HEADER OXIDOREDUCTASE 10-DEC-18 6NBX
TITLE T.ELONGATUS NDH (DATA-SET 2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NAD(P)H DEHYDROGENASE I SUBUNIT 1,NDH-1 SUBUNIT 1,NDH-A;
COMPND 5 EC: 7.1.1.-;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 2;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: NAD(P)H DEHYDROGENASE SUBUNIT 2,NADH-PLASTOQUINONE
COMPND 10 OXIDOREDUCTASE SUBUNIT 2,NDH-1,SUBUNIT 2;
COMPND 11 EC: 7.1.1.-;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 3;
COMPND 14 CHAIN: C;
COMPND 15 SYNONYM: NAD(P)H DEHYDROGENASE SUBUNIT 3,NADH-PLASTOQUINONE
COMPND 16 OXIDOREDUCTASE SUBUNIT 3,NDH-1 SUBUNIT 3,NDH-C;
COMPND 17 EC: 7.1.1.-;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE CHAIN 4 1;
COMPND 20 CHAIN: D;
COMPND 21 SYNONYM: NAD(P)H DEHYDROGENASE I,CHAIN 4 1,NDH-1;
COMPND 22 EC: 1.6.5.-;
COMPND 23 MOL_ID: 5;
COMPND 24 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 4L;
COMPND 25 CHAIN: E;
COMPND 26 SYNONYM: NAD(P)H DEHYDROGENASE SUBUNIT 4L,NADH-PLASTOQUINONE
COMPND 27 OXIDOREDUCTASE SUBUNIT 4L,NDH-1,SUBUNIT 4L,NDH-E;
COMPND 28 EC: 1.6.5.-;
COMPND 29 MOL_ID: 6;
COMPND 30 MOLECULE: NADH DEHYDROGENASE SUBUNIT 5;
COMPND 31 CHAIN: F;
COMPND 32 MOL_ID: 7;
COMPND 33 MOLECULE: NADH-QUINONE OXIDOREDUCTASE SUBUNIT J;
COMPND 34 CHAIN: G;
COMPND 35 EC: 1.6.5.11;
COMPND 36 MOL_ID: 8;
COMPND 37 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT H;
COMPND 38 CHAIN: H;
COMPND 39 SYNONYM: NAD(P)H DEHYDROGENASE SUBUNIT H,NADH-PLASTOQUINONE
COMPND 40 OXIDOREDUCTASE SUBUNIT H,NDH-1 SUBUNIT H,NDH-H;
COMPND 41 EC: 1.6.5.-;
COMPND 42 MOL_ID: 9;
COMPND 43 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT I;
COMPND 44 CHAIN: I;
COMPND 45 SYNONYM: NAD(P)H DEHYDROGENASE I SUBUNIT I,NDH-1 SUBUNIT I,NDH-I;
COMPND 46 EC: 1.6.5.-;
COMPND 47 MOL_ID: 10;
COMPND 48 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT J;
COMPND 49 CHAIN: J;
COMPND 50 SYNONYM: NAD(P)H DEHYDROGENASE SUBUNIT J,NADH-PLASTOQUINONE
COMPND 51 OXIDOREDUCTASE SUBUNIT J,NDH-1 SUBUNIT J,NDH-J;
COMPND 52 EC: 1.6.5.-;
COMPND 53 MOL_ID: 11;
COMPND 54 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT K;
COMPND 55 CHAIN: K;
COMPND 56 SYNONYM: NAD(P)H DEHYDROGENASE I SUBUNIT K,NDH-1 SUBUNIT K,NDH-K;
COMPND 57 EC: 1.6.5.-;
COMPND 58 MOL_ID: 12;
COMPND 59 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT L;
COMPND 60 CHAIN: L;
COMPND 61 SYNONYM: NAD(P)H DEHYDROGENASE I SUBUNIT L,NDH-1 SUBUNIT L,NDH-L;
COMPND 62 EC: 1.6.5.-;
COMPND 63 MOL_ID: 13;
COMPND 64 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT M;
COMPND 65 CHAIN: M;
COMPND 66 SYNONYM: NAD(P)H DEHYDROGENASE I SUBUNIT M,NDH-M;
COMPND 67 EC: 1.6.5.-;
COMPND 68 MOL_ID: 14;
COMPND 69 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT N;
COMPND 70 CHAIN: N;
COMPND 71 SYNONYM: NAD(P)H DEHYDROGENASE I SUBUNIT N,NDH-N;
COMPND 72 EC: 1.6.5.-;
COMPND 73 MOL_ID: 15;
COMPND 74 MOLECULE: NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT O;
COMPND 75 CHAIN: O;
COMPND 76 SYNONYM: NAD(P)H DEHYDROGENASE I SUBUNIT O,NDH-1 SUBUNIT O,NDH-O;
COMPND 77 EC: 1.6.5.-;
COMPND 78 MOL_ID: 16;
COMPND 79 MOLECULE: PROTON-TRANSLOCATING NADH-QUINONE DEHYDROGENASE SUBUNIT P
COMPND 80 NDHP;
COMPND 81 CHAIN: P;
COMPND 82 MOL_ID: 17;
COMPND 83 MOLECULE: PROTON-TRANSLOCATING NADH-QUINONE DEHYDROGENASE SUBUNIT Q
COMPND 84 NDHQ;
COMPND 85 CHAIN: Q;
COMPND 86 MOL_ID: 18;
COMPND 87 MOLECULE: TLR0636 PROTEIN;
COMPND 88 CHAIN: S
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 3 ORGANISM_TAXID: 197221;
SOURCE 4 STRAIN: BP-1;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 7 ORGANISM_TAXID: 197221;
SOURCE 8 STRAIN: BP-1;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 11 ORGANISM_TAXID: 197221;
SOURCE 12 STRAIN: BP-1;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 15 ORGANISM_TAXID: 197221;
SOURCE 16 STRAIN: BP-1;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 19 ORGANISM_TAXID: 197221;
SOURCE 20 STRAIN: BP-1;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 23 ORGANISM_TAXID: 197221;
SOURCE 24 STRAIN: BP-1;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 27 ORGANISM_TAXID: 197221;
SOURCE 28 STRAIN: BP-1;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 31 ORGANISM_TAXID: 197221;
SOURCE 32 STRAIN: BP-1;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 35 ORGANISM_TAXID: 197221;
SOURCE 36 STRAIN: BP-1;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 39 ORGANISM_TAXID: 197221;
SOURCE 40 STRAIN: BP-1;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 43 ORGANISM_TAXID: 197221;
SOURCE 44 STRAIN: BP-1;
SOURCE 45 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 47 ORGANISM_TAXID: 197221;
SOURCE 48 STRAIN: BP-1;
SOURCE 49 MOL_ID: 13;
SOURCE 50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 51 ORGANISM_TAXID: 197221;
SOURCE 52 STRAIN: BP-1;
SOURCE 53 MOL_ID: 14;
SOURCE 54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 55 ORGANISM_TAXID: 197221;
SOURCE 56 STRAIN: BP-1;
SOURCE 57 MOL_ID: 15;
SOURCE 58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 59 ORGANISM_TAXID: 197221;
SOURCE 60 STRAIN: BP-1;
SOURCE 61 MOL_ID: 16;
SOURCE 62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 63 ORGANISM_TAXID: 197221;
SOURCE 64 STRAIN: BP-1;
SOURCE 65 MOL_ID: 17;
SOURCE 66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 67 ORGANISM_TAXID: 197221;
SOURCE 68 STRAIN: BP-1;
SOURCE 69 MOL_ID: 18;
SOURCE 70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);
SOURCE 71 ORGANISM_TAXID: 197221;
SOURCE 72 STRAIN: BP-1
KEYWDS PHOTOSYNTHESIS, BIOENERGETICS, MEMBRANE PROTEIN COMPLEX,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR T.G.LAUGHLIN,A.BAYNE,J.-F.TREMPE,D.F.SAVAGE,K.M.DAVIES
REVDAT 4 18-DEC-19 6NBX 1 SCALE
REVDAT 3 04-DEC-19 6NBX 1 REMARK
REVDAT 2 06-MAR-19 6NBX 1 JRNL
REVDAT 1 27-FEB-19 6NBX 0
JRNL AUTH T.G.LAUGHLIN,A.N.BAYNE,J.F.TREMPE,D.F.SAVAGE,K.M.DAVIES
JRNL TITL STRUCTURE OF THE COMPLEX I-LIKE MOLECULE NDH OF OXYGENIC
JRNL TITL 2 PHOTOSYNTHESIS.
JRNL REF NATURE V. 566 411 2019
JRNL REFN ESSN 1476-4687
JRNL PMID 30742075
JRNL DOI 10.1038/S41586-019-0921-0
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : GAUTOMATCH, SERIALEM, GCTF, RELION,
REMARK 3 COOT, PHENIX, RELION, RELION, RELION,
REMARK 3 PHENIX
REMARK 3 RECONSTRUCTION SCHEMA : BACK PROJECTION
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 6NBQ
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : RIGID BODY FIT
REMARK 3 REFINEMENT TARGET : CORELATION COEFFICIENT
REMARK 3 OVERALL ANISOTROPIC B VALUE : 20.000
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.500
REMARK 3 NUMBER OF PARTICLES : 34655
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 6NBX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1000238521.
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 : NAD(P)H DEHYDROGENASE-LIKE
REMARK 245 COMPLEX (NDH/NDH-1_1/NDH1L)FROM
REMARK 245 T.ELONGATUS
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.03
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : INCUBATE ON GRID FOR 30 SECONDS
REMARK 245 AND BLOT 2.5 SECONDS BEFORE
REMARK 245 PLUNGING
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 6.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 1385
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 60.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTADECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, S
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 MET A 1
REMARK 465 GLU A 2
REMARK 465 SER A 3
REMARK 465 GLY A 4
REMARK 465 ILE A 5
REMARK 465 ASP A 6
REMARK 465 LEU A 7
REMARK 465 GLN A 8
REMARK 465 GLY A 9
REMARK 465 GLN A 10
REMARK 465 PHE A 11
REMARK 465 ILE A 12
REMARK 465 SER A 13
REMARK 465 ALA A 14
REMARK 465 LEU A 15
REMARK 465 GLN A 16
REMARK 465 SER A 17
REMARK 465 LEU A 18
REMARK 465 GLY A 19
REMARK 465 LEU A 20
REMARK 465 SER A 21
REMARK 465 HIS A 22
REMARK 465 ASP A 23
REMARK 465 LEU A 24
REMARK 465 ALA A 25
REMARK 465 LYS A 26
REMARK 465 LEU A 27
REMARK 465 LYS A 363
REMARK 465 LEU A 364
REMARK 465 ALA A 365
REMARK 465 PHE A 366
REMARK 465 PRO A 367
REMARK 465 VAL A 368
REMARK 465 ALA A 369
REMARK 465 PHE A 370
REMARK 465 GLY A 371
REMARK 465 GLY A 372
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 LEU B 3
REMARK 465 VAL B 4
REMARK 465 THR B 5
REMARK 465 LEU B 6
REMARK 465 ALA B 7
REMARK 465 GLY B 8
REMARK 465 GLN B 9
REMARK 465 LEU B 10
REMARK 465 GLN B 494
REMARK 465 LEU B 495
REMARK 465 ALA B 496
REMARK 465 ASN B 497
REMARK 465 GLN B 498
REMARK 465 PRO B 499
REMARK 465 THR B 500
REMARK 465 VAL B 501
REMARK 465 MET B 502
REMARK 465 GLU B 503
REMARK 465 VAL B 504
REMARK 465 ALA B 505
REMARK 465 TYR B 506
REMARK 465 GLN B 507
REMARK 465 ALA B 508
REMARK 465 LEU B 509
REMARK 465 SER B 510
REMARK 465 PRO B 511
REMARK 465 ALA B 512
REMARK 465 GLY B 513
REMARK 465 LYS B 514
REMARK 465 SER B 515
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 ALA C 3
REMARK 465 ILE C 4
REMARK 465 PRO C 5
REMARK 465 ARG C 6
REMARK 465 LEU C 7
REMARK 465 ARG C 8
REMARK 465 ASP C 9
REMARK 465 THR C 10
REMARK 465 ALA C 11
REMARK 465 THR C 12
REMARK 465 LYS C 46
REMARK 465 SER C 47
REMARK 465 GLY C 48
REMARK 465 ARG C 49
REMARK 465 MET C 50
REMARK 465 ILE C 51
REMARK 465 ARG C 52
REMARK 465 LEU C 53
REMARK 465 THR C 54
REMARK 465 THR C 55
REMARK 465 TYR C 56
REMARK 465 GLU C 57
REMARK 465 SER C 58
REMARK 465 GLY C 59
REMARK 465 MET C 60
REMARK 465 GLU C 61
REMARK 465 PRO C 62
REMARK 465 ILE C 63
REMARK 465 GLY C 64
REMARK 465 SER C 132
REMARK 465 MET D 1
REMARK 465 LEU D 506
REMARK 465 ALA D 507
REMARK 465 GLN D 508
REMARK 465 GLN D 509
REMARK 465 THR D 510
REMARK 465 GLU D 511
REMARK 465 GLN D 512
REMARK 465 PRO D 513
REMARK 465 LEU D 514
REMARK 465 GLY D 515
REMARK 465 ILE D 516
REMARK 465 LEU D 517
REMARK 465 PRO D 518
REMARK 465 MET D 519
REMARK 465 VAL D 520
REMARK 465 ALA D 521
REMARK 465 PRO D 522
REMARK 465 GLN D 523
REMARK 465 LEU D 524
REMARK 465 LYS D 525
REMARK 465 ALA D 526
REMARK 465 ASN D 527
REMARK 465 ALA D 528
REMARK 465 GLN D 529
REMARK 465 THR F 656
REMARK 465 MET G 1
REMARK 465 ASP G 2
REMARK 465 LEU G 3
REMARK 465 VAL G 195
REMARK 465 ALA G 196
REMARK 465 LEU G 197
REMARK 465 SER G 198
REMARK 465 GLU G 199
REMARK 465 LYS G 200
REMARK 465 MET H 1
REMARK 465 PRO H 2
REMARK 465 MET I 1
REMARK 465 LYS I 2
REMARK 465 PHE I 3
REMARK 465 LEU I 4
REMARK 465 ASN I 5
REMARK 465 THR I 190
REMARK 465 ALA I 191
REMARK 465 LYS I 192
REMARK 465 SER I 193
REMARK 465 SER I 194
REMARK 465 GLU I 195
REMARK 465 ASN I 196
REMARK 465 MET J 1
REMARK 465 SER J 2
REMARK 465 ASP J 3
REMARK 465 THR J 4
REMARK 465 PRO J 5
REMARK 465 GLU J 6
REMARK 465 ALA J 7
REMARK 465 MET K 1
REMARK 465 THR K 2
REMARK 465 ASN K 3
REMARK 465 THR K 4
REMARK 465 THR K 5
REMARK 465 SER K 6
REMARK 465 GLY K 219
REMARK 465 ILE K 220
REMARK 465 ALA K 221
REMARK 465 VAL K 222
REMARK 465 PRO K 223
REMARK 465 ALA K 224
REMARK 465 LEU K 225
REMARK 465 GLY K 226
REMARK 465 GLU K 227
REMARK 465 ALA K 228
REMARK 465 VAL K 229
REMARK 465 SER K 230
REMARK 465 GLU K 231
REMARK 465 THR K 232
REMARK 465 THR K 233
REMARK 465 SER K 234
REMARK 465 VAL K 235
REMARK 465 ALA K 236
REMARK 465 GLU K 237
REMARK 465 MET L 1
REMARK 465 ALA L 2
REMARK 465 VAL L 3
REMARK 465 SER L 4
REMARK 465 THR L 5
REMARK 465 GLU L 6
REMARK 465 LEU L 7
REMARK 465 LEU L 8
REMARK 465 VAL L 9
REMARK 465 LEU L 10
REMARK 465 MET N 1
REMARK 465 ALA N 150
REMARK 465 MET O 1
REMARK 465 MET P 0
REMARK 465 ASP P 1
REMARK 465 MET Q 1
REMARK 465 ALA Q 45
REMARK 465 MET S 1
REMARK 465 ILE S 2
REMARK 465 ARG S 3
REMARK 465 PRO S 4
REMARK 465 ILE S 5
REMARK 465 ALA S 6
REMARK 465 ASP S 7
REMARK 465 THR S 8
REMARK 465 TYR S 9
REMARK 465 PRO S 10
REMARK 465 LEU S 11
REMARK 465 LEU S 12
REMARK 465 PRO S 13
REMARK 465 LEU S 14
REMARK 465 SER S 15
REMARK 465 LYS S 16
REMARK 465 ALA S 17
REMARK 465 GLN S 18
REMARK 465 MET S 19
REMARK 465 GLY S 20
REMARK 465 GLN S 21
REMARK 465 ARG S 22
REMARK 465 GLN S 23
REMARK 465 GLU S 24
REMARK 465 ILE S 25
REMARK 465 ILE S 26
REMARK 465 ASN S 27
REMARK 465 SER S 28
REMARK 465 HIS S 29
REMARK 465 LYS S 30
REMARK 465 ARG S 31
REMARK 465 LEU S 32
REMARK 465 TRP S 33
REMARK 465 ASP S 34
REMARK 465 LYS S 35
REMARK 465 THR S 36
REMARK 465 MET S 37
REMARK 465 ALA S 38
REMARK 465 THR S 39
REMARK 465 ASP S 40
REMARK 465 LEU S 41
REMARK 465 ILE S 42
REMARK 465 VAL S 100
REMARK 465 THR S 101
REMARK 465 PRO S 102
REMARK 465 LYS S 103
REMARK 465 GLU S 104
REMARK 465 LYS S 105
REMARK 465 ALA S 106
REMARK 465 LYS S 107
REMARK 465 ALA S 108
REMARK 465 LYS S 109
REMARK 465 LYS S 110
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 LEU A 28 CG CD1 CD2
REMARK 470 TRP A 29 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 29 CZ3 CH2
REMARK 470 GLU A 66 CG CD OE1 OE2
REMARK 470 ASP A 79 CG OD1 OD2
REMARK 470 GLU A 87 CG CD OE1 OE2
REMARK 470 ASP A 88 CG OD1 OD2
REMARK 470 ASN A 93 CG OD1 ND2
REMARK 470 ASP A 95 CG OD1 OD2
REMARK 470 GLU A 194 CG CD OE1 OE2
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 GLU A 228 CG CD OE1 OE2
REMARK 470 ASP A 233 CG OD1 OD2
REMARK 470 LEU A 234 CG CD1 CD2
REMARK 470 GLU A 236 CG CD OE1 OE2
REMARK 470 GLU A 238 CG CD OE1 OE2
REMARK 470 GLU A 239 CG CD OE1 OE2
REMARK 470 GLU A 240 CG CD OE1 OE2
REMARK 470 LEU A 241 CG CD1 CD2
REMARK 470 VAL A 242 CG1 CG2
REMARK 470 GLU A 248 CG CD OE1 OE2
REMARK 470 LEU A 286 CG CD1 CD2
REMARK 470 GLU A 287 CG CD OE1 OE2
REMARK 470 THR A 288 OG1 CG2
REMARK 470 ILE A 289 CG1 CG2 CD1
REMARK 470 ASN A 291 CG OD1 ND2
REMARK 470 LEU A 292 CG CD1 CD2
REMARK 470 LEU A 293 CG CD1 CD2
REMARK 470 GLU A 297 CG CD OE1 OE2
REMARK 470 ASP A 342 CG OD1 OD2
REMARK 470 GLU B 18 CG CD OE1 OE2
REMARK 470 GLN B 38 CG CD OE1 NE2
REMARK 470 ASP B 40 CG OD1 OD2
REMARK 470 ASP B 77 CG OD1 OD2
REMARK 470 GLU B 103 CG CD OE1 OE2
REMARK 470 GLU B 111 CG CD OE1 OE2
REMARK 470 GLU B 131 CG CD OE1 OE2
REMARK 470 GLU B 140 CG CD OE1 OE2
REMARK 470 ASP B 156 CG OD1 OD2
REMARK 470 GLU B 161 CG CD OE1 OE2
REMARK 470 GLU B 204 CG CD OE1 OE2
REMARK 470 ASP B 272 CG OD1 OD2
REMARK 470 GLU B 323 CG CD OE1 OE2
REMARK 470 ASP B 357 CG OD1 OD2
REMARK 470 GLU B 361 CG CD OE1 OE2
REMARK 470 ASP B 369 CG OD1 OD2
REMARK 470 GLU B 436 CG CD OE1 OE2
REMARK 470 GLU B 439 CG CD OE1 OE2
REMARK 470 GLU B 442 CG CD OE1 OE2
REMARK 470 ARG B 445 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 449 CG CD OE1 OE2
REMARK 470 ASN C 71 CG OD1 ND2
REMARK 470 ARG C 73 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 85 CG OD1 OD2
REMARK 470 GLU C 108 CG CD OE1 OE2
REMARK 470 ARG C 127 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 130 CG CD OE1 OE2
REMARK 470 ASP D 26 CG OD1 OD2
REMARK 470 THR D 28 OG1 CG2
REMARK 470 LYS D 30 CG CD CE NZ
REMARK 470 ASP D 58 CG OD1 OD2
REMARK 470 GLU D 144 CG CD OE1 OE2
REMARK 470 GLU D 146 CG CD OE1 OE2
REMARK 470 ASP D 192 CG OD1 OD2
REMARK 470 GLU D 241 CG CD OE1 OE2
REMARK 470 ASP D 355 CG OD1 OD2
REMARK 470 GLU D 398 CG CD OE1 OE2
REMARK 470 ASP D 409 CG OD1 OD2
REMARK 470 GLU D 446 CG CD OE1 OE2
REMARK 470 LYS D 448 CG CD CE NZ
REMARK 470 GLU D 449 CG CD OE1 OE2
REMARK 470 GLU D 452 CG CD OE1 OE2
REMARK 470 GLU D 454 CG CD OE1 OE2
REMARK 470 LEU D 456 CG CD1 CD2
REMARK 470 VAL D 457 CG1 CG2
REMARK 470 ASP D 458 CG OD1 OD2
REMARK 470 GLU D 460 CG CD OE1 OE2
REMARK 470 GLU D 463 CG CD OE1 OE2
REMARK 470 GLU D 501 CG CD OE1 OE2
REMARK 470 THR D 505 OG1 CG2
REMARK 470 GLU E 73 CG CD OE1 OE2
REMARK 470 ASP E 89 CG OD1 OD2
REMARK 470 GLU E 94 CG CD OE1 OE2
REMARK 470 GLU F 31 CG CD OE1 OE2
REMARK 470 ASP F 186 CG OD1 OD2
REMARK 470 MET F 367 CG SD CE
REMARK 470 GLU F 368 CG CD OE1 OE2
REMARK 470 ASN F 374 CG OD1 ND2
REMARK 470 ASP F 376 CG OD1 OD2
REMARK 470 LEU F 377 CG CD1 CD2
REMARK 470 GLN F 379 CG CD OE1 NE2
REMARK 470 ASP F 380 CG OD1 OD2
REMARK 470 MET F 381 CG SD CE
REMARK 470 ARG F 382 CG CD NE CZ NH1 NH2
REMARK 470 TYR F 383 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET F 384 CG SD CE
REMARK 470 LEU F 387 CG CD1 CD2
REMARK 470 ARG F 388 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 389 CG CD CE NZ
REMARK 470 TYR F 390 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET F 391 CG SD CE
REMARK 470 PHE F 454 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS F 457 CG CD CE NZ
REMARK 470 PHE F 458 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG F 459 CG CD NE CZ NH1 NH2
REMARK 470 ASN F 460 CG OD1 ND2
REMARK 470 VAL F 461 CG1 CG2
REMARK 470 PRO F 462 CG CD
REMARK 470 PRO F 463 CG CD
REMARK 470 GLU F 464 CG CD OE1 OE2
REMARK 470 ARG F 465 CG CD NE CZ NH1 NH2
REMARK 470 GLN F 466 CG CD OE1 NE2
REMARK 470 GLU F 467 CG CD OE1 OE2
REMARK 470 HIS F 468 CG ND1 CD2 CE1 NE2
REMARK 470 HIS F 469 CG ND1 CD2 CE1 NE2
REMARK 470 ASP F 470 CG OD1 OD2
REMARK 470 HIS F 471 CG ND1 CD2 CE1 NE2
REMARK 470 HIS F 472 CG ND1 CD2 CE1 NE2
REMARK 470 SER F 473 OG
REMARK 470 HIS F 474 CG ND1 CD2 CE1 NE2
REMARK 470 HIS F 475 CG ND1 CD2 CE1 NE2
REMARK 470 VAL F 478 CG1 CG2
REMARK 470 PRO F 479 CG CD
REMARK 470 GLU F 481 CG CD OE1 OE2
REMARK 470 GLN F 655 CG CD OE1 NE2
REMARK 470 ASP G 56 CG OD1 OD2
REMARK 470 LYS G 83 CG CD CE NZ
REMARK 470 ARG G 84 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 85 CG CD OE1 OE2
REMARK 470 THR G 86 OG1 CG2
REMARK 470 TYR G 87 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR G 88 OG1 CG2
REMARK 470 PRO G 89 CG CD
REMARK 470 VAL G 90 CG1 CG2
REMARK 470 PRO G 91 CG CD
REMARK 470 ARG G 93 CG CD NE CZ NH1 NH2
REMARK 470 TRP G 94 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP G 94 CZ3 CH2
REMARK 470 LEU G 95 CG CD1 CD2
REMARK 470 ASP G 130 CG OD1 OD2
REMARK 470 ARG G 167 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 168 CG CD OE1 OE2
REMARK 470 LEU G 169 CG CD1 CD2
REMARK 470 VAL G 170 CG1 CG2
REMARK 470 LEU G 171 CG CD1 CD2
REMARK 470 GLU G 172 CG CD OE1 OE2
REMARK 470 GLU G 186 CG CD OE1 OE2
REMARK 470 ASP H 33 CG OD1 OD2
REMARK 470 GLU H 35 CG CD OE1 OE2
REMARK 470 ASP H 36 CG OD1 OD2
REMARK 470 ASP H 39 CG OD1 OD2
REMARK 470 ASP H 181 CG OD1 OD2
REMARK 470 GLU H 213 CG CD OE1 OE2
REMARK 470 GLU H 214 CG CD OE1 OE2
REMARK 470 LYS H 231 CG CD CE NZ
REMARK 470 ASP H 244 CG OD1 OD2
REMARK 470 ASP H 249 CG OD1 OD2
REMARK 470 THR H 254 OG1 CG2
REMARK 470 GLU H 255 CG CD OE1 OE2
REMARK 470 ASP H 257 CG OD1 OD2
REMARK 470 LEU H 297 CG CD1 CD2
REMARK 470 GLU H 298 CG CD OE1 OE2
REMARK 470 LYS H 301 CG CD CE NZ
REMARK 470 GLU H 303 CG CD OE1 OE2
REMARK 470 LYS H 314 CG CD CE NZ
REMARK 470 ASP H 393 CG OD1 OD2
REMARK 470 GLN I 6 CG CD OE1 NE2
REMARK 470 ILE I 7 CG1 CG2 CD1
REMARK 470 LYS I 12 CG CD CE NZ
REMARK 470 GLU I 13 CG CD OE1 OE2
REMARK 470 GLU I 87 CG CD OE1 OE2
REMARK 470 GLU I 92 CG CD OE1 OE2
REMARK 470 GLU I 133 CG CD OE1 OE2
REMARK 470 ARG I 179 CG CD NE CZ NH1 NH2
REMARK 470 ASP J 89 CG OD1 OD2
REMARK 470 GLU J 93 CG CD OE1 OE2
REMARK 470 GLU J 121 CG CD OE1 OE2
REMARK 470 GLU J 145 CG CD OE1 OE2
REMARK 470 GLU J 166 CG CD OE1 OE2
REMARK 470 GLU K 17 CG CD OE1 OE2
REMARK 470 GLU K 24 CG CD OE1 OE2
REMARK 470 GLU K 56 CG CD OE1 OE2
REMARK 470 ASP K 142 CG OD1 OD2
REMARK 470 GLU K 169 CG CD OE1 OE2
REMARK 470 ASP M 19 CG OD1 OD2
REMARK 470 GLU M 21 CG CD OE1 OE2
REMARK 470 GLU M 43 CG CD OE1 OE2
REMARK 470 GLU M 67 CG CD OE1 OE2
REMARK 470 GLU M 78 CG CD OE1 OE2
REMARK 470 GLU N 30 CG CD OE1 OE2
REMARK 470 ASP N 54 CG OD1 OD2
REMARK 470 GLU O 67 CG CD OE1 OE2
REMARK 470 GLN P 35 CG CD OE1 NE2
REMARK 470 ASN P 39 CG OD1 ND2
REMARK 470 SER P 41 OG
REMARK 470 ASP S 72 CG OD1 OD2
REMARK 470 GLU S 96 CG CD OE1 OE2
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 ASP F 90 C - N - CA ANGL. DEV. = 24.8 DEGREES
REMARK 500 CYS H 180 CA - CB - SG ANGL. DEV. = 9.6 DEGREES
REMARK 500 CYS J 63 CA - CB - SG ANGL. DEV. = 10.0 DEGREES
REMARK 500 TRP J 119 CA - CB - CG ANGL. DEV. = 11.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 67 -4.65 67.11
REMARK 500 TYR A 172 31.42 -98.72
REMARK 500 PRO A 231 51.55 -96.85
REMARK 500 ALA A 243 19.74 -143.58
REMARK 500 GLN A 246 47.93 -92.07
REMARK 500 TRP A 280 29.04 44.27
REMARK 500 PHE A 282 149.64 -172.00
REMARK 500 PRO A 283 -169.93 -72.73
REMARK 500 ARG B 37 -6.79 73.49
REMARK 500 PRO B 65 45.87 -82.24
REMARK 500 LYS B 154 -8.69 63.80
REMARK 500 SER B 157 10.18 59.64
REMARK 500 HIS B 191 69.79 60.42
REMARK 500 PHE B 267 74.62 -118.85
REMARK 500 ALA B 295 53.23 -93.50
REMARK 500 THR B 356 70.22 37.15
REMARK 500 TYR B 366 -11.78 75.26
REMARK 500 MET B 431 44.87 -84.44
REMARK 500 MET B 432 -39.85 -135.39
REMARK 500 SER B 441 -63.68 -96.77
REMARK 500 GLU B 449 72.05 60.15
REMARK 500 LEU B 477 37.79 -98.42
REMARK 500 LEU C 129 39.46 -97.63
REMARK 500 ASP D 26 75.99 55.53
REMARK 500 PRO D 27 45.90 -89.34
REMARK 500 ASN D 60 50.50 38.48
REMARK 500 ASP D 85 -168.84 -101.63
REMARK 500 ALA D 106 46.36 -91.71
REMARK 500 GLN D 134 72.54 -105.14
REMARK 500 LEU D 147 -50.14 -121.51
REMARK 500 ALA D 322 52.50 -93.65
REMARK 500 THR D 359 -56.32 -121.39
REMARK 500 LEU D 360 7.42 59.70
REMARK 500 ALA D 406 47.90 -88.16
REMARK 500 ASP D 409 49.87 -93.02
REMARK 500 ILE D 441 -50.87 -120.84
REMARK 500 LEU D 450 18.29 58.83
REMARK 500 VAL D 451 -61.28 -124.11
REMARK 500 ASP D 458 -165.67 -160.95
REMARK 500 ALA D 459 107.83 -160.46
REMARK 500 TYR D 480 82.57 -154.12
REMARK 500 ASN E 87 -63.13 -94.50
REMARK 500 ASP E 89 21.39 -77.75
REMARK 500 ASN E 97 58.90 -99.40
REMARK 500 TYR F 7 33.18 -97.09
REMARK 500 ALA F 116 4.53 81.43
REMARK 500 TYR F 166 4.92 54.94
REMARK 500 ALA F 242 67.74 60.05
REMARK 500 THR F 311 40.65 39.41
REMARK 500 MET F 381 77.87 57.82
REMARK 500
REMARK 500 THIS ENTRY HAS 127 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR F 383 MET F 384 -147.35
REMARK 500 MET F 384 GLY F 385 -141.59
REMARK 500 SER F 561 PRO F 562 141.99
REMARK 500 PRO K 106 SER K 107 -148.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 I 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 K 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6NBQ RELATED DB: PDB
REMARK 900 RELATED ID: EMD-0415 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-0416 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-0417 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-0418 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-0419 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-0420 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-0425 RELATED DB: EMDB
REMARK 900 T.ELONGATUS NDH (DATA-SET 2)
DBREF 6NBX A 1 372 UNP Q8DL32 NU1C_THEEB 1 372
DBREF 6NBX B 1 515 UNP Q8DMR6 NU2C_THEEB 1 515
DBREF 6NBX C 1 132 UNP Q8DJ02 NU3C_THEEB 1 132
DBREF 6NBX D 1 529 UNP Q8DKY0 NU4C1_THEEB 1 529
DBREF 6NBX E 1 101 UNP Q8DL29 Q8DL29_THEEB 1 101
DBREF 6NBX F 1 656 UNP Q8DKX9 Q8DKX9_THEEB 1 656
DBREF 6NBX G 1 200 UNP Q8DL30 Q8DL30_THEEB 1 200
DBREF 6NBX H 1 394 UNP Q8DJD9 NDHH_THEEB 1 394
DBREF 6NBX I 1 196 UNP Q8DL31 NDHI_THEEB 1 196
DBREF 6NBX J 1 168 UNP Q8DJ01 NDHJ_THEEB 1 168
DBREF 6NBX K 1 237 UNP Q8DKZ4 NDHK_THEEB 1 237
DBREF 6NBX L 1 76 UNP Q8DKZ3 NDHL_THEEB 1 76
DBREF 6NBX M 1 111 UNP Q8DLN5 NDHM_THEEB 1 111
DBREF 6NBX N 1 150 UNP Q8DJU2 NDHN_THEEB 1 150
DBREF 6NBX O 1 70 UNP Q8DMU4 NDHO_THEEB 1 70
DBREF 6NBX P 0 43 UNP V5V507 V5V507_9CYAN 1 44
DBREF 6NBX Q 1 45 PDB 6NBX 6NBX 1 45
DBREF 6NBX S 1 110 UNP Q8DL61 Q8DL61_THEEB 1 110
SEQRES 1 A 372 MET GLU SER GLY ILE ASP LEU GLN GLY GLN PHE ILE SER
SEQRES 2 A 372 ALA LEU GLN SER LEU GLY LEU SER HIS ASP LEU ALA LYS
SEQRES 3 A 372 LEU LEU TRP LEU PRO LEU PRO MET LEU MET MET LEU ILE
SEQRES 4 A 372 VAL ALA THR VAL GLY VAL LEU VAL ALA VAL TRP LEU GLU
SEQRES 5 A 372 ARG LYS ILE SER ALA ALA VAL GLN GLN ARG ILE GLY PRO
SEQRES 6 A 372 GLU TYR ILE GLY PRO LEU GLY ILE LEU ALA PRO LEU ALA
SEQRES 7 A 372 ASP GLY LEU LYS LEU ILE PHE LYS GLU ASP VAL LEU PRO
SEQRES 8 A 372 ALA ASN SER ASP ARG TRP LEU PHE THR LEU GLY PRO ALA
SEQRES 9 A 372 VAL VAL VAL ILE PRO VAL PHE LEU SER TYR ILE ILE VAL
SEQRES 10 A 372 PRO PHE GLY GLN ASN LEU LEU ILE SER ASN LEU ALA MET
SEQRES 11 A 372 GLY VAL PHE LEU TRP ILE ALA LEU SER SER ILE ALA PRO
SEQRES 12 A 372 ILE GLY LEU LEU MET ALA GLY TYR ALA SER ASN ASN LYS
SEQRES 13 A 372 TYR SER LEU LEU GLY GLY LEU ARG ALA ALA ALA GLN SER
SEQRES 14 A 372 ILE SER TYR GLU ILE PRO LEU ALA LEU ALA VAL LEU ALA
SEQRES 15 A 372 VAL ALA MET MET SER ASN GLY LEU GLY THR VAL GLU ILE
SEQRES 16 A 372 VAL GLU GLN GLN SER GLN TYR GLY ILE LEU SER TRP ASN
SEQRES 17 A 372 VAL TRP ARG GLN PRO ILE GLY PHE LEU VAL PHE TRP ILE
SEQRES 18 A 372 ALA ALA LEU ALA GLU CYS GLU ARG LEU PRO PHE ASP LEU
SEQRES 19 A 372 PRO GLU ALA GLU GLU GLU LEU VAL ALA GLY TYR GLN THR
SEQRES 20 A 372 GLU TYR ALA GLY MET LYS PHE ALA LEU PHE TYR LEU GLY
SEQRES 21 A 372 ALA TYR VAL ASN LEU VAL LEU SER ALA LEU LEU VAL SER
SEQRES 22 A 372 VAL LEU TYR PHE GLY GLY TRP SER PHE PRO ILE PRO LEU
SEQRES 23 A 372 GLU THR ILE ALA ASN LEU LEU GLY VAL SER GLU THR ASN
SEQRES 24 A 372 PRO PHE LEU GLN ILE ALA PHE ALA VAL LEU GLY ILE THR
SEQRES 25 A 372 MET THR LEU ILE LYS ALA TYR PHE PHE VAL PHE LEU ALA
SEQRES 26 A 372 ILE LEU LEU ARG TRP THR VAL PRO ARG VAL ARG ILE ASP
SEQRES 27 A 372 GLN LEU LEU ASP LEU GLY TRP LYS PHE LEU LEU PRO VAL
SEQRES 28 A 372 GLY LEU VAL ASN LEU LEU LEU THR ALA GLY LEU LYS LEU
SEQRES 29 A 372 ALA PHE PRO VAL ALA PHE GLY GLY
SEQRES 1 B 515 MET ASP LEU VAL THR LEU ALA GLY GLN LEU ASN ALA GLY
SEQRES 2 B 515 THR ILE LEU PRO GLU THR ILE LEU ILE VAL THR LEU LEU
SEQRES 3 B 515 VAL VAL LEU LEU ALA ASP LEU ILE GLN GLY ARG GLN ALA
SEQRES 4 B 515 ASP ARG TRP THR PRO TYR PHE ALA ILE VAL GLY LEU GLY
SEQRES 5 B 515 GLY ALA ILE ALA THR MET ILE PRO LEU TRP THR GLN PRO
SEQRES 6 B 515 ALA THR ILE SER PHE PHE GLY SER PHE ILE SER ASP HIS
SEQRES 7 B 515 LEU SER LEU PHE PHE ARG GLY LEU ILE ALA LEU SER ALA
SEQRES 8 B 515 LEU GLY THR ILE LEU MET SER ILE ARG TYR VAL GLU GLN
SEQRES 9 B 515 THR GLY SER SER LEU GLY GLU PHE MET THR ILE LEU LEU
SEQRES 10 B 515 THR ALA THR VAL GLY GLY MET PHE ILE ALA GLY ALA GLN
SEQRES 11 B 515 GLU LEU VAL PHE ILE PHE VAL ALA LEU GLU THR LEU SER
SEQRES 12 B 515 ILE ALA SER TYR LEU LEU THR GLY TYR THR LYS ARG ASP
SEQRES 13 B 515 SER ARG SER ASN GLU ALA ALA LEU LYS TYR LEU LEU ILE
SEQRES 14 B 515 GLY ALA ALA SER SER ALA ILE PHE LEU TYR GLY SER SER
SEQRES 15 B 515 LEU LEU TYR GLY LEU SER GLY GLY HIS THR GLN LEU PRO
SEQRES 16 B 515 ALA ILE ALA GLN ALA LEU SER SER GLU SER LEU GLY LEU
SEQRES 17 B 515 VAL VAL ALA LEU VAL PHE VAL ILE ALA GLY ILE SER PHE
SEQRES 18 B 515 LYS ILE SER ALA VAL PRO PHE HIS GLN TRP THR PRO ASP
SEQRES 19 B 515 VAL TYR GLU GLY ALA PRO THR PRO VAL VAL ALA PHE LEU
SEQRES 20 B 515 SER VAL GLY SER LYS ALA ALA GLY PHE ALA LEU ALA ILE
SEQRES 21 B 515 ARG PHE LEU THR LEU ALA PHE PRO SER VAL THR ASP GLN
SEQRES 22 B 515 TRP GLN LEU ILE PHE THR VAL LEU ALA ILE LEU SER MET
SEQRES 23 B 515 ILE LEU GLY ASN VAL VAL ALA LEU ALA GLN THR SER MET
SEQRES 24 B 515 LYS ARG MET LEU ALA TYR SER SER ILE GLY GLN ALA GLY
SEQRES 25 B 515 PHE VAL MET ILE GLY PHE VAL VAL GLY THR GLU ALA GLY
SEQRES 26 B 515 TYR ALA SER MET LEU PHE TYR LEU LEU VAL TYR LEU PHE
SEQRES 27 B 515 MET ASN LEU GLY ALA PHE THR CYS VAL ILE LEU PHE SER
SEQRES 28 B 515 LEU ARG THR GLY THR ASP GLN ILE SER GLU TYR ALA GLY
SEQRES 29 B 515 LEU TYR GLN LYS ASP PRO LEU LEU THR LEU GLY LEU SER
SEQRES 30 B 515 LEU CYS LEU LEU SER LEU GLY GLY ILE PRO PRO LEU ALA
SEQRES 31 B 515 GLY PHE PHE GLY LYS ILE TYR LEU PHE TRP ALA GLY TRP
SEQRES 32 B 515 GLN ALA GLY ALA TYR GLY LEU VAL LEU LEU GLY LEU LEU
SEQRES 33 B 515 THR SER VAL ILE SER ILE TYR TYR TYR ILE ARG VAL VAL
SEQRES 34 B 515 LYS MET MET VAL VAL LYS GLU PRO GLN GLU MET SER GLU
SEQRES 35 B 515 ALA VAL ARG ASN TYR PRO GLU VAL SER TRP SER SER PHE
SEQRES 36 B 515 GLY LEU ARG PRO LEU GLN VAL GLY LEU VAL MET THR VAL
SEQRES 37 B 515 ILE ALA THR SER LEU ALA GLY ILE LEU ALA ASN PRO LEU
SEQRES 38 B 515 PHE ASN LEU VAL ASN THR ALA VAL TRP ASP VAL PRO GLN
SEQRES 39 B 515 LEU ALA ASN GLN PRO THR VAL MET GLU VAL ALA TYR GLN
SEQRES 40 B 515 ALA LEU SER PRO ALA GLY LYS SER
SEQRES 1 C 132 MET VAL ALA ILE PRO ARG LEU ARG ASP THR ALA THR VAL
SEQRES 2 C 132 PHE VAL LEU SER GLY TYR GLU TYR PHE LEU GLY PHE LEU
SEQRES 3 C 132 ILE ILE CYS SER LEU VAL PRO VAL LEU ALA LEU ALA ALA
SEQRES 4 C 132 SER ALA LEU LEU ARG PRO LYS SER GLY ARG MET ILE ARG
SEQRES 5 C 132 LEU THR THR TYR GLU SER GLY MET GLU PRO ILE GLY GLY
SEQRES 6 C 132 ALA TRP ILE GLN PHE ASN VAL ARG TYR TYR MET PHE ALA
SEQRES 7 C 132 LEU VAL PHE VAL ILE PHE ASP VAL GLU THR VAL PHE LEU
SEQRES 8 C 132 TYR PRO TRP ALA VAL ALA PHE HIS GLN LEU GLY LEU LEU
SEQRES 9 C 132 ALA PHE ILE GLU ALA LEU ILE PHE ILE ALA ILE LEU VAL
SEQRES 10 C 132 VAL ALA LEU VAL TYR ALA TRP ARG LYS ARG ALA LEU GLU
SEQRES 11 C 132 TRP SER
SEQRES 1 D 529 MET SER THR PHE PRO TRP LEU THR THR ILE ILE LEU PHE
SEQRES 2 D 529 PRO ILE VAL ALA ALA LEU ALA ILE PRO PHE ILE PRO ASP
SEQRES 3 D 529 PRO THR GLY LYS GLY ARG PRO ILE ARG TRP TYR ALA LEU
SEQRES 4 D 529 ALA VAL GLY LEU ILE ASP PHE ALA LEU ILE VAL TYR ALA
SEQRES 5 D 529 PHE THR ASN PHE TYR ASP LEU ASN THR PRO GLY MET GLN
SEQRES 6 D 529 LEU TRP GLU SER TYR ASP TRP ILE PRO GLU ILE GLY LEU
SEQRES 7 D 529 ARG TRP SER VAL GLY ALA ASP GLY LEU SER MET PRO LEU
SEQRES 8 D 529 ILE LEU LEU THR GLY PHE ILE THR THR LEU ALA ILE LEU
SEQRES 9 D 529 ALA ALA TRP PRO VAL THR LEU LYS PRO ARG LEU PHE TYR
SEQRES 10 D 529 PHE LEU MET LEU ALA MET TYR GLY GLY GLN ILE ALA VAL
SEQRES 11 D 529 PHE ALA VAL GLN ASP MET LEU VAL PHE PHE LEU ALA TRP
SEQRES 12 D 529 GLU LEU GLU LEU ILE PRO VAL TYR LEU LEU LEU ALA ILE
SEQRES 13 D 529 TRP GLY GLY HIS LYS ARG GLN TYR ALA ALA THR LYS PHE
SEQRES 14 D 529 ILE LEU TYR THR ALA GLY SER SER LEU PHE ILE LEU VAL
SEQRES 15 D 529 ALA GLY LEU ALA MET ALA PHE TYR GLY ASP THR VAL SER
SEQRES 16 D 529 PHE ASP MET GLN THR LEU ALA ALA LYS ASP TYR ALA LEU
SEQRES 17 D 529 GLY PHE GLN LEU LEU VAL TYR ALA GLY PHE LEU VAL ALA
SEQRES 18 D 529 TYR GLY VAL LYS LEU PRO ILE VAL PRO LEU HIS THR TRP
SEQRES 19 D 529 LEU PRO ASP ALA HIS GLY GLU ALA THR ALA PRO VAL HIS
SEQRES 20 D 529 MET LEU LEU ALA GLY ILE LEU LEU LYS MET GLY GLY TYR
SEQRES 21 D 529 ALA LEU ILE ARG MET ASN VAL ASP MET LEU PRO ALA ALA
SEQRES 22 D 529 HIS ALA LYS PHE ALA PRO VAL LEU VAL ILE LEU GLY VAL
SEQRES 23 D 529 VAL ASN ILE ILE TYR ALA ALA LEU THR SER TYR ALA GLN
SEQRES 24 D 529 ARG ASN LEU LYS ARG LYS ILE ALA TYR SER SER ILE SER
SEQRES 25 D 529 HIS ILE GLY PHE VAL LEU ILE GLY ILE ALA SER PHE THR
SEQRES 26 D 529 ASN LEU GLY MET SER GLY ALA VAL LEU GLN MET VAL SER
SEQRES 27 D 529 HIS GLY LEU ILE GLY ALA SER LEU PHE PHE LEU VAL GLY
SEQRES 28 D 529 ALA THR TYR ASP ARG THR HIS THR LEU ILE LEU GLU GLU
SEQRES 29 D 529 MET GLY GLY VAL GLY GLN LYS MET LYS LYS ILE PHE ALA
SEQRES 30 D 529 MET PHE THR ALA CYS SER LEU ALA SER LEU ALA LEU PRO
SEQRES 31 D 529 GLY MET SER GLY PHE VAL ALA GLU LEU MET VAL PHE ILE
SEQRES 32 D 529 GLY PHE ALA THR SER ASP ALA TYR SER LEU PRO PHE ARG
SEQRES 33 D 529 VAL ILE VAL VAL PHE LEU ALA ALA VAL GLY VAL ILE LEU
SEQRES 34 D 529 THR PRO ILE TYR LEU LEU SER MET LEU ARG GLU ILE PHE
SEQRES 35 D 529 TYR GLY PRO GLU ASN LYS GLU LEU VAL GLU HIS GLU ALA
SEQRES 36 D 529 LEU VAL ASP ALA GLU PRO ARG GLU VAL PHE ILE ILE ALA
SEQRES 37 D 529 CYS LEU LEU VAL PRO ILE ILE GLY ILE GLY LEU TYR PRO
SEQRES 38 D 529 LYS LEU LEU THR GLN ILE TYR ASP ALA THR THR GLY GLN
SEQRES 39 D 529 VAL ILE ALA ARG ALA ARG GLU VAL LEU PRO THR LEU ALA
SEQRES 40 D 529 GLN GLN THR GLU GLN PRO LEU GLY ILE LEU PRO MET VAL
SEQRES 41 D 529 ALA PRO GLN LEU LYS ALA ASN ALA GLN
SEQRES 1 E 101 MET GLN LEU THR TYR VAL LEU ILE LEU ALA ALA LEU LEU
SEQRES 2 E 101 PHE CYS ILE GLY ILE TYR GLY LEU VAL THR SER ARG ASN
SEQRES 3 E 101 ALA VAL ARG VAL LEU MET SER ILE GLU LEU LEU LEU ASN
SEQRES 4 E 101 ALA VAL ASN LEU ASN LEU ILE GLY PHE ALA ASN TYR LEU
SEQRES 5 E 101 ASP GLY GLN GLN ILE LYS GLY GLN VAL PHE ALA VAL PHE
SEQRES 6 E 101 VAL ILE THR VAL ALA ALA ALA GLU ALA ALA VAL GLY LEU
SEQRES 7 E 101 ALA ILE ILE LEU ALA ILE TYR ARG ASN ARG ASP THR VAL
SEQRES 8 E 101 ASP MET GLU LYS PHE ASN LEU LEU LYS TRP
SEQRES 1 F 656 MET GLU PRO LEU TYR GLN TYR ALA TRP LEU ILE PRO VAL
SEQRES 2 F 656 LEU PRO LEU LEU GLY ALA LEU ILE VAL GLY PHE GLY LEU
SEQRES 3 F 656 ILE ALA PHE SER GLU THR THR SER LYS LEU ARG ARG PRO
SEQRES 4 F 656 SER ALA ILE PHE ILE MET ALA LEU MET ALA ILE ALA MET
SEQRES 5 F 656 GLY HIS SER LEU THR LEU PHE TRP SER GLN VAL GLN GLY
SEQRES 6 F 656 HIS LEU PRO TYR THR GLN MET ILE GLU TRP ALA ALA ALA
SEQRES 7 F 656 GLY ASN LEU HIS ILE ALA MET GLY TYR VAL ILE ASP PRO
SEQRES 8 F 656 LEU ALA ALA LEU MET LEU VAL ILE VAL THR THR VAL ALA
SEQRES 9 F 656 PHE LEU VAL MET LEU TYR SER ASP GLY TYR MET ALA HIS
SEQRES 10 F 656 ASP PRO GLY TYR VAL ARG PHE PHE ALA TYR LEU SER LEU
SEQRES 11 F 656 PHE GLY SER SER MET LEU GLY LEU VAL VAL SER PRO ASN
SEQRES 12 F 656 LEU VAL GLN VAL TYR ILE PHE TRP GLU LEU VAL GLY MET
SEQRES 13 F 656 CYS SER TYR LEU LEU ILE GLY PHE TRP TYR ASP ARG LYS
SEQRES 14 F 656 SER ALA ALA GLU ALA ALA GLN LYS ALA PHE VAL THR ASN
SEQRES 15 F 656 ARG VAL GLY ASP PHE GLY LEU LEU LEU GLY MET VAL GLY
SEQRES 16 F 656 LEU PHE TRP ALA THR GLY THR PHE ASP PHE ALA GLY MET
SEQRES 17 F 656 GLY ASP ARG LEU THR GLU LEU VAL ASN THR GLY LEU LEU
SEQRES 18 F 656 SER PRO SER LEU ALA ALA ILE LEU ALA ILE LEU VAL PHE
SEQRES 19 F 656 LEU GLY PRO VAL ALA LYS SER ALA GLN PHE PRO LEU HIS
SEQRES 20 F 656 VAL TRP LEU PRO ASP ALA MET GLU GLY PRO THR PRO ILE
SEQRES 21 F 656 SER ALA LEU ILE HIS ALA ALA THR MET VAL ALA ALA GLY
SEQRES 22 F 656 VAL PHE LEU ILE ALA ARG MET PHE PRO VAL PHE GLU GLN
SEQRES 23 F 656 LEU PRO GLN VAL MET THR THR ILE ALA TRP THR GLY ALA
SEQRES 24 F 656 PHE THR ALA PHE MET GLY ALA THR ILE ALA ILE THR GLN
SEQRES 25 F 656 ASN ASP ILE LYS LYS SER LEU ALA TYR SER THR ILE SER
SEQRES 26 F 656 GLN LEU GLY TYR MET VAL MET GLY MET GLY VAL GLY ALA
SEQRES 27 F 656 TYR SER ALA GLY LEU PHE HIS LEU MET THR HIS ALA TYR
SEQRES 28 F 656 PHE LYS ALA MET LEU PHE LEU GLY SER GLY SER VAL ILE
SEQRES 29 F 656 HIS SER MET GLU GLY VAL VAL GLY HIS ASN PRO ASP LEU
SEQRES 30 F 656 ALA GLN ASP MET ARG TYR MET GLY GLY LEU ARG LYS TYR
SEQRES 31 F 656 MET PRO ILE THR GLY ALA THR PHE LEU VAL GLY CYS LEU
SEQRES 32 F 656 ALA ILE SER GLY VAL PRO PRO PHE ALA GLY PHE TRP SER
SEQRES 33 F 656 LYS ASP GLU ILE LEU GLY ALA VAL PHE HIS ALA ASN PRO
SEQRES 34 F 656 ALA MET TRP LEU LEU THR TRP LEU THR ALA GLY LEU THR
SEQRES 35 F 656 ALA PHE TYR MET PHE ARG MET TYR PHE MET THR PHE GLU
SEQRES 36 F 656 GLY LYS PHE ARG ASN VAL PRO PRO GLU ARG GLN GLU HIS
SEQRES 37 F 656 HIS ASP HIS HIS SER HIS HIS ALA ALA VAL PRO HIS GLU
SEQRES 38 F 656 SER PRO TRP THR MET THR LEU PRO LEU VAL VAL LEU ALA
SEQRES 39 F 656 ILE PRO SER THR LEU ILE GLY PHE VAL GLY THR PRO PHE
SEQRES 40 F 656 ASN ASN LEU PHE GLU VAL PHE ILE HIS ALA PRO GLY GLU
SEQRES 41 F 656 GLU LYS VAL ALA GLU HIS ALA VAL ASP LEU THR GLU PHE
SEQRES 42 F 656 LEU ILE LEU GLY GLY SER SER VAL GLY ILE GLY LEU MET
SEQRES 43 F 656 GLY ILE THR VAL ALA TYR LEU MET TYR LEU LYS GLY THR
SEQRES 44 F 656 PRO SER PRO GLN ALA ILE ALA LYS ALA ILE GLN PRO LEU
SEQRES 45 F 656 TYR GLN PHE SER LEU HIS LYS TRP TYR PHE ASP GLU LEU
SEQRES 46 F 656 TYR GLU ALA VAL PHE ILE LYS GLY CYS ARG ARG LEU ALA
SEQRES 47 F 656 ARG GLN VAL LEU GLU VAL ASP TYR ASN VAL VAL ASP GLY
SEQRES 48 F 656 VAL VAL ASN LEU THR GLY PHE VAL THR MET VAL THR GLY
SEQRES 49 F 656 GLU GLY LEU LYS TYR LEU GLN ASN GLY ARG ALA GLN PHE
SEQRES 50 F 656 TYR ALA LEU ILE VAL LEU LEU ALA VAL LEU GLY PHE VAL
SEQRES 51 F 656 ILE PHE SER VAL GLN THR
SEQRES 1 G 200 MET ASP LEU ALA THR LEU THR GLN THR ILE THR PHE PHE
SEQRES 2 G 200 ALA LEU ALA ALA ALA VAL ILE ILE ALA ALA LEU GLY VAL
SEQRES 3 G 200 VAL LEU LEU ASP ASN VAL VAL TYR SER ALA PHE LEU LEU
SEQRES 4 G 200 GLY GLY VAL PHE LEU SER ILE ALA GLY LEU TYR ILE LEU
SEQRES 5 G 200 MET ASN ALA ASP PHE VAL SER ALA ALA GLN ILE LEU ILE
SEQRES 6 G 200 TYR VAL GLY ALA VAL ASN VAL LEU ILE LEU PHE ALA ILE
SEQRES 7 G 200 MET LEU VAL ASN LYS ARG GLU THR TYR THR PRO VAL PRO
SEQRES 8 G 200 GLY ARG TRP LEU ARG GLN GLY GLY ALA ALA VAL VAL SER
SEQRES 9 G 200 LEU GLY VAL PHE ALA LEU LEU THR LYS MET ILE LEU GLN
SEQRES 10 G 200 THR PRO TRP GLN LEU SER SER VAL PRO PRO THR PRO ASP
SEQRES 11 G 200 SER ILE THR THR ILE GLY GLN HIS PHE PHE SER ASP PHE
SEQRES 12 G 200 LEU LEU PRO PHE GLU LEU ALA SER VAL LEU LEU LEU MET
SEQRES 13 G 200 ALA LEU ILE GLY ALA VAL VAL LEU ALA ARG ARG GLU LEU
SEQRES 14 G 200 VAL LEU GLU PRO GLU PRO ILE LEU GLY GLU GLU VAL VAL
SEQRES 15 G 200 PRO PRO LEU GLU LEU PRO GLU ARG PRO ARG GLU PRO VAL
SEQRES 16 G 200 ALA LEU SER GLU LYS
SEQRES 1 H 394 MET PRO LYS ILE GLU THR ARG THR GLU PRO MET VAL ILE
SEQRES 2 H 394 ASN MET GLY PRO HIS HIS PRO SER MET HIS GLY VAL LEU
SEQRES 3 H 394 ARG LEU MET VAL THR LEU ASP GLY GLU ASP VAL ILE ASP
SEQRES 4 H 394 CYS GLU PRO VAL ILE GLY TYR LEU HIS ARG GLY MET GLU
SEQRES 5 H 394 LYS ILE ALA GLU ASN ARG THR ASN ILE MET PHE ILE PRO
SEQRES 6 H 394 TYR VAL SER ARG TRP ASP TYR ALA ALA GLY MET PHE ASN
SEQRES 7 H 394 GLU ALA VAL THR VAL ASN ALA PRO GLU LYS LEU ALA GLY
SEQRES 8 H 394 ILE PRO VAL PRO LYS ARG ALA SER TYR ILE ARG VAL ILE
SEQRES 9 H 394 MET LEU GLU LEU ASN ARG ILE ALA ASN HIS LEU LEU TRP
SEQRES 10 H 394 LEU GLY PRO PHE LEU ALA ASP VAL GLY ALA GLN THR PRO
SEQRES 11 H 394 PHE PHE TYR ILE PHE ARG GLU ARG GLU TYR ILE TYR ASP
SEQRES 12 H 394 LEU PHE GLU ALA ALA THR GLY MET ARG PHE ILE ASN ASN
SEQRES 13 H 394 ASN TYR PHE ARG ILE GLY GLY VAL ALA ALA ASP LEU THR
SEQRES 14 H 394 TYR GLY TRP VAL THR LYS CYS ARG ASP PHE CYS ASP TYR
SEQRES 15 H 394 PHE LEU PRO LYS VAL ASP GLU TYR GLU ARG LEU ILE THR
SEQRES 16 H 394 ASN ASN PRO ILE PHE VAL ARG ARG LEU GLN GLY VAL GLY
SEQRES 17 H 394 LYS ILE SER ARG GLU GLU ALA ILE ASN TRP GLY LEU SER
SEQRES 18 H 394 GLY PRO MET LEU ARG ALA SER GLY VAL LYS TRP ASP LEU
SEQRES 19 H 394 ARG LYS VAL ASP HIS TYR GLU CYS TYR ASP ASP PHE ASP
SEQRES 20 H 394 TRP ASP VAL PRO VAL ALA THR GLU GLY ASP CYS LEU ALA
SEQRES 21 H 394 ARG TYR ILE VAL ARG ILE GLN GLU MET ARG GLU SER VAL
SEQRES 22 H 394 LYS ILE ILE ARG GLN ALA LEU ASP GLY LEU PRO GLY GLY
SEQRES 23 H 394 PRO TYR GLU ASN LEU GLU ALA LYS ARG MET LEU GLU GLY
SEQRES 24 H 394 ALA LYS SER GLU TRP ASN GLY PHE ASP TYR GLN TYR ILE
SEQRES 25 H 394 GLY LYS LYS LEU SER PRO THR PHE LYS ILE PRO LYS GLY
SEQRES 26 H 394 GLU HIS TYR VAL ARG VAL GLU SER GLY LYS GLY GLU LEU
SEQRES 27 H 394 GLY ILE TYR LEU ILE GLY ASP ASP ASN VAL PHE PRO TRP
SEQRES 28 H 394 ARG TRP LYS ILE ARG PRO PRO ASP PHE ASN ASN LEU GLN
SEQRES 29 H 394 VAL LEU PRO GLN LEU LEU LYS GLY MET LYS VAL ALA ASP
SEQRES 30 H 394 ILE VAL ALA ILE LEU GLY SER ILE ASP VAL ILE MET GLY
SEQRES 31 H 394 SER VAL ASP ARG
SEQRES 1 I 196 MET LYS PHE LEU ASN GLN ILE THR ASN TYR ALA LYS GLU
SEQRES 2 I 196 ALA VAL GLN SER ALA LYS TYR ILE GLY GLN GLY LEU SER
SEQRES 3 I 196 VAL THR PHE ASP HIS MET ARG ARG ARG PRO ILE THR VAL
SEQRES 4 I 196 GLN TYR PRO TYR GLU LYS LEU ILE PRO SER GLU ARG PHE
SEQRES 5 I 196 ARG GLY ARG ILE HIS PHE GLU PHE ASP LYS CYS ILE ALA
SEQRES 6 I 196 CYS GLU VAL CYS VAL ARG VAL CYS PRO ILE ASN LEU PRO
SEQRES 7 I 196 VAL VAL ASP TRP VAL PHE ASN LYS GLU LEU LYS LYS LYS
SEQRES 8 I 196 GLU LEU LYS HIS TYR SER ILE ASP PHE GLY VAL CYS ILE
SEQRES 9 I 196 PHE CYS ALA ASN CYS VAL GLU TYR CYS PRO THR ASN CYS
SEQRES 10 I 196 LEU SER VAL THR GLU GLU TYR GLU LEU ALA THR TYR ASP
SEQRES 11 I 196 ARG HIS GLU LEU ASN TYR ASP SER VAL ALA MET GLY ARG
SEQRES 12 I 196 ILE PRO TYR LYS VAL THR GLN ASP PRO MET VAL THR PRO
SEQRES 13 I 196 ILE ARG GLU PHE ALA TYR LEU PRO ALA GLY VAL MET SER
SEQRES 14 I 196 GLY HIS ASP LEU PRO ALA GLY ALA GLN ARG ALA GLY GLU
SEQRES 15 I 196 ARG PRO GLU ALA ILE ALA ASN THR ALA LYS SER SER GLU
SEQRES 16 I 196 ASN
SEQRES 1 J 168 MET SER ASP THR PRO GLU ALA PRO ILE VAL GLU ALA GLY
SEQRES 2 J 168 PRO VAL GLY ARG LEU LEU GLN SER GLN ASN LEU SER VAL
SEQRES 3 J 168 GLU SER LEU GLY ARG ASP ALA SER GLY VAL GLU MET ILE
SEQRES 4 J 168 LYS VAL ASP ARG ASP ARG LEU LEU ALA VAL CYS GLN THR
SEQRES 5 J 168 LEU TYR ALA ASP GLY PHE ASN TYR LEU ARG CYS GLN ALA
SEQRES 6 J 168 ALA TYR ASP SER GLY PRO GLY GLN ASP LEU VAL SER THR
SEQRES 7 J 168 TYR HIS LEU ILE LYS LEU SER ASP ASN ALA ASP ARG PRO
SEQRES 8 J 168 PRO GLU VAL ARG ILE LYS VAL PHE VAL PRO ARG ASP ASP
SEQRES 9 J 168 PRO ARG VAL PRO SER VAL TYR TRP ILE TRP LYS THR ALA
SEQRES 10 J 168 ASP TRP GLN GLU ARG GLU SER TYR ASP MET PHE GLY ILE
SEQRES 11 J 168 VAL TYR GLU GLY HIS PRO ASN LEU LYS ARG ILE LEU MET
SEQRES 12 J 168 PRO GLU ASP TRP VAL GLY TRP PRO LEU ARG LYS ASP TYR
SEQRES 13 J 168 ILE THR PRO ASP PHE TYR GLU LEU GLN GLU ALA TYR
SEQRES 1 K 237 MET THR ASN THR THR SER PRO ALA ILE LEU ASN PRO ILE
SEQRES 2 K 237 ALA ARG PRO GLU VAL PRO GLN GLU LEU ALA GLU ASN ILE
SEQRES 3 K 237 ILE LEU THR SER LEU ASN ASP VAL TYR ASP TRP ALA ARG
SEQRES 4 K 237 LEU SER SER LEU TRP PRO LEU MET TYR GLY THR ALA CYS
SEQRES 5 K 237 CYS PHE ILE GLU PHE ALA ALA MET ILE GLY SER ARG PHE
SEQRES 6 K 237 ASP PHE ASP ARG PHE GLY LEU VAL PRO ARG ASN SER PRO
SEQRES 7 K 237 ARG GLN ALA ASP LEU ILE ILE THR SER GLY THR ILE THR
SEQRES 8 K 237 MET LYS MET ALA PRO ALA LEU VAL ARG LEU TYR GLU GLN
SEQRES 9 K 237 MET PRO SER PRO LYS TYR VAL ILE ALA MET GLY ALA CYS
SEQRES 10 K 237 THR ILE THR GLY GLY MET PHE SER SER ASP SER TYR SER
SEQRES 11 K 237 ALA VAL ARG GLY VAL ASP LYS LEU ILE PRO VAL ASP VAL
SEQRES 12 K 237 TYR LEU PRO GLY CYS PRO PRO ARG PRO GLU ALA ILE MET
SEQRES 13 K 237 ASP ALA ILE VAL LYS LEU ARG LYS LYS ILE ALA ASN GLU
SEQRES 14 K 237 HIS ILE ASN GLU ARG GLY ASN LEU ALA GLN THR HIS ARG
SEQRES 15 K 237 LEU PHE THR ALA LYS HIS LYS MET LYS PRO VAL PRO PRO
SEQRES 16 K 237 ILE LEU THR GLY GLN TYR LEU ASN ALA PRO SER ARG GLN
SEQRES 17 K 237 ALA PRO PRO PRO ALA LEU ALA ALA ALA MET GLY ILE ALA
SEQRES 18 K 237 VAL PRO ALA LEU GLY GLU ALA VAL SER GLU THR THR SER
SEQRES 19 K 237 VAL ALA GLU
SEQRES 1 L 76 MET ALA VAL SER THR GLU LEU LEU VAL LEU GLY VAL TYR
SEQRES 2 L 76 GLY ALA LEU ALA GLY LEU TYR LEU LEU VAL VAL PRO ALA
SEQRES 3 L 76 ILE VAL TYR ALA TYR LEU ASN ALA ARG TRP TYR VAL ALA
SEQRES 4 L 76 SER SER PHE GLU ARG ALA PHE MET TYR PHE LEU VAL THR
SEQRES 5 L 76 PHE PHE PHE PRO GLY LEU LEU LEU LEU ALA PRO PHE ILE
SEQRES 6 L 76 ASN PHE ARG PRO GLN PRO ARG SER LEU ASN SER
SEQRES 1 M 111 MET LEU LEU LYS SER THR THR ARG HIS VAL HIS ILE TYR
SEQRES 2 M 111 ALA GLY HIS VAL VAL ASP GLY GLU VAL HIS PRO ASP THR
SEQRES 3 M 111 GLU THR LEU THR LEU ASN VAL ASP PRO ASP ASN GLU LEU
SEQRES 4 M 111 GLU TRP ASN GLU ALA ALA LEU ALA LYS VAL GLU ALA LYS
SEQRES 5 M 111 PHE ARG GLU LEU VAL ALA ASN ALA ALA GLY GLU ASP LEU
SEQRES 6 M 111 THR GLU TYR ASN LEU ARG ARG ILE GLY SER ASP LEU GLU
SEQRES 7 M 111 HIS PHE ILE ARG SER LEU LEU MET GLN GLY GLU ILE GLY
SEQRES 8 M 111 TYR ASN LEU ASN SER ARG VAL ARG ASN TYR SER LEU GLY
SEQRES 9 M 111 ILE PRO ARG VAL ASN HIS SER
SEQRES 1 N 150 MET GLY LEU LEU ALA GLY TYR GLN PHE VAL LYS ASP LEU
SEQRES 2 N 150 GLU SER ALA GLY ALA LEU ALA LEU PHE VAL PRO PRO GLU
SEQRES 3 N 150 GLY GLY PHE GLU GLY ARG TYR GLN ARG ARG LEU ARG SER
SEQRES 4 N 150 LYS GLY TYR THR THR LEU PRO MET SER ALA PRO GLY LEU
SEQRES 5 N 150 GLY ASP LEU ALA ALA TYR LEU THR GLN GLU HIS GLY ILE
SEQRES 6 N 150 ARG PRO ALA HIS THR GLY LYS GLU ASP ILE ARG VAL TYR
SEQRES 7 N 150 PHE GLN PRO PRO LEU VAL THR TYR HIS LEU GLU ASN LEU
SEQRES 8 N 150 PRO PRO ASN ALA LYS GLY LEU VAL LEU TRP LEU ILE ASP
SEQRES 9 N 150 GLY LYS ARG LEU SER LYS GLN GLU PHE ALA TYR LEU ALA
SEQRES 10 N 150 GLN LEU THR GLN THR LEU PRO LYS PHE LYS VAL VAL VAL
SEQRES 11 N 150 GLU VAL GLY GLY ASP ARG VAL VAL ARG TRP GLU PRO LEU
SEQRES 12 N 150 ALA ASP TRP VAL ALA ALA ALA
SEQRES 1 O 70 MET ALA ILE LYS LYS GLY ASP LEU VAL LYS VAL VAL ALA
SEQRES 2 O 70 GLU LYS LEU ALA ASN SER LEU GLU ALA LEU ALA SER ASP
SEQRES 3 O 70 HIS ARG TYR PRO PRO TYR LEU PHE GLU GLY ARG GLY GLU
SEQRES 4 O 70 VAL VAL ASP ILE ARG GLY ASP TYR ALA GLN ILE LYS PHE
SEQRES 5 O 70 PRO VAL PRO THR PRO THR VAL TRP LEU ARG LEU ASP GLN
SEQRES 6 O 70 LEU GLU VAL ALA GLN
SEQRES 1 P 44 MET ASP ALA VAL ILE SER VAL LYS PRO ILE LEU LEU ALA
SEQRES 2 P 44 MET THR PRO VAL PHE ILE LEU LEU CYS LEU PHE PHE GLY
SEQRES 3 P 44 THR ARG ASN GLY PHE TYR ASP THR ASP GLN TYR HIS GLY
SEQRES 4 P 44 ASN GLY SER ALA HIS
SEQRES 1 Q 45 MET ALA THR ASP PHE ASN ARG GLY ILE MET LYS PHE ASP
SEQRES 2 Q 45 GLY ALA ASP SER PRO ALA MET ILE ALA ILE SER ALA VAL
SEQRES 3 Q 45 LEU ILE LEU GLY PHE ILE ALA GLY LEU ILE TRP TRP ALA
SEQRES 4 Q 45 LEU HIS THR ALA TYR ALA
SEQRES 1 S 110 MET ILE ARG PRO ILE ALA ASP THR TYR PRO LEU LEU PRO
SEQRES 2 S 110 LEU SER LYS ALA GLN MET GLY GLN ARG GLN GLU ILE ILE
SEQRES 3 S 110 ASN SER HIS LYS ARG LEU TRP ASP LYS THR MET ALA THR
SEQRES 4 S 110 ASP LEU ILE MET THR ILE LEU PRO GLY MET THR VAL LYS
SEQRES 5 S 110 VAL THR ASN PRO ASN ASP THR TYR TYR GLN PHE GLN GLY
SEQRES 6 S 110 ILE VAL GLN ARG ILE THR ASP GLY LYS VAL ALA VAL LEU
SEQRES 7 S 110 PHE GLU GLY GLY ASN TRP ASP LYS LEU VAL THR PHE GLN
SEQRES 8 S 110 ALA SER GLU LEU GLU PRO VAL VAL VAL THR PRO LYS GLU
SEQRES 9 S 110 LYS ALA LYS ALA LYS LYS
HET SF4 I 201 8
HET SF4 I 202 8
HET SF4 K 301 8
HETNAM SF4 IRON/SULFUR CLUSTER
FORMUL 19 SF4 3(FE4 S4)
HELIX 1 AA1 PRO A 31 ALA A 41 1 11
HELIX 2 AA2 THR A 42 VAL A 59 1 18
HELIX 3 AA3 LEU A 74 PHE A 85 1 12
HELIX 4 AA4 ARG A 96 LEU A 101 1 6
HELIX 5 AA5 GLY A 102 VAL A 107 1 6
HELIX 6 AA6 VAL A 107 SER A 113 1 7
HELIX 7 AA7 TYR A 114 ILE A 116 5 3
HELIX 8 AA8 GLY A 131 SER A 139 1 9
HELIX 9 AA9 ILE A 141 LEU A 146 1 6
HELIX 10 AB1 LEU A 146 TYR A 151 1 6
HELIX 11 AB2 ASN A 155 ILE A 170 1 16
HELIX 12 AB3 GLU A 173 ASN A 188 1 16
HELIX 13 AB4 GLY A 191 GLU A 197 1 7
HELIX 14 AB5 TRP A 207 GLN A 212 1 6
HELIX 15 AB6 GLY A 215 GLU A 228 1 14
HELIX 16 AB7 GLY A 251 LEU A 259 1 9
HELIX 17 AB8 ALA A 261 TYR A 276 1 16
HELIX 18 AB9 ASN A 299 VAL A 308 1 10
HELIX 19 AC1 MET A 313 LEU A 328 1 16
HELIX 20 AC2 ARG A 336 TRP A 345 1 10
HELIX 21 AC3 PHE A 347 ALA A 360 1 14
HELIX 22 AC4 ILE B 20 GLN B 35 1 16
HELIX 23 AC5 GLN B 38 ARG B 41 5 4
HELIX 24 AC6 TRP B 42 THR B 57 1 16
HELIX 25 AC7 MET B 58 THR B 63 1 6
HELIX 26 AC8 PHE B 70 SER B 73 5 4
HELIX 27 AC9 ASP B 77 GLY B 106 1 30
HELIX 28 AD1 LEU B 109 PHE B 125 1 17
HELIX 29 AD2 GLU B 131 GLY B 151 1 21
HELIX 30 AD3 ARG B 158 SER B 188 1 31
HELIX 31 AD4 GLN B 193 GLN B 199 1 7
HELIX 32 AD5 SER B 205 PHE B 214 1 10
HELIX 33 AD6 VAL B 215 ILE B 223 1 9
HELIX 34 AD7 TRP B 231 TYR B 236 1 6
HELIX 35 AD8 PRO B 240 SER B 248 1 9
HELIX 36 AD9 VAL B 249 THR B 264 1 16
HELIX 37 AE1 GLN B 273 VAL B 291 1 19
HELIX 38 AE2 SER B 298 GLY B 321 1 24
HELIX 39 AE3 THR B 322 THR B 354 1 33
HELIX 40 AE4 ASP B 369 GLY B 385 1 17
HELIX 41 AE5 LEU B 389 TRP B 403 1 15
HELIX 42 AE6 GLY B 409 VAL B 434 1 26
HELIX 43 AE7 GLY B 456 LEU B 473 1 18
HELIX 44 AE8 LEU B 477 THR B 487 1 11
HELIX 45 AE9 TYR C 19 SER C 40 1 22
HELIX 46 AF1 ARG C 73 ALA C 97 1 25
HELIX 47 AF2 LEU C 103 LYS C 126 1 24
HELIX 48 AF3 TRP D 6 LEU D 19 1 14
HELIX 49 AF4 ARG D 32 TYR D 57 1 26
HELIX 50 AF5 SER D 88 ALA D 105 1 18
HELIX 51 AF6 LYS D 112 VAL D 133 1 22
HELIX 52 AF7 VAL D 138 GLU D 144 1 7
HELIX 53 AF8 LEU D 147 TRP D 157 1 11
HELIX 54 AF9 ARG D 162 PHE D 189 1 28
HELIX 55 AG1 GLN D 199 LYS D 204 1 6
HELIX 56 AG2 ALA D 207 VAL D 224 1 18
HELIX 57 AG3 TRP D 234 HIS D 239 1 6
HELIX 58 AG4 THR D 243 ALA D 251 1 9
HELIX 59 AG5 ILE D 253 VAL D 267 1 15
HELIX 60 AG6 LEU D 270 ALA D 278 1 9
HELIX 61 AG7 ALA D 278 ALA D 298 1 21
HELIX 62 AG8 ASN D 301 ALA D 322 1 22
HELIX 63 AG9 THR D 325 HIS D 358 1 34
HELIX 64 AH1 GLY D 367 MET D 372 1 6
HELIX 65 AH2 LYS D 373 LEU D 384 1 12
HELIX 66 AH3 ALA D 385 ALA D 388 5 4
HELIX 67 AH4 MET D 392 ALA D 406 1 15
HELIX 68 AH5 SER D 412 ALA D 424 1 13
HELIX 69 AH6 ALA D 424 GLU D 440 1 17
HELIX 70 AH7 ARG D 462 LEU D 479 1 18
HELIX 71 AH8 TYR D 480 LEU D 484 5 5
HELIX 72 AH9 TYR D 488 GLU D 501 1 14
HELIX 73 AI1 GLN E 2 SER E 24 1 23
HELIX 74 AI2 VAL E 28 TYR E 51 1 24
HELIX 75 AI3 LYS E 58 ARG E 88 1 31
HELIX 76 AI4 GLU F 2 GLN F 6 1 5
HELIX 77 AI5 TRP F 9 ILE F 27 1 19
HELIX 78 AI6 PHE F 29 SER F 34 1 6
HELIX 79 AI7 LEU F 36 GLN F 64 1 29
HELIX 80 AI8 ASP F 90 MET F 115 1 26
HELIX 81 AI9 GLY F 120 VAL F 140 1 21
HELIX 82 AJ1 VAL F 145 PHE F 150 1 6
HELIX 83 AJ2 PHE F 150 GLY F 163 1 14
HELIX 84 AJ3 ARG F 168 THR F 200 1 33
HELIX 85 AJ4 PHE F 205 GLY F 219 1 15
HELIX 86 AJ5 ALA F 226 LEU F 235 1 10
HELIX 87 AJ6 GLY F 236 SER F 241 1 6
HELIX 88 AJ7 TRP F 249 MET F 254 1 6
HELIX 89 AJ8 PRO F 257 ILE F 264 1 8
HELIX 90 AJ9 ALA F 271 MET F 280 1 10
HELIX 91 AK1 MET F 280 GLU F 285 1 6
HELIX 92 AK2 LEU F 287 ILE F 310 1 24
HELIX 93 AK3 ASP F 314 MET F 332 1 19
HELIX 94 AK4 TYR F 339 GLU F 368 1 30
HELIX 95 AK5 LEU F 387 MET F 391 5 5
HELIX 96 AK6 ALA F 396 ALA F 404 1 9
HELIX 97 AK7 ASP F 418 ALA F 423 1 6
HELIX 98 AK8 LEU F 433 PHE F 454 1 22
HELIX 99 AK9 HIS F 469 HIS F 474 1 6
HELIX 100 AL1 PRO F 483 THR F 487 5 5
HELIX 101 AL2 LEU F 488 LEU F 493 1 6
HELIX 102 AL3 ALA F 494 ILE F 500 1 7
HELIX 103 AL4 PHE F 507 HIS F 516 1 10
HELIX 104 AL5 THR F 531 SER F 539 1 9
HELIX 105 AL6 SER F 539 LEU F 553 1 15
HELIX 106 AL7 ILE F 569 HIS F 578 1 10
HELIX 107 AL8 LYS F 579 TYR F 581 5 3
HELIX 108 AL9 PHE F 582 VAL F 589 1 8
HELIX 109 AM1 VAL F 589 ALA F 598 1 10
HELIX 110 AM2 ALA F 598 VAL F 608 1 11
HELIX 111 AM3 VAL F 608 GLY F 617 1 10
HELIX 112 AM4 THR F 620 LYS F 628 1 9
HELIX 113 AM5 ARG F 634 SER F 653 1 20
HELIX 114 AM6 THR G 5 LEU G 24 1 20
HELIX 115 AM7 LEU G 24 LEU G 29 1 6
HELIX 116 AM8 ASN G 31 MET G 53 1 23
HELIX 117 AM9 ALA G 55 TYR G 66 1 12
HELIX 118 AN1 ALA G 69 LEU G 80 1 12
HELIX 119 AN2 GLY G 99 THR G 118 1 20
HELIX 120 AN3 LEU G 144 LEU G 164 1 21
HELIX 121 AN4 GLY H 50 ALA H 55 1 6
HELIX 122 AN5 GLU H 56 ARG H 58 5 3
HELIX 123 AN6 PHE H 63 SER H 68 1 6
HELIX 124 AN7 MET H 76 ASN H 84 1 9
HELIX 125 AN8 PRO H 95 VAL H 125 1 31
HELIX 126 AN9 GLN H 128 PRO H 130 5 3
HELIX 127 AO1 PHE H 131 THR H 149 1 19
HELIX 128 AO2 TRP H 172 CYS H 180 1 9
HELIX 129 AO3 PHE H 183 THR H 195 1 13
HELIX 130 AO4 ILE H 199 ARG H 203 5 5
HELIX 131 AO5 SER H 211 TRP H 218 1 8
HELIX 132 AO6 SER H 221 GLY H 229 5 9
HELIX 133 AO7 ASP H 233 ASP H 238 1 6
HELIX 134 AO8 ASP H 257 GLY H 282 1 26
HELIX 135 AO9 PRO H 287 GLU H 298 1 12
HELIX 136 AP1 VAL H 365 LEU H 370 1 6
HELIX 137 AP2 ILE H 378 GLY H 383 1 6
HELIX 138 AP3 SER H 384 ASP H 386 5 3
HELIX 139 AP4 ALA I 14 LYS I 19 1 6
HELIX 140 AP5 ILE I 21 PHE I 29 1 9
HELIX 141 AP6 ASP I 30 MET I 32 5 3
HELIX 142 AP7 GLU I 67 VAL I 72 1 6
HELIX 143 AP8 ASP I 130 GLU I 133 5 4
HELIX 144 AP9 VAL J 15 SER J 21 1 7
HELIX 145 AQ1 ARG J 45 GLY J 57 1 13
HELIX 146 AQ2 TRP J 114 ALA J 117 5 4
HELIX 147 AQ3 ASP J 118 PHE J 128 1 11
HELIX 148 AQ4 ASN K 25 SER K 41 1 17
HELIX 149 AQ5 PHE K 54 GLY K 62 1 9
HELIX 150 AQ6 ALA K 95 GLN K 104 1 10
HELIX 151 AQ7 GLY K 134 LEU K 138 5 5
HELIX 152 AQ8 ARG K 151 ALA K 167 1 17
HELIX 153 AQ9 HIS K 170 ARG K 174 5 5
HELIX 154 AR1 LEU L 16 LEU L 22 1 7
HELIX 155 AR2 LEU L 22 ARG L 35 1 14
HELIX 156 AR3 PHE L 42 THR L 52 1 11
HELIX 157 AR4 PHE L 54 LEU L 59 1 6
HELIX 158 AR5 ALA M 44 VAL M 49 1 6
HELIX 159 AR6 VAL M 49 ALA M 60 1 12
HELIX 160 AR7 THR M 66 GLU M 78 1 13
HELIX 161 AR8 PHE M 80 MET M 86 1 7
HELIX 162 AR9 TYR N 7 GLY N 17 1 11
HELIX 163 AS1 ARG N 32 LYS N 40 1 9
HELIX 164 AS2 ASP N 54 THR N 60 1 7
HELIX 165 AS3 PRO N 82 LEU N 91 1 10
HELIX 166 AS4 ASP N 104 LEU N 108 5 5
HELIX 167 AS5 SER N 109 GLN N 118 1 10
HELIX 168 AS6 LEU N 143 ALA N 148 1 6
HELIX 169 AS7 VAL P 6 LEU P 11 1 6
HELIX 170 AS8 MET P 13 GLY P 25 1 13
HELIX 171 AS9 SER Q 17 ALA Q 43 1 27
SHEET 1 AA1 2 ILE B 68 SER B 69 0
SHEET 2 AA1 2 PHE B 74 ILE B 75 -1 O PHE B 74 N SER B 69
SHEET 1 AA2 2 TRP C 67 GLN C 69 0
SHEET 2 AA2 2 GLU H 5 ARG H 7 1 O GLU H 5 N ILE C 68
SHEET 1 AA3 2 GLU D 68 ILE D 73 0
SHEET 2 AA3 2 LEU D 78 VAL D 82 -1 O TRP D 80 N TYR D 70
SHEET 1 AA4 2 TYR F 69 GLN F 71 0
SHEET 2 AA4 2 TYR F 87 ILE F 89 -1 O TYR F 87 N GLN F 71
SHEET 1 AA5 2 GLU F 74 ALA F 77 0
SHEET 2 AA5 2 HIS F 82 ALA F 84 -1 O ILE F 83 N TRP F 75
SHEET 1 AA6 3 MET H 11 ASN H 14 0
SHEET 2 AA6 3 LEU H 28 ASP H 33 -1 O LEU H 32 N MET H 11
SHEET 3 AA6 3 ASP H 36 PRO H 42 -1 O ASP H 39 N THR H 31
SHEET 1 AA7 2 PHE H 159 ARG H 160 0
SHEET 2 AA7 2 GLY H 163 VAL H 164 -1 O GLY H 163 N ARG H 160
SHEET 1 AA8 3 GLY H 325 GLU H 326 0
SHEET 2 AA8 3 GLU H 337 GLY H 344 -1 O GLY H 344 N GLY H 325
SHEET 3 AA8 3 VAL H 329 GLU H 332 -1 N VAL H 331 O LEU H 338
SHEET 1 AA9 3 GLY H 325 GLU H 326 0
SHEET 2 AA9 3 GLU H 337 GLY H 344 -1 O GLY H 344 N GLY H 325
SHEET 3 AA9 3 PRO H 350 ARG H 356 -1 O ARG H 356 N GLY H 339
SHEET 1 AB1 2 ILE I 56 HIS I 57 0
SHEET 2 AB1 2 SER I 119 VAL I 120 -1 O SER I 119 N HIS I 57
SHEET 1 AB2 3 VAL I 79 VAL I 83 0
SHEET 2 AB2 3 GLU I 92 ASP I 99 -1 O LYS I 94 N ASP I 81
SHEET 3 AB2 3 ASN I 135 TYR I 136 -1 O TYR I 136 N ILE I 98
SHEET 1 AB3 5 GLU J 27 ARG J 31 0
SHEET 2 AB3 5 GLU J 37 VAL J 41 -1 O MET J 38 N LEU J 29
SHEET 3 AB3 5 GLU J 93 VAL J 100 1 O ARG J 95 N ILE J 39
SHEET 4 AB3 5 LEU J 75 ILE J 82 -1 N TYR J 79 O ILE J 96
SHEET 5 AB3 5 TYR J 60 ASP J 68 -1 N TYR J 60 O ILE J 82
SHEET 1 AB4 2 ARG J 106 PRO J 108 0
SHEET 2 AB4 2 VAL J 131 GLU J 133 1 O VAL J 131 N VAL J 107
SHEET 1 AB5 2 ILE K 9 LEU K 10 0
SHEET 2 AB5 2 ARG M 107 VAL M 108 -1 O ARG M 107 N LEU K 10
SHEET 1 AB6 4 PRO K 45 LEU K 46 0
SHEET 2 AB6 4 LEU K 83 SER K 87 1 O LEU K 83 N LEU K 46
SHEET 3 AB6 4 VAL K 111 MET K 114 1 O ILE K 112 N THR K 86
SHEET 4 AB6 4 VAL K 141 VAL K 143 1 O ASP K 142 N VAL K 111
SHEET 1 AB7 2 LEU K 183 LYS K 187 0
SHEET 2 AB7 2 THR M 28 ASN M 32 -1 O LEU M 29 N ALA K 186
SHEET 1 AB8 2 LYS K 191 PRO K 192 0
SHEET 2 AB8 2 ASP M 64 LEU M 65 1 O LEU M 65 N LYS K 191
SHEET 1 AB9 2 LYS M 4 THR M 6 0
SHEET 2 AB9 2 HIS M 11 TYR M 13 -1 O ILE M 12 N SER M 5
SHEET 1 AC1 2 GLY M 15 VAL M 18 0
SHEET 2 AC1 2 GLU M 21 PRO M 24 -1 O HIS M 23 N HIS M 16
SHEET 1 AC2 2 LEU M 39 GLU M 40 0
SHEET 2 AC2 2 GLY M 91 TYR M 92 -1 O GLY M 91 N GLU M 40
SHEET 1 AC3 5 THR N 43 THR N 44 0
SHEET 2 AC3 5 LEU N 98 LEU N 100 1 O VAL N 99 N THR N 43
SHEET 3 AC3 5 PHE N 126 GLY N 134 1 O LYS N 127 N LEU N 98
SHEET 4 AC3 5 ALA N 18 VAL N 23 1 N LEU N 19 O VAL N 128
SHEET 5 AC3 5 ARG N 139 PRO N 142 -1 O ARG N 139 N PHE N 22
SHEET 1 AC4 2 HIS N 63 ILE N 65 0
SHEET 2 AC4 2 TYR N 78 GLN N 80 -1 O TYR N 78 N ILE N 65
SHEET 1 AC5 5 VAL O 59 ARG O 62 0
SHEET 2 AC5 5 TYR O 47 LYS O 51 -1 N ALA O 48 O LEU O 61
SHEET 3 AC5 5 GLY O 38 ARG O 44 -1 N VAL O 41 O GLN O 49
SHEET 4 AC5 5 LEU O 8 VAL O 11 -1 N VAL O 9 O GLY O 38
SHEET 5 AC5 5 LEU O 66 VAL O 68 -1 O GLU O 67 N LYS O 10
SHEET 1 AC6 5 LEU S 87 PHE S 90 0
SHEET 2 AC6 5 VAL S 75 LEU S 78 -1 N VAL S 75 O PHE S 90
SHEET 3 AC6 5 GLN S 64 GLN S 68 -1 N ILE S 66 O LEU S 78
SHEET 4 AC6 5 THR S 50 VAL S 53 -1 N VAL S 51 O GLY S 65
SHEET 5 AC6 5 LEU S 95 VAL S 98 -1 O VAL S 98 N THR S 50
SSBOND 1 CYS H 176 CYS H 180 1555 1555 2.06
CISPEP 1 PRO B 387 PRO B 388 0 3.36
CISPEP 2 CYS K 148 PRO K 149 0 -11.45
SITE 1 AC1 8 CYS I 73 PRO I 74 CYS I 103 ILE I 104
SITE 2 AC1 8 CYS I 106 ALA I 107 ASN I 108 CYS I 109
SITE 1 AC2 10 CYS I 63 CYS I 66 GLU I 67 VAL I 68
SITE 2 AC2 10 CYS I 69 TYR I 112 CYS I 113 THR I 115
SITE 3 AC2 10 CYS I 117 LEU I 118
SITE 1 AC3 6 CYS K 52 CYS K 53 GLY K 88 THR K 89
SITE 2 AC3 6 CYS K 117 CYS K 148
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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
(ATOM LINES ARE NOT SHOWN.)
END
