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HEADER LIGASE 11-APR-16 5JA1
TITLE ENTF, A TERMINAL NONRIBOSOMAL PEPTIDE SYNTHETASE MODULE BOUND TO THE
TITLE 2 MBTH-LIKE PROTEIN YBDZ
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;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ENTEROBACTIN BIOSYNTHESIS PROTEIN YBDZ;
COMPND 10 CHAIN: B;
COMPND 11 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 VARIANT: W3110;
SOURCE 6 GENE: ENTF, B0586, JW0578;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMIS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 14 ORGANISM_TAXID: 83333;
SOURCE 15 STRAIN: K12;
SOURCE 16 VARIANT: W3110;
SOURCE 17 GENE: YBDZ, B4511, JW0577;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS NONRIBOSOMAL PEPTIDE SYNTHETASE, NRPS, CONDENSATION, ADENYLATION,
KEYWDS 2 PCP, THIOESTERASE, MBTH-LIKE PROTEIN, PHOSPHOPANTETHEINE,
KEYWDS 3 BIOSYNTHETIC PROTEIN, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.R.MILLER,A.M.GULICK
REVDAT 1 14-SEP-16 5JA1 0
JRNL AUTH B.R.MILLER,E.J.DRAKE,C.SHI,C.C.ALDRICH,A.M.GULICK
JRNL TITL STRUCTURES OF A NONRIBOSOMAL PEPTIDE SYNTHETASE MODULE BOUND
JRNL TITL 2 TO MBTH-LIKE PROTEINS SUPPORT A HIGHLY DYNAMIC DOMAIN
JRNL TITL 3 ARCHITECTURE.
JRNL REF J.BIOL.CHEM. 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 27597544
JRNL DOI 10.1074/JBC.M116.746297
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH E.J.DRAKE,B.R.MILLER,C.SHI,J.T.TARRASCH,J.A.SUNDLOV,
REMARK 1 AUTH 2 C.L.ALLEN,G.SKINIOTIS,C.C.ALDRICH,A.M.GULICK
REMARK 1 TITL STRUCTURES OF TWO DISTINCT CONFORMATIONS OF
REMARK 1 TITL 2 HOLO-NON-RIBOSOMAL PEPTIDE SYNTHETASES.
REMARK 1 REF NATURE V. 529 235 2016
REMARK 1 REFN ESSN 1476-4687
REMARK 1 PMID 26762461
REMARK 1 DOI 10.1038/NATURE16163
REMARK 2
REMARK 2 RESOLUTION. 3.00 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 31768
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 : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1585
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 56.3175 - 6.6687 0.89 2755 133 0.1664 0.1719
REMARK 3 2 6.6687 - 5.2944 0.92 2732 137 0.1836 0.2276
REMARK 3 3 5.2944 - 4.6255 0.92 2717 146 0.1432 0.1896
REMARK 3 4 4.6255 - 4.2028 0.93 2743 144 0.1471 0.1705
REMARK 3 5 4.2028 - 3.9016 0.94 2750 146 0.1703 0.2230
REMARK 3 6 3.9016 - 3.6716 0.94 2717 155 0.1898 0.2515
REMARK 3 7 3.6716 - 3.4878 0.94 2774 156 0.1909 0.2573
REMARK 3 8 3.4878 - 3.3360 0.94 2723 155 0.2114 0.3056
REMARK 3 9 3.3360 - 3.2076 0.95 2760 139 0.2290 0.3214
REMARK 3 10 3.2076 - 3.0969 0.95 2809 121 0.2427 0.2909
REMARK 3 11 3.0969 - 3.0001 0.94 2703 153 0.2567 0.3189
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.620
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.38
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 : 0.002 10094
REMARK 3 ANGLE : 0.567 13837
REMARK 3 CHIRALITY : 0.041 1589
REMARK 3 PLANARITY : 0.004 1809
REMARK 3 DIHEDRAL : 10.763 5993
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 21:186 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.2154 43.4097 33.2935
REMARK 3 T TENSOR
REMARK 3 T11: 0.1938 T22: 0.1707
REMARK 3 T33: 0.2405 T12: -0.0403
REMARK 3 T13: -0.0634 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 2.2018 L22: 2.5583
REMARK 3 L33: 2.1293 L12: -1.5107
REMARK 3 L13: 0.2985 L23: 0.6217
REMARK 3 S TENSOR
REMARK 3 S11: 0.1290 S12: 0.2650 S13: 0.1678
REMARK 3 S21: 0.0079 S22: -0.0379 S23: -0.4406
REMARK 3 S31: 0.0110 S32: 0.3040 S33: -0.0957
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 187:429 )
REMARK 3 ORIGIN FOR THE GROUP (A): -52.5075 17.7832 22.3675
REMARK 3 T TENSOR
REMARK 3 T11: 0.1661 T22: 0.2338
REMARK 3 T33: 0.1658 T12: 0.0442
REMARK 3 T13: -0.0083 T23: -0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 1.1254 L22: 2.3891
REMARK 3 L33: 1.3987 L12: 0.1902
REMARK 3 L13: 0.5301 L23: 1.0379
REMARK 3 S TENSOR
REMARK 3 S11: 0.0633 S12: 0.2032 S13: 0.0208
REMARK 3 S21: 0.0064 S22: -0.0187 S23: -0.1658
REMARK 3 S31: 0.0155 S32: 0.1841 S33: -0.0171
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 430:444 )
REMARK 3 ORIGIN FOR THE GROUP (A): -72.0219 8.6051 7.4051
REMARK 3 T TENSOR
REMARK 3 T11: 0.1724 T22: 0.3086
REMARK 3 T33: 0.3122 T12: -0.0191
REMARK 3 T13: -0.0825 T23: -0.0483
REMARK 3 L TENSOR
REMARK 3 L11: 2.4129 L22: 1.8626
REMARK 3 L33: 7.3567 L12: 2.0718
REMARK 3 L13: 2.4116 L23: 2.6405
REMARK 3 S TENSOR
REMARK 3 S11: -0.5643 S12: -0.5486 S13: 0.1978
REMARK 3 S21: -0.1551 S22: 0.1376 S23: -0.0842
REMARK 3 S31: -0.2973 S32: -0.4375 S33: 0.3949
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 445:857 )
REMARK 3 ORIGIN FOR THE GROUP (A): -65.6462 1.8645 -25.1722
REMARK 3 T TENSOR
REMARK 3 T11: 0.1158 T22: 0.0832
REMARK 3 T33: 0.1774 T12: -0.0028
REMARK 3 T13: -0.0015 T23: 0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 1.0715 L22: 0.6599
REMARK 3 L33: 2.1978 L12: 0.2490
REMARK 3 L13: 0.2410 L23: 0.3097
REMARK 3 S TENSOR
REMARK 3 S11: -0.0328 S12: 0.0722 S13: 0.0416
REMARK 3 S21: -0.0798 S22: 0.1330 S23: -0.0796
REMARK 3 S31: 0.0326 S32: 0.0559 S33: -0.0850
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 858:963 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.7878 2.0670 -16.8217
REMARK 3 T TENSOR
REMARK 3 T11: 0.2729 T22: 0.3631
REMARK 3 T33: 0.2675 T12: 0.0672
REMARK 3 T13: -0.0266 T23: -0.0903
REMARK 3 L TENSOR
REMARK 3 L11: 4.2124 L22: 1.9622
REMARK 3 L33: 1.9341 L12: -0.9605
REMARK 3 L13: 0.4657 L23: 0.3735
REMARK 3 S TENSOR
REMARK 3 S11: -0.1676 S12: -0.3158 S13: -0.0620
REMARK 3 S21: 0.1424 S22: 0.3443 S23: -0.1421
REMARK 3 S31: -0.0970 S32: 0.5881 S33: -0.1113
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN A AND RESID 970:1041 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.1751 15.5365 -36.3061
REMARK 3 T TENSOR
REMARK 3 T11: 0.4144 T22: 0.6695
REMARK 3 T33: 0.6167 T12: -0.0791
REMARK 3 T13: 0.1103 T23: 0.1488
REMARK 3 L TENSOR
REMARK 3 L11: 4.5210 L22: 2.1558
REMARK 3 L33: 1.6665 L12: 0.3056
REMARK 3 L13: -1.1608 L23: 0.0594
REMARK 3 S TENSOR
REMARK 3 S11: 0.0828 S12: 0.6314 S13: 0.5854
REMARK 3 S21: -0.4671 S22: -0.2506 S23: -0.5989
REMARK 3 S31: -0.3630 S32: 1.2055 S33: 0.0037
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN A AND RESID 1052:1292 )
REMARK 3 ORIGIN FOR THE GROUP (A): -62.2030 7.9874 -68.5721
REMARK 3 T TENSOR
REMARK 3 T11: 0.5586 T22: 0.7667
REMARK 3 T33: 0.3388 T12: -0.2397
REMARK 3 T13: 0.0125 T23: 0.0750
REMARK 3 L TENSOR
REMARK 3 L11: 1.9415 L22: 2.0279
REMARK 3 L33: 2.5259 L12: 0.7154
REMARK 3 L13: -1.0861 L23: -1.1670
REMARK 3 S TENSOR
REMARK 3 S11: -0.4101 S12: 0.9472 S13: 0.0680
REMARK 3 S21: -0.5820 S22: 0.4793 S23: -0.1585
REMARK 3 S31: 0.4639 S32: -0.6145 S33: 0.0077
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN B AND RESID 3:68 )
REMARK 3 ORIGIN FOR THE GROUP (A): -60.9504 -15.2498 -2.8952
REMARK 3 T TENSOR
REMARK 3 T11: 0.4325 T22: 0.1257
REMARK 3 T33: 0.2029 T12: -0.0079
REMARK 3 T13: -0.0475 T23: 0.0607
REMARK 3 L TENSOR
REMARK 3 L11: 2.4696 L22: 1.1351
REMARK 3 L33: 4.0307 L12: -0.2305
REMARK 3 L13: 0.5893 L23: 1.4495
REMARK 3 S TENSOR
REMARK 3 S11: -0.0224 S12: -0.3981 S13: -0.3719
REMARK 3 S21: -0.1409 S22: 0.1916 S23: -0.1014
REMARK 3 S31: 0.5879 S32: 0.2457 S33: -0.2460
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5JA1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220119.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-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 : NULL
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
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31781
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 56.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.14250
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.0500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.39700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.140
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 4ZXJ
REMARK 200
REMARK 200 REMARK: LONG FLAT NEEDLES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS TRIS PROPANE, 50-150 MM
REMARK 280 MGCL2, AND 15-28% POLYETHYLENE GLYCOL 4000, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 287.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z+1/2
REMARK 290 4555 -X+1/2,Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 67.90368
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.83950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 91.09300
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 67.90368
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.83950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 91.09300
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 HIS A 4
REMARK 465 LEU A 5
REMARK 465 PRO A 6
REMARK 465 LEU A 7
REMARK 465 VAL A 8
REMARK 465 ALA A 9
REMARK 465 ALA A 10
REMARK 465 GLN A 11
REMARK 465 PRO A 12
REMARK 465 GLY A 13
REMARK 465 ILE A 14
REMARK 465 TRP A 15
REMARK 465 MET A 16
REMARK 465 ALA A 17
REMARK 465 GLU A 18
REMARK 465 LYS A 19
REMARK 465 LEU A 20
REMARK 465 GLU A 64
REMARK 465 ASP A 65
REMARK 465 ASN A 66
REMARK 465 GLY A 67
REMARK 465 GLU A 68
REMARK 465 GLY A 336
REMARK 465 ARG A 337
REMARK 465 ALA A 338
REMARK 465 LYS A 964
REMARK 465 ALA A 965
REMARK 465 GLN A 966
REMARK 465 ALA A 967
REMARK 465 PRO A 968
REMARK 465 GLY A 969
REMARK 465 ILE A 1042
REMARK 465 ASP A 1043
REMARK 465 ALA A 1044
REMARK 465 GLU A 1045
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 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 SER A 1206
REMARK 465 THR A 1207
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 ARG A 1293
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLN B 69
REMARK 465 GLU B 70
REMARK 465 ALA B 71
REMARK 465 GLN B 72
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 GLU A 22 CG CD OE1 OE2
REMARK 470 GLU A 38 CG CD OE1 OE2
REMARK 470 MET A 60 CG SD CE
REMARK 470 THR A 63 OG1 CG2
REMARK 470 TRP A 70 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 70 CZ3 CH2
REMARK 470 GLN A 71 CG CD OE1 NE2
REMARK 470 ARG A 110 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 115 CG CD CE NZ
REMARK 470 GLN A 182 CG CD OE1 NE2
REMARK 470 ARG A 185 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 188 CG CD OE1 OE2
REMARK 470 GLU A 199 CG CD OE1 OE2
REMARK 470 ARG A 202 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 218 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 342 CG CD OE1 OE2
REMARK 470 GLU A 499 CG CD OE1 OE2
REMARK 470 LYS A 545 CG CD CE NZ
REMARK 470 GLU A 549 CG CD OE1 OE2
REMARK 470 ASP A 550 CG OD1 OD2
REMARK 470 ASP A 560 CG OD1 OD2
REMARK 470 ASP A 561 CG OD1 OD2
REMARK 470 GLN A 707 CG CD OE1 NE2
REMARK 470 ARG A 710 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 711 CG CD OE1 NE2
REMARK 470 ARG A 769 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 846 CG OD1 OD2
REMARK 470 GLU A 928 CG CD OE1 OE2
REMARK 470 GLN A 944 CG CD OE1 NE2
REMARK 470 LYS A 952 CG CD CE NZ
REMARK 470 LYS A 956 CG CD CE NZ
REMARK 470 GLU A 962 CG CD OE1 OE2
REMARK 470 LEU A 963 CG CD1 CD2
REMARK 470 ARG A 970 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 973 CG CD CE NZ
REMARK 470 SER A 976 OG
REMARK 470 GLU A 977 CG CD OE1 OE2
REMARK 470 THR A 978 OG1 CG2
REMARK 470 VAL A 992 CG1 CG2
REMARK 470 ASP A 994 CG OD1 OD2
REMARK 470 LYS A1011 CG CD CE NZ
REMARK 470 ARG A1022 CG CD NE CZ NH1 NH2
REMARK 470 SER A1033 OG
REMARK 470 MET A1052 CG SD CE
REMARK 470 GLU A1062 CG CD OE1 OE2
REMARK 470 ASN A1103 CG OD1 ND2
REMARK 470 GLU A1114 CG CD OE1 OE2
REMARK 470 GLU A1117 CG CD OE1 OE2
REMARK 470 LEU A1120 CG CD1 CD2
REMARK 470 GLN A1145 CG CD OE1 NE2
REMARK 470 ARG A1150 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1157 CG CD OE1 NE2
REMARK 470 LEU A1161 CG CD1 CD2
REMARK 470 GLU A1185 CG CD OE1 OE2
REMARK 470 GLU A1189 CG CD OE1 OE2
REMARK 470 GLN A1202 CG CD OE1 NE2
REMARK 470 GLU A1208 CG CD OE1 OE2
REMARK 470 HIS A1228 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A1233 CG OD1 OD2
REMARK 470 LYS A1235 CG CD CE NZ
REMARK 470 GLU A1242 CG CD OE1 OE2
REMARK 470 ARG A1253 CG CD NE CZ NH1 NH2
REMARK 470 ILE A1259 CG1 CG2 CD1
REMARK 470 GLU A1261 CG CD OE1 OE2
REMARK 470 LEU A1262 CG CD1 CD2
REMARK 470 ILE A1264 CG1 CG2 CD1
REMARK 470 ARG A1266 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1267 CG CD OE1 NE2
REMARK 470 ASP A1268 CG OD1 OD2
REMARK 470 LYS A1282 CG CD CE NZ
REMARK 470 PHE B 3 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL B 32 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O LEU B 60 O HOH B 101 2.15
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 26 61.96 62.75
REMARK 500 VAL A 111 -26.36 69.05
REMARK 500 SER A 113 172.43 60.91
REMARK 500 LYS A 115 108.43 -46.49
REMARK 500 LEU A 117 23.90 -78.59
REMARK 500 GLN A 121 -67.49 -129.15
REMARK 500 LEU A 122 88.99 73.14
REMARK 500 TYR A 184 -179.07 -66.89
REMARK 500 ARG A 185 -27.37 65.74
REMARK 500 GLN A 191 -37.13 72.30
REMARK 500 ALA A 220 -72.08 -67.72
REMARK 500 ILE A 224 -169.48 -123.66
REMARK 500 LEU A 243 71.64 -104.80
REMARK 500 PHE A 275 -165.76 -106.95
REMARK 500 VAL A 290 -40.69 -139.38
REMARK 500 ASP A 377 -76.69 -133.51
REMARK 500 ASP A 476 -152.02 -123.42
REMARK 500 THR A 634 -165.85 -129.33
REMARK 500 PHE A 655 -37.60 -130.22
REMARK 500 SER A 712 -45.05 -140.34
REMARK 500 ALA A 752 79.30 55.10
REMARK 500 VAL A 753 -86.18 69.46
REMARK 500 VAL A 779 -169.67 -78.20
REMARK 500 ILE A 786 90.69 59.18
REMARK 500 ASP A 918 75.07 53.92
REMARK 500 PRO A 946 89.54 -69.42
REMARK 500 LEU A 953 99.30 60.51
REMARK 500 LYS A 973 -108.97 -5.41
REMARK 500 ALA A 974 -149.32 170.40
REMARK 500 ALA A 995 170.84 -56.85
REMARK 500 THR A1034 143.68 -170.09
REMARK 500 PRO A1073 -159.30 -82.01
REMARK 500 TYR A1137 110.66 64.98
REMARK 500 SER A1138 -121.19 59.09
REMARK 500 GLU A1185 -30.05 66.23
REMARK 500 GLN A1202 16.38 58.52
REMARK 500 PHE A1210 30.62 -86.88
REMARK 500 PRO A1231 -70.04 -59.69
REMARK 500 PHE A1232 90.29 52.98
REMARK 500 PRO A1257 30.92 -92.58
REMARK 500 ILE A1259 102.93 -169.47
REMARK 500 SER B 4 -91.41 62.44
REMARK 500 GLN B 67 -65.47 -127.57
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 PRO A 24 SER A 25 -147.08
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
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1302
DBREF 5JA1 A 1 1293 UNP P11454 ENTF_ECOLI 1 1293
DBREF 5JA1 B 1 72 UNP P18393 YBDZ_ECOLI 1 72
SEQADV 5JA1 GLY A -1 UNP P11454 EXPRESSION TAG
SEQADV 5JA1 HIS A 0 UNP P11454 EXPRESSION TAG
SEQADV 5JA1 GLY B -1 UNP P18393 EXPRESSION TAG
SEQADV 5JA1 HIS B 0 UNP P18393 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
SEQRES 1 B 74 GLY HIS MET ALA PHE SER ASN PRO PHE ASP ASP PRO GLN
SEQRES 2 B 74 GLY ALA PHE TYR ILE LEU ARG ASN ALA GLN GLY GLN PHE
SEQRES 3 B 74 SER LEU TRP PRO GLN GLN CYS VAL LEU PRO ALA GLY TRP
SEQRES 4 B 74 ASP ILE VAL CYS GLN PRO GLN SER GLN ALA SER CYS GLN
SEQRES 5 B 74 GLN TRP LEU GLU ALA HIS TRP ARG THR LEU THR PRO THR
SEQRES 6 B 74 ASN PHE THR GLN LEU GLN GLU ALA GLN
HET 75C A1301 49
HET CL A1302 1
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
HETNAM CL CHLORIDE ION
FORMUL 3 75C C25 H44 N9 O13 P S2
FORMUL 4 CL CL 1-
FORMUL 5 HOH *49(H2 O)
HELIX 1 AA1 ASP A 40 ALA A 55 1 16
HELIX 2 AA2 ASP A 92 GLN A 106 1 15
HELIX 3 AA3 SER A 145 LEU A 161 1 17
HELIX 4 AA4 PRO A 173 TYR A 184 1 12
HELIX 5 AA5 GLU A 188 GLN A 203 1 16
HELIX 6 AA6 GLY A 234 LEU A 243 1 10
HELIX 7 AA7 GLN A 247 ASN A 265 1 19
HELIX 8 AA8 GLY A 280 ALA A 286 1 7
HELIX 9 AA9 THR A 305 ARG A 322 1 18
HELIX 10 AB1 ASP A 327 ASP A 334 1 8
HELIX 11 AB2 ASP A 402 ASP A 423 1 22
HELIX 12 AB3 LEU A 435 ASN A 446 1 12
HELIX 13 AB4 THR A 456 THR A 468 1 13
HELIX 14 AB5 TYR A 483 ARG A 500 1 18
HELIX 15 AB6 SER A 515 ALA A 528 1 14
HELIX 16 AB7 PRO A 540 ARG A 552 1 13
HELIX 17 AB8 GLN A 562 VAL A 569 5 8
HELIX 18 AB9 GLN A 617 TYR A 631 1 15
HELIX 19 AC1 VAL A 649 TRP A 656 1 8
HELIX 20 AC2 PRO A 657 ILE A 659 5 3
HELIX 21 AC3 ASP A 674 GLY A 686 1 13
HELIX 22 AC4 VAL A 693 SER A 703 1 11
HELIX 23 AC5 THR A 705 CYS A 713 1 9
HELIX 24 AC6 ALA A 714 LEU A 716 5 3
HELIX 25 AC7 PRO A 727 THR A 738 1 12
HELIX 26 AC8 PRO A 748 ALA A 752 5 5
HELIX 27 AC9 PHE A 761 GLN A 767 1 7
HELIX 28 AD1 ARG A 816 ARG A 823 1 8
HELIX 29 AD2 LEU A 869 GLN A 877 1 9
HELIX 30 AD3 ASN A 893 ALA A 897 5 5
HELIX 31 AD4 ASP A 918 ARG A 927 1 10
HELIX 32 AD5 PRO A 931 VAL A 935 5 5
HELIX 33 AD6 GLU A 977 GLY A 989 1 13
HELIX 34 AD7 HIS A 1005 VAL A 1020 1 16
HELIX 35 AD8 THR A 1025 ALA A 1032 1 8
HELIX 36 AD9 THR A 1034 ILE A 1041 1 8
HELIX 37 AE1 ALA A 1078 LEU A 1088 5 11
HELIX 38 AE2 GLY A 1104 ALA A 1109 1 6
HELIX 39 AE3 ASN A 1111 GLU A 1117 1 7
HELIX 40 AE4 ALA A 1118 GLN A 1127 1 10
HELIX 41 AE5 SER A 1138 LEU A 1151 1 14
HELIX 42 AE6 GLU A 1185 ALA A 1200 1 16
HELIX 43 AE7 PHE A 1210 ARG A 1222 1 13
HELIX 44 AE8 LEU A 1223 ALA A 1227 5 5
HELIX 45 AE9 PRO A 1251 SER A 1256 1 6
HELIX 46 AF1 PRO A 1257 ILE A 1259 5 3
HELIX 47 AF2 THR A 1279 LEU A 1291 1 13
HELIX 48 AF3 ASN B 5 ASP B 9 5 5
HELIX 49 AF4 SER B 45 TRP B 57 1 13
SHEET 1 AA1 4 ILE A 85 ASP A 86 0
SHEET 2 AA1 4 ILE A 123 GLN A 124 1 O GLN A 124 N ILE A 85
SHEET 3 AA1 4 ARG A 129 HIS A 137 -1 O TYR A 131 N ILE A 123
SHEET 4 AA1 4 VAL A 118 HIS A 120 -1 N PHE A 119 O ARG A 135
SHEET 1 AA2 5 ILE A 85 ASP A 86 0
SHEET 2 AA2 5 ILE A 123 GLN A 124 1 O GLN A 124 N ILE A 85
SHEET 3 AA2 5 ARG A 129 HIS A 137 -1 O TYR A 131 N ILE A 123
SHEET 4 AA2 5 SER A 28 THR A 36 -1 N HIS A 31 O GLN A 134
SHEET 5 AA2 5 GLN A 364 ALA A 371 -1 O GLN A 366 N GLU A 34
SHEET 1 AA3 2 MET A 60 PHE A 62 0
SHEET 2 AA3 2 GLN A 71 VAL A 73 -1 O TRP A 72 N ARG A 61
SHEET 1 AA4 6 LEU A 225 PHE A 231 0
SHEET 2 AA4 6 LEU A 390 ALA A 396 -1 O ILE A 394 N LEU A 227
SHEET 3 AA4 6 LEU A 378 PRO A 384 -1 N PHE A 383 O SER A 391
SHEET 4 AA4 6 PRO A 347 ASN A 350 1 N VAL A 348 O LEU A 380
SHEET 5 AA4 6 ASP A 268 MET A 276 1 N GLY A 272 O PRO A 347
SHEET 6 AA4 6 LEU A 291 HIS A 299 -1 O ASN A 292 N PHE A 275
SHEET 1 AA5 4 LEU A 480 SER A 482 0
SHEET 2 AA5 4 PRO A 472 ALA A 475 -1 N LEU A 474 O PHE A 481
SHEET 3 AA5 4 LYS A 663 MET A 666 1 O LEU A 664 N ALA A 473
SHEET 4 AA5 4 VAL A 638 GLN A 641 1 N VAL A 639 O LYS A 663
SHEET 1 AA6 4 ALA A 531 PRO A 534 0
SHEET 2 AA6 4 SER A 507 ALA A 511 1 N VAL A 508 O LEU A 533
SHEET 3 AA6 4 LEU A 555 THR A 558 1 O ILE A 557 N ALA A 511
SHEET 4 AA6 4 SER A 574 CYS A 576 1 O LEU A 575 N THR A 558
SHEET 1 AA7 3 THR A 597 THR A 603 0
SHEET 2 AA7 3 LYS A 611 GLY A 616 -1 O VAL A 613 N ILE A 601
SHEET 3 AA7 3 GLY A 812 LEU A 814 -1 O LEU A 814 N GLY A 612
SHEET 1 AA8 5 THR A 689 PHE A 692 0
SHEET 2 AA8 5 GLN A 718 CYS A 721 1 O PHE A 720 N PHE A 692
SHEET 3 AA8 5 LEU A 742 TYR A 746 1 O HIS A 743 N CYS A 721
SHEET 4 AA8 5 SER A 756 PRO A 759 -1 O TYR A 758 N ASN A 744
SHEET 5 AA8 5 TYR A 777 PRO A 778 -1 O TYR A 777 N TRP A 757
SHEET 1 AA9 4 THR A 782 LEU A 784 0
SHEET 2 AA9 4 GLY A 800 GLY A 806 -1 O THR A 805 N GLY A 783
SHEET 3 AA9 4 ARG A 834 TRP A 844 -1 O TYR A 836 N LEU A 804
SHEET 4 AA9 4 PHE A 824 ALA A 826 -1 N ILE A 825 O MET A 835
SHEET 1 AB1 4 THR A 782 LEU A 784 0
SHEET 2 AB1 4 GLY A 800 GLY A 806 -1 O THR A 805 N GLY A 783
SHEET 3 AB1 4 ARG A 834 TRP A 844 -1 O TYR A 836 N LEU A 804
SHEET 4 AB1 4 VAL A 850 ARG A 855 -1 O GLY A 854 N VAL A 841
SHEET 1 AB2 2 GLN A 859 ILE A 862 0
SHEET 2 AB2 2 GLN A 865 GLU A 868 -1 O ILE A 867 N LEU A 860
SHEET 1 AB3 3 GLN A 884 CYS A 890 0
SHEET 2 AB3 3 GLN A 904 VAL A 910 -1 O VAL A 906 N HIS A 888
SHEET 3 AB3 3 VAL A 938 GLN A 941 1 O LEU A 940 N GLY A 907
SHEET 1 AB4 7 ILE A1057 ARG A1061 0
SHEET 2 AB4 7 SER A1093 ILE A1097 -1 O GLY A1096 N LEU A1058
SHEET 3 AB4 7 THR A1067 PHE A1071 1 N LEU A1068 O SER A1093
SHEET 4 AB4 7 TYR A1132 LEU A1135 1 O TYR A1133 N PHE A1069
SHEET 5 AB4 7 VAL A1158 LEU A1164 1 O GLY A1162 N LEU A1134
SHEET 6 AB4 7 LYS A1235 ALA A1241 1 O THR A1237 N LEU A1161
SHEET 7 AB4 7 GLU A1261 GLN A1267 1 O ASP A1263 N LEU A1238
SHEET 1 AB5 3 PHE B 24 PRO B 28 0
SHEET 2 AB5 3 PHE B 14 ARG B 18 -1 N LEU B 17 O SER B 25
SHEET 3 AB5 3 ASP B 38 GLN B 44 -1 O VAL B 40 N ILE B 16
LINK OG SER A1006 P1 75C A1301 1555 1555 1.61
CISPEP 1 GLY A 288 PRO A 289 0 -3.35
CISPEP 2 ARG A 1101 PRO A 1102 0 -5.93
CISPEP 3 GLY A 1130 PRO A 1131 0 -0.79
CISPEP 4 ARG A 1154 GLY A 1155 0 14.19
SITE 1 AC1 27 PHE A 647 ASP A 648 ARG A 673 VAL A 693
SITE 2 AC1 27 SER A 722 GLY A 723 GLU A 724 ALA A 725
SITE 3 AC1 27 ASN A 744 LEU A 745 TYR A 746 GLY A 747
SITE 4 AC1 27 PRO A 748 THR A 749 VAL A 753 ASP A 754
SITE 5 AC1 27 ILE A 775 ASP A 840 TYR A 852 ARG A 855
SITE 6 AC1 27 LYS A 861 ARG A 863 GLY A 864 GLN A 865
SITE 7 AC1 27 ARG A 866 SER A1006 HOH A1420
SITE 1 AC2 2 LYS A 861 ARG A 903
CRYST1 161.185 57.679 183.945 90.00 97.93 90.00 I 1 2 1 4
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 0.006204 0.000000 0.000864 0.00000
SCALE2 0.000000 0.017337 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005489 0.00000
TER 9264 ASN A1292
TER 9795 LEU B 68
MASTER 583 0 2 49 56 0 8 6 9876 2 50 106
END |