HEADER LIGASE 11-APR-16 5JA2
TITLE ENTF, A TERMINAL NONRIBOSOMAL PEPTIDE SYNTHETASE MODULE BOUND TO THE
TITLE 2 NON-NATIVE MBTH-LIKE PROTEIN PA2412
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: MBTH-LIKE PROTEIN PA2412;
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: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 /
SOURCE 14 PAO1 / 1C / PRS 101 / LMG 12228);
SOURCE 15 ORGANISM_TAXID: 208964;
SOURCE 16 STRAIN: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
SOURCE 17 GENE: PA2412;
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 5 27-SEP-23 5JA2 1 REMARK
REVDAT 4 25-DEC-19 5JA2 1 REMARK
REVDAT 3 20-SEP-17 5JA2 1 JRNL REMARK
REVDAT 2 16-NOV-16 5JA2 1 JRNL
REVDAT 1 14-SEP-16 5JA2 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. V. 291 22559 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) : 58.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 31728
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.820
REMARK 3 FREE R VALUE TEST SET COUNT : 1529
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 58.9851 - 6.6694 0.93 2817 156 0.1804 0.2194
REMARK 3 2 6.6694 - 5.2948 0.97 2803 142 0.2162 0.2236
REMARK 3 3 5.2948 - 4.6258 0.93 2738 145 0.1714 0.2082
REMARK 3 4 4.6258 - 4.2030 0.96 2769 138 0.1734 0.2254
REMARK 3 5 4.2030 - 3.9018 0.97 2804 135 0.1891 0.2406
REMARK 3 6 3.9018 - 3.6718 0.92 2643 117 0.2078 0.2548
REMARK 3 7 3.6718 - 3.4879 0.95 2765 130 0.2197 0.2326
REMARK 3 8 3.4879 - 3.3361 0.96 2737 137 0.2478 0.3053
REMARK 3 9 3.3361 - 3.2077 0.98 2770 153 0.2592 0.2621
REMARK 3 10 3.2077 - 3.0970 0.96 2788 139 0.2645 0.3452
REMARK 3 11 3.0970 - 3.0002 0.90 2565 137 0.2927 0.3204
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.250
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 65.60
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 10130
REMARK 3 ANGLE : 0.547 13887
REMARK 3 CHIRALITY : 0.040 1603
REMARK 3 PLANARITY : 0.005 1814
REMARK 3 DIHEDRAL : 10.754 6009
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 18:186 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.8102 11.7387 32.5641
REMARK 3 T TENSOR
REMARK 3 T11: 0.7336 T22: 0.3126
REMARK 3 T33: 0.4182 T12: -0.0229
REMARK 3 T13: -0.0722 T23: 0.0110
REMARK 3 L TENSOR
REMARK 3 L11: 4.8684 L22: 4.2463
REMARK 3 L33: 1.9336 L12: -3.1108
REMARK 3 L13: -0.1522 L23: 1.1811
REMARK 3 S TENSOR
REMARK 3 S11: 0.1274 S12: 0.1753 S13: 0.1989
REMARK 3 S21: 0.1938 S22: 0.0379 S23: -0.4285
REMARK 3 S31: 0.0503 S32: 0.4039 S33: -0.1651
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 187:429 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.4275 -13.8622 22.0820
REMARK 3 T TENSOR
REMARK 3 T11: 0.6279 T22: 0.3633
REMARK 3 T33: 0.3321 T12: 0.0708
REMARK 3 T13: 0.0658 T23: 0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 2.4382 L22: 3.7543
REMARK 3 L33: 1.8328 L12: 1.2335
REMARK 3 L13: 1.4194 L23: 1.3899
REMARK 3 S TENSOR
REMARK 3 S11: -0.0368 S12: 0.3476 S13: 0.1520
REMARK 3 S21: 0.2693 S22: 0.0564 S23: -0.0863
REMARK 3 S31: 0.0457 S32: 0.2465 S33: -0.0149
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 430:444 )
REMARK 3 ORIGIN FOR THE GROUP (A): -71.1711 -22.8685 7.2878
REMARK 3 T TENSOR
REMARK 3 T11: 0.5726 T22: 0.3438
REMARK 3 T33: 0.2643 T12: -0.0010
REMARK 3 T13: 0.0207 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 8.7503 L22: 5.7119
REMARK 3 L33: 5.0263 L12: 5.2025
REMARK 3 L13: 1.9355 L23: 4.6174
REMARK 3 S TENSOR
REMARK 3 S11: -0.3991 S12: -0.1371 S13: 0.1586
REMARK 3 S21: -0.0294 S22: -0.1082 S23: -0.0169
REMARK 3 S31: 0.6307 S32: -0.1654 S33: 0.4541
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 445:857 )
REMARK 3 ORIGIN FOR THE GROUP (A): -64.9346 -29.3950 -25.0721
REMARK 3 T TENSOR
REMARK 3 T11: 0.5353 T22: 0.2023
REMARK 3 T33: 0.3241 T12: -0.0271
REMARK 3 T13: 0.1099 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 2.5985 L22: 1.0569
REMARK 3 L33: 3.0560 L12: 0.6192
REMARK 3 L13: 0.4036 L23: 0.7558
REMARK 3 S TENSOR
REMARK 3 S11: -0.0443 S12: 0.0201 S13: -0.0394
REMARK 3 S21: -0.1962 S22: 0.1415 S23: -0.0944
REMARK 3 S31: 0.0458 S32: 0.1647 S33: -0.0947
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 858:963 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.0239 -28.9019 -16.8894
REMARK 3 T TENSOR
REMARK 3 T11: 0.5190 T22: 0.5125
REMARK 3 T33: 0.4003 T12: 0.0256
REMARK 3 T13: 0.0962 T23: -0.1340
REMARK 3 L TENSOR
REMARK 3 L11: 8.8091 L22: 4.3579
REMARK 3 L33: 4.2444 L12: -2.9150
REMARK 3 L13: 2.0127 L23: -1.1986
REMARK 3 S TENSOR
REMARK 3 S11: -0.1190 S12: -0.2113 S13: 0.2083
REMARK 3 S21: 0.1716 S22: 0.1433 S23: -0.3735
REMARK 3 S31: -0.0620 S32: 0.7416 S33: -0.0638
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN A AND RESID 971:1043 )
REMARK 3 ORIGIN FOR THE GROUP (A): -36.7108 -15.9413 -36.6000
REMARK 3 T TENSOR
REMARK 3 T11: 0.9207 T22: 1.2058
REMARK 3 T33: 0.8504 T12: -0.0156
REMARK 3 T13: 0.2834 T23: 0.2235
REMARK 3 L TENSOR
REMARK 3 L11: 1.6910 L22: 6.0166
REMARK 3 L33: 2.1364 L12: 1.6356
REMARK 3 L13: 0.9902 L23: -1.6969
REMARK 3 S TENSOR
REMARK 3 S11: 0.3609 S12: 1.7288 S13: 0.9878
REMARK 3 S21: -0.5337 S22: -0.3930 S23: -1.0258
REMARK 3 S31: 0.7835 S32: 1.5967 S33: -0.0952
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN A AND RESID 1052:1292 )
REMARK 3 ORIGIN FOR THE GROUP (A): -62.4274 -23.2146 -68.5552
REMARK 3 T TENSOR
REMARK 3 T11: 1.0410 T22: 1.2289
REMARK 3 T33: 0.4920 T12: -0.3882
REMARK 3 T13: 0.0775 T23: 0.0599
REMARK 3 L TENSOR
REMARK 3 L11: 3.8523 L22: 3.9428
REMARK 3 L33: 6.5207 L12: 0.8998
REMARK 3 L13: -1.9427 L23: -0.2720
REMARK 3 S TENSOR
REMARK 3 S11: -0.5761 S12: 1.4287 S13: 0.2023
REMARK 3 S21: -1.1131 S22: 0.7014 S23: -0.0850
REMARK 3 S31: 0.7645 S32: -0.9386 S33: -0.1654
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN B AND RESID 0:67 )
REMARK 3 ORIGIN FOR THE GROUP (A): -61.5986 -46.3104 -1.5276
REMARK 3 T TENSOR
REMARK 3 T11: 0.7728 T22: 0.7658
REMARK 3 T33: 0.6780 T12: 0.0651
REMARK 3 T13: 0.0229 T23: 0.3811
REMARK 3 L TENSOR
REMARK 3 L11: 3.6141 L22: 7.4472
REMARK 3 L33: 7.9999 L12: 2.2392
REMARK 3 L13: 0.8860 L23: 0.1954
REMARK 3 S TENSOR
REMARK 3 S11: 0.5350 S12: -0.9765 S13: -0.8309
REMARK 3 S21: 0.6098 S22: -0.5974 S23: -0.6845
REMARK 3 S31: 1.0939 S32: 0.4835 S33: -0.0404
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 5JA2 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_1000220163.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-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 : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31728
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 58.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.10260
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6600
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 (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.62140
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.370
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: 5JA1
REMARK 200
REMARK 200 REMARK: NULL
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 67.54007
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.84500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 90.40654
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 67.54007
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.84500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 90.40654
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: 2440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 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 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 ARG A 970
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 GLY A 1155
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 1204
REMARK 465 THR A 1205
REMARK 465 SER A 1206
REMARK 465 THR A 1207
REMARK 465 ILE A 1259
REMARK 465 ALA A 1260
REMARK 465 ARG A 1293
REMARK 465 GLY B -1
REMARK 465 ASP B 68
REMARK 465 LYS B 69
REMARK 465 ALA B 70
REMARK 465 ALA B 71
REMARK 465 GLY 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 LYS A 19 CG CD CE NZ
REMARK 470 GLU A 22 CG CD OE1 OE2
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 VAL A 69 CG1 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 LYS A 115 CG CD CE NZ
REMARK 470 GLU A 179 CG CD OE1 OE2
REMARK 470 ARG A 185 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 202 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 203 CG CD OE1 NE2
REMARK 470 ARG A 218 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 LYS A 318 CG CD CE NZ
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 ARG A 325 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 333 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 342 CG CD OE1 OE2
REMARK 470 LYS A 398 CG CD CE NZ
REMARK 470 GLU A 499 CG CD OE1 OE2
REMARK 470 LYS A 503 CG CD CE NZ
REMARK 470 LYS A 545 CG CD CE NZ
REMARK 470 ASP A 560 CG OD1 OD2
REMARK 470 LEU A 572 CG CD1 CD2
REMARK 470 ARG A 609 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 711 CG CD OE1 NE2
REMARK 470 ASP A 729 CG OD1 OD2
REMARK 470 ARG A 769 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 846 CG OD1 OD2
REMARK 470 ARG A 874 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 883 CG CD OE1 OE2
REMARK 470 GLN A 944 CG CD OE1 NE2
REMARK 470 ASN A 950 CG OD1 ND2
REMARK 470 LYS A 952 CG CD CE NZ
REMARK 470 LYS A 956 CG CD CE NZ
REMARK 470 LYS A 973 CG CD CE NZ
REMARK 470 ILE A 979 CG1 CG2 CD1
REMARK 470 VAL A 992 CG1 CG2
REMARK 470 GLN A 993 CG CD OE1 NE2
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 GLN A1023 CG CD OE1 NE2
REMARK 470 SER A1033 OG
REMARK 470 THR A1034 OG1 CG2
REMARK 470 LEU A1038 CG CD1 CD2
REMARK 470 ILE A1042 CG1 CG2 CD1
REMARK 470 ASP A1043 CG OD1 OD2
REMARK 470 ARG A1051 CG CD NE CZ NH1 NH2
REMARK 470 MET A1052 CG SD CE
REMARK 470 GLU A1055 CG CD OE1 OE2
REMARK 470 ARG A1101 CG CD NE CZ NH1 NH2
REMARK 470 ASN A1103 CG OD1 ND2
REMARK 470 HIS A1129 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A1145 CG CD OE1 NE2
REMARK 470 ARG A1150 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1152 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1157 CG CD OE1 NE2
REMARK 470 LEU A1182 CG CD1 CD2
REMARK 470 ASP A1183 CG OD1 OD2
REMARK 470 GLU A1185 CG CD OE1 OE2
REMARK 470 GLU A1189 CG CD OE1 OE2
REMARK 470 GLU A1195 CG CD OE1 OE2
REMARK 470 GLN A1202 CG CD OE1 NE2
REMARK 470 GLU A1208 CG CD OE1 OE2
REMARK 470 LEU A1209 CG CD1 CD2
REMARK 470 LEU A1224 CG CD1 CD2
REMARK 470 HIS A1228 CG ND1 CD2 CE1 NE2
REMARK 470 PHE A1232 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP A1233 CG OD1 OD2
REMARK 470 LYS A1235 CG CD CE NZ
REMARK 470 PHE A1239 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A1242 CG CD OE1 OE2
REMARK 470 GLN A1246 CG CD OE1 NE2
REMARK 470 GLU A1247 CG CD OE1 OE2
REMARK 470 MET A1249 CG SD CE
REMARK 470 GLU A1252 CG CD OE1 OE2
REMARK 470 ARG A1253 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1261 CG CD OE1 OE2
REMARK 470 ILE A1264 CG1 CG2 CD1
REMARK 470 ARG A1266 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1282 CG CD CE NZ
REMARK 470 HIS B 0 CG ND1 CD2 CE1 NE2
REMARK 470 MET B 1 CG SD CE
REMARK 470 ARG B 7 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 9 CG OD1 OD2
REMARK 470 ILE B 10 CG1 CG2 CD1
REMARK 470 GLN B 11 CG CD OE1 NE2
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 GLU B 52 CG CD OE1 OE2
REMARK 470 MET B 67 CG SD CE
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 OG1 THR A 57 OG1 THR A 287 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 21 -73.20 -107.35
REMARK 500 ASP A 142 -169.81 -129.31
REMARK 500 PRO A 165 -175.94 -69.05
REMARK 500 PHE A 275 -163.85 -111.70
REMARK 500 ASP A 377 -72.07 -119.36
REMARK 500 ALA A 473 -63.46 -120.82
REMARK 500 ASP A 476 -158.35 -148.91
REMARK 500 THR A 607 -79.46 -110.59
REMARK 500 PHE A 655 -44.10 -133.74
REMARK 500 GLU A 670 33.17 38.67
REMARK 500 SER A 712 -54.68 -127.55
REMARK 500 THR A 738 -53.01 -122.29
REMARK 500 ALA A 752 78.45 52.47
REMARK 500 VAL A 753 -101.04 62.11
REMARK 500 VAL A 779 -164.81 -79.17
REMARK 500 ASP A 788 -161.55 -100.85
REMARK 500 ASP A 918 74.78 56.55
REMARK 500 PRO A 946 90.49 -68.42
REMARK 500 SER A 948 -80.26 -144.24
REMARK 500 ALA A 949 -79.49 -94.06
REMARK 500 LEU A 953 88.18 59.23
REMARK 500 ALA A 974 -162.05 -71.64
REMARK 500 PRO A1073 -158.08 -75.69
REMARK 500 PRO A1102 99.69 -60.95
REMARK 500 SER A1138 -116.98 56.50
REMARK 500 PRO A1231 -19.46 -48.12
REMARK 500 PHE A1232 84.38 51.25
REMARK 500 THR A1244 -153.25 -91.32
REMARK 500 GLN A1246 -135.54 -87.12
REMARK 500 GLU A1247 97.00 60.37
REMARK 500 MET A1249 24.73 -76.42
REMARK 500 SER A1250 159.33 -47.41
REMARK 500 PRO A1251 -32.21 -29.31
REMARK 500 PRO A1257 31.08 -81.20
REMARK 500 THR B 2 81.04 53.43
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 BU9 A 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BU9 A 1303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JA2 RELATED DB: PDB
DBREF 5JA2 A 1 1293 UNP P11454 ENTF_ECOLI 1 1293
DBREF 5JA2 B 1 72 UNP Q9I169 Q9I169_PSEAE 1 72
SEQADV 5JA2 GLY A -1 UNP P11454 EXPRESSION TAG
SEQADV 5JA2 HIS A 0 UNP P11454 EXPRESSION TAG
SEQADV 5JA2 GLY B -1 UNP Q9I169 EXPRESSION TAG
SEQADV 5JA2 HIS B 0 UNP Q9I169 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 THR SER VAL PHE ASP ARG ASP ASP ILE GLN
SEQRES 2 B 74 PHE GLN VAL VAL VAL ASN HIS GLU GLU GLN TYR SER ILE
SEQRES 3 B 74 TRP PRO GLU TYR LYS GLU ILE PRO GLN GLY TRP ARG ALA
SEQRES 4 B 74 ALA GLY LYS SER GLY LEU LYS LYS ASP CYS LEU ALA TYR
SEQRES 5 B 74 ILE GLU GLU VAL TRP THR ASP MET ARG PRO LEU SER LEU
SEQRES 6 B 74 ARG GLN HIS MET ASP LYS ALA ALA GLY
HET 75C A1301 49
HET BU9 A1302 6
HET BU9 A1303 6
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 BU9 MESO-2,3-BUTANEDIOL
FORMUL 3 75C C25 H44 N9 O13 P S2
FORMUL 4 BU9 2(C4 H10 O2)
FORMUL 6 HOH *15(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 ARG A 162 1 18
HELIX 4 AA4 PRO A 173 SER A 187 1 15
HELIX 5 AA5 SER A 187 GLN A 203 1 17
HELIX 6 AA6 GLY A 234 LEU A 243 1 10
HELIX 7 AA7 GLN A 247 CYS A 264 1 18
HELIX 8 AA8 GLY A 280 THR A 285 1 6
HELIX 9 AA9 THR A 305 ARG A 322 1 18
HELIX 10 AB1 ASP A 327 SER A 335 1 9
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 SER A 567 1 6
HELIX 18 AB9 GLN A 617 TYR A 631 1 15
HELIX 19 AC1 PHE A 647 VAL A 649 5 3
HELIX 20 AC2 SER A 650 PHE A 655 1 6
HELIX 21 AC3 TRP A 656 ILE A 659 5 4
HELIX 22 AC4 ASP A 674 GLY A 686 1 13
HELIX 23 AC5 VAL A 693 SER A 703 1 11
HELIX 24 AC6 THR A 705 CYS A 713 1 9
HELIX 25 AC7 ALA A 714 LEU A 716 5 3
HELIX 26 AC8 ALA A 728 THR A 738 1 11
HELIX 27 AC9 PRO A 748 ALA A 752 5 5
HELIX 28 AD1 PHE A 761 GLN A 767 1 7
HELIX 29 AD2 ARG A 816 ARG A 823 1 8
HELIX 30 AD3 LEU A 869 GLN A 877 1 9
HELIX 31 AD4 ASN A 893 ALA A 897 5 5
HELIX 32 AD5 ASP A 918 ARG A 927 1 10
HELIX 33 AD6 PRO A 931 VAL A 935 5 5
HELIX 34 AD7 SER A 976 GLY A 989 1 14
HELIX 35 AD8 HIS A 1005 VAL A 1020 1 16
HELIX 36 AD9 THR A 1025 ALA A 1032 1 8
HELIX 37 AE1 THR A 1034 ASP A 1043 1 10
HELIX 38 AE2 ALA A 1078 SER A 1085 5 8
HELIX 39 AE3 GLY A 1104 ALA A 1109 1 6
HELIX 40 AE4 ALA A 1118 LEU A 1124 1 7
HELIX 41 AE5 SER A 1138 ALA A 1153 1 16
HELIX 42 AE6 ASP A 1183 ALA A 1200 1 18
HELIX 43 AE7 THR A 1211 THR A 1225 1 15
HELIX 44 AE8 SER A 1250 TRP A 1255 1 6
HELIX 45 AE9 VAL A 1272 ILE A 1275 5 4
HELIX 46 AF1 SER A 1276 ASN A 1292 1 17
HELIX 47 AF2 SER B 3 ARG B 7 5 5
HELIX 48 AF3 LYS B 44 TRP B 55 1 12
HELIX 49 AF4 PRO B 60 ARG B 64 5 5
SHEET 1 AA1 5 GLU A 83 ASP A 86 0
SHEET 2 AA1 5 PHE A 119 GLN A 124 1 O LEU A 122 N ILE A 85
SHEET 3 AA1 5 ARG A 129 HIS A 137 -1 O TYR A 131 N ILE A 123
SHEET 4 AA1 5 SER A 28 GLY A 37 -1 N HIS A 31 O GLN A 134
SHEET 5 AA1 5 VAL A 363 ALA A 371 -1 O HIS A 368 N TYR A 32
SHEET 1 AA2 2 ARG A 61 THR A 63 0
SHEET 2 AA2 2 TRP A 70 TRP A 72 -1 O TRP A 72 N ARG A 61
SHEET 1 AA3 6 ILE A 224 PHE A 231 0
SHEET 2 AA3 6 LEU A 390 ASN A 397 -1 O ILE A 394 N LEU A 227
SHEET 3 AA3 6 LEU A 378 PRO A 384 -1 N PHE A 383 O SER A 391
SHEET 4 AA3 6 PRO A 347 ASN A 350 1 N ASN A 350 O LEU A 380
SHEET 5 AA3 6 ASP A 268 MET A 276 1 N GLY A 272 O LEU A 349
SHEET 6 AA3 6 LEU A 291 HIS A 299 -1 O LEU A 294 N PHE A 273
SHEET 1 AA4 4 LEU A 480 SER A 482 0
SHEET 2 AA4 4 PRO A 472 ALA A 475 -1 N LEU A 474 O PHE A 481
SHEET 3 AA4 4 LYS A 663 MET A 666 1 O LEU A 664 N ALA A 473
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 ALA A 511 1 N VAL A 508 O LEU A 533
SHEET 3 AA5 4 LEU A 555 THR A 558 1 O ILE A 557 N ALA A 511
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 LYS A 611 N THR A 603
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 CYS A 721 1 O PHE A 720 N PHE A 692
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 2 LEU A 726 PRO A 727 0
SHEET 2 AA8 2 SER A 772 VAL A 773 -1 O VAL A 773 N LEU A 726
SHEET 1 AA9 4 THR A 782 LEU A 787 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 ALA A 842 N GLY A 800
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 787 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 ALA A 842 N GLY A 800
SHEET 4 AB1 4 VAL A 850 ARG A 855 -1 O GLU A 851 N ARG A 843
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 CYS A1070 1 N LEU A1068 O SER A1093
SHEET 4 AB4 7 TYR A1132 TYR A1137 1 O TYR A1133 N PHE A1069
SHEET 5 AB4 7 VAL A1158 LEU A1164 1 O PHE A1160 N LEU A1134
SHEET 6 AB4 7 ALA A1236 ALA A1241 1 O PHE A1239 N LEU A1163
SHEET 7 AB4 7 LEU A1262 GLN A1267 1 O TYR A1265 N VAL A1240
SHEET 1 AB5 3 TYR B 22 PRO B 26 0
SHEET 2 AB5 3 GLN B 11 VAL B 16 -1 N VAL B 15 O SER B 23
SHEET 3 AB5 3 ARG B 36 LEU B 43 -1 O ARG B 36 N VAL B 16
LINK OG SER A1006 P1 75C A1301 1555 1555 1.62
CISPEP 1 GLY A 340 ASP A 341 0 0.47
SITE 1 AC1 25 PHE A 647 ASP A 648 ARG A 673 VAL A 693
SITE 2 AC1 25 SER A 722 GLY A 723 GLU A 724 ALA A 725
SITE 3 AC1 25 ASN A 744 LEU A 745 TYR A 746 GLY A 747
SITE 4 AC1 25 THR A 749 VAL A 753 ASP A 754 ASP A 840
SITE 5 AC1 25 TYR A 852 ARG A 855 LYS A 861 ARG A 863
SITE 6 AC1 25 GLY A 864 GLN A 865 ARG A 866 SER A1006
SITE 7 AC1 25 HOH A1410
SITE 1 AC2 5 SER A 606 LYS A 611 SER A 822 ARG A 823
SITE 2 AC2 5 ARG A 837
SITE 1 AC3 6 LEU A 109 ARG A 110 SER A 113 LYS A 115
SITE 2 AC3 6 PRO A 116 ARG A 135
CRYST1 159.270 57.690 182.424 90.00 97.62 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 0.006279 0.000000 0.000840 0.00000
SCALE2 0.000000 0.017334 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005531 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
