HEADER VIRAL PROTEIN/IMMUNE SYSTEM 14-JUL-22 8DP1 TITLE CRYO-EM STRUCTURE OF HIV-1 ENV(BG505.T332N SOSIP) IN COMPLEX WITH TITLE 2 DH1030.1 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: DH1030.1 FAB LIGHT CHAIN; COMPND 3 CHAIN: M, F, O; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: DH1030.1 FAB HEAVY CHAIN; COMPND 7 CHAIN: R, E, N; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: ENVELOPE GLYCOPROTEIN GP41; COMPND 11 CHAIN: S, H, Q; COMPND 12 FRAGMENT: UNP RESIDUES 509-661; COMPND 13 SYNONYM: ENV POLYPROTEIN; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: ENVELOPE GLYCOPROTEIN GP120; COMPND 17 CHAIN: W, B, J; COMPND 18 FRAGMENT: GP120; COMPND 19 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 3 ORGANISM_TAXID: 9544; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MACACA MULATTA; SOURCE 8 ORGANISM_TAXID: 9544; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 13 ORGANISM_TAXID: 11676; SOURCE 14 GENE: ENV; SOURCE 15 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 4; SOURCE 18 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1; SOURCE 19 ORGANISM_TAXID: 11676; SOURCE 20 GENE: ENV; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS HIV-1 ENV, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR S.GOBEIL,P.ACHARYA JRNL AUTH S.M.GOBEIL,K.JANOWSKA,V.STALLS,K.MANSOURI,R.J.EDWARDS, JRNL AUTH 2 R.C.HENDERSON,K.WIEHE,K.SAUNDERS,P.ACHARYA,W.WILLIAMS, JRNL AUTH 3 B.F.HAYNES JRNL TITL SHARED RECOGNITION MECHANISM FOR HIV-1 ENVELOPE-REACTIVE V3 JRNL TITL 2 GLYCAN BROADLY NEUTRALIZING B CELL LINEAGE MATURATION IN JRNL TITL 3 HUMANS AND MACAQUES JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.46 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : COOT, UCSF CHIMERAX, ISOLDE, UCSF REMARK 3 CHIMERAX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6MTJ 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) : 3.460 REMARK 3 NUMBER OF PARTICLES : 441080 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 8DP1 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_1000267067. 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 : HIV-1 ENV(BG505.T332N SOSIP) IN REMARK 245 COMPLEX WITH DH1030.1 FAB REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 1.00 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) : 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) : 54.00 REMARK 245 ILLUMINATION MODE : OTHER 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: M, R, S, W, B, E, F, H, J, N, REMARK 350 AND CHAINS: O, Q, A, C, D, G, I, K, L, REMARK 350 AND CHAINS: P, T, U, V, X, Y, Z, a REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU M 218 REMARK 465 CYS M 219 REMARK 465 LYS R 226 REMARK 465 THR R 227 REMARK 465 CYS R 228 REMARK 465 GLY R 229 REMARK 465 GLY R 230 REMARK 465 ALA S 512 REMARK 465 VAL S 513 REMARK 465 GLY S 514 REMARK 465 ILE S 515 REMARK 465 GLY S 516 REMARK 465 GLN S 550 REMARK 465 GLN S 551 REMARK 465 GLN S 552 REMARK 465 SER S 553 REMARK 465 ASN S 554 REMARK 465 LEU S 555 REMARK 465 LEU S 556 REMARK 465 ARG S 557 REMARK 465 ALA S 558 REMARK 465 PRO S 559 REMARK 465 GLU S 560 REMARK 465 ALA S 561 REMARK 465 GLN S 562 REMARK 465 GLN S 563 REMARK 465 ASP S 664 REMARK 465 ALA W 31 REMARK 465 LYS W 59 REMARK 465 ALA W 60 REMARK 465 TYR W 61 REMARK 465 GLU W 62 REMARK 465 THR W 63 REMARK 465 GLU W 64 REMARK 465 GLU W 185A REMARK 465 ASN W 185B REMARK 465 GLN W 185C REMARK 465 GLY W 185D REMARK 465 ASN W 185E REMARK 465 ARG W 185F REMARK 465 SER W 185G REMARK 465 ASN W 185H REMARK 465 ASN W 185I REMARK 465 SER W 185J REMARK 465 THR W 400 REMARK 465 SER W 401 REMARK 465 VAL W 402 REMARK 465 GLN W 403 REMARK 465 GLY W 404 REMARK 465 SER W 405 REMARK 465 ASN W 406 REMARK 465 SER W 407 REMARK 465 THR W 408 REMARK 465 GLY W 459 REMARK 465 SER W 460 REMARK 465 THR W 461 REMARK 465 ASN W 462 REMARK 465 SER W 463 REMARK 465 THR W 464 REMARK 465 VAL W 505 REMARK 465 VAL W 506 REMARK 465 GLY W 507 REMARK 465 ARG W 508 REMARK 465 ARG W 509 REMARK 465 ARG W 510 REMARK 465 ARG W 511 REMARK 465 ARG W 512 REMARK 465 ARG W 513 REMARK 465 ALA B 31 REMARK 465 LYS B 59 REMARK 465 ALA B 60 REMARK 465 TYR B 61 REMARK 465 GLU B 62 REMARK 465 THR B 63 REMARK 465 GLU B 64 REMARK 465 GLU B 185A REMARK 465 ASN B 185B REMARK 465 GLN B 185C REMARK 465 GLY B 185D REMARK 465 ASN B 185E REMARK 465 ARG B 185F REMARK 465 SER B 185G REMARK 465 ASN B 185H REMARK 465 ASN B 185I REMARK 465 SER B 185J REMARK 465 THR B 400 REMARK 465 SER B 401 REMARK 465 VAL B 402 REMARK 465 GLN B 403 REMARK 465 GLY B 404 REMARK 465 SER B 405 REMARK 465 ASN B 406 REMARK 465 SER B 407 REMARK 465 THR B 408 REMARK 465 GLY B 459 REMARK 465 SER B 460 REMARK 465 THR B 461 REMARK 465 ASN B 462 REMARK 465 SER B 463 REMARK 465 THR B 464 REMARK 465 VAL B 505 REMARK 465 VAL B 506 REMARK 465 GLY B 507 REMARK 465 ARG B 508 REMARK 465 ARG B 509 REMARK 465 ARG B 510 REMARK 465 ARG B 511 REMARK 465 ARG B 512 REMARK 465 ARG B 513 REMARK 465 LYS E 226 REMARK 465 THR E 227 REMARK 465 CYS E 228 REMARK 465 GLY E 229 REMARK 465 GLY E 230 REMARK 465 GLU F 218 REMARK 465 CYS F 219 REMARK 465 ALA H 512 REMARK 465 VAL H 513 REMARK 465 GLY H 514 REMARK 465 ILE H 515 REMARK 465 GLY H 516 REMARK 465 GLN H 550 REMARK 465 GLN H 551 REMARK 465 GLN H 552 REMARK 465 SER H 553 REMARK 465 ASN H 554 REMARK 465 LEU H 555 REMARK 465 LEU H 556 REMARK 465 ARG H 557 REMARK 465 ALA H 558 REMARK 465 PRO H 559 REMARK 465 GLU H 560 REMARK 465 ALA H 561 REMARK 465 GLN H 562 REMARK 465 GLN H 563 REMARK 465 ASP H 664 REMARK 465 ALA J 31 REMARK 465 LYS J 59 REMARK 465 ALA J 60 REMARK 465 TYR J 61 REMARK 465 GLU J 62 REMARK 465 THR J 63 REMARK 465 GLU J 64 REMARK 465 GLU J 185A REMARK 465 ASN J 185B REMARK 465 GLN J 185C REMARK 465 GLY J 185D REMARK 465 ASN J 185E REMARK 465 ARG J 185F REMARK 465 SER J 185G REMARK 465 ASN J 185H REMARK 465 ASN J 185I REMARK 465 SER J 185J REMARK 465 THR J 400 REMARK 465 SER J 401 REMARK 465 VAL J 402 REMARK 465 GLN J 403 REMARK 465 GLY J 404 REMARK 465 SER J 405 REMARK 465 ASN J 406 REMARK 465 SER J 407 REMARK 465 THR J 408 REMARK 465 GLY J 459 REMARK 465 SER J 460 REMARK 465 THR J 461 REMARK 465 ASN J 462 REMARK 465 SER J 463 REMARK 465 THR J 464 REMARK 465 VAL J 505 REMARK 465 VAL J 506 REMARK 465 GLY J 507 REMARK 465 ARG J 508 REMARK 465 ARG J 509 REMARK 465 ARG J 510 REMARK 465 ARG J 511 REMARK 465 ARG J 512 REMARK 465 ARG J 513 REMARK 465 LYS N 226 REMARK 465 THR N 227 REMARK 465 CYS N 228 REMARK 465 GLY N 229 REMARK 465 GLY N 230 REMARK 465 GLU O 218 REMARK 465 CYS O 219 REMARK 465 ALA Q 512 REMARK 465 VAL Q 513 REMARK 465 GLY Q 514 REMARK 465 ILE Q 515 REMARK 465 GLY Q 516 REMARK 465 GLN Q 550 REMARK 465 GLN Q 551 REMARK 465 GLN Q 552 REMARK 465 SER Q 553 REMARK 465 ASN Q 554 REMARK 465 LEU Q 555 REMARK 465 LEU Q 556 REMARK 465 ARG Q 557 REMARK 465 ALA Q 558 REMARK 465 PRO Q 559 REMARK 465 GLU Q 560 REMARK 465 ALA Q 561 REMARK 465 GLN Q 562 REMARK 465 GLN Q 563 REMARK 465 ASP Q 664 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 ARG M 66 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG M 82 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG M 113 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG M 216 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG R 56 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG R 65 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG R 100 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG S 542 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG S 617 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 THR W 123 CA - CB - OG1 ANGL. DEV. = 17.6 DEGREES REMARK 500 ARG W 298 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 ARG W 308 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG W 350 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 ARG W 456 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG W 480 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG W 500 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 ARG B 298 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 ARG B 308 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG B 327 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 ARG B 350 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG B 469 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 ARG B 476 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG B 480 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG B 500 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 TYR E 33 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 ARG E 56 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG E 65 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG E 100 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG F 82 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG F 216 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG H 542 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG H 617 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 PRO J 124 C - N - CD ANGL. DEV. = -13.5 DEGREES REMARK 500 PRO J 124 CA - N - CD ANGL. DEV. = -10.9 DEGREES REMARK 500 ARG J 178 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG J 298 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES REMARK 500 ARG J 308 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG J 327 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG J 350 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 ARG J 480 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 ARG J 500 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 TYR N 33 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES REMARK 500 ARG N 56 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG N 65 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 ARG N 100 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 ARG O 66 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG O 113 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG O 147 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG Q 542 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 ARG Q 588 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 51 ANGLE DEVIATIONS. 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 VAL M 56 -42.15 66.65 REMARK 500 ASP R 99 -138.49 -120.72 REMARK 500 LEU R 136 75.39 -103.06 REMARK 500 PRO R 159 -179.68 -68.06 REMARK 500 ASN R 167 74.02 58.87 REMARK 500 PHE S 519 77.46 53.47 REMARK 500 LEU S 568 43.98 -78.72 REMARK 500 ILE S 622 -71.49 -91.62 REMARK 500 ASN S 625 -62.41 -141.07 REMARK 500 ASN W 88 -14.59 57.90 REMARK 500 THR W 135 4.42 -64.94 REMARK 500 ILE W 138 -163.35 -68.54 REMARK 500 ASP W 141 -38.70 61.22 REMARK 500 LYS W 189 23.04 -72.49 REMARK 500 THR W 198 -36.45 -142.87 REMARK 500 HIS W 249 170.25 -59.38 REMARK 500 GLN W 258 -49.81 62.92 REMARK 500 ASN W 262 -6.75 54.97 REMARK 500 GLU W 269 154.73 60.75 REMARK 500 ASN W 276 88.32 -153.29 REMARK 500 PHE W 391 77.11 -102.05 REMARK 500 ASN W 392 62.90 -154.95 REMARK 500 SER W 410 -17.64 59.17 REMARK 500 ASP W 412 89.50 -68.80 REMARK 500 ASN B 88 -8.85 56.74 REMARK 500 PRO B 124 -18.00 -49.59 REMARK 500 THR B 135 101.43 -54.90 REMARK 500 ILE B 138 -163.96 -74.68 REMARK 500 ASP B 141 -25.06 60.74 REMARK 500 LYS B 189 27.06 -73.57 REMARK 500 HIS B 249 173.87 -59.53 REMARK 500 GLN B 258 -49.31 64.57 REMARK 500 GLU B 269 151.37 61.96 REMARK 500 ASN B 276 87.53 -162.33 REMARK 500 ASN B 301 75.95 -101.46 REMARK 500 PHE B 391 72.47 -108.91 REMARK 500 ASN B 392 63.64 -153.66 REMARK 500 SER B 410 1.29 59.42 REMARK 500 ASP E 99 -131.54 -120.78 REMARK 500 LEU E 136 74.65 -107.03 REMARK 500 ALA E 137 154.64 -49.65 REMARK 500 SER E 173 94.77 -62.74 REMARK 500 VAL F 56 -36.72 67.35 REMARK 500 SER F 57 -14.94 -144.62 REMARK 500 ASN F 143 74.96 52.82 REMARK 500 PHE H 519 92.23 50.99 REMARK 500 LEU H 523 -0.99 60.78 REMARK 500 LEU H 545 -45.89 -139.15 REMARK 500 SER H 546 -79.25 -72.75 REMARK 500 LEU H 568 43.41 -79.58 REMARK 500 REMARK 500 THIS ENTRY HAS 79 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 TYR M 54 0.07 SIDE_CHAIN REMARK 500 TYR M 145 0.07 SIDE_CHAIN REMARK 500 TYR M 197 0.09 SIDE_CHAIN REMARK 500 TYR R 94 0.07 SIDE_CHAIN REMARK 500 TYR R 206 0.10 SIDE_CHAIN REMARK 500 ARG E 100 0.10 SIDE_CHAIN REMARK 500 TYR E 206 0.11 SIDE_CHAIN REMARK 500 TYR F 54 0.07 SIDE_CHAIN REMARK 500 TYR F 145 0.08 SIDE_CHAIN REMARK 500 TYR F 197 0.09 SIDE_CHAIN REMARK 500 ARG H 617 0.08 SIDE_CHAIN REMARK 500 TYR N 206 0.07 SIDE_CHAIN REMARK 500 TYR O 145 0.09 SIDE_CHAIN REMARK 500 TYR O 197 0.07 SIDE_CHAIN REMARK 500 ARG Q 588 0.08 SIDE_CHAIN REMARK 500 ARG Q 617 0.07 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG K 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8DOW RELATED DB: PDB REMARK 900 RELATED ID: 8DKF RELATED DB: PDB REMARK 900 RELATED ID: EMD-27628 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF HIV-1 ENV(BG505.T332N SOSIP) IN COMPLEX WITH REMARK 900 DH1030.1 FAB DBREF 8DP1 M 1 219 PDB 8DP1 8DP1 1 219 DBREF 8DP1 R 1 230 PDB 8DP1 8DP1 1 230 DBREF 8DP1 S 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8DP1 W 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 8DP1 B 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 8DP1 E 1 230 PDB 8DP1 8DP1 1 230 DBREF 8DP1 F 1 219 PDB 8DP1 8DP1 1 219 DBREF 8DP1 H 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 DBREF 8DP1 J 31 508 UNP Q2N0S6 Q2N0S6_9HIV1 30 505 DBREF 8DP1 N 1 230 PDB 8DP1 8DP1 1 230 DBREF 8DP1 O 1 219 PDB 8DP1 8DP1 1 219 DBREF 8DP1 Q 512 664 UNP Q2N0S6 Q2N0S6_9HIV1 509 661 SEQADV 8DP1 PRO S 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8DP1 CYS S 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 8DP1 ALA W 137 UNP Q2N0S6 ASN 136 ENGINEERED MUTATION SEQADV 8DP1 ASN W 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 8DP1 CYS W 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8DP1 ARG W 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ARG W 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ARG W 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ARG W 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ARG W 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ALA B 137 UNP Q2N0S6 ASN 136 ENGINEERED MUTATION SEQADV 8DP1 ASN B 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 8DP1 CYS B 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8DP1 ARG B 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ARG B 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ARG B 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ARG B 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ARG B 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 PRO H 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8DP1 CYS H 605 UNP Q2N0S6 THR 602 CONFLICT SEQADV 8DP1 ALA J 137 UNP Q2N0S6 ASN 136 ENGINEERED MUTATION SEQADV 8DP1 ASN J 332 UNP Q2N0S6 THR 330 ENGINEERED MUTATION SEQADV 8DP1 CYS J 501 UNP Q2N0S6 ALA 498 CONFLICT SEQADV 8DP1 ARG J 509 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ARG J 510 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ARG J 511 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ARG J 512 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 ARG J 513 UNP Q2N0S6 EXPRESSION TAG SEQADV 8DP1 PRO Q 559 UNP Q2N0S6 ILE 556 CONFLICT SEQADV 8DP1 CYS Q 605 UNP Q2N0S6 THR 602 CONFLICT SEQRES 1 M 219 TYR VAL VAL MET THR GLN SER PRO LEU SER LEU PRO ILE SEQRES 2 M 219 THR PRO GLY GLN PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 M 219 GLN ARG LEU LEU HIS SER ASP GLY ASN THR TYR LEU ALA SEQRES 4 M 219 TRP TYR GLN GLN ARG PRO GLY GLN PRO PRO ARG ARG LEU SEQRES 5 M 219 ILE TYR GLU VAL SER LYS LEU ASP SER GLY VAL PRO ASP SEQRES 6 M 219 ARG PHE SER GLY SER GLY ALA GLY THR ASP PHE THR LEU SEQRES 7 M 219 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 M 219 TYR CYS GLY GLN ASN THR TYR LEU PRO TYR SER PHE GLY SEQRES 9 M 219 GLN GLY SER LYS VAL GLU ILE LYS ARG ALA VAL ALA ALA SEQRES 10 M 219 PRO SER VAL PHE ILE PHE PRO PRO SER GLU ASP GLN VAL SEQRES 11 M 219 LYS SER GLY THR VAL SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 M 219 PHE TYR PRO ARG GLU ALA SER VAL LYS TRP LYS VAL ASP SEQRES 13 M 219 GLY VAL LEU LYS THR GLY ASN SER GLN GLU SER VAL THR SEQRES 14 M 219 GLU GLN ASP SER LYS ASP ASN THR TYR SER LEU SER SER SEQRES 15 M 219 THR LEU THR LEU SER ASN THR ASP TYR GLN SER HIS ASN SEQRES 16 M 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 M 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 R 230 GLU VAL GLN LEU ALA GLU SER GLY GLY GLY LEU THR LYS SEQRES 2 R 230 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 R 230 PHE THR PHE SER ASP PHE TYR MET ASP TRP VAL ARG GLN SEQRES 4 R 230 THR PRO GLY LYS GLY LEU GLU TRP VAL SER ARG ILE ASN SEQRES 5 R 230 ASN ASP GLY ARG ASN LYS TRP TYR ALA ASP SER VAL ARG SEQRES 6 R 230 GLY ARG PHE THR VAL SER ARG GLU ASN ALA LYS ASN THR SEQRES 7 R 230 LEU TYR LEU GLN MET ASP SER LEU ARG ALA GLU ASP THR SEQRES 8 R 230 ALA VAL TYR TYR CYS ALA ARG ASP ARG PRO VAL TYR ARG SEQRES 9 R 230 TYR TRP SER GLY GLY TYR HIS LEU ASP PRO TRP GLY GLN SEQRES 10 R 230 GLY VAL VAL VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 R 230 PRO SER VAL PHE PRO LEU ALA PRO SER SER ARG SER THR SEQRES 12 R 230 SER GLU SER THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 R 230 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 R 230 SER LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 R 230 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 R 230 VAL PRO SER SER SER LEU GLY THR GLN THR TYR VAL CYS SEQRES 17 R 230 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 R 230 ARG VAL GLU ILE LYS THR CYS GLY GLY SEQRES 1 S 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 S 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 S 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 S 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 S 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 S 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 S 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 S 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 S 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 S 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 S 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 S 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 W 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 W 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 W 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 W 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 W 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 W 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 W 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 W 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 W 481 THR ASN ALA ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 W 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 W 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 W 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 W 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 W 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 W 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 W 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 W 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 W 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 W 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 W 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 W 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 W 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 W 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 W 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 W 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 W 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 W 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 W 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 W 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 W 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 W 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 W 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 W 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 W 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 W 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 W 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 W 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 B 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 B 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 B 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 B 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 B 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 B 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 B 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 B 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 B 481 THR ASN ALA ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 B 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 B 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 B 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 B 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 B 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 B 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 B 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 B 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 B 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 B 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 B 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 B 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 B 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 B 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 B 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 B 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 B 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 B 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 B 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 B 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 B 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 B 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 B 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 B 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 B 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 B 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 B 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 B 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 E 230 GLU VAL GLN LEU ALA GLU SER GLY GLY GLY LEU THR LYS SEQRES 2 E 230 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 230 PHE THR PHE SER ASP PHE TYR MET ASP TRP VAL ARG GLN SEQRES 4 E 230 THR PRO GLY LYS GLY LEU GLU TRP VAL SER ARG ILE ASN SEQRES 5 E 230 ASN ASP GLY ARG ASN LYS TRP TYR ALA ASP SER VAL ARG SEQRES 6 E 230 GLY ARG PHE THR VAL SER ARG GLU ASN ALA LYS ASN THR SEQRES 7 E 230 LEU TYR LEU GLN MET ASP SER LEU ARG ALA GLU ASP THR SEQRES 8 E 230 ALA VAL TYR TYR CYS ALA ARG ASP ARG PRO VAL TYR ARG SEQRES 9 E 230 TYR TRP SER GLY GLY TYR HIS LEU ASP PRO TRP GLY GLN SEQRES 10 E 230 GLY VAL VAL VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 E 230 PRO SER VAL PHE PRO LEU ALA PRO SER SER ARG SER THR SEQRES 12 E 230 SER GLU SER THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 E 230 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 E 230 SER LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 E 230 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 E 230 VAL PRO SER SER SER LEU GLY THR GLN THR TYR VAL CYS SEQRES 17 E 230 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 E 230 ARG VAL GLU ILE LYS THR CYS GLY GLY SEQRES 1 F 219 TYR VAL VAL MET THR GLN SER PRO LEU SER LEU PRO ILE SEQRES 2 F 219 THR PRO GLY GLN PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 F 219 GLN ARG LEU LEU HIS SER ASP GLY ASN THR TYR LEU ALA SEQRES 4 F 219 TRP TYR GLN GLN ARG PRO GLY GLN PRO PRO ARG ARG LEU SEQRES 5 F 219 ILE TYR GLU VAL SER LYS LEU ASP SER GLY VAL PRO ASP SEQRES 6 F 219 ARG PHE SER GLY SER GLY ALA GLY THR ASP PHE THR LEU SEQRES 7 F 219 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 F 219 TYR CYS GLY GLN ASN THR TYR LEU PRO TYR SER PHE GLY SEQRES 9 F 219 GLN GLY SER LYS VAL GLU ILE LYS ARG ALA VAL ALA ALA SEQRES 10 F 219 PRO SER VAL PHE ILE PHE PRO PRO SER GLU ASP GLN VAL SEQRES 11 F 219 LYS SER GLY THR VAL SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 F 219 PHE TYR PRO ARG GLU ALA SER VAL LYS TRP LYS VAL ASP SEQRES 13 F 219 GLY VAL LEU LYS THR GLY ASN SER GLN GLU SER VAL THR SEQRES 14 F 219 GLU GLN ASP SER LYS ASP ASN THR TYR SER LEU SER SER SEQRES 15 F 219 THR LEU THR LEU SER ASN THR ASP TYR GLN SER HIS ASN SEQRES 16 F 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 F 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 H 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 H 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 H 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 H 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 H 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 H 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 H 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 H 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 H 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 H 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 H 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 H 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP SEQRES 1 J 481 ALA GLU ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO SEQRES 2 J 481 VAL TRP LYS ASP ALA GLU THR THR LEU PHE CYS ALA SER SEQRES 3 J 481 ASP ALA LYS ALA TYR GLU THR GLU LYS HIS ASN VAL TRP SEQRES 4 J 481 ALA THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN SEQRES 5 J 481 GLU ILE HIS LEU GLU ASN VAL THR GLU GLU PHE ASN MET SEQRES 6 J 481 TRP LYS ASN ASN MET VAL GLU GLN MET HIS THR ASP ILE SEQRES 7 J 481 ILE SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS SEQRES 8 J 481 LEU THR PRO LEU CYS VAL THR LEU GLN CYS THR ASN VAL SEQRES 9 J 481 THR ASN ALA ILE THR ASP ASP MET ARG GLY GLU LEU LYS SEQRES 10 J 481 ASN CYS SER PHE ASN MET THR THR GLU LEU ARG ASP LYS SEQRES 11 J 481 LYS GLN LYS VAL TYR SER LEU PHE TYR ARG LEU ASP VAL SEQRES 12 J 481 VAL GLN ILE ASN GLU ASN GLN GLY ASN ARG SER ASN ASN SEQRES 13 J 481 SER ASN LYS GLU TYR ARG LEU ILE ASN CYS ASN THR SER SEQRES 14 J 481 ALA ILE THR GLN ALA CYS PRO LYS VAL SER PHE GLU PRO SEQRES 15 J 481 ILE PRO ILE HIS TYR CYS ALA PRO ALA GLY PHE ALA ILE SEQRES 16 J 481 LEU LYS CYS LYS ASP LYS LYS PHE ASN GLY THR GLY PRO SEQRES 17 J 481 CYS PRO SER VAL SER THR VAL GLN CYS THR HIS GLY ILE SEQRES 18 J 481 LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER SEQRES 19 J 481 LEU ALA GLU GLU GLU VAL MET ILE ARG SER GLU ASN ILE SEQRES 20 J 481 THR ASN ASN ALA LYS ASN ILE LEU VAL GLN PHE ASN THR SEQRES 21 J 481 PRO VAL GLN ILE ASN CYS THR ARG PRO ASN ASN ASN THR SEQRES 22 J 481 ARG LYS SER ILE ARG ILE GLY PRO GLY GLN ALA PHE TYR SEQRES 23 J 481 ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS SEQRES 24 J 481 CYS ASN VAL SER LYS ALA THR TRP ASN GLU THR LEU GLY SEQRES 25 J 481 LYS VAL VAL LYS GLN LEU ARG LYS HIS PHE GLY ASN ASN SEQRES 26 J 481 THR ILE ILE ARG PHE ALA ASN SER SER GLY GLY ASP LEU SEQRES 27 J 481 GLU VAL THR THR HIS SER PHE ASN CYS GLY GLY GLU PHE SEQRES 28 J 481 PHE TYR CYS ASN THR SER GLY LEU PHE ASN SER THR TRP SEQRES 29 J 481 ILE SER ASN THR SER VAL GLN GLY SER ASN SER THR GLY SEQRES 30 J 481 SER ASN ASP SER ILE THR LEU PRO CYS ARG ILE LYS GLN SEQRES 31 J 481 ILE ILE ASN MET TRP GLN ARG ILE GLY GLN ALA MET TYR SEQRES 32 J 481 ALA PRO PRO ILE GLN GLY VAL ILE ARG CYS VAL SER ASN SEQRES 33 J 481 ILE THR GLY LEU ILE LEU THR ARG ASP GLY GLY SER THR SEQRES 34 J 481 ASN SER THR THR GLU THR PHE ARG PRO GLY GLY GLY ASP SEQRES 35 J 481 MET ARG ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS SEQRES 36 J 481 VAL VAL LYS ILE GLU PRO LEU GLY VAL ALA PRO THR ARG SEQRES 37 J 481 CYS LYS ARG ARG VAL VAL GLY ARG ARG ARG ARG ARG ARG SEQRES 1 N 230 GLU VAL GLN LEU ALA GLU SER GLY GLY GLY LEU THR LYS SEQRES 2 N 230 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 N 230 PHE THR PHE SER ASP PHE TYR MET ASP TRP VAL ARG GLN SEQRES 4 N 230 THR PRO GLY LYS GLY LEU GLU TRP VAL SER ARG ILE ASN SEQRES 5 N 230 ASN ASP GLY ARG ASN LYS TRP TYR ALA ASP SER VAL ARG SEQRES 6 N 230 GLY ARG PHE THR VAL SER ARG GLU ASN ALA LYS ASN THR SEQRES 7 N 230 LEU TYR LEU GLN MET ASP SER LEU ARG ALA GLU ASP THR SEQRES 8 N 230 ALA VAL TYR TYR CYS ALA ARG ASP ARG PRO VAL TYR ARG SEQRES 9 N 230 TYR TRP SER GLY GLY TYR HIS LEU ASP PRO TRP GLY GLN SEQRES 10 N 230 GLY VAL VAL VAL THR VAL SER SER ALA SER THR LYS GLY SEQRES 11 N 230 PRO SER VAL PHE PRO LEU ALA PRO SER SER ARG SER THR SEQRES 12 N 230 SER GLU SER THR ALA ALA LEU GLY CYS LEU VAL LYS ASP SEQRES 13 N 230 TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY SEQRES 14 N 230 SER LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU SEQRES 15 N 230 GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR SEQRES 16 N 230 VAL PRO SER SER SER LEU GLY THR GLN THR TYR VAL CYS SEQRES 17 N 230 ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS SEQRES 18 N 230 ARG VAL GLU ILE LYS THR CYS GLY GLY SEQRES 1 O 219 TYR VAL VAL MET THR GLN SER PRO LEU SER LEU PRO ILE SEQRES 2 O 219 THR PRO GLY GLN PRO ALA SER ILE SER CYS ARG SER SER SEQRES 3 O 219 GLN ARG LEU LEU HIS SER ASP GLY ASN THR TYR LEU ALA SEQRES 4 O 219 TRP TYR GLN GLN ARG PRO GLY GLN PRO PRO ARG ARG LEU SEQRES 5 O 219 ILE TYR GLU VAL SER LYS LEU ASP SER GLY VAL PRO ASP SEQRES 6 O 219 ARG PHE SER GLY SER GLY ALA GLY THR ASP PHE THR LEU SEQRES 7 O 219 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 O 219 TYR CYS GLY GLN ASN THR TYR LEU PRO TYR SER PHE GLY SEQRES 9 O 219 GLN GLY SER LYS VAL GLU ILE LYS ARG ALA VAL ALA ALA SEQRES 10 O 219 PRO SER VAL PHE ILE PHE PRO PRO SER GLU ASP GLN VAL SEQRES 11 O 219 LYS SER GLY THR VAL SER VAL VAL CYS LEU LEU ASN ASN SEQRES 12 O 219 PHE TYR PRO ARG GLU ALA SER VAL LYS TRP LYS VAL ASP SEQRES 13 O 219 GLY VAL LEU LYS THR GLY ASN SER GLN GLU SER VAL THR SEQRES 14 O 219 GLU GLN ASP SER LYS ASP ASN THR TYR SER LEU SER SER SEQRES 15 O 219 THR LEU THR LEU SER ASN THR ASP TYR GLN SER HIS ASN SEQRES 16 O 219 VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER SEQRES 17 O 219 PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 Q 153 ALA VAL GLY ILE GLY ALA VAL PHE LEU GLY PHE LEU GLY SEQRES 2 Q 153 ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR LEU SEQRES 3 Q 153 THR VAL GLN ALA ARG ASN LEU LEU SER GLY ILE VAL GLN SEQRES 4 Q 153 GLN GLN SER ASN LEU LEU ARG ALA PRO GLU ALA GLN GLN SEQRES 5 Q 153 HIS LEU LEU LYS LEU THR VAL TRP GLY ILE LYS GLN LEU SEQRES 6 Q 153 GLN ALA ARG VAL LEU ALA VAL GLU ARG TYR LEU ARG ASP SEQRES 7 Q 153 GLN GLN LEU LEU GLY ILE TRP GLY CYS SER GLY LYS LEU SEQRES 8 Q 153 ILE CYS CYS THR ASN VAL PRO TRP ASN SER SER TRP SER SEQRES 9 Q 153 ASN ARG ASN LEU SER GLU ILE TRP ASP ASN MET THR TRP SEQRES 10 Q 153 LEU GLN TRP ASP LYS GLU ILE SER ASN TYR THR GLN ILE SEQRES 11 Q 153 ILE TYR GLY LEU LEU GLU GLU SER GLN ASN GLN GLN GLU SEQRES 12 Q 153 LYS ASN GLU GLN ASP LEU LEU ALA LEU ASP HET NAG S 701 14 HET NAG S 702 14 HET NAG S 703 14 HET NAG W 601 14 HET NAG W 602 14 HET NAG W 603 14 HET NAG W 604 14 HET NAG W 605 14 HET NAG W 606 14 HET NAG W 607 14 HET NAG W 608 14 HET NAG B 601 14 HET NAG B 602 14 HET NAG B 603 14 HET NAG B 604 14 HET NAG B 605 14 HET NAG B 606 14 HET NAG B 607 14 HET NAG B 608 14 HET NAG H 701 14 HET NAG H 702 14 HET NAG H 703 14 HET NAG J 601 14 HET NAG J 602 14 HET NAG J 603 14 HET NAG J 604 14 HET NAG J 605 14 HET NAG J 606 14 HET NAG J 607 14 HET NAG J 608 14 HET NAG Q 701 14 HET NAG Q 702 14 HET NAG Q 703 14 HET NAG A 1 14 HET NAG A 2 14 HET BMA A 3 11 HET MAN A 4 11 HET MAN A 5 11 HET MAN A 6 11 HET MAN A 7 11 HET MAN A 8 11 HET MAN A 9 11 HET MAN A 10 11 HET NAG C 1 14 HET NAG C 2 14 HET BMA C 3 11 HET NAG D 1 14 HET NAG D 2 14 HET BMA D 3 11 HET NAG G 1 14 HET NAG G 2 14 HET NAG I 1 14 HET NAG I 2 14 HET NAG K 1 14 HET NAG K 2 14 HET BMA K 3 11 HET MAN K 4 11 HET MAN K 5 11 HET MAN K 6 11 HET MAN K 7 11 HET MAN K 8 11 HET MAN K 9 11 HET MAN K 10 11 HET NAG L 1 14 HET NAG L 2 14 HET BMA L 3 11 HET NAG P 1 14 HET NAG P 2 14 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 V 1 14 HET NAG V 2 14 HET BMA V 3 11 HET MAN V 4 11 HET MAN V 5 11 HET MAN V 6 11 HET MAN V 7 11 HET MAN V 8 11 HET MAN V 9 11 HET MAN V 10 11 HET NAG X 1 14 HET NAG X 2 14 HET BMA X 3 11 HET NAG Y 1 14 HET NAG Y 2 14 HET NAG Z 1 14 HET NAG Z 2 14 HET NAG a 1 14 HET NAG a 2 14 HET BMA a 3 11 HET MAN a 4 11 HET MAN a 5 11 HETNAM NAG N-ACETYL-D-GLUCOSAMINE HETNAM BMA BETA-D-MANNOSE HETNAM MAN ALPHA-D-MANNOSE FORMUL 13 NAG 63(C8 H15 N O6) FORMUL 46 BMA 9(C6 H12 O6) FORMUL 46 MAN 23(C6 H12 O6) HELIX 1 AA1 GLU M 84 VAL M 88 5 5 HELIX 2 AA2 ASP M 128 SER M 132 5 5 HELIX 3 AA3 ASN M 188 SER M 193 1 6 HELIX 4 AA4 THR R 28 SER R 30 5 3 HELIX 5 AA5 ASN R 74 LYS R 76 5 3 HELIX 6 AA6 ARG R 87 THR R 91 5 5 HELIX 7 AA7 SER R 139 GLU R 145 1 7 HELIX 8 AA8 SER R 199 LEU R 201 5 3 HELIX 9 AA9 THR S 529 SER S 534 1 6 HELIX 10 AB1 THR S 536 ARG S 542 1 7 HELIX 11 AB2 THR S 569 TRP S 596 1 28 HELIX 12 AB3 LEU S 619 ASP S 624 1 6 HELIX 13 AB4 THR S 627 SER S 636 1 10 HELIX 14 AB5 TYR S 638 ALA S 662 1 25 HELIX 15 AB6 ALA W 70 CYS W 74 5 5 HELIX 16 AB7 ASN W 99 LYS W 117 1 19 HELIX 17 AB8 LEU W 122 CYS W 126 5 5 HELIX 18 AB9 ASP W 141 GLY W 152 5 4 HELIX 19 AC1 SER W 334 GLY W 354 1 21 HELIX 20 AC2 ASP W 368 THR W 373 1 6 HELIX 21 AC3 THR W 387 LEU W 390 5 4 HELIX 22 AC4 MET W 475 TYR W 484 1 10 HELIX 23 AC5 ALA B 70 CYS B 74 5 5 HELIX 24 AC6 ASN B 99 LYS B 117 1 19 HELIX 25 AC7 LEU B 122 CYS B 126 5 5 HELIX 26 AC8 LYS B 335 GLY B 354 1 20 HELIX 27 AC9 ASP B 368 THR B 373 1 6 HELIX 28 AD1 THR B 387 LEU B 390 5 4 HELIX 29 AD2 MET B 475 TYR B 484 1 10 HELIX 30 AD3 THR E 28 SER E 30 5 3 HELIX 31 AD4 ASN E 74 LYS E 76 5 3 HELIX 32 AD5 ARG E 87 THR E 91 5 5 HELIX 33 AD6 ARG E 141 GLU E 145 5 5 HELIX 34 AD7 SER E 199 LEU E 201 5 3 HELIX 35 AD8 LYS E 213 ASN E 216 5 4 HELIX 36 AD9 GLU F 84 VAL F 88 5 5 HELIX 37 AE1 SER F 126 LYS F 131 1 6 HELIX 38 AE2 ASN F 188 SER F 193 1 6 HELIX 39 AE3 THR H 529 SER H 534 1 6 HELIX 40 AE4 LEU H 537 ARG H 542 1 6 HELIX 41 AE5 THR H 569 TRP H 596 1 28 HELIX 42 AE6 LEU H 619 ASP H 624 1 6 HELIX 43 AE7 THR H 627 SER H 636 1 10 HELIX 44 AE8 TYR H 638 ALA H 662 1 25 HELIX 45 AE9 ALA J 70 CYS J 74 5 5 HELIX 46 AF1 ASN J 98 LYS J 117 1 20 HELIX 47 AF2 ASP J 141 GLY J 152 5 4 HELIX 48 AF3 ASN J 195 THR J 198 5 4 HELIX 49 AF4 LYS J 335 PHE J 353 1 19 HELIX 50 AF5 ASP J 368 THR J 373 1 6 HELIX 51 AF6 THR J 387 LEU J 390 5 4 HELIX 52 AF7 MET J 475 TYR J 484 1 10 HELIX 53 AF8 THR N 28 SER N 30 5 3 HELIX 54 AF9 ASN N 74 LYS N 76 5 3 HELIX 55 AG1 ARG N 87 THR N 91 5 5 HELIX 56 AG2 SER N 139 SER N 144 1 6 HELIX 57 AG3 SER N 199 LEU N 201 5 3 HELIX 58 AG4 GLU O 84 VAL O 88 5 5 HELIX 59 AG5 SER O 126 LYS O 131 1 6 HELIX 60 AG6 ASN O 188 SER O 193 1 6 HELIX 61 AG7 THR Q 529 SER Q 534 1 6 HELIX 62 AG8 THR Q 536 ARG Q 542 1 7 HELIX 63 AG9 THR Q 569 TRP Q 596 1 28 HELIX 64 AH1 ASN Q 618 ASP Q 624 1 7 HELIX 65 AH2 THR Q 627 SER Q 636 1 10 HELIX 66 AH3 TYR Q 638 ALA Q 662 1 25 SHEET 1 AA1 4 MET M 4 GLN M 6 0 SHEET 2 AA1 4 ALA M 19 SER M 25 -1 O ARG M 24 N THR M 5 SHEET 3 AA1 4 ASP M 75 ILE M 80 -1 O ILE M 80 N ALA M 19 SHEET 4 AA1 4 PHE M 67 ALA M 72 -1 N SER M 70 O THR M 77 SHEET 1 AA2 7 SER M 10 ILE M 13 0 SHEET 2 AA2 7 LEU M 38 GLN M 43 0 SHEET 3 AA2 7 ARG M 50 TYR M 54 -1 O LEU M 52 N TRP M 40 SHEET 4 AA2 7 LYS M 58 LEU M 59 -1 O LYS M 58 N TYR M 54 SHEET 5 AA2 7 GLY M 89 GLN M 95 -1 O TYR M 92 N TYR M 41 SHEET 6 AA2 7 SER M 102 PHE M 103 -1 O SER M 102 N GLN M 95 SHEET 7 AA2 7 SER M 107 ILE M 111 -1 O SER M 107 N TYR M 91 SHEET 1 AA3 4 SER M 119 PHE M 123 0 SHEET 2 AA3 4 THR M 134 PHE M 144 -1 O LEU M 140 N PHE M 121 SHEET 3 AA3 4 TYR M 178 SER M 187 -1 O LEU M 180 N LEU M 141 SHEET 4 AA3 4 SER M 164 VAL M 168 -1 N SER M 167 O SER M 181 SHEET 1 AA4 4 VAL M 158 LEU M 159 0 SHEET 2 AA4 4 ALA M 149 VAL M 155 -1 N VAL M 155 O VAL M 158 SHEET 3 AA4 4 VAL M 196 HIS M 203 -1 O GLU M 200 N LYS M 152 SHEET 4 AA4 4 VAL M 210 ASN M 215 -1 O VAL M 210 N VAL M 201 SHEET 1 AA5 4 GLN R 3 SER R 7 0 SHEET 2 AA5 4 LEU R 18 SER R 25 -1 O ALA R 23 N ALA R 5 SHEET 3 AA5 4 THR R 78 MET R 83 -1 O LEU R 79 N CYS R 22 SHEET 4 AA5 4 PHE R 68 GLU R 73 -1 N SER R 71 O TYR R 80 SHEET 1 AA6 7 LEU R 11 THR R 12 0 SHEET 2 AA6 7 PHE R 32 THR R 40 0 SHEET 3 AA6 7 GLY R 44 ILE R 51 -1 O GLU R 46 N ARG R 38 SHEET 4 AA6 7 LYS R 58 TYR R 60 -1 O TRP R 59 N ARG R 50 SHEET 5 AA6 7 ALA R 92 TYR R 103 -1 O TYR R 95 N VAL R 37 SHEET 6 AA6 7 TRP R 106 SER R 107 -1 O TRP R 106 N TYR R 103 SHEET 7 AA6 7 VAL R 119 VAL R 123 -1 O VAL R 119 N TYR R 94 SHEET 1 AA7 5 SER R 132 LEU R 136 0 SHEET 2 AA7 5 THR R 147 TYR R 157 -1 O LYS R 155 N SER R 132 SHEET 3 AA7 5 VAL R 175 THR R 177 0 SHEET 4 AA7 5 VAL R 181 LEU R 182 0 SHEET 5 AA7 5 TYR R 188 PRO R 197 -1 O SER R 189 N VAL R 181 SHEET 1 AA8 3 THR R 163 TRP R 166 0 SHEET 2 AA8 3 VAL R 207 ASN R 211 -1 O ASN R 209 N SER R 165 SHEET 3 AA8 3 LYS R 218 ARG R 222 -1 O VAL R 219 N VAL R 210 SHEET 1 AA9 3 ILE S 603 PRO S 609 0 SHEET 2 AA9 3 TRP W 35 TYR W 40 -1 O VAL W 38 N CYS S 604 SHEET 3 AA9 3 LEU W 494 THR W 499 -1 O GLY W 495 N TYR W 39 SHEET 1 AB1 5 TRP W 45 ASP W 47 0 SHEET 2 AB1 5 TYR W 486 ILE W 491 -1 O LYS W 490 N LYS W 46 SHEET 3 AB1 5 PHE W 223 CYS W 228 -1 N LEU W 226 O LYS W 487 SHEET 4 AB1 5 VAL W 242 VAL W 245 -1 O SER W 243 N LYS W 227 SHEET 5 AB1 5 GLU W 83 HIS W 85 -1 N ILE W 84 O THR W 244 SHEET 1 AB2 2 PHE W 53 ALA W 55 0 SHEET 2 AB2 2 HIS W 216 CYS W 218 -1 O HIS W 216 N ALA W 55 SHEET 1 AB3 2 GLU W 91 ASN W 94 0 SHEET 2 AB3 2 THR W 236 CYS W 239 -1 O CYS W 239 N GLU W 91 SHEET 1 AB4 5 LYS W 169 TYR W 177 0 SHEET 2 AB4 5 LEU W 154 THR W 162 -1 N LYS W 155 O PHE W 176 SHEET 3 AB4 5 LEU W 129 ASN W 133 -1 N GLN W 130 O SER W 158 SHEET 4 AB4 5 GLU W 190 LEU W 193 -1 O TYR W 191 N LEU W 129 SHEET 5 AB4 5 VAL W 181 GLN W 183 -1 N VAL W 182 O ARG W 192 SHEET 1 AB5 3 ALA W 200 GLN W 203 0 SHEET 2 AB5 3 GLN W 432 TYR W 435 1 O TYR W 435 N THR W 202 SHEET 3 AB5 3 ILE W 423 ILE W 424 -1 N ILE W 424 O MET W 434 SHEET 1 AB612 LEU W 259 LEU W 261 0 SHEET 2 AB612 MET W 271 ARG W 273 0 SHEET 3 AB612 ILE W 284 GLY W 312 -1 O LEU W 285 N ARG W 273 SHEET 4 AB612 GLN W 315 ILE W 323 -1 O PHE W 317 N ILE W 307 SHEET 5 AB612 HIS W 330 VAL W 333 -1 O ASN W 332 N ASN W 295 SHEET 6 AB612 ILE W 359 PHE W 361 0 SHEET 7 AB612 HIS W 374 CYS W 378 0 SHEET 8 AB612 GLU W 381 CYS W 385 -1 O PHE W 383 N PHE W 376 SHEET 9 AB612 SER W 393 TRP W 395 -1 O TRP W 395 N ILE W 359 SHEET 10 AB612 ILE W 414 LYS W 421 -1 O ARG W 419 N TYR W 384 SHEET 11 AB612 GLY W 441 ARG W 456 -1 O ILE W 449 N VAL W 292 SHEET 12 AB612 GLU W 466 PRO W 470 -1 O ARG W 469 N THR W 455 SHEET 1 AB7 3 LEU B 494 THR B 499 0 SHEET 2 AB7 3 TRP B 35 TYR B 40 -1 N TRP B 35 O THR B 499 SHEET 3 AB7 3 ILE H 603 PRO H 609 -1 O CYS H 604 N VAL B 38 SHEET 1 AB8 5 TRP B 45 ASP B 47 0 SHEET 2 AB8 5 TYR B 486 ILE B 491 -1 O LYS B 490 N LYS B 46 SHEET 3 AB8 5 PHE B 223 CYS B 228 -1 N ALA B 224 O VAL B 489 SHEET 4 AB8 5 VAL B 242 VAL B 245 -1 O SER B 243 N LYS B 227 SHEET 5 AB8 5 GLU B 83 HIS B 85 -1 N ILE B 84 O THR B 244 SHEET 1 AB9 2 PHE B 53 ALA B 55 0 SHEET 2 AB9 2 HIS B 216 CYS B 218 -1 O HIS B 216 N ALA B 55 SHEET 1 AC1 2 GLU B 91 ASN B 94 0 SHEET 2 AC1 2 THR B 236 CYS B 239 -1 O CYS B 239 N GLU B 91 SHEET 1 AC2 5 LYS B 169 TYR B 177 0 SHEET 2 AC2 5 LEU B 154 THR B 162 -1 N PHE B 159 O VAL B 172 SHEET 3 AC2 5 LEU B 129 ASN B 133 -1 N GLN B 130 O SER B 158 SHEET 4 AC2 5 GLU B 190 LEU B 193 -1 O TYR B 191 N LEU B 129 SHEET 5 AC2 5 VAL B 181 GLN B 183 -1 N VAL B 182 O ARG B 192 SHEET 1 AC3 3 ALA B 200 GLN B 203 0 SHEET 2 AC3 3 GLN B 432 TYR B 435 1 O TYR B 435 N THR B 202 SHEET 3 AC3 3 ILE B 423 ILE B 424 -1 N ILE B 424 O MET B 434 SHEET 1 AC412 LEU B 259 LEU B 261 0 SHEET 2 AC412 MET B 271 ARG B 273 0 SHEET 3 AC412 ILE B 284 GLY B 312 -1 O LEU B 285 N ARG B 273 SHEET 4 AC412 GLN B 315 ILE B 323 -1 O PHE B 317 N ILE B 307 SHEET 5 AC412 HIS B 330 SER B 334 -1 O ASN B 332 N ASN B 295 SHEET 6 AC412 ILE B 359 PHE B 361 0 SHEET 7 AC412 HIS B 374 CYS B 378 0 SHEET 8 AC412 GLU B 381 CYS B 385 -1 O GLU B 381 N CYS B 378 SHEET 9 AC412 SER B 393 TRP B 395 -1 O TRP B 395 N ILE B 359 SHEET 10 AC412 SER B 413 LYS B 421 -1 O ARG B 419 N TYR B 384 SHEET 11 AC412 GLY B 441 ARG B 456 -1 O ILE B 449 N VAL B 292 SHEET 12 AC412 GLU B 466 PRO B 470 -1 O ARG B 469 N THR B 455 SHEET 1 AC5 4 GLN E 3 SER E 7 0 SHEET 2 AC5 4 LEU E 18 SER E 25 -1 O SER E 21 N SER E 7 SHEET 3 AC5 4 THR E 78 MET E 83 -1 O LEU E 79 N CYS E 22 SHEET 4 AC5 4 PHE E 68 GLU E 73 -1 N SER E 71 O TYR E 80 SHEET 1 AC6 7 GLY E 10 THR E 12 0 SHEET 2 AC6 7 PHE E 32 THR E 40 0 SHEET 3 AC6 7 GLY E 44 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 4 AC6 7 LYS E 58 TYR E 60 -1 O TRP E 59 N ARG E 50 SHEET 5 AC6 7 ALA E 92 TYR E 103 -1 O TYR E 95 N VAL E 37 SHEET 6 AC6 7 TRP E 106 SER E 107 -1 O TRP E 106 N TYR E 103 SHEET 7 AC6 7 VAL E 119 VAL E 123 -1 O VAL E 119 N TYR E 94 SHEET 1 AC7 5 SER E 132 LEU E 136 0 SHEET 2 AC7 5 THR E 147 TYR E 157 -1 O LYS E 155 N SER E 132 SHEET 3 AC7 5 HIS E 176 THR E 177 0 SHEET 4 AC7 5 VAL E 181 LEU E 182 0 SHEET 5 AC7 5 TYR E 188 PRO E 197 -1 O SER E 189 N VAL E 181 SHEET 1 AC8 3 THR E 163 TRP E 166 0 SHEET 2 AC8 3 VAL E 207 HIS E 212 -1 O ASN E 209 N SER E 165 SHEET 3 AC8 3 THR E 217 ARG E 222 -1 O VAL E 219 N VAL E 210 SHEET 1 AC9 4 MET F 4 GLN F 6 0 SHEET 2 AC9 4 ALA F 19 SER F 25 -1 O ARG F 24 N THR F 5 SHEET 3 AC9 4 ASP F 75 ILE F 80 -1 O PHE F 76 N CYS F 23 SHEET 4 AC9 4 PHE F 67 ALA F 72 -1 N SER F 70 O THR F 77 SHEET 1 AD1 7 SER F 10 ILE F 13 0 SHEET 2 AD1 7 LEU F 38 GLN F 43 0 SHEET 3 AD1 7 ARG F 50 TYR F 54 -1 O ARG F 50 N GLN F 42 SHEET 4 AD1 7 LYS F 58 LEU F 59 -1 O LYS F 58 N TYR F 54 SHEET 5 AD1 7 GLY F 89 GLN F 95 -1 O GLY F 94 N ALA F 39 SHEET 6 AD1 7 SER F 102 PHE F 103 -1 O SER F 102 N GLN F 95 SHEET 7 AD1 7 SER F 107 ILE F 111 -1 O SER F 107 N TYR F 91 SHEET 1 AD2 4 SER F 119 PHE F 123 0 SHEET 2 AD2 4 THR F 134 PHE F 144 -1 O LEU F 140 N PHE F 121 SHEET 3 AD2 4 TYR F 178 SER F 187 -1 O LEU F 180 N LEU F 141 SHEET 4 AD2 4 SER F 164 VAL F 168 -1 N SER F 167 O SER F 181 SHEET 1 AD3 4 VAL F 158 LEU F 159 0 SHEET 2 AD3 4 ALA F 149 VAL F 155 -1 N VAL F 155 O VAL F 158 SHEET 3 AD3 4 VAL F 196 HIS F 203 -1 O GLU F 200 N LYS F 152 SHEET 4 AD3 4 VAL F 210 ASN F 215 -1 O VAL F 210 N VAL F 201 SHEET 1 AD4 3 LEU J 494 THR J 499 0 SHEET 2 AD4 3 TRP J 35 TYR J 40 -1 N TYR J 39 O GLY J 495 SHEET 3 AD4 3 ILE Q 603 PRO Q 609 -1 O CYS Q 604 N VAL J 38 SHEET 1 AD5 5 TRP J 45 ASP J 47 0 SHEET 2 AD5 5 TYR J 486 ILE J 491 -1 O LYS J 490 N LYS J 46 SHEET 3 AD5 5 PHE J 223 CYS J 228 -1 N LEU J 226 O LYS J 487 SHEET 4 AD5 5 VAL J 242 VAL J 245 -1 O SER J 243 N LYS J 227 SHEET 5 AD5 5 GLU J 83 HIS J 85 -1 N ILE J 84 O THR J 244 SHEET 1 AD6 2 PHE J 53 ALA J 55 0 SHEET 2 AD6 2 HIS J 216 CYS J 218 -1 O CYS J 218 N PHE J 53 SHEET 1 AD7 2 HIS J 66 ASN J 67 0 SHEET 2 AD7 2 VAL J 208 SER J 209 1 O SER J 209 N HIS J 66 SHEET 1 AD8 2 GLU J 91 ASN J 94 0 SHEET 2 AD8 2 THR J 236 CYS J 239 -1 O CYS J 239 N GLU J 91 SHEET 1 AD9 5 LYS J 169 TYR J 177 0 SHEET 2 AD9 5 LEU J 154 THR J 162 -1 N LYS J 155 O PHE J 176 SHEET 3 AD9 5 LEU J 129 ASN J 133 -1 N GLN J 130 O SER J 158 SHEET 4 AD9 5 GLU J 190 LEU J 193 -1 O TYR J 191 N LEU J 129 SHEET 5 AD9 5 VAL J 181 GLN J 183 -1 N VAL J 182 O ARG J 192 SHEET 1 AE1 3 ALA J 200 GLN J 203 0 SHEET 2 AE1 3 GLN J 432 TYR J 435 1 O TYR J 435 N THR J 202 SHEET 3 AE1 3 ILE J 423 ILE J 424 -1 N ILE J 424 O MET J 434 SHEET 1 AE212 LEU J 259 LEU J 261 0 SHEET 2 AE212 MET J 271 ARG J 273 0 SHEET 3 AE212 ILE J 284 GLY J 312 -1 O LEU J 285 N ARG J 273 SHEET 4 AE212 GLN J 315 ILE J 323 -1 O PHE J 317 N ILE J 307 SHEET 5 AE212 HIS J 330 SER J 334 -1 O ASN J 332 N ASN J 295 SHEET 6 AE212 ILE J 359 PHE J 361 0 SHEET 7 AE212 HIS J 374 CYS J 378 0 SHEET 8 AE212 GLU J 381 CYS J 385 -1 O GLU J 381 N CYS J 378 SHEET 9 AE212 SER J 393 TRP J 395 -1 O TRP J 395 N ILE J 359 SHEET 10 AE212 SER J 413 LYS J 421 -1 O ARG J 419 N TYR J 384 SHEET 11 AE212 GLY J 441 ARG J 456 -1 O SER J 447 N ILE J 294 SHEET 12 AE212 GLU J 466 PRO J 470 -1 O ARG J 469 N THR J 455 SHEET 1 AE3 4 GLN N 3 SER N 7 0 SHEET 2 AE3 4 LEU N 18 SER N 25 -1 O SER N 21 N SER N 7 SHEET 3 AE3 4 THR N 78 MET N 83 -1 O MET N 83 N LEU N 18 SHEET 4 AE3 4 PHE N 68 GLU N 73 -1 N SER N 71 O TYR N 80 SHEET 1 AE4 7 GLY N 10 THR N 12 0 SHEET 2 AE4 7 PHE N 32 THR N 40 0 SHEET 3 AE4 7 GLY N 44 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 4 AE4 7 LYS N 58 TYR N 60 -1 O TRP N 59 N ARG N 50 SHEET 5 AE4 7 ALA N 92 TYR N 103 -1 O TYR N 95 N VAL N 37 SHEET 6 AE4 7 TRP N 106 SER N 107 -1 O TRP N 106 N TYR N 103 SHEET 7 AE4 7 VAL N 119 VAL N 123 -1 O VAL N 119 N TYR N 94 SHEET 1 AE5 5 SER N 132 LEU N 136 0 SHEET 2 AE5 5 THR N 147 TYR N 157 -1 O LYS N 155 N SER N 132 SHEET 3 AE5 5 HIS N 176 THR N 177 0 SHEET 4 AE5 5 VAL N 181 LEU N 182 0 SHEET 5 AE5 5 TYR N 188 PRO N 197 -1 O SER N 189 N VAL N 181 SHEET 1 AE6 3 THR N 163 TRP N 166 0 SHEET 2 AE6 3 VAL N 207 ASN N 211 -1 O ASN N 209 N SER N 165 SHEET 3 AE6 3 LYS N 218 ARG N 222 -1 O VAL N 219 N VAL N 210 SHEET 1 AE7 4 MET O 4 GLN O 6 0 SHEET 2 AE7 4 ALA O 19 SER O 25 -1 O ARG O 24 N THR O 5 SHEET 3 AE7 4 ASP O 75 ILE O 80 -1 O PHE O 76 N CYS O 23 SHEET 4 AE7 4 PHE O 67 ALA O 72 -1 N SER O 70 O THR O 77 SHEET 1 AE8 7 SER O 10 ILE O 13 0 SHEET 2 AE8 7 LEU O 38 GLN O 43 0 SHEET 3 AE8 7 ARG O 50 TYR O 54 -1 O LEU O 52 N TRP O 40 SHEET 4 AE8 7 LYS O 58 LEU O 59 -1 O LYS O 58 N TYR O 54 SHEET 5 AE8 7 GLY O 89 GLN O 95 -1 O TYR O 92 N TYR O 41 SHEET 6 AE8 7 SER O 102 PHE O 103 -1 O SER O 102 N GLN O 95 SHEET 7 AE8 7 SER O 107 ILE O 111 -1 O SER O 107 N TYR O 91 SHEET 1 AE9 4 SER O 119 PHE O 123 0 SHEET 2 AE9 4 THR O 134 PHE O 144 -1 O ASN O 142 N SER O 119 SHEET 3 AE9 4 TYR O 178 SER O 187 -1 O LEU O 180 N LEU O 141 SHEET 4 AE9 4 SER O 164 VAL O 168 -1 N SER O 167 O SER O 181 SHEET 1 AF1 4 VAL O 158 LEU O 159 0 SHEET 2 AF1 4 ALA O 149 VAL O 155 -1 N VAL O 155 O VAL O 158 SHEET 3 AF1 4 VAL O 196 HIS O 203 -1 O THR O 202 N SER O 150 SHEET 4 AF1 4 VAL O 210 ASN O 215 -1 O VAL O 210 N VAL O 201 SSBOND 1 CYS M 23 CYS M 93 1555 1555 2.04 SSBOND 2 CYS M 139 CYS M 199 1555 1555 2.04 SSBOND 3 CYS R 22 CYS R 96 1555 1555 2.04 SSBOND 4 CYS R 152 CYS R 208 1555 1555 2.04 SSBOND 5 CYS S 598 CYS S 604 1555 1555 2.03 SSBOND 6 CYS S 605 CYS W 501 1555 1555 2.04 SSBOND 7 CYS W 54 CYS W 74 1555 1555 2.04 SSBOND 8 CYS W 119 CYS W 205 1555 1555 2.03 SSBOND 9 CYS W 126 CYS W 196 1555 1555 2.04 SSBOND 10 CYS W 131 CYS W 157 1555 1555 2.03 SSBOND 11 CYS W 218 CYS W 247 1555 1555 2.03 SSBOND 12 CYS W 228 CYS W 239 1555 1555 2.04 SSBOND 13 CYS W 296 CYS W 331 1555 1555 2.04 SSBOND 14 CYS W 378 CYS W 445 1555 1555 2.04 SSBOND 15 CYS W 385 CYS W 418 1555 1555 2.03 SSBOND 16 CYS B 54 CYS B 74 1555 1555 2.04 SSBOND 17 CYS B 119 CYS B 205 1555 1555 2.04 SSBOND 18 CYS B 126 CYS B 196 1555 1555 2.04 SSBOND 19 CYS B 131 CYS B 157 1555 1555 2.03 SSBOND 20 CYS B 218 CYS B 247 1555 1555 2.04 SSBOND 21 CYS B 228 CYS B 239 1555 1555 2.04 SSBOND 22 CYS B 296 CYS B 331 1555 1555 2.04 SSBOND 23 CYS B 378 CYS B 445 1555 1555 2.03 SSBOND 24 CYS B 385 CYS B 418 1555 1555 2.03 SSBOND 25 CYS B 501 CYS H 605 1555 1555 2.03 SSBOND 26 CYS E 22 CYS E 96 1555 1555 2.03 SSBOND 27 CYS E 152 CYS E 208 1555 1555 2.04 SSBOND 28 CYS F 23 CYS F 93 1555 1555 2.04 SSBOND 29 CYS F 139 CYS F 199 1555 1555 2.03 SSBOND 30 CYS H 598 CYS H 604 1555 1555 2.03 SSBOND 31 CYS J 54 CYS J 74 1555 1555 2.03 SSBOND 32 CYS J 119 CYS J 205 1555 1555 2.03 SSBOND 33 CYS J 126 CYS J 196 1555 1555 2.04 SSBOND 34 CYS J 131 CYS J 157 1555 1555 2.03 SSBOND 35 CYS J 218 CYS J 247 1555 1555 2.03 SSBOND 36 CYS J 228 CYS J 239 1555 1555 2.04 SSBOND 37 CYS J 296 CYS J 331 1555 1555 2.04 SSBOND 38 CYS J 378 CYS J 445 1555 1555 2.04 SSBOND 39 CYS J 385 CYS J 418 1555 1555 2.03 SSBOND 40 CYS J 501 CYS Q 605 1555 1555 2.02 SSBOND 41 CYS N 22 CYS N 96 1555 1555 2.03 SSBOND 42 CYS N 152 CYS N 208 1555 1555 2.03 SSBOND 43 CYS O 23 CYS O 93 1555 1555 2.05 SSBOND 44 CYS O 139 CYS O 199 1555 1555 2.03 SSBOND 45 CYS Q 598 CYS Q 604 1555 1555 2.03 LINK ND2 ASN S 611 C1 NAG S 701 1555 1555 1.45 LINK ND2 ASN S 625 C1 NAG S 702 1555 1555 1.44 LINK ND2 ASN S 637 C1 NAG S 703 1555 1555 1.45 LINK ND2 ASN W 133 C1 NAG W 601 1555 1555 1.45 LINK ND2 ASN W 156 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN W 160 C1 NAG W 602 1555 1555 1.45 LINK ND2 ASN W 197 C1 NAG W 603 1555 1555 1.45 LINK ND2 ASN W 234 C1 NAG W 604 1555 1555 1.45 LINK ND2 ASN W 262 C1 NAG C 1 1555 1555 1.45 LINK ND2 ASN W 276 C1 NAG W 605 1555 1555 1.46 LINK ND2 ASN W 295 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN W 301 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN W 332 C1 NAG A 1 1555 1555 1.45 LINK ND2 ASN W 355 C1 NAG W 606 1555 1555 1.45 LINK ND2 ASN W 363 C1 NAG W 607 1555 1555 1.45 LINK ND2 ASN W 386 C1 NAG W 608 1555 1555 1.45 LINK ND2 ASN B 133 C1 NAG B 601 1555 1555 1.45 LINK ND2 ASN B 156 C1 NAG L 1 1555 1555 1.45 LINK ND2 ASN B 160 C1 NAG B 602 1555 1555 1.45 LINK ND2 ASN B 197 C1 NAG B 603 1555 1555 1.45 LINK ND2 ASN B 234 C1 NAG B 604 1555 1555 1.44 LINK ND2 ASN B 262 C1 NAG U 1 1555 1555 1.45 LINK ND2 ASN B 276 C1 NAG B 605 1555 1555 1.46 LINK ND2 ASN B 295 C1 NAG P 1 1555 1555 1.45 LINK ND2 ASN B 301 C1 NAG T 1 1555 1555 1.45 LINK ND2 ASN B 355 C1 NAG B 606 1555 1555 1.45 LINK ND2 ASN B 363 C1 NAG B 607 1555 1555 1.45 LINK ND2 ASN B 386 C1 NAG B 608 1555 1555 1.44 LINK ND2 ASN H 611 C1 NAG H 701 1555 1555 1.45 LINK ND2 ASN H 625 C1 NAG H 702 1555 1555 1.44 LINK ND2 ASN H 637 C1 NAG H 703 1555 1555 1.45 LINK ND2 ASN J 133 C1 NAG J 601 1555 1555 1.45 LINK ND2 ASN J 156 C1 NAG X 1 1555 1555 1.45 LINK ND2 ASN J 160 C1 NAG J 602 1555 1555 1.45 LINK ND2 ASN J 197 C1 NAG J 603 1555 1555 1.45 LINK ND2 ASN J 234 C1 NAG J 604 1555 1555 1.45 LINK ND2 ASN J 262 C1 NAG a 1 1555 1555 1.44 LINK ND2 ASN J 276 C1 NAG J 605 1555 1555 1.46 LINK ND2 ASN J 295 C1 NAG Y 1 1555 1555 1.45 LINK ND2 ASN J 301 C1 NAG Z 1 1555 1555 1.44 LINK ND2 ASN J 332 C1 NAG V 1 1555 1555 1.45 LINK ND2 ASN J 355 C1 NAG J 606 1555 1555 1.45 LINK ND2 ASN J 363 C1 NAG J 607 1555 1555 1.45 LINK ND2 ASN J 386 C1 NAG J 608 1555 1555 1.45 LINK ND2 ASN Q 611 C1 NAG Q 701 1555 1555 1.45 LINK ND2 ASN Q 625 C1 NAG Q 702 1555 1555 1.44 LINK ND2 ASN Q 637 C1 NAG Q 703 1555 1555 1.44 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.46 LINK O4 NAG A 2 C1 BMA A 3 1555 1555 1.45 LINK O3 BMA A 3 C1 MAN A 4 1555 1555 1.44 LINK O6 BMA A 3 C1 MAN A 7 1555 1555 1.45 LINK O2 MAN A 4 C1 MAN A 5 1555 1555 1.43 LINK O2 MAN A 5 C1 MAN A 6 1555 1555 1.44 LINK O6 MAN A 7 C1 MAN A 8 1555 1555 1.47 LINK O3 MAN A 7 C1 MAN A 10 1555 1555 1.47 LINK O2 MAN A 8 C1 MAN A 9 1555 1555 1.46 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.46 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.47 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.47 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.48 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.47 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.48 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.45 LINK O4 NAG K 2 C1 BMA K 3 1555 1555 1.44 LINK O3 BMA K 3 C1 MAN K 4 1555 1555 1.44 LINK O6 BMA K 3 C1 MAN K 7 1555 1555 1.46 LINK O2 MAN K 4 C1 MAN K 5 1555 1555 1.43 LINK O2 MAN K 5 C1 MAN K 6 1555 1555 1.44 LINK O6 MAN K 7 C1 MAN K 8 1555 1555 1.47 LINK O3 MAN K 7 C1 MAN K 10 1555 1555 1.47 LINK O2 MAN K 8 C1 MAN K 9 1555 1555 1.45 LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.46 LINK O4 NAG L 2 C1 BMA L 3 1555 1555 1.47 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.47 LINK O4 NAG T 1 C1 NAG T 2 1555 1555 1.46 LINK O4 NAG U 1 C1 NAG U 2 1555 1555 1.46 LINK O4 NAG U 2 C1 BMA U 3 1555 1555 1.46 LINK O4 NAG V 1 C1 NAG V 2 1555 1555 1.46 LINK O4 NAG V 2 C1 BMA V 3 1555 1555 1.44 LINK O3 BMA V 3 C1 MAN V 4 1555 1555 1.45 LINK O6 BMA V 3 C1 MAN V 7 1555 1555 1.45 LINK O2 MAN V 4 C1 MAN V 5 1555 1555 1.43 LINK O2 MAN V 5 C1 MAN V 6 1555 1555 1.44 LINK O6 MAN V 7 C1 MAN V 8 1555 1555 1.47 LINK O3 MAN V 7 C1 MAN V 10 1555 1555 1.47 LINK O2 MAN V 8 C1 MAN V 9 1555 1555 1.45 LINK O4 NAG X 1 C1 NAG X 2 1555 1555 1.46 LINK O4 NAG X 2 C1 BMA X 3 1555 1555 1.47 LINK O4 NAG Y 1 C1 NAG Y 2 1555 1555 1.48 LINK O4 NAG Z 1 C1 NAG Z 2 1555 1555 1.46 LINK O4 NAG a 1 C1 NAG a 2 1555 1555 1.45 LINK O4 NAG a 2 C1 BMA a 3 1555 1555 1.48 LINK O3 BMA a 3 C1 MAN a 4 1555 1555 1.48 LINK O6 BMA a 3 C1 MAN a 5 1555 1555 1.47 CISPEP 1 LEU M 99 PRO M 100 0 -13.08 CISPEP 2 TYR M 145 PRO M 146 0 -10.61 CISPEP 3 ASP R 113 PRO R 114 0 -7.59 CISPEP 4 PHE R 158 PRO R 159 0 -19.05 CISPEP 5 GLU R 160 PRO R 161 0 4.46 CISPEP 6 ASP E 113 PRO E 114 0 -4.12 CISPEP 7 PHE E 158 PRO E 159 0 -19.33 CISPEP 8 GLU E 160 PRO E 161 0 8.83 CISPEP 9 LEU F 99 PRO F 100 0 -8.46 CISPEP 10 TYR F 145 PRO F 146 0 -10.45 CISPEP 11 ASP N 113 PRO N 114 0 -5.05 CISPEP 12 PHE N 158 PRO N 159 0 -19.85 CISPEP 13 GLU N 160 PRO N 161 0 4.28 CISPEP 14 LEU O 99 PRO O 100 0 -14.14 CISPEP 15 TYR O 145 PRO O 146 0 -5.78 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