HEADER BIOSYNTHETIC PROTEIN 25-AUG-16 5T3D
TITLE CRYSTAL STRUCTURE OF HOLO-ENTF A NONRIBOSOMAL PEPTIDE SYNTHETASE IN
TITLE 2 THE THIOESTER-FORMING CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENTEROBACTIN SYNTHASE COMPONENT F;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ENTEROCHELIN SYNTHASE F,SERINE-ACTIVATING ENZYME,SERYL-AMP
COMPND 5 LIGASE;
COMPND 6 EC: 2.7.7.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: ENTF, B0586, JW0578;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS NONRIBOSOMAL PEPTIDE SYNTHETASE, NRPS, CONDENSATION, ADENYLATION,
KEYWDS 2 PCP, THIOESTERASE, PHOSPHOPANTETHEINE, BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.R.MILLER,E.J.DRAKE,J.A.SUNDLOV,A.M.GULICK
REVDAT 4 25-DEC-19 5T3D 1 COMPND
REVDAT 3 10-OCT-18 5T3D 1 COMPND JRNL
REVDAT 2 13-SEP-17 5T3D 1 REMARK
REVDAT 1 21-SEP-16 5T3D 0
SPRSDE 21-SEP-16 5T3D 4ZXJ
JRNL AUTH E.J.DRAKE,B.R.MILLER,C.SHI,J.T.TARRASCH,J.A.SUNDLOV,
JRNL AUTH 2 C.L.ALLEN,G.SKINIOTIS,C.C.ALDRICH,A.M.GULICK
JRNL TITL STRUCTURES OF TWO DISTINCT CONFORMATIONS OF
JRNL TITL 2 HOLO-NON-RIBOSOMAL PEPTIDE SYNTHETASES.
JRNL REF NATURE V. 529 235 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 26762461
JRNL DOI 10.1038/NATURE16163
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 38741
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1943
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 60.4415 - 6.7461 1.00 2853 142 0.1711 0.1960
REMARK 3 2 6.7461 - 5.3556 1.00 2688 151 0.1917 0.2385
REMARK 3 3 5.3556 - 4.6789 1.00 2658 150 0.1529 0.1922
REMARK 3 4 4.6789 - 4.2512 1.00 2632 137 0.1484 0.1984
REMARK 3 5 4.2512 - 3.9466 1.00 2633 144 0.1460 0.1898
REMARK 3 6 3.9466 - 3.7139 1.00 2609 132 0.1689 0.2222
REMARK 3 7 3.7139 - 3.5280 1.00 2633 109 0.1836 0.2605
REMARK 3 8 3.5280 - 3.3744 1.00 2597 143 0.2167 0.2704
REMARK 3 9 3.3744 - 3.2445 1.00 2583 147 0.2131 0.2695
REMARK 3 10 3.2445 - 3.1326 1.00 2585 141 0.2244 0.2753
REMARK 3 11 3.1326 - 3.0346 1.00 2610 131 0.2443 0.3121
REMARK 3 12 3.0346 - 2.9479 1.00 2580 136 0.2441 0.3366
REMARK 3 13 2.9479 - 2.8703 1.00 2586 131 0.2721 0.2935
REMARK 3 14 2.8703 - 2.8002 1.00 2551 149 0.3074 0.3499
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.650
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 62.71
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.012 8046
REMARK 3 ANGLE : 1.307 11035
REMARK 3 CHIRALITY : 0.062 1277
REMARK 3 PLANARITY : 0.008 1446
REMARK 3 DIHEDRAL : 10.067 4807
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' ((RESSEQ 4:186))
REMARK 3 ORIGIN FOR THE GROUP (A): 93.9377 99.2125 40.8226
REMARK 3 T TENSOR
REMARK 3 T11: 0.8591 T22: 0.7672
REMARK 3 T33: 0.5351 T12: 0.2971
REMARK 3 T13: 0.1172 T23: 0.0750
REMARK 3 L TENSOR
REMARK 3 L11: 3.8567 L22: 4.5482
REMARK 3 L33: 3.5451 L12: -0.8017
REMARK 3 L13: -1.3108 L23: -0.1419
REMARK 3 S TENSOR
REMARK 3 S11: 0.5925 S12: 0.7834 S13: 0.6788
REMARK 3 S21: -0.8903 S22: -0.2883 S23: 0.2757
REMARK 3 S31: -0.4327 S32: -0.5687 S33: -0.2709
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' ((RESSEQ 187:429))
REMARK 3 ORIGIN FOR THE GROUP (A): 88.8806 103.5162 66.6947
REMARK 3 T TENSOR
REMARK 3 T11: 0.3995 T22: 0.5177
REMARK 3 T33: 0.6928 T12: 0.0794
REMARK 3 T13: 0.0880 T23: 0.0538
REMARK 3 L TENSOR
REMARK 3 L11: 3.3736 L22: 3.9186
REMARK 3 L33: 6.3701 L12: -2.6250
REMARK 3 L13: -2.6761 L23: 2.5559
REMARK 3 S TENSOR
REMARK 3 S11: -0.0690 S12: -0.2620 S13: 0.3652
REMARK 3 S21: 0.2460 S22: 0.2201 S23: -0.1575
REMARK 3 S31: 0.2463 S32: 0.2842 S33: -0.1048
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' ((RESSEQ 445:857))
REMARK 3 ORIGIN FOR THE GROUP (A): 54.8539 135.8733 81.9713
REMARK 3 T TENSOR
REMARK 3 T11: 0.5428 T22: 0.4220
REMARK 3 T33: 0.2770 T12: 0.0656
REMARK 3 T13: -0.0047 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 1.9135 L22: 1.5268
REMARK 3 L33: 3.0722 L12: -0.0458
REMARK 3 L13: -0.1728 L23: -0.1170
REMARK 3 S TENSOR
REMARK 3 S11: -0.0103 S12: -0.1536 S13: 0.1768
REMARK 3 S21: 0.1054 S22: 0.1387 S23: 0.0774
REMARK 3 S31: -0.6665 S32: -0.3449 S33: -0.1461
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' ((RESSEQ 858:964))
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4293 107.9354 72.8648
REMARK 3 T TENSOR
REMARK 3 T11: 0.2988 T22: 0.3997
REMARK 3 T33: 0.3545 T12: -0.1018
REMARK 3 T13: -0.0354 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 5.6051 L22: 4.6337
REMARK 3 L33: 4.1977 L12: 0.8311
REMARK 3 L13: -1.1367 L23: -0.7417
REMARK 3 S TENSOR
REMARK 3 S11: 0.0387 S12: 0.1563 S13: -0.6751
REMARK 3 S21: -0.2362 S22: 0.0426 S23: -0.1060
REMARK 3 S31: 0.3312 S32: -0.3027 S33: -0.0606
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' ((RESSEQ 972:1045))
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0841 121.6814 58.0851
REMARK 3 T TENSOR
REMARK 3 T11: 0.5737 T22: 0.9378
REMARK 3 T33: 0.5305 T12: -0.1463
REMARK 3 T13: -0.1141 T23: 0.2305
REMARK 3 L TENSOR
REMARK 3 L11: 8.4011 L22: 7.7407
REMARK 3 L33: 3.0264 L12: -3.7664
REMARK 3 L13: 4.4635 L23: -1.0776
REMARK 3 S TENSOR
REMARK 3 S11: -0.0234 S12: 0.4373 S13: -0.6625
REMARK 3 S21: -0.9730 S22: 0.4342 S23: 1.2281
REMARK 3 S31: 0.3448 S32: -0.7312 S33: -0.4484
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' ((RESSEQ 430:444))
REMARK 3 ORIGIN FOR THE GROUP (A): 87.3846 126.1376 80.9348
REMARK 3 T TENSOR
REMARK 3 T11: 0.6257 T22: 0.9974
REMARK 3 T33: 1.0845 T12: -0.3419
REMARK 3 T13: -0.1087 T23: -0.2334
REMARK 3 L TENSOR
REMARK 3 L11: 0.6642 L22: 4.7844
REMARK 3 L33: 0.4710 L12: -1.1630
REMARK 3 L13: 0.1585 L23: -0.1079
REMARK 3 S TENSOR
REMARK 3 S11: -0.2256 S12: 0.2039 S13: 0.3642
REMARK 3 S21: 1.0664 S22: -0.2429 S23: -2.3178
REMARK 3 S31: -0.2964 S32: 0.5797 S33: 0.4440
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' ((RESSEQ 965:971))
REMARK 3 ORIGIN FOR THE GROUP (A): 32.0925 105.9074 56.6664
REMARK 3 T TENSOR
REMARK 3 T11: 1.3631 T22: 1.3613
REMARK 3 T33: 1.9198 T12: -0.7354
REMARK 3 T13: -0.5283 T23: 0.2522
REMARK 3 L TENSOR
REMARK 3 L11: 5.1293 L22: 3.3545
REMARK 3 L33: 3.5765 L12: -2.4658
REMARK 3 L13: 3.9324 L23: -2.8373
REMARK 3 S TENSOR
REMARK 3 S11: 1.7241 S12: -1.7290 S13: -3.1724
REMARK 3 S21: 1.9804 S22: -1.2982 S23: -0.4698
REMARK 3 S31: 0.8687 S32: 0.4832 S33: -0.4614
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 5T3D IS THE REPLACEMENT FOR 4ZXJ IN
REMARK 3 WHICH LIGAND WAS REFINED WITH INCORRECT STEREOCHEMISTRY. THE
REMARK 3 ONLY DIFFERENCE BETWEEN 5T3D AND 4ZXJ IS THAT STEREOCHEMISTRY OF
REMARK 3 THE LIGAND WAS CHANGED, FOLLOWED BY A SINGLE CYCLE OF REFINEMENT.
REMARK 4
REMARK 4 5T3D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000223610.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 113.15
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : M
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 0.3.8
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38818
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 60.427
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.63500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BTP PH 7.5, 125-150 MM MGCL2,
REMARK 280 AND 22-28% PEG 4000,, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.47000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 63.85550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 63.85550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.73500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 63.85550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 63.85550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 140.20500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 63.85550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.85550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 46.73500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 63.85550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.85550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 140.20500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 93.47000
REMARK 290
REMARK 290 REMARK: NULL
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 GLU A 1046
REMARK 465 ASP A 1047
REMARK 465 SER A 1048
REMARK 465 THR A 1049
REMARK 465 ARG A 1050
REMARK 465 ARG A 1051
REMARK 465 MET A 1052
REMARK 465 GLY A 1053
REMARK 465 PHE A 1054
REMARK 465 GLU A 1055
REMARK 465 THR A 1056
REMARK 465 ILE A 1057
REMARK 465 LEU A 1058
REMARK 465 PRO A 1059
REMARK 465 LEU A 1060
REMARK 465 ARG A 1061
REMARK 465 GLU A 1062
REMARK 465 GLY A 1063
REMARK 465 ASN A 1064
REMARK 465 GLY A 1065
REMARK 465 PRO A 1066
REMARK 465 THR A 1067
REMARK 465 LEU A 1068
REMARK 465 PHE A 1069
REMARK 465 CYS A 1070
REMARK 465 PHE A 1071
REMARK 465 HIS A 1072
REMARK 465 PRO A 1073
REMARK 465 ALA A 1074
REMARK 465 SER A 1075
REMARK 465 GLY A 1076
REMARK 465 PHE A 1077
REMARK 465 ALA A 1078
REMARK 465 TRP A 1079
REMARK 465 GLN A 1080
REMARK 465 PHE A 1081
REMARK 465 SER A 1082
REMARK 465 VAL A 1083
REMARK 465 LEU A 1084
REMARK 465 SER A 1085
REMARK 465 ARG A 1086
REMARK 465 TYR A 1087
REMARK 465 LEU A 1088
REMARK 465 ASP A 1089
REMARK 465 PRO A 1090
REMARK 465 GLN A 1091
REMARK 465 TRP A 1092
REMARK 465 SER A 1093
REMARK 465 ILE A 1094
REMARK 465 ILE A 1095
REMARK 465 GLY A 1096
REMARK 465 ILE A 1097
REMARK 465 GLN A 1098
REMARK 465 SER A 1099
REMARK 465 PRO A 1100
REMARK 465 ARG A 1101
REMARK 465 PRO A 1102
REMARK 465 ASN A 1103
REMARK 465 GLY A 1104
REMARK 465 PRO A 1105
REMARK 465 MET A 1106
REMARK 465 GLN A 1107
REMARK 465 THR A 1108
REMARK 465 ALA A 1109
REMARK 465 ALA A 1110
REMARK 465 ASN A 1111
REMARK 465 LEU A 1112
REMARK 465 ASP A 1113
REMARK 465 GLU A 1114
REMARK 465 VAL A 1115
REMARK 465 CYS A 1116
REMARK 465 GLU A 1117
REMARK 465 ALA A 1118
REMARK 465 HIS A 1119
REMARK 465 LEU A 1120
REMARK 465 ALA A 1121
REMARK 465 THR A 1122
REMARK 465 LEU A 1123
REMARK 465 LEU A 1124
REMARK 465 GLU A 1125
REMARK 465 GLN A 1126
REMARK 465 GLN A 1127
REMARK 465 PRO A 1128
REMARK 465 HIS A 1129
REMARK 465 GLY A 1130
REMARK 465 PRO A 1131
REMARK 465 TYR A 1132
REMARK 465 TYR A 1133
REMARK 465 LEU A 1134
REMARK 465 LEU A 1135
REMARK 465 GLY A 1136
REMARK 465 TYR A 1137
REMARK 465 SER A 1138
REMARK 465 LEU A 1139
REMARK 465 GLY A 1140
REMARK 465 GLY A 1141
REMARK 465 THR A 1142
REMARK 465 LEU A 1143
REMARK 465 ALA A 1144
REMARK 465 GLN A 1145
REMARK 465 GLY A 1146
REMARK 465 ILE A 1147
REMARK 465 ALA A 1148
REMARK 465 ALA A 1149
REMARK 465 ARG A 1150
REMARK 465 LEU A 1151
REMARK 465 ARG A 1152
REMARK 465 ALA A 1153
REMARK 465 ARG A 1154
REMARK 465 GLY A 1155
REMARK 465 GLU A 1156
REMARK 465 GLN A 1157
REMARK 465 VAL A 1158
REMARK 465 ALA A 1159
REMARK 465 PHE A 1160
REMARK 465 LEU A 1161
REMARK 465 GLY A 1162
REMARK 465 LEU A 1163
REMARK 465 LEU A 1164
REMARK 465 ASP A 1165
REMARK 465 THR A 1166
REMARK 465 TRP A 1167
REMARK 465 PRO A 1168
REMARK 465 PRO A 1169
REMARK 465 GLU A 1170
REMARK 465 THR A 1171
REMARK 465 GLN A 1172
REMARK 465 ASN A 1173
REMARK 465 TRP A 1174
REMARK 465 GLN A 1175
REMARK 465 GLU A 1176
REMARK 465 LYS A 1177
REMARK 465 GLU A 1178
REMARK 465 ALA A 1179
REMARK 465 ASN A 1180
REMARK 465 GLY A 1181
REMARK 465 LEU A 1182
REMARK 465 ASP A 1183
REMARK 465 PRO A 1184
REMARK 465 GLU A 1185
REMARK 465 VAL A 1186
REMARK 465 LEU A 1187
REMARK 465 ALA A 1188
REMARK 465 GLU A 1189
REMARK 465 ILE A 1190
REMARK 465 ASN A 1191
REMARK 465 ARG A 1192
REMARK 465 GLU A 1193
REMARK 465 ARG A 1194
REMARK 465 GLU A 1195
REMARK 465 ALA A 1196
REMARK 465 PHE A 1197
REMARK 465 LEU A 1198
REMARK 465 ALA A 1199
REMARK 465 ALA A 1200
REMARK 465 GLN A 1201
REMARK 465 GLN A 1202
REMARK 465 GLY A 1203
REMARK 465 SER A 1204
REMARK 465 THR A 1205
REMARK 465 SER A 1206
REMARK 465 THR A 1207
REMARK 465 GLU A 1208
REMARK 465 LEU A 1209
REMARK 465 PHE A 1210
REMARK 465 THR A 1211
REMARK 465 THR A 1212
REMARK 465 ILE A 1213
REMARK 465 GLU A 1214
REMARK 465 GLY A 1215
REMARK 465 ASN A 1216
REMARK 465 TYR A 1217
REMARK 465 ALA A 1218
REMARK 465 ASP A 1219
REMARK 465 ALA A 1220
REMARK 465 VAL A 1221
REMARK 465 ARG A 1222
REMARK 465 LEU A 1223
REMARK 465 LEU A 1224
REMARK 465 THR A 1225
REMARK 465 THR A 1226
REMARK 465 ALA A 1227
REMARK 465 HIS A 1228
REMARK 465 SER A 1229
REMARK 465 VAL A 1230
REMARK 465 PRO A 1231
REMARK 465 PHE A 1232
REMARK 465 ASP A 1233
REMARK 465 GLY A 1234
REMARK 465 LYS A 1235
REMARK 465 ALA A 1236
REMARK 465 THR A 1237
REMARK 465 LEU A 1238
REMARK 465 PHE A 1239
REMARK 465 VAL A 1240
REMARK 465 ALA A 1241
REMARK 465 GLU A 1242
REMARK 465 ARG A 1243
REMARK 465 THR A 1244
REMARK 465 LEU A 1245
REMARK 465 GLN A 1246
REMARK 465 GLU A 1247
REMARK 465 GLY A 1248
REMARK 465 MET A 1249
REMARK 465 SER A 1250
REMARK 465 PRO A 1251
REMARK 465 GLU A 1252
REMARK 465 ARG A 1253
REMARK 465 ALA A 1254
REMARK 465 TRP A 1255
REMARK 465 SER A 1256
REMARK 465 PRO A 1257
REMARK 465 TRP A 1258
REMARK 465 ILE A 1259
REMARK 465 ALA A 1260
REMARK 465 GLU A 1261
REMARK 465 LEU A 1262
REMARK 465 ASP A 1263
REMARK 465 ILE A 1264
REMARK 465 TYR A 1265
REMARK 465 ARG A 1266
REMARK 465 GLN A 1267
REMARK 465 ASP A 1268
REMARK 465 CYS A 1269
REMARK 465 ALA A 1270
REMARK 465 HIS A 1271
REMARK 465 VAL A 1272
REMARK 465 ASP A 1273
REMARK 465 ILE A 1274
REMARK 465 ILE A 1275
REMARK 465 SER A 1276
REMARK 465 PRO A 1277
REMARK 465 GLY A 1278
REMARK 465 THR A 1279
REMARK 465 PHE A 1280
REMARK 465 GLU A 1281
REMARK 465 LYS A 1282
REMARK 465 ILE A 1283
REMARK 465 GLY A 1284
REMARK 465 PRO A 1285
REMARK 465 ILE A 1286
REMARK 465 ILE A 1287
REMARK 465 ARG A 1288
REMARK 465 ALA A 1289
REMARK 465 THR A 1290
REMARK 465 LEU A 1291
REMARK 465 ASN A 1292
REMARK 465 ARG A 1293
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 HIS A 4 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 5 CG CD1 CD2
REMARK 470 LEU A 7 CG CD1 CD2
REMARK 470 LYS A 19 CG CD CE NZ
REMARK 470 GLU A 22 CG CD OE1 OE2
REMARK 470 GLU A 38 CG CD OE1 OE2
REMARK 470 ARG A 46 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 61 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 65 CG OD1 OD2
REMARK 470 ASN A 66 CG OD1 ND2
REMARK 470 THR A 78 OG1 CG2
REMARK 470 ASP A 86 CG OD1 OD2
REMARK 470 LEU A 87 CG CD1 CD2
REMARK 470 THR A 89 OG1 CG2
REMARK 470 ASN A 90 CG OD1 ND2
REMARK 470 ASP A 92 CG OD1 OD2
REMARK 470 HIS A 94 CG ND1 CD2 CE1 NE2
REMARK 470 LEU A 100 CG CD1 CD2
REMARK 470 GLN A 102 CG CD OE1 NE2
REMARK 470 LYS A 115 CG CD CE NZ
REMARK 470 GLN A 124 CG CD OE1 NE2
REMARK 470 VAL A 125 CG1 CG2
REMARK 470 ASP A 127 CG OD1 OD2
REMARK 470 ASN A 128 CG OD1 ND2
REMARK 470 ARG A 129 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 182 CG CD OE1 NE2
REMARK 470 GLN A 183 CG CD OE1 NE2
REMARK 470 GLU A 186 CG CD OE1 OE2
REMARK 470 GLU A 188 CG CD OE1 OE2
REMARK 470 ARG A 192 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 202 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 228 CG CD CE NZ
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 GLU A 235 CG CD OE1 OE2
REMARK 470 ARG A 237 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 238 CG CD OE1 NE2
REMARK 470 LEU A 243 CG CD1 CD2
REMARK 470 VAL A 246 CG1 CG2
REMARK 470 GLN A 247 CG CD OE1 NE2
REMARK 470 ARG A 248 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 251 CG CD1 CD2
REMARK 470 LYS A 318 CG CD CE NZ
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 ARG A 322 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 337 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 341 CG OD1 OD2
REMARK 470 GLU A 342 CG CD OE1 OE2
REMARK 470 LYS A 352 CG CD CE NZ
REMARK 470 PHE A 354 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A 355 CG OD1 OD2
REMARK 470 LYS A 398 CG CD CE NZ
REMARK 470 GLU A 411 CG CD OE1 OE2
REMARK 470 GLU A 636 CG CD OE1 OE2
REMARK 470 LYS A 717 CG CD CE NZ
REMARK 470 LYS A 956 CG CD CE NZ
REMARK 470 LYS A 964 CG CD CE NZ
REMARK 470 GLN A 966 CG CD OE1 NE2
REMARK 470 LYS A 973 CG CD CE NZ
REMARK 470 ARG A1022 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1045 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP A 506 O HOH A 1401 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 721 CB CYS A 721 SG -0.122
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 9 -114.45 55.48
REMARK 500 SER A 25 43.22 -150.85
REMARK 500 LEU A 87 83.87 -55.31
REMARK 500 ARG A 88 -90.92 -130.20
REMARK 500 ASN A 90 -117.63 -134.77
REMARK 500 GLN A 124 -58.93 -166.76
REMARK 500 ALA A 126 22.71 175.64
REMARK 500 ASP A 127 44.75 -66.61
REMARK 500 ASN A 128 19.72 50.13
REMARK 500 GLU A 186 69.53 -104.33
REMARK 500 GLN A 247 45.72 -96.20
REMARK 500 ARG A 248 -63.88 60.54
REMARK 500 ALA A 339 89.55 57.72
REMARK 500 VAL A 353 158.79 -45.10
REMARK 500 ASP A 359 61.16 -111.58
REMARK 500 ASP A 377 -81.75 -134.69
REMARK 500 THR A 537 -5.10 -58.57
REMARK 500 LEU A 555 132.89 -171.22
REMARK 500 ASN A 578 17.61 -155.63
REMARK 500 GLN A 584 55.16 -151.13
REMARK 500 VAL A 753 -56.57 79.90
REMARK 500 LEU A 814 109.51 -48.22
REMARK 500 ALA A 830 79.37 -159.95
REMARK 500 ASP A 857 -159.88 -138.98
REMARK 500 ASP A 954 76.46 -113.96
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 GLY A 635 GLU A 636 141.17
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 75C A 1301
DBREF 5T3D A 1 1293 UNP P11454 ENTF_ECOLI 1 1293
SEQADV 5T3D GLY A -1 UNP P11454 EXPRESSION TAG
SEQADV 5T3D HIS A 0 UNP P11454 EXPRESSION TAG
SEQRES 1 A 1295 GLY HIS MET SER GLN HIS LEU PRO LEU VAL ALA ALA GLN
SEQRES 2 A 1295 PRO GLY ILE TRP MET ALA GLU LYS LEU SER GLU LEU PRO
SEQRES 3 A 1295 SER ALA TRP SER VAL ALA HIS TYR VAL GLU LEU THR GLY
SEQRES 4 A 1295 GLU VAL ASP SER PRO LEU LEU ALA ARG ALA VAL VAL ALA
SEQRES 5 A 1295 GLY LEU ALA GLN ALA ASP THR LEU ARG MET ARG PHE THR
SEQRES 6 A 1295 GLU ASP ASN GLY GLU VAL TRP GLN TRP VAL ASP ASP ALA
SEQRES 7 A 1295 LEU THR PHE GLU LEU PRO GLU ILE ILE ASP LEU ARG THR
SEQRES 8 A 1295 ASN ILE ASP PRO HIS GLY THR ALA GLN ALA LEU MET GLN
SEQRES 9 A 1295 ALA ASP LEU GLN GLN ASP LEU ARG VAL ASP SER GLY LYS
SEQRES 10 A 1295 PRO LEU VAL PHE HIS GLN LEU ILE GLN VAL ALA ASP ASN
SEQRES 11 A 1295 ARG TRP TYR TRP TYR GLN ARG TYR HIS HIS LEU LEU VAL
SEQRES 12 A 1295 ASP GLY PHE SER PHE PRO ALA ILE THR ARG GLN ILE ALA
SEQRES 13 A 1295 ASN ILE TYR CYS THR TRP LEU ARG GLY GLU PRO THR PRO
SEQRES 14 A 1295 ALA SER PRO PHE THR PRO PHE ALA ASP VAL VAL GLU GLU
SEQRES 15 A 1295 TYR GLN GLN TYR ARG GLU SER GLU ALA TRP GLN ARG ASP
SEQRES 16 A 1295 ALA ALA PHE TRP ALA GLU GLN ARG ARG GLN LEU PRO PRO
SEQRES 17 A 1295 PRO ALA SER LEU SER PRO ALA PRO LEU PRO GLY ARG SER
SEQRES 18 A 1295 ALA SER ALA ASP ILE LEU ARG LEU LYS LEU GLU PHE THR
SEQRES 19 A 1295 ASP GLY GLU PHE ARG GLN LEU ALA THR GLN LEU SER GLY
SEQRES 20 A 1295 VAL GLN ARG THR ASP LEU ALA LEU ALA LEU ALA ALA LEU
SEQRES 21 A 1295 TRP LEU GLY ARG LEU CYS ASN ARG MET ASP TYR ALA ALA
SEQRES 22 A 1295 GLY PHE ILE PHE MET ARG ARG LEU GLY SER ALA ALA LEU
SEQRES 23 A 1295 THR ALA THR GLY PRO VAL LEU ASN VAL LEU PRO LEU GLY
SEQRES 24 A 1295 ILE HIS ILE ALA ALA GLN GLU THR LEU PRO GLU LEU ALA
SEQRES 25 A 1295 THR ARG LEU ALA ALA GLN LEU LYS LYS MET ARG ARG HIS
SEQRES 26 A 1295 GLN ARG TYR ASP ALA GLU GLN ILE VAL ARG ASP SER GLY
SEQRES 27 A 1295 ARG ALA ALA GLY ASP GLU PRO LEU PHE GLY PRO VAL LEU
SEQRES 28 A 1295 ASN ILE LYS VAL PHE ASP TYR GLN LEU ASP ILE PRO ASP
SEQRES 29 A 1295 VAL GLN ALA GLN THR HIS THR LEU ALA THR GLY PRO VAL
SEQRES 30 A 1295 ASN ASP LEU GLU LEU ALA LEU PHE PRO ASP VAL HIS GLY
SEQRES 31 A 1295 ASP LEU SER ILE GLU ILE LEU ALA ASN LYS GLN ARG TYR
SEQRES 32 A 1295 ASP GLU PRO THR LEU ILE GLN HIS ALA GLU ARG LEU LYS
SEQRES 33 A 1295 MET LEU ILE ALA GLN PHE ALA ALA ASP PRO ALA LEU LEU
SEQRES 34 A 1295 CYS GLY ASP VAL ASP ILE MET LEU PRO GLY GLU TYR ALA
SEQRES 35 A 1295 GLN LEU ALA GLN LEU ASN ALA THR GLN VAL GLU ILE PRO
SEQRES 36 A 1295 GLU THR THR LEU SER ALA LEU VAL ALA GLU GLN ALA ALA
SEQRES 37 A 1295 LYS THR PRO ASP ALA PRO ALA LEU ALA ASP ALA ARG TYR
SEQRES 38 A 1295 LEU PHE SER TYR ARG GLU MET ARG GLU GLN VAL VAL ALA
SEQRES 39 A 1295 LEU ALA ASN LEU LEU ARG GLU ARG GLY VAL LYS PRO GLY
SEQRES 40 A 1295 ASP SER VAL ALA VAL ALA LEU PRO ARG SER VAL PHE LEU
SEQRES 41 A 1295 THR LEU ALA LEU HIS ALA ILE VAL GLU ALA GLY ALA ALA
SEQRES 42 A 1295 TRP LEU PRO LEU ASP THR GLY TYR PRO ASP ASP ARG LEU
SEQRES 43 A 1295 LYS MET MET LEU GLU ASP ALA ARG PRO SER LEU LEU ILE
SEQRES 44 A 1295 THR THR ASP ASP GLN LEU PRO ARG PHE SER ASP VAL PRO
SEQRES 45 A 1295 ASN LEU THR SER LEU CYS TYR ASN ALA PRO LEU THR PRO
SEQRES 46 A 1295 GLN GLY SER ALA PRO LEU GLN LEU SER GLN PRO HIS HIS
SEQRES 47 A 1295 THR ALA TYR ILE ILE PHE THR SER GLY SER THR GLY ARG
SEQRES 48 A 1295 PRO LYS GLY VAL MET VAL GLY GLN THR ALA ILE VAL ASN
SEQRES 49 A 1295 ARG LEU LEU TRP MET GLN ASN HIS TYR PRO LEU THR GLY
SEQRES 50 A 1295 GLU ASP VAL VAL ALA GLN LYS THR PRO CYS SER PHE ASP
SEQRES 51 A 1295 VAL SER VAL TRP GLU PHE PHE TRP PRO PHE ILE ALA GLY
SEQRES 52 A 1295 ALA LYS LEU VAL MET ALA GLU PRO GLU ALA HIS ARG ASP
SEQRES 53 A 1295 PRO LEU ALA MET GLN GLN PHE PHE ALA GLU TYR GLY VAL
SEQRES 54 A 1295 THR THR THR HIS PHE VAL PRO SER MET LEU ALA ALA PHE
SEQRES 55 A 1295 VAL ALA SER LEU THR PRO GLN THR ALA ARG GLN SER CYS
SEQRES 56 A 1295 ALA THR LEU LYS GLN VAL PHE CYS SER GLY GLU ALA LEU
SEQRES 57 A 1295 PRO ALA ASP LEU CYS ARG GLU TRP GLN GLN LEU THR GLY
SEQRES 58 A 1295 ALA PRO LEU HIS ASN LEU TYR GLY PRO THR GLU ALA ALA
SEQRES 59 A 1295 VAL ASP VAL SER TRP TYR PRO ALA PHE GLY GLU GLU LEU
SEQRES 60 A 1295 ALA GLN VAL ARG GLY SER SER VAL PRO ILE GLY TYR PRO
SEQRES 61 A 1295 VAL TRP ASN THR GLY LEU ARG ILE LEU ASP ALA MET MET
SEQRES 62 A 1295 HIS PRO VAL PRO PRO GLY VAL ALA GLY ASP LEU TYR LEU
SEQRES 63 A 1295 THR GLY ILE GLN LEU ALA GLN GLY TYR LEU GLY ARG PRO
SEQRES 64 A 1295 ASP LEU THR ALA SER ARG PHE ILE ALA ASP PRO PHE ALA
SEQRES 65 A 1295 PRO GLY GLU ARG MET TYR ARG THR GLY ASP VAL ALA ARG
SEQRES 66 A 1295 TRP LEU ASP ASN GLY ALA VAL GLU TYR LEU GLY ARG SER
SEQRES 67 A 1295 ASP ASP GLN LEU LYS ILE ARG GLY GLN ARG ILE GLU LEU
SEQRES 68 A 1295 GLY GLU ILE ASP ARG VAL MET GLN ALA LEU PRO ASP VAL
SEQRES 69 A 1295 GLU GLN ALA VAL THR HIS ALA CYS VAL ILE ASN GLN ALA
SEQRES 70 A 1295 ALA ALA THR GLY GLY ASP ALA ARG GLN LEU VAL GLY TYR
SEQRES 71 A 1295 LEU VAL SER GLN SER GLY LEU PRO LEU ASP THR SER ALA
SEQRES 72 A 1295 LEU GLN ALA GLN LEU ARG GLU THR LEU PRO PRO HIS MET
SEQRES 73 A 1295 VAL PRO VAL VAL LEU LEU GLN LEU PRO GLN LEU PRO LEU
SEQRES 74 A 1295 SER ALA ASN GLY LYS LEU ASP ARG LYS ALA LEU PRO LEU
SEQRES 75 A 1295 PRO GLU LEU LYS ALA GLN ALA PRO GLY ARG ALA PRO LYS
SEQRES 76 A 1295 ALA GLY SER GLU THR ILE ILE ALA ALA ALA PHE SER SER
SEQRES 77 A 1295 LEU LEU GLY CYS ASP VAL GLN ASP ALA ASP ALA ASP PHE
SEQRES 78 A 1295 PHE ALA LEU GLY GLY HIS SER LEU LEU ALA MET LYS LEU
SEQRES 79 A 1295 ALA ALA GLN LEU SER ARG GLN VAL ALA ARG GLN VAL THR
SEQRES 80 A 1295 PRO GLY GLN VAL MET VAL ALA SER THR VAL ALA LYS LEU
SEQRES 81 A 1295 ALA THR ILE ILE ASP ALA GLU GLU ASP SER THR ARG ARG
SEQRES 82 A 1295 MET GLY PHE GLU THR ILE LEU PRO LEU ARG GLU GLY ASN
SEQRES 83 A 1295 GLY PRO THR LEU PHE CYS PHE HIS PRO ALA SER GLY PHE
SEQRES 84 A 1295 ALA TRP GLN PHE SER VAL LEU SER ARG TYR LEU ASP PRO
SEQRES 85 A 1295 GLN TRP SER ILE ILE GLY ILE GLN SER PRO ARG PRO ASN
SEQRES 86 A 1295 GLY PRO MET GLN THR ALA ALA ASN LEU ASP GLU VAL CYS
SEQRES 87 A 1295 GLU ALA HIS LEU ALA THR LEU LEU GLU GLN GLN PRO HIS
SEQRES 88 A 1295 GLY PRO TYR TYR LEU LEU GLY TYR SER LEU GLY GLY THR
SEQRES 89 A 1295 LEU ALA GLN GLY ILE ALA ALA ARG LEU ARG ALA ARG GLY
SEQRES 90 A 1295 GLU GLN VAL ALA PHE LEU GLY LEU LEU ASP THR TRP PRO
SEQRES 91 A 1295 PRO GLU THR GLN ASN TRP GLN GLU LYS GLU ALA ASN GLY
SEQRES 92 A 1295 LEU ASP PRO GLU VAL LEU ALA GLU ILE ASN ARG GLU ARG
SEQRES 93 A 1295 GLU ALA PHE LEU ALA ALA GLN GLN GLY SER THR SER THR
SEQRES 94 A 1295 GLU LEU PHE THR THR ILE GLU GLY ASN TYR ALA ASP ALA
SEQRES 95 A 1295 VAL ARG LEU LEU THR THR ALA HIS SER VAL PRO PHE ASP
SEQRES 96 A 1295 GLY LYS ALA THR LEU PHE VAL ALA GLU ARG THR LEU GLN
SEQRES 97 A 1295 GLU GLY MET SER PRO GLU ARG ALA TRP SER PRO TRP ILE
SEQRES 98 A 1295 ALA GLU LEU ASP ILE TYR ARG GLN ASP CYS ALA HIS VAL
SEQRES 99 A 1295 ASP ILE ILE SER PRO GLY THR PHE GLU LYS ILE GLY PRO
SEQRES 100 A 1295 ILE ILE ARG ALA THR LEU ASN ARG
HET 75C A1301 49
HETNAM 75C 5'-({[(2R,3S)-3-AMINO-4-HYDROXY-2-{[2-({N-[(2R)-2-
HETNAM 2 75C HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)BUTANOYL]-BETA-
HETNAM 3 75C ALANYL}AMINO)ETHYL]SULFANYL}BUTYL]SULFONYL}AMINO)-5'-
HETNAM 4 75C DEOXYADENOSINE
FORMUL 2 75C C25 H44 N9 O13 P S2
FORMUL 3 HOH *13(H2 O)
HELIX 1 AA1 ALA A 10 SER A 21 1 12
HELIX 2 AA2 ASP A 40 ALA A 55 1 16
HELIX 3 AA3 ASP A 56 LEU A 58 5 3
HELIX 4 AA4 HIS A 94 LEU A 105 1 12
HELIX 5 AA5 ARG A 110 GLY A 114 5 5
HELIX 6 AA6 SER A 145 ARG A 162 1 18
HELIX 7 AA7 PRO A 173 GLU A 186 1 14
HELIX 8 AA8 SER A 187 LEU A 204 1 18
HELIX 9 AA9 GLY A 234 SER A 244 1 11
HELIX 10 AB1 ARG A 248 ASN A 265 1 18
HELIX 11 AB2 SER A 281 ALA A 286 5 6
HELIX 12 AB3 THR A 305 HIS A 323 1 19
HELIX 13 AB4 ASP A 327 SER A 335 1 9
HELIX 14 AB5 ASP A 402 ASP A 423 1 22
HELIX 15 AB6 LEU A 427 VAL A 431 5 5
HELIX 16 AB7 GLY A 437 ASN A 446 1 10
HELIX 17 AB8 THR A 456 THR A 468 1 13
HELIX 18 AB9 TYR A 483 ARG A 500 1 18
HELIX 19 AC1 SER A 515 ALA A 528 1 14
HELIX 20 AC2 PRO A 540 ARG A 552 1 13
HELIX 21 AC3 PRO A 564 VAL A 569 5 6
HELIX 22 AC4 GLN A 617 TYR A 631 1 15
HELIX 23 AC5 VAL A 649 GLY A 661 1 13
HELIX 24 AC6 GLU A 670 ARG A 673 5 4
HELIX 25 AC7 ASP A 674 TYR A 685 1 12
HELIX 26 AC8 VAL A 693 SER A 703 1 11
HELIX 27 AC9 THR A 705 CYS A 713 1 9
HELIX 28 AD1 PRO A 727 GLY A 739 1 13
HELIX 29 AD2 PHE A 761 GLN A 767 1 7
HELIX 30 AD3 ARG A 816 ARG A 823 1 8
HELIX 31 AD4 LEU A 869 ALA A 878 1 10
HELIX 32 AD5 ASN A 893 ALA A 897 5 5
HELIX 33 AD6 ASP A 918 LEU A 930 1 13
HELIX 34 AD7 PRO A 931 VAL A 935 5 5
HELIX 35 AD8 ASP A 954 LEU A 958 5 5
HELIX 36 AD9 GLY A 975 GLY A 989 1 15
HELIX 37 AE1 HIS A 1005 VAL A 1020 1 16
HELIX 38 AE2 THR A 1025 ALA A 1032 1 8
HELIX 39 AE3 THR A 1034 ALA A 1044 1 11
SHEET 1 AA1 3 LEU A 5 PRO A 6 0
SHEET 2 AA1 3 GLU A 68 VAL A 73 -1 O GLN A 71 N LEU A 5
SHEET 3 AA1 3 MET A 60 ASP A 65 -1 N ARG A 61 O TRP A 72
SHEET 1 AA2 5 GLU A 83 ILE A 85 0
SHEET 2 AA2 5 VAL A 118 ILE A 123 1 O LEU A 122 N ILE A 85
SHEET 3 AA2 5 TRP A 130 HIS A 137 -1 O TYR A 131 N ILE A 123
SHEET 4 AA2 5 SER A 28 LEU A 35 -1 N LEU A 35 O TRP A 130
SHEET 5 AA2 5 THR A 367 ALA A 371 -1 O HIS A 368 N TYR A 32
SHEET 1 AA3 6 ILE A 224 PHE A 231 0
SHEET 2 AA3 6 LEU A 390 ASN A 397 -1 O LEU A 390 N PHE A 231
SHEET 3 AA3 6 LEU A 378 PRO A 384 -1 N GLU A 379 O LEU A 395
SHEET 4 AA3 6 PRO A 347 ASN A 350 1 N ASN A 350 O LEU A 382
SHEET 5 AA3 6 ASP A 268 PHE A 275 1 N GLY A 272 O LEU A 349
SHEET 6 AA3 6 ASN A 292 HIS A 299 -1 O LEU A 296 N ALA A 271
SHEET 1 AA4 4 LEU A 480 SER A 482 0
SHEET 2 AA4 4 PRO A 472 ALA A 475 -1 N ALA A 473 O PHE A 481
SHEET 3 AA4 4 LYS A 663 MET A 666 1 O LEU A 664 N ALA A 475
SHEET 4 AA4 4 VAL A 638 GLN A 641 1 N VAL A 639 O LYS A 663
SHEET 1 AA5 4 ALA A 531 PRO A 534 0
SHEET 2 AA5 4 SER A 507 VAL A 510 1 N VAL A 510 O LEU A 533
SHEET 3 AA5 4 LEU A 555 THR A 558 1 O ILE A 557 N ALA A 509
SHEET 4 AA5 4 SER A 574 CYS A 576 1 O LEU A 575 N THR A 558
SHEET 1 AA6 3 THR A 597 THR A 603 0
SHEET 2 AA6 3 LYS A 611 GLY A 616 -1 O VAL A 615 N ALA A 598
SHEET 3 AA6 3 GLY A 812 TYR A 813 -1 O GLY A 812 N MET A 614
SHEET 1 AA7 5 THR A 689 PHE A 692 0
SHEET 2 AA7 5 GLN A 718 SER A 722 1 O PHE A 720 N THR A 690
SHEET 3 AA7 5 LEU A 742 TYR A 746 1 O LEU A 745 N CYS A 721
SHEET 4 AA7 5 SER A 756 PRO A 759 -1 O TYR A 758 N ASN A 744
SHEET 5 AA7 5 TYR A 777 PRO A 778 -1 O TYR A 777 N TRP A 757
SHEET 1 AA8 4 THR A 782 LEU A 787 0
SHEET 2 AA8 4 GLY A 800 GLY A 806 -1 O TYR A 803 N ARG A 785
SHEET 3 AA8 4 ARG A 834 TRP A 844 -1 O TYR A 836 N LEU A 804
SHEET 4 AA8 4 PHE A 824 ALA A 826 -1 N ILE A 825 O MET A 835
SHEET 1 AA9 4 THR A 782 LEU A 787 0
SHEET 2 AA9 4 GLY A 800 GLY A 806 -1 O TYR A 803 N ARG A 785
SHEET 3 AA9 4 ARG A 834 TRP A 844 -1 O TYR A 836 N LEU A 804
SHEET 4 AA9 4 VAL A 850 ARG A 855 -1 O GLU A 851 N ARG A 843
SHEET 1 AB1 2 GLN A 859 ILE A 862 0
SHEET 2 AB1 2 GLN A 865 GLU A 868 -1 O ILE A 867 N LEU A 860
SHEET 1 AB2 3 VAL A 882 CYS A 890 0
SHEET 2 AB2 3 GLN A 904 SER A 911 -1 O VAL A 906 N HIS A 888
SHEET 3 AB2 3 VAL A 938 GLN A 941 1 O LEU A 940 N GLY A 907
LINK OG SER A1006 P1 75C A1301 1555 1555 1.57
CISPEP 1 GLN A 124 VAL A 125 0 3.60
SITE 1 AC1 26 PHE A 647 ASP A 648 VAL A 649 ARG A 673
SITE 2 AC1 26 VAL A 693 SER A 722 GLY A 723 GLU A 724
SITE 3 AC1 26 ALA A 725 ASN A 744 LEU A 745 TYR A 746
SITE 4 AC1 26 GLY A 747 PRO A 748 THR A 749 VAL A 753
SITE 5 AC1 26 ASP A 754 ILE A 775 ASP A 840 TYR A 852
SITE 6 AC1 26 LYS A 861 ARG A 863 GLY A 864 GLN A 865
SITE 7 AC1 26 ARG A 866 SER A1006
CRYST1 127.711 127.711 186.940 90.00 90.00 90.00 P 41 21 2 8
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 0.007830 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007830 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005349 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
