HEADER VIRAL PROTEIN/IMMUNE SYSTEM 20-DEC-21 7T9T TITLE CRYO-EM STRUCTURE OF CH235.12 IN COMPLEX WITH HIV-1 ENV TRIMER TITLE 2 CH505TF.N279K.SOSIP.664 WITH COMPLEX GLYCANS COMPND MOL_ID: 1; COMPND 2 MOLECULE: ENVELOPE GLYCOPROTEIN GP160; COMPND 3 CHAIN: A, E, I; 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, J; COMPND 9 SYNONYM: TRANSMEMBRANE PROTEIN GP41, TM, GP41; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: CH235.12 FAB HEAVY CHAIN; COMPND 13 CHAIN: C, G, K; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: CH235.12 FAB LIGHT CHAIN; COMPND 17 CHAIN: D, H, 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: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; 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: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 27 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX, CH235.12, IMMUNE SYSTEM, KEYWDS 2 COMPLEX GLYCANS, CH505TF, SOSIP EXPDTA ELECTRON MICROSCOPY AUTHOR K.MANNE,P.ACHARYA JRNL AUTH K.MANNE JRNL TITL CRYO-EM STRUCTURE OF CH235.12 IN COMPLEX WITH HIV-1 ENV JRNL TITL 2 TRIMER CH505TF.N279K.G458Y.SOSIP.664 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : LATITUDE, CRYOSPARC, UCSF CHIMERA, REMARK 3 COOT, ROSETTAEM, COOT, PHENIX, ISOLDE, REMARK 3 CRYOSPARC, CRYOSPARC, CRYOSPARC, REMARK 3 CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6UDA REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : AB INITIO MODEL 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) : 3.700 REMARK 3 NUMBER OF PARTICLES : 53398 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 7T9T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000261896. 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 : TRIMERIC HIV-1 ENV IN COMPLEX REMARK 245 WITH CH235.12 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : BLOT FOR 2.5 S BEFORE PLUNGING REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 750.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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) : 65.94 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: DODECAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, REMARK 350 AND CHAINS: K, L, a, b, c, d, M, N, O, REMARK 350 AND CHAINS: P, Q, R, S, T, U, V, W, X, Y, REMARK 350 AND CHAINS: Z 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 63 REMARK 465 LYS A 64 REMARK 465 VAL A 65 REMARK 465 HIS A 66 REMARK 465 ASN A 67 REMARK 465 VAL A 68 REMARK 465 TRP A 69 REMARK 465 ALA A 70 REMARK 465 LYS A 155 REMARK 465 ASN A 156 REMARK 465 GLY A 312 REMARK 465 PRO A 313 REMARK 465 SER A 399 REMARK 465 THR A 400 REMARK 465 ASP A 401 REMARK 465 MET A 402 REMARK 465 ALA A 403 REMARK 465 ASN A 404 REMARK 465 SER A 405 REMARK 465 THR A 406 REMARK 465 GLU A 407 REMARK 465 THR A 408 REMARK 465 GLY B 505 REMARK 465 ARG B 506 REMARK 465 ARG B 507 REMARK 465 ARG B 508 REMARK 465 ARG B 509 REMARK 465 ARG B 510 REMARK 465 ARG B 511 REMARK 465 ALA B 512 REMARK 465 VAL B 513 REMARK 465 GLY B 514 REMARK 465 ILE B 515 REMARK 465 GLY B 516 REMARK 465 ALA B 517 REMARK 465 GLY B 547 REMARK 465 ILE B 548 REMARK 465 VAL B 549 REMARK 465 GLN B 550 REMARK 465 GLN B 551 REMARK 465 GLN B 552 REMARK 465 SER B 553 REMARK 465 ASN B 554 REMARK 465 LEU B 555 REMARK 465 LEU B 556 REMARK 465 ARG B 557 REMARK 465 ALA B 558 REMARK 465 PRO B 559 REMARK 465 GLU B 560 REMARK 465 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 LEU B 568 REMARK 465 THR B 569 REMARK 465 VAL B 570 REMARK 465 TRP B 571 REMARK 465 LYS C 129 REMARK 465 SER C 130 REMARK 465 THR C 131 REMARK 465 SER C 132 REMARK 465 GLY C 133 REMARK 465 GLU D 213 REMARK 465 CYS D 214 REMARK 465 LYS E 63 REMARK 465 LYS E 64 REMARK 465 VAL E 65 REMARK 465 HIS E 66 REMARK 465 ASN E 67 REMARK 465 VAL E 68 REMARK 465 TRP E 69 REMARK 465 ALA E 70 REMARK 465 MET E 154 REMARK 465 LYS E 155 REMARK 465 ASN E 156 REMARK 465 GLY E 312 REMARK 465 SER E 399 REMARK 465 THR E 400 REMARK 465 ASP E 401 REMARK 465 MET E 402 REMARK 465 ALA E 403 REMARK 465 ASN E 404 REMARK 465 SER E 405 REMARK 465 THR E 406 REMARK 465 GLU E 407 REMARK 465 THR E 408 REMARK 465 GLY F 505 REMARK 465 ARG F 506 REMARK 465 ARG F 507 REMARK 465 ARG F 508 REMARK 465 ARG F 509 REMARK 465 ARG F 510 REMARK 465 ARG F 511 REMARK 465 ALA F 512 REMARK 465 VAL F 513 REMARK 465 GLY F 514 REMARK 465 ILE F 515 REMARK 465 GLY F 516 REMARK 465 ALA F 517 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 SER F 553 REMARK 465 ASN F 554 REMARK 465 LEU F 555 REMARK 465 LEU F 556 REMARK 465 ARG F 557 REMARK 465 ALA F 558 REMARK 465 PRO F 559 REMARK 465 GLU F 560 REMARK 465 ALA F 561 REMARK 465 GLN F 562 REMARK 465 GLN F 563 REMARK 465 HIS F 564 REMARK 465 LEU F 565 REMARK 465 LEU F 566 REMARK 465 LYS F 567 REMARK 465 LEU F 568 REMARK 465 THR F 569 REMARK 465 VAL F 570 REMARK 465 TRP F 571 REMARK 465 LYS G 129 REMARK 465 SER G 130 REMARK 465 THR G 131 REMARK 465 SER G 132 REMARK 465 GLY G 133 REMARK 465 GLU H 213 REMARK 465 CYS H 214 REMARK 465 LYS I 63 REMARK 465 LYS I 64 REMARK 465 VAL I 65 REMARK 465 HIS I 66 REMARK 465 ASN I 67 REMARK 465 VAL I 68 REMARK 465 TRP I 69 REMARK 465 ALA I 70 REMARK 465 LYS I 155 REMARK 465 ASN I 156 REMARK 465 GLY I 312 REMARK 465 PRO I 313 REMARK 465 SER I 399 REMARK 465 THR I 400 REMARK 465 ASP I 401 REMARK 465 MET I 402 REMARK 465 ALA I 403 REMARK 465 ASN I 404 REMARK 465 SER I 405 REMARK 465 THR I 406 REMARK 465 GLU I 407 REMARK 465 THR I 408 REMARK 465 GLY J 505 REMARK 465 ARG J 506 REMARK 465 ARG J 507 REMARK 465 ARG J 508 REMARK 465 ARG J 509 REMARK 465 ARG J 510 REMARK 465 ARG J 511 REMARK 465 ALA J 512 REMARK 465 VAL J 513 REMARK 465 GLY J 514 REMARK 465 ILE J 515 REMARK 465 GLY J 516 REMARK 465 ALA J 517 REMARK 465 GLY J 547 REMARK 465 ILE J 548 REMARK 465 VAL J 549 REMARK 465 GLN J 550 REMARK 465 GLN J 551 REMARK 465 GLN J 552 REMARK 465 SER J 553 REMARK 465 ASN J 554 REMARK 465 LEU J 555 REMARK 465 LEU J 556 REMARK 465 ARG J 557 REMARK 465 ALA J 558 REMARK 465 PRO J 559 REMARK 465 GLU J 560 REMARK 465 ALA J 561 REMARK 465 GLN J 562 REMARK 465 GLN J 563 REMARK 465 HIS J 564 REMARK 465 LEU J 565 REMARK 465 LEU J 566 REMARK 465 LYS J 567 REMARK 465 LEU J 568 REMARK 465 THR J 569 REMARK 465 VAL J 570 REMARK 465 TRP J 571 REMARK 465 LYS K 129 REMARK 465 SER K 130 REMARK 465 THR K 131 REMARK 465 SER K 132 REMARK 465 GLY K 133 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 TRP A 316 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 316 CZ3 CH2 REMARK 470 TRP E 316 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP E 316 CZ3 CH2 REMARK 470 TRP I 316 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP I 316 CZ3 CH2 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 O ASN B 625 OG1 THR B 627 2.04 REMARK 500 OG1 THR I 37 O CYS J 604 2.16 REMARK 500 OH TYR G 84 O GLN G 171 2.19 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 ASP A 57 -165.63 -79.92 REMARK 500 ASP A 78 85.62 -153.98 REMARK 500 LEU A 122 34.73 -96.92 REMARK 500 THR A 135 52.65 -95.59 REMARK 500 ILE A 142 -55.64 -120.04 REMARK 500 GLU A 143 -9.89 72.43 REMARK 500 LEU A 165 -17.46 -140.45 REMARK 500 PRO A 212 76.79 -68.66 REMARK 500 THR A 234 50.64 -91.77 REMARK 500 GLN A 258 -9.32 74.63 REMARK 500 LEU A 259 148.47 -177.97 REMARK 500 PHE A 376 -178.21 -171.62 REMARK 500 ASN A 461 72.97 60.74 REMARK 500 ASN A 462 32.50 78.80 REMARK 500 GLU A 490 73.11 -111.44 REMARK 500 LYS B 574 36.17 -95.05 REMARK 500 SER B 615 -10.20 76.34 REMARK 500 ASN B 616 16.56 53.50 REMARK 500 MET B 626 -126.85 49.00 REMARK 500 LYS C 214 58.24 -95.12 REMARK 500 ARG D 30 -134.15 57.43 REMARK 500 LYS D 39 -168.10 -78.17 REMARK 500 ALA D 51 -8.50 73.13 REMARK 500 SER D 52 -17.12 -140.34 REMARK 500 TYR D 91 24.23 -141.63 REMARK 500 ASP D 170 15.27 -140.30 REMARK 500 ASP E 57 -165.79 -79.32 REMARK 500 LEU E 122 33.25 -97.12 REMARK 500 THR E 163 -166.92 -79.70 REMARK 500 HIS E 249 -178.42 -69.50 REMARK 500 GLN E 258 -10.29 74.65 REMARK 500 LEU E 259 148.36 -179.39 REMARK 500 TRP E 427 -36.94 -39.88 REMARK 500 ASN E 461 73.18 60.32 REMARK 500 ASN E 462 32.82 78.22 REMARK 500 GLU E 490 73.21 -112.78 REMARK 500 PHE F 522 -105.39 52.30 REMARK 500 LYS F 574 36.48 -94.88 REMARK 500 SER F 613 -13.18 80.46 REMARK 500 ASN F 616 34.39 -98.10 REMARK 500 SER G 25 -97.79 -157.04 REMARK 500 ARG H 30 -134.56 55.55 REMARK 500 LYS H 39 -168.01 -78.35 REMARK 500 ALA H 51 -8.53 72.70 REMARK 500 SER H 52 -16.77 -140.48 REMARK 500 ASP H 170 15.09 -140.48 REMARK 500 PRO H 204 79.22 -69.38 REMARK 500 TYR I 61 27.19 48.81 REMARK 500 LEU I 122 32.23 -96.12 REMARK 500 THR I 132 -52.28 -120.50 REMARK 500 REMARK 500 THIS ENTRY HAS 66 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 7T9S RELATED DB: PDB REMARK 900 CRYO-EM STRUCTURE OF CH235.12 IN COMPLEX WITH HIV-1 ENV TRIMER REMARK 900 CH505TF.N279K.G458Y.SOSIP.664 WITH COMPLEX GLYCANS REMARK 900 RELATED ID: EMD-25767 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF CH235.12 IN COMPLEX WITH HIV-1 ENV TRIMER REMARK 900 CH505TF.N279K.SOSIP.664 WITH COMPLEX GLYCANS DBREF 7T9T A 35 503 UNP M4M0W3 M4M0W3_9HIV1 31 488 DBREF 7T9T B 511 664 UNP Q2N0S5 Q2N0S5_9HIV1 508 661 DBREF 7T9T C 1 216 PDB 7T9T 7T9T 1 216 DBREF 7T9T D 1 214 PDB 7T9T 7T9T 1 214 DBREF 7T9T E 35 503 UNP M4M0W3 M4M0W3_9HIV1 31 488 DBREF 7T9T F 511 664 UNP Q2N0S5 Q2N0S5_9HIV1 508 661 DBREF 7T9T G 1 216 PDB 7T9T 7T9T 1 216 DBREF 7T9T H 1 214 PDB 7T9T 7T9T 1 214 DBREF 7T9T I 35 503 UNP M4M0W3 M4M0W3_9HIV1 31 488 DBREF 7T9T J 511 664 UNP Q2N0S5 Q2N0S5_9HIV1 508 661 DBREF 7T9T K 1 216 PDB 7T9T 7T9T 1 216 DBREF 7T9T L 1 214 PDB 7T9T 7T9T 1 214 SEQADV 7T9T GLU A 32 UNP M4M0W3 EXPRESSION TAG SEQADV 7T9T ASN A 33 UNP M4M0W3 EXPRESSION TAG SEQADV 7T9T LEU A 34 UNP M4M0W3 EXPRESSION TAG SEQADV 7T9T LYS A 64 UNP M4M0W3 GLU 60 CONFLICT SEQADV 7T9T TRP A 316 UNP M4M0W3 ALA 301 CONFLICT SEQADV 7T9T LYS A 488 UNP M4M0W3 GLU 473 CONFLICT SEQADV 7T9T ILE A 489 UNP M4M0W3 VAL 474 CONFLICT SEQADV 7T9T GLU A 490 UNP M4M0W3 LYS 475 CONFLICT SEQADV 7T9T ARG A 498 UNP M4M0W3 ASN 483 CONFLICT SEQADV 7T9T CYS A 499 UNP M4M0W3 ALA 484 CONFLICT SEQADV 7T9T LYS A 500 UNP M4M0W3 ARG 485 CONFLICT SEQADV 7T9T GLY B 505 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG B 506 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG B 507 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG B 508 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG B 509 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG B 510 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T PRO B 559 UNP Q2N0S5 ILE 556 CONFLICT SEQADV 7T9T CYS B 605 UNP Q2N0S5 THR 602 CONFLICT SEQADV 7T9T GLU E 32 UNP M4M0W3 EXPRESSION TAG SEQADV 7T9T ASN E 33 UNP M4M0W3 EXPRESSION TAG SEQADV 7T9T LEU E 34 UNP M4M0W3 EXPRESSION TAG SEQADV 7T9T LYS E 64 UNP M4M0W3 GLU 60 CONFLICT SEQADV 7T9T TRP E 316 UNP M4M0W3 ALA 301 CONFLICT SEQADV 7T9T LYS E 488 UNP M4M0W3 GLU 473 CONFLICT SEQADV 7T9T ILE E 489 UNP M4M0W3 VAL 474 CONFLICT SEQADV 7T9T GLU E 490 UNP M4M0W3 LYS 475 CONFLICT SEQADV 7T9T ARG E 498 UNP M4M0W3 ASN 483 CONFLICT SEQADV 7T9T CYS E 499 UNP M4M0W3 ALA 484 CONFLICT SEQADV 7T9T LYS E 500 UNP M4M0W3 ARG 485 CONFLICT SEQADV 7T9T GLY F 505 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG F 506 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG F 507 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG F 508 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG F 509 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG F 510 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T PRO F 559 UNP Q2N0S5 ILE 556 CONFLICT SEQADV 7T9T CYS F 605 UNP Q2N0S5 THR 602 CONFLICT SEQADV 7T9T GLU I 32 UNP M4M0W3 EXPRESSION TAG SEQADV 7T9T ASN I 33 UNP M4M0W3 EXPRESSION TAG SEQADV 7T9T LEU I 34 UNP M4M0W3 EXPRESSION TAG SEQADV 7T9T LYS I 64 UNP M4M0W3 GLU 60 CONFLICT SEQADV 7T9T TRP I 316 UNP M4M0W3 ALA 301 CONFLICT SEQADV 7T9T LYS I 488 UNP M4M0W3 GLU 473 CONFLICT SEQADV 7T9T ILE I 489 UNP M4M0W3 VAL 474 CONFLICT SEQADV 7T9T GLU I 490 UNP M4M0W3 LYS 475 CONFLICT SEQADV 7T9T ARG I 498 UNP M4M0W3 ASN 483 CONFLICT SEQADV 7T9T CYS I 499 UNP M4M0W3 ALA 484 CONFLICT SEQADV 7T9T LYS I 500 UNP M4M0W3 ARG 485 CONFLICT SEQADV 7T9T GLY J 505 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG J 506 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG J 507 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG J 508 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG J 509 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T ARG J 510 UNP Q2N0S5 EXPRESSION TAG SEQADV 7T9T PRO J 559 UNP Q2N0S5 ILE 556 CONFLICT SEQADV 7T9T CYS J 605 UNP Q2N0S5 THR 602 CONFLICT SEQRES 1 A 461 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 A 461 TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER ASP SEQRES 3 A 461 ALA LYS ALA TYR GLU LYS LYS VAL HIS ASN VAL TRP ALA SEQRES 4 A 461 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 5 A 461 MET VAL LEU LYS ASN VAL THR GLU ASN PHE ASN MET TRP SEQRES 6 A 461 LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP VAL ILE SEQRES 7 A 461 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 A 461 THR PRO LEU CYS VAL THR LEU ASN CYS THR ASN ALA THR SEQRES 9 A 461 ALA SER ASN SER SER ILE ILE GLU GLY MET LYS ASN CYS SEQRES 10 A 461 SER PHE ASN ILE THR THR GLU LEU ARG ASP LYS ARG GLU SEQRES 11 A 461 LYS LYS ASN ALA LEU PHE TYR LYS LEU ASP ILE VAL GLN SEQRES 12 A 461 LEU ASP GLY ASN SER SER GLN TYR ARG LEU ILE ASN CYS SEQRES 13 A 461 ASN THR SER VAL ILE THR GLN ALA CYS PRO LYS VAL SER SEQRES 14 A 461 PHE ASP PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY SEQRES 15 A 461 TYR ALA ILE LEU LYS CYS ASN ASN LYS THR PHE THR GLY SEQRES 16 A 461 THR GLY PRO CYS ASN ASN VAL SER THR VAL GLN CYS THR SEQRES 17 A 461 HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU SEQRES 18 A 461 ASN GLY SER LEU ALA GLU GLY GLU ILE ILE ILE ARG SER SEQRES 19 A 461 GLU ASN ILE THR LYS ASN VAL LYS THR ILE ILE VAL HIS SEQRES 20 A 461 LEU ASN GLU SER VAL LYS ILE GLU CYS THR ARG PRO ASN SEQRES 21 A 461 ASN LYS THR ARG THR SER ILE ARG ILE GLY PRO GLY GLN SEQRES 22 A 461 TRP PHE TYR ALA THR GLY GLN VAL ILE GLY ASP ILE ARG SEQRES 23 A 461 GLU ALA TYR CYS ASN ILE ASN GLU SER LYS TRP ASN GLU SEQRES 24 A 461 THR LEU GLN ARG VAL SER LYS LYS LEU LYS GLU TYR PHE SEQRES 25 A 461 PRO HIS LYS ASN ILE THR PHE GLN PRO SER SER GLY GLY SEQRES 26 A 461 ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 27 A 461 GLU PHE PHE TYR CYS ASN THR SER SER LEU PHE ASN ARG SEQRES 28 A 461 THR TYR MET ALA ASN SER THR ASP MET ALA ASN SER THR SEQRES 29 A 461 GLU THR ASN SER THR ARG THR ILE THR ILE HIS CYS ARG SEQRES 30 A 461 ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL GLY ARG SEQRES 31 A 461 ALA MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS SEQRES 32 A 461 ILE SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY SEQRES 33 A 461 GLY LYS ASN ASN THR GLU THR PHE ARG PRO GLY GLY GLY SEQRES 34 A 461 ASN MET LYS ASP ASN TRP ARG SER GLU LEU TYR LYS TYR SEQRES 35 A 461 LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR SEQRES 36 A 461 ARG CYS LYS ARG ARG VAL SEQRES 1 B 160 GLY ARG ARG ARG ARG ARG ARG ALA VAL GLY ILE GLY ALA SEQRES 2 B 160 VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET SEQRES 3 B 160 GLY ALA ALA SER MET THR LEU THR VAL GLN ALA ARG ASN SEQRES 4 B 160 LEU LEU SER GLY ILE VAL GLN GLN GLN SER ASN LEU LEU SEQRES 5 B 160 ARG ALA PRO GLU ALA GLN GLN HIS LEU LEU LYS LEU THR SEQRES 6 B 160 VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA SEQRES 7 B 160 VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE SEQRES 8 B 160 TRP GLY CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL SEQRES 9 B 160 PRO TRP ASN SER SER TRP SER ASN ARG ASN LEU SER GLU SEQRES 10 B 160 ILE TRP ASP ASN MET THR TRP LEU GLN TRP ASP LYS GLU SEQRES 11 B 160 ILE SER ASN TYR THR GLN ILE ILE TYR GLY LEU LEU GLU SEQRES 12 B 160 GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU SEQRES 13 B 160 LEU ALA LEU ASP SEQRES 1 C 225 GLN VAL ARG LEU ALA GLN TYR GLY GLY GLY VAL LYS ARG SEQRES 2 C 225 LEU GLY ALA THR MET THR LEU SER CYS VAL ALA SER GLY SEQRES 3 C 225 TYR THR PHE ASN ASP TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 C 225 ALA PRO GLY GLN GLY PHE GLU LEU LEU GLY TYR ILE ASP SEQRES 5 C 225 PRO ALA ASN GLY ARG PRO ASP TYR ALA GLY ALA LEU ARG SEQRES 6 C 225 GLU ARG LEU SER PHE TYR ARG ASP LYS SER MET GLU THR SEQRES 7 C 225 LEU TYR MET ASP LEU ARG SER LEU ARG TYR ASP ASP THR SEQRES 8 C 225 ALA MET TYR TYR CYS VAL ARG ASN VAL GLY THR ALA GLY SEQRES 9 C 225 SER LEU LEU HIS TYR ASP HIS TRP GLY SER GLY SER PRO SEQRES 10 C 225 VAL ILE VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 C 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 C 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 C 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 C 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 C 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 C 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 C 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 C 225 PRO LYS SER CYS SEQRES 1 D 213 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER ALA SEQRES 2 D 213 SER PRO GLY GLU ARG VAL THR LEU THR CYS ARG ALA SER SEQRES 3 D 213 ARG SER VAL ARG ASN ASN VAL ALA TRP TYR GLN HIS LYS SEQRES 4 D 213 GLY GLY GLN SER PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 D 213 THR ARG ALA ALA GLY VAL PRO ALA ARG PHE SER GLY SER SEQRES 6 D 213 ALA SER GLY THR GLU PHE THR LEU ALA ILE SER ASN LEU SEQRES 7 D 213 GLU SER GLU ASP PHE THR VAL TYR PHE CYS LEU GLN TYR SEQRES 8 D 213 ASN ASN TRP TRP THR PHE GLY GLN GLY THR ARG VAL ASP SEQRES 9 D 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 D 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 D 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 D 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 D 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 D 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 D 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 D 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 D 213 ASN ARG GLY GLU CYS SEQRES 1 E 461 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 E 461 TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER ASP SEQRES 3 E 461 ALA LYS ALA TYR GLU LYS LYS VAL HIS ASN VAL TRP ALA SEQRES 4 E 461 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 5 E 461 MET VAL LEU LYS ASN VAL THR GLU ASN PHE ASN MET TRP SEQRES 6 E 461 LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP VAL ILE SEQRES 7 E 461 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 E 461 THR PRO LEU CYS VAL THR LEU ASN CYS THR ASN ALA THR SEQRES 9 E 461 ALA SER ASN SER SER ILE ILE GLU GLY MET LYS ASN CYS SEQRES 10 E 461 SER PHE ASN ILE THR THR GLU LEU ARG ASP LYS ARG GLU SEQRES 11 E 461 LYS LYS ASN ALA LEU PHE TYR LYS LEU ASP ILE VAL GLN SEQRES 12 E 461 LEU ASP GLY ASN SER SER GLN TYR ARG LEU ILE ASN CYS SEQRES 13 E 461 ASN THR SER VAL ILE THR GLN ALA CYS PRO LYS VAL SER SEQRES 14 E 461 PHE ASP PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY SEQRES 15 E 461 TYR ALA ILE LEU LYS CYS ASN ASN LYS THR PHE THR GLY SEQRES 16 E 461 THR GLY PRO CYS ASN ASN VAL SER THR VAL GLN CYS THR SEQRES 17 E 461 HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU SEQRES 18 E 461 ASN GLY SER LEU ALA GLU GLY GLU ILE ILE ILE ARG SER SEQRES 19 E 461 GLU ASN ILE THR LYS ASN VAL LYS THR ILE ILE VAL HIS SEQRES 20 E 461 LEU ASN GLU SER VAL LYS ILE GLU CYS THR ARG PRO ASN SEQRES 21 E 461 ASN LYS THR ARG THR SER ILE ARG ILE GLY PRO GLY GLN SEQRES 22 E 461 TRP PHE TYR ALA THR GLY GLN VAL ILE GLY ASP ILE ARG SEQRES 23 E 461 GLU ALA TYR CYS ASN ILE ASN GLU SER LYS TRP ASN GLU SEQRES 24 E 461 THR LEU GLN ARG VAL SER LYS LYS LEU LYS GLU TYR PHE SEQRES 25 E 461 PRO HIS LYS ASN ILE THR PHE GLN PRO SER SER GLY GLY SEQRES 26 E 461 ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 27 E 461 GLU PHE PHE TYR CYS ASN THR SER SER LEU PHE ASN ARG SEQRES 28 E 461 THR TYR MET ALA ASN SER THR ASP MET ALA ASN SER THR SEQRES 29 E 461 GLU THR ASN SER THR ARG THR ILE THR ILE HIS CYS ARG SEQRES 30 E 461 ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL GLY ARG SEQRES 31 E 461 ALA MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS SEQRES 32 E 461 ILE SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY SEQRES 33 E 461 GLY LYS ASN ASN THR GLU THR PHE ARG PRO GLY GLY GLY SEQRES 34 E 461 ASN MET LYS ASP ASN TRP ARG SER GLU LEU TYR LYS TYR SEQRES 35 E 461 LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR SEQRES 36 E 461 ARG CYS LYS ARG ARG VAL SEQRES 1 F 160 GLY ARG ARG ARG ARG ARG ARG ALA VAL GLY ILE GLY ALA SEQRES 2 F 160 VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET SEQRES 3 F 160 GLY ALA ALA SER MET THR LEU THR VAL GLN ALA ARG ASN SEQRES 4 F 160 LEU LEU SER GLY ILE VAL GLN GLN GLN SER ASN LEU LEU SEQRES 5 F 160 ARG ALA PRO GLU ALA GLN GLN HIS LEU LEU LYS LEU THR SEQRES 6 F 160 VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA SEQRES 7 F 160 VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE SEQRES 8 F 160 TRP GLY CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL SEQRES 9 F 160 PRO TRP ASN SER SER TRP SER ASN ARG ASN LEU SER GLU SEQRES 10 F 160 ILE TRP ASP ASN MET THR TRP LEU GLN TRP ASP LYS GLU SEQRES 11 F 160 ILE SER ASN TYR THR GLN ILE ILE TYR GLY LEU LEU GLU SEQRES 12 F 160 GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU SEQRES 13 F 160 LEU ALA LEU ASP SEQRES 1 G 225 GLN VAL ARG LEU ALA GLN TYR GLY GLY GLY VAL LYS ARG SEQRES 2 G 225 LEU GLY ALA THR MET THR LEU SER CYS VAL ALA SER GLY SEQRES 3 G 225 TYR THR PHE ASN ASP TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 G 225 ALA PRO GLY GLN GLY PHE GLU LEU LEU GLY TYR ILE ASP SEQRES 5 G 225 PRO ALA ASN GLY ARG PRO ASP TYR ALA GLY ALA LEU ARG SEQRES 6 G 225 GLU ARG LEU SER PHE TYR ARG ASP LYS SER MET GLU THR SEQRES 7 G 225 LEU TYR MET ASP LEU ARG SER LEU ARG TYR ASP ASP THR SEQRES 8 G 225 ALA MET TYR TYR CYS VAL ARG ASN VAL GLY THR ALA GLY SEQRES 9 G 225 SER LEU LEU HIS TYR ASP HIS TRP GLY SER GLY SER PRO SEQRES 10 G 225 VAL ILE VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 G 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 G 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 G 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 G 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 G 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 G 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 G 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 G 225 PRO LYS SER CYS SEQRES 1 H 213 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER ALA SEQRES 2 H 213 SER PRO GLY GLU ARG VAL THR LEU THR CYS ARG ALA SER SEQRES 3 H 213 ARG SER VAL ARG ASN ASN VAL ALA TRP TYR GLN HIS LYS SEQRES 4 H 213 GLY GLY GLN SER PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 H 213 THR ARG ALA ALA GLY VAL PRO ALA ARG PHE SER GLY SER SEQRES 6 H 213 ALA SER GLY THR GLU PHE THR LEU ALA ILE SER ASN LEU SEQRES 7 H 213 GLU SER GLU ASP PHE THR VAL TYR PHE CYS LEU GLN TYR SEQRES 8 H 213 ASN ASN TRP TRP THR PHE GLY GLN GLY THR ARG VAL ASP SEQRES 9 H 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 H 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 H 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 H 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 H 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 H 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 H 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 H 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 H 213 ASN ARG GLY GLU CYS SEQRES 1 I 461 GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL SEQRES 2 I 461 TRP LYS GLU ALA LYS THR THR LEU PHE CYS ALA SER ASP SEQRES 3 I 461 ALA LYS ALA TYR GLU LYS LYS VAL HIS ASN VAL TRP ALA SEQRES 4 I 461 THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU SEQRES 5 I 461 MET VAL LEU LYS ASN VAL THR GLU ASN PHE ASN MET TRP SEQRES 6 I 461 LYS ASN ASP MET VAL ASP GLN MET HIS GLU ASP VAL ILE SEQRES 7 I 461 SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU SEQRES 8 I 461 THR PRO LEU CYS VAL THR LEU ASN CYS THR ASN ALA THR SEQRES 9 I 461 ALA SER ASN SER SER ILE ILE GLU GLY MET LYS ASN CYS SEQRES 10 I 461 SER PHE ASN ILE THR THR GLU LEU ARG ASP LYS ARG GLU SEQRES 11 I 461 LYS LYS ASN ALA LEU PHE TYR LYS LEU ASP ILE VAL GLN SEQRES 12 I 461 LEU ASP GLY ASN SER SER GLN TYR ARG LEU ILE ASN CYS SEQRES 13 I 461 ASN THR SER VAL ILE THR GLN ALA CYS PRO LYS VAL SER SEQRES 14 I 461 PHE ASP PRO ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY SEQRES 15 I 461 TYR ALA ILE LEU LYS CYS ASN ASN LYS THR PHE THR GLY SEQRES 16 I 461 THR GLY PRO CYS ASN ASN VAL SER THR VAL GLN CYS THR SEQRES 17 I 461 HIS GLY ILE LYS PRO VAL VAL SER THR GLN LEU LEU LEU SEQRES 18 I 461 ASN GLY SER LEU ALA GLU GLY GLU ILE ILE ILE ARG SER SEQRES 19 I 461 GLU ASN ILE THR LYS ASN VAL LYS THR ILE ILE VAL HIS SEQRES 20 I 461 LEU ASN GLU SER VAL LYS ILE GLU CYS THR ARG PRO ASN SEQRES 21 I 461 ASN LYS THR ARG THR SER ILE ARG ILE GLY PRO GLY GLN SEQRES 22 I 461 TRP PHE TYR ALA THR GLY GLN VAL ILE GLY ASP ILE ARG SEQRES 23 I 461 GLU ALA TYR CYS ASN ILE ASN GLU SER LYS TRP ASN GLU SEQRES 24 I 461 THR LEU GLN ARG VAL SER LYS LYS LEU LYS GLU TYR PHE SEQRES 25 I 461 PRO HIS LYS ASN ILE THR PHE GLN PRO SER SER GLY GLY SEQRES 26 I 461 ASP LEU GLU ILE THR THR HIS SER PHE ASN CYS GLY GLY SEQRES 27 I 461 GLU PHE PHE TYR CYS ASN THR SER SER LEU PHE ASN ARG SEQRES 28 I 461 THR TYR MET ALA ASN SER THR ASP MET ALA ASN SER THR SEQRES 29 I 461 GLU THR ASN SER THR ARG THR ILE THR ILE HIS CYS ARG SEQRES 30 I 461 ILE LYS GLN ILE ILE ASN MET TRP GLN GLU VAL GLY ARG SEQRES 31 I 461 ALA MET TYR ALA PRO PRO ILE ALA GLY ASN ILE THR CYS SEQRES 32 I 461 ILE SER ASN ILE THR GLY LEU LEU LEU THR ARG ASP GLY SEQRES 33 I 461 GLY LYS ASN ASN THR GLU THR PHE ARG PRO GLY GLY GLY SEQRES 34 I 461 ASN MET LYS ASP ASN TRP ARG SER GLU LEU TYR LYS TYR SEQRES 35 I 461 LYS VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR SEQRES 36 I 461 ARG CYS LYS ARG ARG VAL SEQRES 1 J 160 GLY ARG ARG ARG ARG ARG ARG ALA VAL GLY ILE GLY ALA SEQRES 2 J 160 VAL PHE LEU GLY PHE LEU GLY ALA ALA GLY SER THR MET SEQRES 3 J 160 GLY ALA ALA SER MET THR LEU THR VAL GLN ALA ARG ASN SEQRES 4 J 160 LEU LEU SER GLY ILE VAL GLN GLN GLN SER ASN LEU LEU SEQRES 5 J 160 ARG ALA PRO GLU ALA GLN GLN HIS LEU LEU LYS LEU THR SEQRES 6 J 160 VAL TRP GLY ILE LYS GLN LEU GLN ALA ARG VAL LEU ALA SEQRES 7 J 160 VAL GLU ARG TYR LEU ARG ASP GLN GLN LEU LEU GLY ILE SEQRES 8 J 160 TRP GLY CYS SER GLY LYS LEU ILE CYS CYS THR ASN VAL SEQRES 9 J 160 PRO TRP ASN SER SER TRP SER ASN ARG ASN LEU SER GLU SEQRES 10 J 160 ILE TRP ASP ASN MET THR TRP LEU GLN TRP ASP LYS GLU SEQRES 11 J 160 ILE SER ASN TYR THR GLN ILE ILE TYR GLY LEU LEU GLU SEQRES 12 J 160 GLU SER GLN ASN GLN GLN GLU LYS ASN GLU GLN ASP LEU SEQRES 13 J 160 LEU ALA LEU ASP SEQRES 1 K 225 GLN VAL ARG LEU ALA GLN TYR GLY GLY GLY VAL LYS ARG SEQRES 2 K 225 LEU GLY ALA THR MET THR LEU SER CYS VAL ALA SER GLY SEQRES 3 K 225 TYR THR PHE ASN ASP TYR TYR ILE HIS TRP VAL ARG GLN SEQRES 4 K 225 ALA PRO GLY GLN GLY PHE GLU LEU LEU GLY TYR ILE ASP SEQRES 5 K 225 PRO ALA ASN GLY ARG PRO ASP TYR ALA GLY ALA LEU ARG SEQRES 6 K 225 GLU ARG LEU SER PHE TYR ARG ASP LYS SER MET GLU THR SEQRES 7 K 225 LEU TYR MET ASP LEU ARG SER LEU ARG TYR ASP ASP THR SEQRES 8 K 225 ALA MET TYR TYR CYS VAL ARG ASN VAL GLY THR ALA GLY SEQRES 9 K 225 SER LEU LEU HIS TYR ASP HIS TRP GLY SER GLY SER PRO SEQRES 10 K 225 VAL ILE VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 K 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 K 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 K 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 K 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 K 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 K 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 K 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU SEQRES 18 K 225 PRO LYS SER CYS SEQRES 1 L 213 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER ALA SEQRES 2 L 213 SER PRO GLY GLU ARG VAL THR LEU THR CYS ARG ALA SER SEQRES 3 L 213 ARG SER VAL ARG ASN ASN VAL ALA TRP TYR GLN HIS LYS SEQRES 4 L 213 GLY GLY GLN SER PRO ARG LEU LEU ILE TYR ASP ALA SER SEQRES 5 L 213 THR ARG ALA ALA GLY VAL PRO ALA ARG PHE SER GLY SER SEQRES 6 L 213 ALA SER GLY THR GLU PHE THR LEU ALA ILE SER ASN LEU SEQRES 7 L 213 GLU SER GLU ASP PHE THR VAL TYR PHE CYS LEU GLN TYR SEQRES 8 L 213 ASN ASN TRP TRP THR PHE GLY GLN GLY THR ARG VAL ASP SEQRES 9 L 213 ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE SEQRES 10 L 213 PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER SEQRES 11 L 213 VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA SEQRES 12 L 213 LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY SEQRES 13 L 213 ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP SEQRES 14 L 213 SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS SEQRES 15 L 213 ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL SEQRES 16 L 213 THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE SEQRES 17 L 213 ASN ARG GLY GLU CYS HET NAG A 601 14 HET NAG A 602 14 HET NAG E 601 14 HET NAG E 602 14 HET NAG I 601 14 HET NAG I 602 14 HET NAG a 1 14 HET NAG a 2 14 HET BMA a 3 11 HET NAG a 4 14 HET NAG b 1 14 HET NAG b 2 14 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 MAN d 4 11 HET MAN d 5 11 HET MAN d 6 11 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 NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET NAG O 4 14 HET NAG P 1 14 HET NAG P 2 14 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 MAN R 4 11 HET MAN R 5 11 HET MAN R 6 11 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 NAG U 4 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 MAN X 4 11 HET MAN X 5 11 HET MAN X 6 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 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 13 NAG 45(C8 H15 N O6) FORMUL 19 BMA 12(C6 H12 O6) FORMUL 22 MAN 9(C6 H12 O6) HELIX 1 AA1 ASP A 99 LYS A 117 1 19 HELIX 2 AA2 LEU A 122 VAL A 127 5 6 HELIX 3 AA3 GLU A 335 LYS A 350 1 16 HELIX 4 AA4 ASP A 368 THR A 373 1 6 HELIX 5 AA5 MET A 473 SER A 479 1 7 HELIX 6 AA6 THR B 536 ARG B 542 1 7 HELIX 7 AA7 LEU B 576 TRP B 596 1 21 HELIX 8 AA8 ASN B 618 TRP B 623 1 6 HELIX 9 AA9 THR B 627 SER B 636 1 10 HELIX 10 AB1 TYR B 638 ALA B 662 1 25 HELIX 11 AB2 THR C 28 TYR C 32 5 5 HELIX 12 AB3 GLY C 61 ARG C 64 5 4 HELIX 13 AB4 ARG C 83 THR C 87 5 5 HELIX 14 AB5 SER C 156 ALA C 158 5 3 HELIX 15 AB6 SER C 187 THR C 191 5 5 HELIX 16 AB7 SER D 121 SER D 127 1 7 HELIX 17 AB8 SER D 182 GLU D 187 1 6 HELIX 18 AB9 ASP E 99 LYS E 117 1 19 HELIX 19 AC1 LEU E 122 VAL E 127 5 6 HELIX 20 AC2 GLU E 335 LYS E 350 1 16 HELIX 21 AC3 ASP E 368 THR E 373 1 6 HELIX 22 AC4 THR E 387 ASN E 392 1 6 HELIX 23 AC5 MET E 473 ARG E 478 1 6 HELIX 24 AC6 GLY F 521 ALA F 526 5 6 HELIX 25 AC7 GLY F 531 MET F 535 5 5 HELIX 26 AC8 THR F 536 ARG F 542 1 7 HELIX 27 AC9 LEU F 576 TRP F 596 1 21 HELIX 28 AD1 ASN F 618 TRP F 623 1 6 HELIX 29 AD2 THR F 627 SER F 636 1 10 HELIX 30 AD3 TYR F 638 ALA F 662 1 25 HELIX 31 AD4 THR G 28 TYR G 32 5 5 HELIX 32 AD5 GLY G 61 ARG G 64 5 4 HELIX 33 AD6 ARG G 83 THR G 87 5 5 HELIX 34 AD7 SER G 156 ALA G 158 5 3 HELIX 35 AD8 SER G 187 THR G 191 5 5 HELIX 36 AD9 SER H 121 SER H 127 1 7 HELIX 37 AE1 SER H 182 GLU H 187 1 6 HELIX 38 AE2 ASP I 99 LYS I 117 1 19 HELIX 39 AE3 LEU I 122 VAL I 127 5 6 HELIX 40 AE4 GLU I 335 LYS I 350 1 16 HELIX 41 AE5 ASP I 368 THR I 373 1 6 HELIX 42 AE6 THR I 387 ASN I 392 1 6 HELIX 43 AE7 MET I 473 SER I 479 1 7 HELIX 44 AE8 GLY J 531 MET J 535 5 5 HELIX 45 AE9 THR J 536 ARG J 542 1 7 HELIX 46 AF1 GLN J 575 TRP J 596 1 22 HELIX 47 AF2 THR J 627 SER J 636 1 10 HELIX 48 AF3 TYR J 638 ALA J 662 1 25 HELIX 49 AF4 THR K 28 TYR K 32 5 5 HELIX 50 AF5 GLY K 61 ARG K 64 5 4 HELIX 51 AF6 ARG K 83 THR K 87 5 5 HELIX 52 AF7 SER K 156 ALA K 158 5 3 HELIX 53 AF8 SER K 187 THR K 191 5 5 HELIX 54 AF9 SER L 121 SER L 127 1 7 HELIX 55 AG1 SER L 182 GLU L 187 1 6 SHEET 1 AA1 3 GLY A 493 THR A 497 0 SHEET 2 AA1 3 TRP A 35 TYR A 39 -1 N TRP A 35 O THR A 497 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 GLU A 47 0 SHEET 2 AA2 5 TYR A 484 ILE A 489 -1 O LYS A 488 N LYS A 46 SHEET 3 AA2 5 TYR A 223 CYS A 228 -1 N LEU A 226 O LYS A 485 SHEET 4 AA2 5 VAL A 242 VAL A 245 -1 O SER A 243 N LYS A 227 SHEET 5 AA2 5 MET A 84 VAL A 85 -1 N MET 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 3 LEU A 129 ASN A 130 0 SHEET 2 AA4 3 GLN A 190 LEU A 193 -1 O TYR A 191 N LEU A 129 SHEET 3 AA4 3 ILE A 181 GLN A 183 -1 N VAL A 182 O ARG A 192 SHEET 1 AA5 2 GLU A 143 GLY A 144 0 SHEET 2 AA5 2 PHE A 176 TYR A 177 -1 O PHE A 176 N GLY A 144 SHEET 1 AA6 2 SER A 158 THR A 162 0 SHEET 2 AA6 2 ARG A 169 ASN A 173 -1 O GLU A 170 N ILE A 161 SHEET 1 AA7 3 VAL A 200 GLN A 203 0 SHEET 2 AA7 3 ARG A 432 TYR A 435 1 O ALA A 433 N THR A 202 SHEET 3 AA7 3 ILE A 423 ASN A 425 -1 N ILE A 424 O MET A 434 SHEET 1 AA811 LEU A 259 LEU A 261 0 SHEET 2 AA811 ILE A 271 ARG A 273 0 SHEET 3 AA811 ILE A 284 ARG A 298 -1 O HIS A 287 N ILE A 271 SHEET 4 AA811 TYR A 330 ASN A 334 -1 O ASN A 332 N GLU A 295 SHEET 5 AA811 ILE A 358 PHE A 361 0 SHEET 6 AA811 HIS A 374 CYS A 378 0 SHEET 7 AA811 GLU A 381 CYS A 385 -1 O PHE A 383 N PHE A 376 SHEET 8 AA811 ARG A 393 TYR A 395 -1 O TYR A 395 N ILE A 358 SHEET 9 AA811 THR A 413 ILE A 420 -1 O ARG A 419 N TYR A 384 SHEET 10 AA811 ILE A 443 ARG A 456 -1 O ILE A 443 N ARG A 298 SHEET 11 AA811 GLU A 464 PRO A 468 -1 O ARG A 467 N THR A 455 SHEET 1 AA9 2 ASN A 301 ARG A 308 0 SHEET 2 AA9 2 TRP A 316 ILE A 323 -1 O ILE A 323 N ASN A 301 SHEET 1 AB1 4 ARG C 3 TYR C 7 0 SHEET 2 AB1 4 THR C 19 SER C 25 -1 O SER C 25 N ARG C 3 SHEET 3 AB1 4 THR C 77 LEU C 82 -1 O LEU C 78 N CYS C 22 SHEET 4 AB1 4 LEU C 67 ASP C 72 -1 N SER C 68 O ASP C 81 SHEET 1 AB2 7 GLY C 10 LYS C 12 0 SHEET 2 AB2 7 TYR C 33 GLN C 39 0 SHEET 3 AB2 7 GLU C 46 ILE C 51 -1 O ILE C 51 N ILE C 34 SHEET 4 AB2 7 PRO C 57 TYR C 59 -1 O ASP C 58 N TYR C 50 SHEET 5 AB2 7 ALA C 88 GLY C 97 -1 O VAL C 93 N HIS C 35 SHEET 6 AB2 7 LEU C 100B HIS C 100D-1 O HIS C 100D N VAL C 96 SHEET 7 AB2 7 SER C 107 VAL C 111 -1 O SER C 107 N TYR C 90 SHEET 1 AB3 5 SER C 120 LEU C 124 0 SHEET 2 AB3 5 THR C 135 TYR C 145 -1 O LEU C 141 N PHE C 122 SHEET 3 AB3 5 HIS C 164 THR C 165 0 SHEET 4 AB3 5 VAL C 169 LEU C 170 0 SHEET 5 AB3 5 TYR C 176 PRO C 185 -1 O SER C 177 N VAL C 169 SHEET 1 AB4 3 THR C 151 TRP C 154 0 SHEET 2 AB4 3 CYS C 196 HIS C 200 -1 O ASN C 197 N SER C 153 SHEET 3 AB4 3 THR C 205 VAL C 207 -1 O VAL C 207 N VAL C 198 SHEET 1 AB5 4 THR D 5 SER D 7 0 SHEET 2 AB5 4 VAL D 19 ARG D 24 -1 O ARG D 24 N THR D 5 SHEET 3 AB5 4 GLU D 70 ILE D 75 -1 O LEU D 73 N LEU D 21 SHEET 4 AB5 4 PHE D 62 SER D 67 -1 N SER D 63 O ALA D 74 SHEET 1 AB6 7 THR D 10 ALA D 13 0 SHEET 2 AB6 7 VAL D 33 HIS D 38 0 SHEET 3 AB6 7 ARG D 45 TYR D 49 -1 O ILE D 48 N TRP D 35 SHEET 4 AB6 7 THR D 53 ARG D 54 -1 O THR D 53 N TYR D 49 SHEET 5 AB6 7 VAL D 85 GLN D 90 -1 O VAL D 85 N HIS D 38 SHEET 6 AB6 7 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 7 AB6 7 THR D 102 ILE D 106 -1 O THR D 102 N TYR D 86 SHEET 1 AB7 4 SER D 114 PHE D 118 0 SHEET 2 AB7 4 VAL D 132 PHE D 139 -1 O VAL D 133 N PHE D 118 SHEET 3 AB7 4 TYR D 173 LEU D 179 -1 O LEU D 175 N LEU D 136 SHEET 4 AB7 4 SER D 159 VAL D 163 -1 N GLN D 160 O THR D 178 SHEET 1 AB8 4 ALA D 153 GLN D 155 0 SHEET 2 AB8 4 LYS D 145 VAL D 150 -1 N VAL D 150 O ALA D 153 SHEET 3 AB8 4 VAL D 191 THR D 197 -1 O ALA D 193 N LYS D 149 SHEET 4 AB8 4 VAL D 205 ASN D 210 -1 O VAL D 205 N VAL D 196 SHEET 1 AB9 3 GLY E 493 THR E 497 0 SHEET 2 AB9 3 TRP E 35 TYR E 39 -1 N TRP E 35 O THR E 497 SHEET 3 AB9 3 ILE F 603 PRO F 609 -1 O VAL F 608 N VAL E 36 SHEET 1 AC1 5 TRP E 45 GLU E 47 0 SHEET 2 AC1 5 LYS E 485 ILE E 489 -1 O LYS E 488 N LYS E 46 SHEET 3 AC1 5 TYR E 223 CYS E 228 -1 N LEU E 226 O LYS E 485 SHEET 4 AC1 5 VAL E 242 VAL E 245 -1 O SER E 243 N LYS E 227 SHEET 5 AC1 5 MET E 84 VAL E 85 -1 N MET E 84 O THR E 244 SHEET 1 AC2 2 PHE E 53 ALA E 55 0 SHEET 2 AC2 2 HIS E 216 CYS E 218 -1 O HIS E 216 N ALA E 55 SHEET 1 AC3 3 LEU E 129 ASN E 130 0 SHEET 2 AC3 3 GLN E 190 LEU E 193 -1 O TYR E 191 N LEU E 129 SHEET 3 AC3 3 ILE E 181 GLN E 183 -1 N VAL E 182 O ARG E 192 SHEET 1 AC4 2 SER E 158 THR E 162 0 SHEET 2 AC4 2 ARG E 169 ASN E 173 -1 O LYS E 172 N PHE E 159 SHEET 1 AC5 3 ILE E 201 GLN E 203 0 SHEET 2 AC5 3 ALA E 433 TYR E 435 1 O TYR E 435 N THR E 202 SHEET 3 AC5 3 ILE E 423 ASN E 425 -1 N ILE E 424 O MET E 434 SHEET 1 AC612 LEU E 259 LEU E 261 0 SHEET 2 AC612 ILE E 271 ARG E 273 0 SHEET 3 AC612 ILE E 284 ARG E 308 -1 O ILE E 285 N ARG E 273 SHEET 4 AC612 TRP E 316 ILE E 323 -1 O ILE E 323 N ASN E 301 SHEET 5 AC612 TYR E 330 ASN E 334 -1 O ASN E 332 N GLU E 295 SHEET 6 AC612 ILE E 358 PHE E 361 0 SHEET 7 AC612 HIS E 374 CYS E 378 0 SHEET 8 AC612 GLU E 381 CYS E 385 -1 O PHE E 383 N PHE E 376 SHEET 9 AC612 ARG E 393 TYR E 395 -1 O ARG E 393 N PHE E 361 SHEET 10 AC612 THR E 413 ILE E 420 -1 O ARG E 419 N TYR E 384 SHEET 11 AC612 GLY E 441 ARG E 456 -1 O THR E 450 N LEU E 288 SHEET 12 AC612 GLU E 464 PRO E 468 -1 O ARG E 467 N THR E 455 SHEET 1 AC7 4 ALA G 5 TYR G 7 0 SHEET 2 AC7 4 THR G 19 VAL G 23 -1 O VAL G 23 N ALA G 5 SHEET 3 AC7 4 THR G 77 LEU G 82 -1 O LEU G 78 N CYS G 22 SHEET 4 AC7 4 LEU G 67 ASP G 72 -1 N SER G 68 O ASP G 81 SHEET 1 AC8 7 GLY G 10 LYS G 12 0 SHEET 2 AC8 7 ILE G 34 GLN G 39 0 SHEET 3 AC8 7 GLU G 46 ILE G 51 -1 O ILE G 51 N ILE G 34 SHEET 4 AC8 7 PRO G 57 TYR G 59 -1 O ASP G 58 N TYR G 50 SHEET 5 AC8 7 ALA G 88 ASN G 95 -1 O TYR G 91 N VAL G 37 SHEET 6 AC8 7 TYR G 100E TRP G 103 -1 O HIS G 102 N ARG G 94 SHEET 7 AC8 7 SER G 107 VAL G 111 -1 O SER G 107 N TYR G 90 SHEET 1 AC9 5 SER G 120 LEU G 124 0 SHEET 2 AC9 5 THR G 135 TYR G 145 -1 O LEU G 141 N PHE G 122 SHEET 3 AC9 5 HIS G 164 THR G 165 0 SHEET 4 AC9 5 VAL G 169 LEU G 170 0 SHEET 5 AC9 5 TYR G 176 PRO G 185 -1 O SER G 177 N VAL G 169 SHEET 1 AD1 3 VAL G 150 TRP G 154 0 SHEET 2 AD1 3 ILE G 195 HIS G 200 -1 O ASN G 197 N SER G 153 SHEET 3 AD1 3 LYS G 206 ARG G 210 -1 O LYS G 209 N CYS G 196 SHEET 1 AD2 4 THR H 5 SER H 7 0 SHEET 2 AD2 4 VAL H 19 ARG H 24 -1 O ARG H 24 N THR H 5 SHEET 3 AD2 4 GLU H 70 ILE H 75 -1 O LEU H 73 N LEU H 21 SHEET 4 AD2 4 PHE H 62 SER H 67 -1 N SER H 63 O ALA H 74 SHEET 1 AD3 7 THR H 10 ALA H 13 0 SHEET 2 AD3 7 VAL H 33 HIS H 38 0 SHEET 3 AD3 7 ARG H 45 TYR H 49 -1 O ILE H 48 N TRP H 35 SHEET 4 AD3 7 THR H 53 ARG H 54 -1 O THR H 53 N TYR H 49 SHEET 5 AD3 7 VAL H 85 GLN H 90 -1 O VAL H 85 N HIS H 38 SHEET 6 AD3 7 THR H 97 PHE H 98 -1 O THR H 97 N GLN H 90 SHEET 7 AD3 7 THR H 102 ILE H 106 -1 O THR H 102 N TYR H 86 SHEET 1 AD4 4 SER H 114 PHE H 118 0 SHEET 2 AD4 4 VAL H 132 PHE H 139 -1 O LEU H 135 N PHE H 116 SHEET 3 AD4 4 TYR H 173 LEU H 179 -1 O LEU H 175 N LEU H 136 SHEET 4 AD4 4 SER H 159 VAL H 163 -1 N GLN H 160 O THR H 178 SHEET 1 AD5 4 ALA H 153 GLN H 155 0 SHEET 2 AD5 4 LYS H 145 VAL H 150 -1 N VAL H 150 O ALA H 153 SHEET 3 AD5 4 VAL H 191 THR H 197 -1 O ALA H 193 N LYS H 149 SHEET 4 AD5 4 VAL H 205 ASN H 210 -1 O LYS H 207 N CYS H 194 SHEET 1 AD6 3 GLY I 493 THR I 497 0 SHEET 2 AD6 3 TRP I 35 TYR I 39 -1 N TRP I 35 O THR I 497 SHEET 3 AD6 3 ILE J 603 PRO J 609 -1 O VAL J 608 N VAL I 36 SHEET 1 AD7 5 TRP I 45 GLU I 47 0 SHEET 2 AD7 5 TYR I 484 ILE I 489 -1 O LYS I 488 N LYS I 46 SHEET 3 AD7 5 TYR I 223 CYS I 228 -1 N LEU I 226 O LYS I 485 SHEET 4 AD7 5 VAL I 242 VAL I 245 -1 O SER I 243 N LYS I 227 SHEET 5 AD7 5 MET I 84 LEU I 86 -1 N LEU I 86 O VAL I 242 SHEET 1 AD8 3 LEU I 129 ASN I 130 0 SHEET 2 AD8 3 GLN I 190 LEU I 193 -1 O TYR I 191 N LEU I 129 SHEET 3 AD8 3 ILE I 181 GLN I 183 -1 N VAL I 182 O ARG I 192 SHEET 1 AD9 2 SER I 158 THR I 162 0 SHEET 2 AD9 2 ARG I 169 ASN I 173 -1 O GLU I 170 N ILE I 161 SHEET 1 AE1 3 ILE I 201 GLN I 203 0 SHEET 2 AE1 3 ALA I 433 TYR I 435 1 O TYR I 435 N THR I 202 SHEET 3 AE1 3 ILE I 423 ASN I 425 -1 N ILE I 424 O MET I 434 SHEET 1 AE212 LEU I 259 LEU I 261 0 SHEET 2 AE212 ILE I 271 ARG I 273 0 SHEET 3 AE212 ILE I 284 ILE I 307 -1 O HIS I 287 N ILE I 271 SHEET 4 AE212 PHE I 317 ILE I 323 -1 O ILE I 323 N ASN I 301 SHEET 5 AE212 TYR I 330 ASN I 334 -1 O ASN I 332 N GLU I 295 SHEET 6 AE212 ASN I 357 PHE I 361 0 SHEET 7 AE212 HIS I 374 CYS I 378 0 SHEET 8 AE212 GLU I 381 CYS I 385 -1 O CYS I 385 N HIS I 374 SHEET 9 AE212 ARG I 393 TYR I 395 -1 O TYR I 395 N ILE I 358 SHEET 10 AE212 THR I 413 ILE I 420 -1 O ARG I 419 N TYR I 384 SHEET 11 AE212 GLY I 441 ARG I 456 -1 O THR I 450 N LEU I 288 SHEET 12 AE212 THR I 463 PRO I 468 -1 O ARG I 467 N THR I 455 SHEET 1 AE3 4 ALA K 5 TYR K 7 0 SHEET 2 AE3 4 THR K 19 VAL K 23 -1 O VAL K 23 N ALA K 5 SHEET 3 AE3 4 THR K 77 LEU K 82 -1 O LEU K 78 N CYS K 22 SHEET 4 AE3 4 LEU K 67 ASP K 72 -1 N SER K 68 O ASP K 81 SHEET 1 AE4 7 GLY K 10 LYS K 12 0 SHEET 2 AE4 7 ILE K 34 GLN K 39 0 SHEET 3 AE4 7 GLU K 46 ILE K 51 -1 O ILE K 51 N ILE K 34 SHEET 4 AE4 7 PRO K 57 TYR K 59 -1 O ASP K 58 N TYR K 50 SHEET 5 AE4 7 ALA K 88 ASN K 95 -1 O VAL K 93 N HIS K 35 SHEET 6 AE4 7 TYR K 100E TRP K 103 -1 O HIS K 102 N ARG K 94 SHEET 7 AE4 7 SER K 107 VAL K 111 -1 O SER K 107 N TYR K 90 SHEET 1 AE5 5 SER K 120 LEU K 124 0 SHEET 2 AE5 5 THR K 135 TYR K 145 -1 O LEU K 141 N PHE K 122 SHEET 3 AE5 5 HIS K 164 THR K 165 0 SHEET 4 AE5 5 VAL K 169 LEU K 170 0 SHEET 5 AE5 5 TYR K 176 PRO K 185 -1 O SER K 177 N VAL K 169 SHEET 1 AE6 3 THR K 151 TRP K 154 0 SHEET 2 AE6 3 ILE K 195 ASN K 199 -1 O ASN K 197 N SER K 153 SHEET 3 AE6 3 LYS K 206 ARG K 210 -1 O LYS K 209 N CYS K 196 SHEET 1 AE7 4 THR L 5 SER L 7 0 SHEET 2 AE7 4 VAL L 19 ARG L 24 -1 O ARG L 24 N THR L 5 SHEET 3 AE7 4 GLU L 70 ILE L 75 -1 O ILE L 75 N VAL L 19 SHEET 4 AE7 4 PHE L 62 SER L 67 -1 N SER L 63 O ALA L 74 SHEET 1 AE8 6 THR L 10 ALA L 13 0 SHEET 2 AE8 6 VAL L 33 GLN L 37 0 SHEET 3 AE8 6 ARG L 45 ILE L 48 -1 O ILE L 48 N TRP L 35 SHEET 4 AE8 6 VAL L 85 GLN L 90 -1 O LEU L 89 N ALA L 34 SHEET 5 AE8 6 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 6 AE8 6 THR L 102 ILE L 106 -1 O THR L 102 N TYR L 86 SHEET 1 AE9 4 SER L 114 PHE L 118 0 SHEET 2 AE9 4 VAL L 132 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AE9 4 TYR L 173 LEU L 179 -1 O LEU L 175 N LEU L 136 SHEET 4 AE9 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AF1 4 ALA L 153 GLN L 155 0 SHEET 2 AF1 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AF1 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AF1 4 VAL L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SSBOND 1 CYS A 54 CYS A 74 1555 1555 2.04 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 2.03 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 A 499 CYS B 605 1555 1555 2.02 SSBOND 11 CYS B 598 CYS B 604 1555 1555 2.03 SSBOND 12 CYS D 23 CYS D 88 1555 1555 2.03 SSBOND 13 CYS E 54 CYS E 74 1555 1555 2.04 SSBOND 14 CYS E 119 CYS E 205 1555 1555 2.03 SSBOND 15 CYS E 126 CYS E 196 1555 1555 2.03 SSBOND 16 CYS E 131 CYS E 157 1555 1555 2.03 SSBOND 17 CYS E 218 CYS E 247 1555 1555 2.03 SSBOND 18 CYS E 228 CYS E 239 1555 1555 2.03 SSBOND 19 CYS E 296 CYS E 331 1555 1555 2.03 SSBOND 20 CYS E 378 CYS E 445 1555 1555 2.03 SSBOND 21 CYS E 385 CYS E 418 1555 1555 2.03 SSBOND 22 CYS E 499 CYS F 605 1555 1555 2.02 SSBOND 23 CYS F 598 CYS F 604 1555 1555 2.02 SSBOND 24 CYS H 23 CYS H 88 1555 1555 2.04 SSBOND 25 CYS I 54 CYS I 74 1555 1555 2.04 SSBOND 26 CYS I 119 CYS I 205 1555 1555 2.03 SSBOND 27 CYS I 126 CYS I 196 1555 1555 2.03 SSBOND 28 CYS I 131 CYS I 157 1555 1555 2.03 SSBOND 29 CYS I 218 CYS I 247 1555 1555 2.03 SSBOND 30 CYS I 228 CYS I 239 1555 1555 2.03 SSBOND 31 CYS I 296 CYS I 331 1555 1555 2.03 SSBOND 32 CYS I 378 CYS I 445 1555 1555 2.03 SSBOND 33 CYS I 385 CYS I 418 1555 1555 2.04 SSBOND 34 CYS I 499 CYS J 605 1555 1555 2.02 SSBOND 35 CYS J 598 CYS J 604 1555 1555 2.02 SSBOND 36 CYS L 23 CYS L 88 1555 1555 2.03 LINK ND2 ASN A 160 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN A 197 C1 NAG R 1 1555 1555 1.46 LINK ND2 ASN A 230 C1 NAG A 601 1555 1555 1.44 LINK ND2 ASN A 241 C1 NAG A 602 1555 1555 1.44 LINK ND2 ASN A 262 C1 NAG O 1 1555 1555 1.45 LINK ND2 ASN A 339 C1 NAG N 1 1555 1555 1.44 LINK ND2 ASN A 386 C1 NAG M 1 1555 1555 1.45 LINK ND2 ASN A 392 C1 NAG Q 1 1555 1555 1.44 LINK ND2 ASN E 160 C1 NAG V 1 1555 1555 1.44 LINK ND2 ASN E 197 C1 NAG X 1 1555 1555 1.46 LINK ND2 ASN E 230 C1 NAG E 601 1555 1555 1.44 LINK ND2 ASN E 241 C1 NAG E 602 1555 1555 1.44 LINK ND2 ASN E 262 C1 NAG U 1 1555 1555 1.45 LINK ND2 ASN E 339 C1 NAG T 1 1555 1555 1.44 LINK ND2 ASN E 386 C1 NAG S 1 1555 1555 1.45 LINK ND2 ASN E 392 C1 NAG W 1 1555 1555 1.44 LINK ND2 ASN I 160 C1 NAG b 1 1555 1555 1.44 LINK ND2 ASN I 197 C1 NAG d 1 1555 1555 1.46 LINK ND2 ASN I 230 C1 NAG I 601 1555 1555 1.44 LINK ND2 ASN I 241 C1 NAG I 602 1555 1555 1.44 LINK ND2 ASN I 262 C1 NAG a 1 1555 1555 1.45 LINK ND2 ASN I 339 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN I 386 C1 NAG Y 1 1555 1555 1.44 LINK ND2 ASN I 392 C1 NAG c 1 1555 1555 1.44 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.44 LINK O4 NAG a 2 C1 BMA a 3 1555 1555 1.45 LINK O4 BMA a 3 C1 NAG a 4 1555 1555 1.46 LINK O4 NAG b 1 C1 NAG b 2 1555 1555 1.46 LINK O4 NAG c 1 C1 NAG c 2 1555 1555 1.45 LINK O4 NAG c 2 C1 BMA c 3 1555 1555 1.45 LINK O4 NAG d 1 C1 NAG d 2 1555 1555 1.45 LINK O4 NAG d 2 C1 BMA d 3 1555 1555 1.45 LINK O6 BMA d 3 C1 MAN d 4 1555 1555 1.46 LINK O3 BMA d 3 C1 MAN d 6 1555 1555 1.46 LINK O6 MAN d 4 C1 MAN d 5 1555 1555 1.45 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.45 LINK O4 NAG M 2 C1 BMA M 3 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 O 2 C1 BMA O 3 1555 1555 1.45 LINK O4 BMA O 3 C1 NAG O 4 1555 1555 1.46 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.46 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.45 LINK O4 NAG Q 2 C1 BMA Q 3 1555 1555 1.45 LINK O4 NAG R 1 C1 NAG R 2 1555 1555 1.45 LINK O4 NAG R 2 C1 BMA R 3 1555 1555 1.45 LINK O6 BMA R 3 C1 MAN R 4 1555 1555 1.46 LINK O3 BMA R 3 C1 MAN R 6 1555 1555 1.46 LINK O6 MAN R 4 C1 MAN R 5 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 1.44 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.44 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.44 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.45 LINK O4 BMA U 3 C1 NAG U 4 1555 1555 1.46 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.46 LINK O4 NAG W 1 C1 NAG W 2 1555 1555 1.45 LINK O4 NAG W 2 C1 BMA W 3 1555 1555 1.45 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.45 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.45 LINK O6 BMA X 3 C1 MAN X 4 1555 1555 1.46 LINK O3 BMA X 3 C1 MAN X 6 1555 1555 1.45 LINK O6 MAN X 4 C1 MAN X 5 1555 1555 1.45 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.45 LINK O4 NAG Y 2 C1 BMA Y 3 1555 1555 1.44 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.44 CISPEP 1 VAL A 75 PRO A 76 0 -7.16 CISPEP 2 PHE C 146 PRO C 147 0 -9.11 CISPEP 3 GLU C 148 PRO C 149 0 2.89 CISPEP 4 SER D 7 PRO D 8 0 -3.48 CISPEP 5 TYR D 140 PRO D 141 0 -0.40 CISPEP 6 VAL E 75 PRO E 76 0 -7.73 CISPEP 7 PHE G 146 PRO G 147 0 -8.28 CISPEP 8 GLU G 148 PRO G 149 0 0.64 CISPEP 9 SER H 7 PRO H 8 0 -3.23 CISPEP 10 TYR H 140 PRO H 141 0 0.32 CISPEP 11 VAL I 75 PRO I 76 0 -17.46 CISPEP 12 PHE K 146 PRO K 147 0 -8.36 CISPEP 13 GLU K 148 PRO K 149 0 2.76 CISPEP 14 SER L 7 PRO L 8 0 -3.66 CISPEP 15 TYR L 140 PRO L 141 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