.39 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.45 LINK O4 NAG P 2 C1 BMA P 3 1555 1555 1.45 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.45 LINK O4 NAG S 1 C1 NAG S 2 1555 1555 1.45 LINK O4 NAG S 2 C1 BMA S 3 1555 1555 1.45 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.46 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.45 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.44 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.46 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.45 LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.45 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 LINK O4 NAG Z 2 C1 BMA Z 3 1555 1555 1.45 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.45 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.45 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.44 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.45 LINK O4 NAG e 1 C1 NAG e 2 1555 1555 1.44 LINK O4 NAG f 1 C1 NAG f 2 1555 1555 1.45 LINK O4 NAG f 2 C1 BMA f 3 1555 1555 1.44 LINK O4 NAG g 1 C1 NAG g 2 1555 1555 1.44 LINK O4 NAG h 1 C1 NAG h 2 1555 1555 1.44 LINK O4 NAG h 2 C1 BMA h 3 1555 1555 1.45 LINK O3 BMA h 3 C1 MAN h 4 1555 1555 1.44 LINK O6 BMA h 3 C1 MAN h 5 1555 1555 1.46 LINK O4 NAG i 1 C1 NAG i 2 1555 1555 1.46 LINK O4 NAG j 1 C1 NAG j 2 1555 1555 1.45 LINK O4 NAG j 2 C1 BMA j 3 1555 1555 1.45 LINK O4 NAG k 1 C1 NAG k 2 1555 1555 1.48 LINK O4 NAG l 1 C1 NAG l 2 1555 1555 1.45 LINK O4 NAG l 2 C1 BMA l 3 1555 1555 1.45 LINK O4 NAG m 1 C1 NAG m 2 1555 1555 1.45 LINK O4 NAG n 1 C1 NAG n 2 1555 1555 1.46 LINK O4 NAG o 1 C1 NAG o 2 1555 1555 1.46 LINK O4 NAG p 1 C1 NAG p 2 1555 1555 1.44 LINK O4 NAG p 2 C1 BMA p 3 1555 1555 1.45 LINK O4 NAG q 1 C1 NAG q 2 1555 1555 1.44 LINK O4 NAG r 1 C1 NAG r 2 1555 1555 1.46 LINK O4 NAG s 1 C1 NAG s 2 1555 1555 1.45 LINK O4 NAG s 2 C1 BMA s 3 1555 1555 1.45 LINK O4 NAG t 1 C1 NAG t 2 1555 1555 1.45 LINK O4 NAG u 1 C1 NAG u 2 1555 1555 1.44 LINK O4 NAG u 2 C1 BMA u 3 1555 1555 1.47 LINK O3 BMA u 3 C1 MAN u 4 1555 1555 1.46 LINK O6 BMA u 3 C1 MAN u 6 1555 1555 1.46 LINK O2 MAN u 4 C1 MAN u 5 1555 1555 1.45 LINK O4 NAG v 1 C1 NAG v 2 1555 1555 1.44 CISPEP 1 SER L 7 PRO L 8 0 -1.72 CISPEP 2 HIS L 94 PRO L 95 0 -0.78 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000