HEADER HYDROLASE/DNA 10-OCT-11 3U4Q
TITLE STRUCTURE OF ADDAB-DNA COMPLEX AT 2.8 ANGSTROMS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT HELICASE/NUCLEASE SUBUNIT A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ATP-DEPENDENT HELICASE/NUCLEASE ADDA;
COMPND 5 EC: 3.1.-.-, 3.6.4.12;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ATP-DEPENDENT HELICASE/DEOXYRIBONUCLEASE SUBUNIT B;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: ATP-DEPENDENT HELICASE/NUCLEASE ADDB;
COMPND 12 EC: 3.1.-.-, 3.6.4.12;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: DNA (27-MER);
COMPND 17 CHAIN: X;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: ADDA, BSU10630;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 9 ORGANISM_TAXID: 1423;
SOURCE 10 GENE: ADDB, BSU10620;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES
KEYWDS HELICASE, NUCLEASE, DOUBLE STRAND DNA REPAIR, PROTEIN-DNA COMPLEX,
KEYWDS 2 HYDROLASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SAIKRISHNAN,W.KRAJEWSKI,D.WIGLEY
REVDAT 3 28-FEB-24 3U4Q 1 REMARK SEQADV
REVDAT 2 18-APR-12 3U4Q 1 JRNL
REVDAT 1 21-MAR-12 3U4Q 0
JRNL AUTH K.SAIKRISHNAN,J.T.YEELES,N.S.GILHOOLY,W.W.KRAJEWSKI,
JRNL AUTH 2 M.S.DILLINGHAM,D.B.WIGLEY
JRNL TITL INSIGHTS INTO CHI RECOGNITION FROM THE STRUCTURE OF AN
JRNL TITL 2 ADDAB-TYPE HELICASE-NUCLEASE COMPLEX.
JRNL REF EMBO J. V. 31 1568 2012
JRNL REFN ISSN 0261-4189
JRNL PMID 22307084
JRNL DOI 10.1038/EMBOJ.2012.9
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_750)
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.92
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 64447
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 3203
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 29.9199 - 6.0177 0.92 6028 280 0.2125 0.2533
REMARK 3 2 6.0177 - 4.7827 0.95 6102 318 0.2262 0.2699
REMARK 3 3 4.7827 - 4.1800 0.96 6171 317 0.1963 0.2438
REMARK 3 4 4.1800 - 3.7987 0.96 6166 321 0.2235 0.2840
REMARK 3 5 3.7987 - 3.5268 0.96 6148 327 0.2317 0.2933
REMARK 3 6 3.5268 - 3.3192 0.96 6093 352 0.2483 0.3173
REMARK 3 7 3.3192 - 3.1531 0.96 6178 326 0.2655 0.3187
REMARK 3 8 3.1531 - 3.0160 0.96 6149 311 0.2879 0.3494
REMARK 3 9 3.0160 - 2.9000 0.96 6171 329 0.2958 0.3428
REMARK 3 10 2.9000 - 2.8000 0.95 6038 322 0.3126 0.3503
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 45.17
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.050
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.000
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.36150
REMARK 3 B22 (A**2) : -5.06320
REMARK 3 B33 (A**2) : -2.29840
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -6.20210
REMARK 3 B23 (A**2) : 0.00000
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 19293
REMARK 3 ANGLE : 0.655 26124
REMARK 3 CHIRALITY : 0.047 2854
REMARK 3 PLANARITY : 0.002 3277
REMARK 3 DIHEDRAL : 14.612 7369
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 3U4Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068303.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64678
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 99.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% POLYETHYLENE GLYCOL 4000, 0.1M
REMARK 280 TRIS PH 7.5, 0.8 M SODIUM FORMATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 285K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 69.85700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 99790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 ILE A 3
REMARK 465 PRO A 4
REMARK 465 LYS A 5
REMARK 465 PRO A 6
REMARK 465 ALA A 7
REMARK 465 ASP A 8
REMARK 465 SER A 9
REMARK 465 LYS A 245
REMARK 465 ALA A 246
REMARK 465 PRO A 247
REMARK 465 GLY A 248
REMARK 465 GLY A 249
REMARK 465 PRO A 250
REMARK 465 ALA A 251
REMARK 465 PRO A 252
REMARK 465 ARG A 253
REMARK 465 ALA A 254
REMARK 465 PHE A 286
REMARK 465 LYS A 287
REMARK 465 ARG A 288
REMARK 465 ALA A 289
REMARK 465 LYS A 290
REMARK 465 ALA A 291
REMARK 465 VAL A 292
REMARK 465 LYS A 293
REMARK 465 GLY A 294
REMARK 465 ASP A 295
REMARK 465 GLU A 296
REMARK 465 PHE A 297
REMARK 465 LYS A 385
REMARK 465 GLY A 386
REMARK 465 GLU A 387
REMARK 465 ASN A 532
REMARK 465 ALA A 533
REMARK 465 GLU A 534
REMARK 465 ASP A 535
REMARK 465 THR A 536
REMARK 465 ASP A 537
REMARK 465 ALA A 538
REMARK 465 SER A 539
REMARK 465 GLU A 540
REMARK 465 GLU A 541
REMARK 465 ALA A 542
REMARK 465 GLU A 543
REMARK 465 GLU A 544
REMARK 465 ASP A 571
REMARK 465 GLY A 572
REMARK 465 LYS A 573
REMARK 465 ASP A 774
REMARK 465 LEU A 775
REMARK 465 GLY A 776
REMARK 465 THR A 777
REMARK 465 ALA A 778
REMARK 465 ARG A 779
REMARK 465 GLY A 780
REMARK 465 LEU A 781
REMARK 465 SER A 782
REMARK 465 GLU A 783
REMARK 465 ASP A 929
REMARK 465 LEU A 930
REMARK 465 GLY A 931
REMARK 465 ASP A 932
REMARK 465 LEU A 933
REMARK 465 ALA A 934
REMARK 465 GLY A 935
REMARK 465 VAL A 936
REMARK 465 PRO A 937
REMARK 465 ALA A 938
REMARK 465 LEU A 959
REMARK 465 LEU A 960
REMARK 465 ASP A 961
REMARK 465 ASP A 962
REMARK 465 ASP A 963
REMARK 465 LEU A 964
REMARK 465 GLU A 965
REMARK 465 GLU A 966
REMARK 465 ARG A 967
REMARK 465 MET A 968
REMARK 465 GLU A 969
REMARK 465 GLU A 970
REMARK 465 LYS A 971
REMARK 465 PRO A 985
REMARK 465 GLY A 986
REMARK 465 SER A 987
REMARK 465 GLU A 1018
REMARK 465 ILE A 1019
REMARK 465 LYS A 1020
REMARK 465 ARG A 1021
REMARK 465 LYS A 1022
REMARK 465 ARG A 1023
REMARK 465 GLU A 1024
REMARK 465 TYR A 1025
REMARK 465 GLU A 1026
REMARK 465 ALA A 1033
REMARK 465 PRO A 1034
REMARK 465 VAL A 1035
REMARK 465 LYS A 1036
REMARK 465 PRO A 1037
REMARK 465 ALA A 1038
REMARK 465 ASP A 1039
REMARK 465 GLY A 1040
REMARK 465 SER A 1041
REMARK 465 ILE A 1042
REMARK 465 LEU A 1043
REMARK 465 LYS A 1181
REMARK 465 PHE A 1182
REMARK 465 GLN A 1183
REMARK 465 HIS A 1184
REMARK 465 MET B 1
REMARK 465 GLY B 446
REMARK 465 ASP B 447
REMARK 465 ARG B 448
REMARK 465 PHE B 449
REMARK 465 GLN B 450
REMARK 465 TYR B 451
REMARK 465 ARG B 452
REMARK 465 ARG B 453
REMARK 465 PHE B 454
REMARK 465 VAL B 455
REMARK 465 SER B 456
REMARK 465 LEU B 457
REMARK 465 ASP B 458
REMARK 465 ASP B 459
REMARK 465 ASP B 460
REMARK 465 PHE B 461
REMARK 465 ALA B 462
REMARK 465 GLN B 463
REMARK 465 MET B 1115
REMARK 465 LYS B 1116
REMARK 465 ASN B 1117
REMARK 465 LYS B 1118
REMARK 465 THR B 1119
REMARK 465 PRO B 1120
REMARK 465 CYS B 1121
REMARK 465 THR B 1122
REMARK 465 TYR B 1123
REMARK 465 ASP B 1161
REMARK 465 GLY B 1162
REMARK 465 ASN B 1163
REMARK 465 GLU B 1164
REMARK 465 HIS B 1165
REMARK 465 SER B 1166
REMARK 465 DT X 1
REMARK 465 DC X 2
REMARK 465 DA X 13
REMARK 465 DC X 14
REMARK 465 DT X 15
REMARK 465 DG X 16
REMARK 465 DC X 17
REMARK 465 DT X 18
REMARK 465 DA X 19
REMARK 465 DT X 20
REMARK 465 DT X 21
REMARK 465 DC X 22
REMARK 465 DC X 23
REMARK 465 DC X 24
REMARK 465 DT X 25
REMARK 465 DA X 26
REMARK 465 DG X 27
REMARK 465 DC X 28
REMARK 465 DA X 29
REMARK 465 DG X 30
REMARK 465 DT X 31
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DA X 4 O4' - C1' - N9 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DA X 5 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG X 9 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DA X 43 O4' - C1' - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 DT X 44 C3' - C2' - C1' ANGL. DEV. = -5.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 52 -86.49 -45.60
REMARK 500 ILE A 124 -167.74 -105.07
REMARK 500 ARG A 172 -4.32 98.13
REMARK 500 ALA A 283 -71.27 -77.24
REMARK 500 PRO A 390 97.37 -62.95
REMARK 500 SER A 391 170.69 -57.39
REMARK 500 THR A 430 -156.84 -111.65
REMARK 500 LEU A 448 31.40 75.87
REMARK 500 GLU A 502 -11.51 65.46
REMARK 500 GLN A 508 -4.11 76.22
REMARK 500 ASP A 521 -165.32 -108.90
REMARK 500 PHE A 567 69.55 35.31
REMARK 500 TYR A 582 -33.66 71.37
REMARK 500 GLU A 600 -70.25 -50.58
REMARK 500 THR A 614 -77.13 -102.90
REMARK 500 SER A 615 -167.32 -113.67
REMARK 500 ARG A 771 -87.04 -112.03
REMARK 500 LYS A 797 -144.98 49.96
REMARK 500 ASN A 819 -47.73 -140.97
REMARK 500 LYS A 820 -176.39 -67.43
REMARK 500 LYS A 885 -63.92 -108.52
REMARK 500 ASP A 902 4.24 104.36
REMARK 500 TRP A 903 -64.34 78.31
REMARK 500 ARG A 914 -51.46 -129.04
REMARK 500 HIS A 927 -71.82 -58.92
REMARK 500 PRO A 946 63.23 -64.76
REMARK 500 SER A 956 -13.66 74.69
REMARK 500 ARG A 980 -69.81 -138.10
REMARK 500 ILE A1178 -79.43 -122.69
REMARK 500 ILE B 61 -42.44 -131.88
REMARK 500 GLU B 101 -71.36 -76.28
REMARK 500 VAL B 109 -53.58 -132.18
REMARK 500 ASP B 178 -14.71 76.26
REMARK 500 PHE B 252 38.41 -94.97
REMARK 500 GLU B 298 -79.04 -83.25
REMARK 500 ALA B 299 118.83 -35.71
REMARK 500 PRO B 301 70.08 -69.32
REMARK 500 GLU B 310 -55.97 -145.32
REMARK 500 ASN B 416 -12.61 64.73
REMARK 500 HIS B 537 -72.81 -68.57
REMARK 500 ASP B 594 -78.90 -112.14
REMARK 500 ALA B 609 32.59 -76.77
REMARK 500 SER B 641 -79.38 -54.34
REMARK 500 PHE B 767 73.85 -111.74
REMARK 500 ASN B 770 105.30 -55.06
REMARK 500 GLU B 786 -76.12 -65.91
REMARK 500 CYS B 801 115.41 -177.11
REMARK 500 GLN B 872 72.47 42.22
REMARK 500 ILE B 912 -71.50 -79.66
REMARK 500 LYS B 932 159.67 -47.97
REMARK 500
REMARK 500 THIS ENTRY HAS 53 RAMACHANDRAN OUTLIERS.
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 SO4 B 1167
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO X 49
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3U44 RELATED DB: PDB
REMARK 900 WITH FES4 CLUSTER
DBREF 3U4Q A 1 1232 UNP P23478 ADDA_BACSU 1 1232
DBREF 3U4Q B 1 1166 UNP P23477 ADDB_BACSU 1 1166
DBREF 3U4Q X 1 48 PDB 3U4Q 3U4Q 1 48
SEQADV 3U4Q GLY A 780 UNP P23478 ALA 780 CONFLICT
SEQADV 3U4Q ALA A 1172 UNP P23478 ASP 1172 ENGINEERED MUTATION
SEQADV 3U4Q ASP B 843 UNP P23477 GLU 843 CONFLICT
SEQADV 3U4Q GLU B 844 UNP P23477 GLN 844 CONFLICT
SEQADV 3U4Q ALA B 961 UNP P23477 ASP 961 ENGINEERED MUTATION
SEQRES 1 A 1232 MET ASN ILE PRO LYS PRO ALA ASP SER THR TRP THR ASP
SEQRES 2 A 1232 ASP GLN TRP ASN ALA ILE VAL SER THR GLY GLN ASP ILE
SEQRES 3 A 1232 LEU VAL ALA ALA ALA ALA GLY SER GLY LYS THR ALA VAL
SEQRES 4 A 1232 LEU VAL GLU ARG MET ILE ARG LYS ILE THR ALA GLU GLU
SEQRES 5 A 1232 ASN PRO ILE ASP VAL ASP ARG LEU LEU VAL VAL THR PHE
SEQRES 6 A 1232 THR ASN ALA SER ALA ALA GLU MET LYS HIS ARG ILE ALA
SEQRES 7 A 1232 GLU ALA LEU GLU LYS GLU LEU VAL GLN ARG PRO GLY SER
SEQRES 8 A 1232 LEU HIS ILE ARG ARG GLN LEU SER LEU LEU ASN ARG ALA
SEQRES 9 A 1232 SER ILE SER THR LEU HIS SER PHE CYS LEU GLN VAL LEU
SEQRES 10 A 1232 LYS LYS TYR TYR TYR LEU ILE ASP LEU ASP PRO GLY PHE
SEQRES 11 A 1232 ARG ILE ALA ASP GLN THR GLU GLY GLU LEU ILE GLY ASP
SEQRES 12 A 1232 GLU VAL LEU ASP GLU LEU PHE GLU ASP GLU TYR ALA LYS
SEQRES 13 A 1232 GLY GLU LYS ALA PHE PHE GLU LEU VAL ASP ARG TYR THR
SEQRES 14 A 1232 THR ASP ARG HIS ASP LEU ASP LEU GLN PHE LEU VAL LYS
SEQRES 15 A 1232 GLN VAL TYR GLU TYR SER ARG SER HIS PRO ASN PRO GLU
SEQRES 16 A 1232 ALA TRP LEU GLU SER PHE VAL HIS LEU TYR ASP VAL SER
SEQRES 17 A 1232 GLU LYS SER ALA ILE GLU GLU LEU PRO PHE TYR GLN TYR
SEQRES 18 A 1232 VAL LYS GLU ASP ILE ALA MET VAL LEU ASN GLY ALA LYS
SEQRES 19 A 1232 GLU LYS LEU LEU ARG ALA LEU GLU LEU THR LYS ALA PRO
SEQRES 20 A 1232 GLY GLY PRO ALA PRO ARG ALA ASP ASN PHE LEU ASP ASP
SEQRES 21 A 1232 LEU ALA GLN ILE ASP GLU LEU ILE GLN HIS GLN ASP ASP
SEQRES 22 A 1232 PHE SER GLU LEU TYR LYS ARG VAL PRO ALA VAL SER PHE
SEQRES 23 A 1232 LYS ARG ALA LYS ALA VAL LYS GLY ASP GLU PHE ASP PRO
SEQRES 24 A 1232 ALA LEU LEU ASP GLU ALA THR ASP LEU ARG ASN GLY ALA
SEQRES 25 A 1232 LYS LYS LEU LEU GLU LYS LEU LYS THR ASP TYR PHE THR
SEQRES 26 A 1232 ARG SER PRO GLU GLN HIS LEU LYS SER LEU ALA GLU MET
SEQRES 27 A 1232 LYS PRO VAL ILE GLU THR LEU VAL GLN LEU VAL ILE SER
SEQRES 28 A 1232 TYR GLY LYS ARG PHE GLU ALA ALA LYS GLN GLU LYS SER
SEQRES 29 A 1232 ILE ILE ASP PHE SER ASP LEU GLU HIS TYR CYS LEU ALA
SEQRES 30 A 1232 ILE LEU THR ALA GLU ASN ASP LYS GLY GLU ARG GLU PRO
SEQRES 31 A 1232 SER GLU ALA ALA ARG PHE TYR GLN GLU GLN PHE HIS GLU
SEQRES 32 A 1232 VAL LEU VAL ASP GLU TYR GLN ASP THR ASN LEU VAL GLN
SEQRES 33 A 1232 GLU SER ILE LEU GLN LEU VAL THR SER GLY PRO GLU GLU
SEQRES 34 A 1232 THR GLY ASN LEU PHE MET VAL GLY ASP VAL LYS GLN SER
SEQRES 35 A 1232 ILE TYR ARG PHE ARG LEU ALA GLU PRO LEU LEU PHE LEU
SEQRES 36 A 1232 SER LYS TYR LYS ARG PHE THR GLU SER GLY GLU GLY THR
SEQRES 37 A 1232 GLY ARG LYS ILE ASP LEU ASN LYS ASN PHE ARG SER ARG
SEQRES 38 A 1232 ALA ASP ILE LEU ASP SER THR ASN PHE LEU PHE LYS GLN
SEQRES 39 A 1232 LEU MET GLY GLY LYS ILE GLY GLU VAL ASP TYR ASP GLU
SEQRES 40 A 1232 GLN ALA GLU LEU LYS LEU GLY ALA ALA TYR PRO ASP ASN
SEQRES 41 A 1232 ASP GLU THR GLU THR GLU LEU LEU LEU ILE ASP ASN ALA
SEQRES 42 A 1232 GLU ASP THR ASP ALA SER GLU GLU ALA GLU GLU LEU GLU
SEQRES 43 A 1232 THR VAL GLN PHE GLU ALA LYS ALA ILE ALA LYS GLU ILE
SEQRES 44 A 1232 ARG LYS LEU ILE SER SER PRO PHE LYS VAL TYR ASP GLY
SEQRES 45 A 1232 LYS LYS LYS THR HIS ARG ASN ILE GLN TYR ARG ASP ILE
SEQRES 46 A 1232 VAL ILE LEU LEU ARG SER MET PRO TRP ALA PRO GLN ILE
SEQRES 47 A 1232 MET GLU GLU LEU ARG ALA GLN GLY ILE PRO VAL TYR ALA
SEQRES 48 A 1232 ASN LEU THR SER GLY TYR PHE GLU ALA VAL GLU VAL ALA
SEQRES 49 A 1232 VAL ALA LEU SER VAL LEU LYS VAL ILE ASP ASN PRO TYR
SEQRES 50 A 1232 GLN ASP ILE PRO LEU ALA SER VAL LEU ARG SER PRO ILE
SEQRES 51 A 1232 VAL GLY ALA ASP GLU ASN GLU LEU SER LEU ILE ARG LEU
SEQRES 52 A 1232 GLU ASN LYS LYS ALA PRO TYR TYR GLU ALA MET LYS ASP
SEQRES 53 A 1232 TYR LEU ALA ALA GLY ASP ARG SER ASP GLU LEU TYR GLN
SEQRES 54 A 1232 LYS LEU ASN THR PHE TYR GLY HIS LEU GLN LYS TRP ARG
SEQRES 55 A 1232 ALA PHE SER LYS ASN HIS SER VAL SER GLU LEU ILE TRP
SEQRES 56 A 1232 GLU VAL TYR ARG ASP THR LYS TYR MET ASP TYR VAL GLY
SEQRES 57 A 1232 GLY MET PRO GLY GLY LYS GLN ARG GLN ALA ASN LEU ARG
SEQRES 58 A 1232 VAL LEU TYR ASP ARG ALA ARG GLN TYR GLU SER THR ALA
SEQRES 59 A 1232 PHE ARG GLY LEU PHE ARG PHE LEU ARG PHE ILE GLU ARG
SEQRES 60 A 1232 MET GLN GLU ARG GLY ASP ASP LEU GLY THR ALA ARG GLY
SEQRES 61 A 1232 LEU SER GLU GLN GLU ASP VAL VAL ARG LEU MET THR ILE
SEQRES 62 A 1232 HIS SER SER LYS GLY LEU GLU PHE PRO VAL VAL PHE VAL
SEQRES 63 A 1232 ALA GLY LEU GLY ARG ASN PHE ASN MET MET ASP LEU ASN
SEQRES 64 A 1232 LYS SER TYR LEU LEU ASP LYS GLU LEU GLY PHE GLY THR
SEQRES 65 A 1232 LYS TYR ILE HIS PRO GLN LEU ARG ILE SER TYR PRO THR
SEQRES 66 A 1232 LEU PRO LEU ILE ALA MET LYS LYS LYS MET ARG ARG GLU
SEQRES 67 A 1232 LEU LEU SER GLU GLU LEU ARG VAL LEU TYR VAL ALA LEU
SEQRES 68 A 1232 THR ARG ALA LYS GLU LYS LEU PHE LEU ILE GLY SER CYS
SEQRES 69 A 1232 LYS ASP HIS GLN LYS GLN LEU ALA LYS TRP GLN ALA SER
SEQRES 70 A 1232 ALA SER GLN THR ASP TRP LEU LEU PRO GLU PHE ASP ARG
SEQRES 71 A 1232 TYR GLN ALA ARG THR TYR LEU ASP PHE ILE GLY PRO ALA
SEQRES 72 A 1232 LEU ALA ARG HIS ARG ASP LEU GLY ASP LEU ALA GLY VAL
SEQRES 73 A 1232 PRO ALA HIS ALA ASP ILE SER GLY HIS PRO ALA ARG PHE
SEQRES 74 A 1232 ALA VAL GLN MET ILE HIS SER TYR ASP LEU LEU ASP ASP
SEQRES 75 A 1232 ASP LEU GLU GLU ARG MET GLU GLU LYS SER GLU ARG LEU
SEQRES 76 A 1232 GLU ALA ILE ARG ARG GLY GLU PRO VAL PRO GLY SER PHE
SEQRES 77 A 1232 ALA PHE ASP GLU LYS ALA ARG GLU GLN LEU SER TRP THR
SEQRES 78 A 1232 TYR PRO HIS GLN GLU VAL THR GLN ILE ARG THR LYS GLN
SEQRES 79 A 1232 SER VAL SER GLU ILE LYS ARG LYS ARG GLU TYR GLU ASP
SEQRES 80 A 1232 GLU TYR SER GLY ARG ALA PRO VAL LYS PRO ALA ASP GLY
SEQRES 81 A 1232 SER ILE LEU TYR ARG ARG PRO ALA PHE MET MET LYS LYS
SEQRES 82 A 1232 GLY LEU THR ALA ALA GLU LYS GLY THR ALA MET HIS THR
SEQRES 83 A 1232 VAL MET GLN HIS ILE PRO LEU SER HIS VAL PRO SER ILE
SEQRES 84 A 1232 GLU GLU ALA GLU GLN THR VAL HIS ARG LEU TYR GLU LYS
SEQRES 85 A 1232 GLU LEU LEU THR GLU GLU GLN LYS ASP ALA ILE ASP ILE
SEQRES 86 A 1232 GLU GLU ILE VAL GLN PHE PHE HIS THR GLU ILE GLY GLY
SEQRES 87 A 1232 GLN LEU ILE GLY ALA LYS TRP LYS ASP ARG GLU ILE PRO
SEQRES 88 A 1232 PHE SER LEU ALA LEU PRO ALA LYS GLU ILE TYR PRO ASP
SEQRES 89 A 1232 ALA HIS GLU ALA ASP GLU PRO LEU LEU VAL GLN GLY ILE
SEQRES 90 A 1232 ILE ASP CYS LEU TYR GLU THR GLU ASP GLY LEU TYR LEU
SEQRES 91 A 1232 LEU ALA TYR LYS SER ASP ARG ILE GLU GLY LYS PHE GLN
SEQRES 92 A 1232 HIS GLY PHE GLU GLY ALA ALA PRO ILE LEU LYS LYS ARG
SEQRES 93 A 1232 TYR GLU THR GLN ILE GLN LEU TYR THR LYS ALA VAL GLU
SEQRES 94 A 1232 GLN ILE ALA LYS THR LYS VAL LYS GLY CYS ALA LEU TYR
SEQRES 95 A 1232 PHE PHE ASP GLY GLY HIS ILE LEU THR LEU
SEQRES 1 B 1166 MET GLY ALA GLU PHE LEU VAL GLY ARG SER GLY SER GLY
SEQRES 2 B 1166 LYS THR LYS LEU ILE ILE ASN SER ILE GLN ASP GLU LEU
SEQRES 3 B 1166 ARG ARG ALA PRO PHE GLY LYS PRO ILE ILE PHE LEU VAL
SEQRES 4 B 1166 PRO ASP GLN MET THR PHE LEU MET GLU TYR GLU LEU ALA
SEQRES 5 B 1166 LYS THR PRO ASP MET GLY GLY MET ILE ARG ALA GLN VAL
SEQRES 6 B 1166 PHE SER PHE SER ARG LEU ALA TRP ARG VAL LEU GLN HIS
SEQRES 7 B 1166 THR GLY GLY MET SER ARG PRO PHE LEU THR SER THR GLY
SEQRES 8 B 1166 VAL GLN MET LEU LEU ARG LYS LEU ILE GLU GLU HIS LYS
SEQRES 9 B 1166 GLN GLU PHE LYS VAL TYR GLN LYS ALA SER ASP LYS SER
SEQRES 10 B 1166 GLY PHE THR ALA GLN VAL GLU ARG MET LEU THR GLU PHE
SEQRES 11 B 1166 LYS ARG TYR CYS LEU GLU PRO GLU ASP ILE ARG ARG MET
SEQRES 12 B 1166 ALA GLU SER GLY THR ALA SER GLU TYR ARG GLY GLU ARG
SEQRES 13 B 1166 VAL LEU SER GLU LYS LEU HIS ASP LEU SER ILE LEU TYR
SEQRES 14 B 1166 GLN GLN MET GLU LYS SER LEU ALA ASP GLN TYR LEU HIS
SEQRES 15 B 1166 SER GLU ASP TYR LEU THR LEU LEU ALA GLU HIS ILE PRO
SEQRES 16 B 1166 LEU ALA GLU ASP ILE LYS GLY ALA HIS ILE TYR VAL ASP
SEQRES 17 B 1166 GLY PHE TYR GLN PHE THR PRO GLN GLU PHE ARG VAL LEU
SEQRES 18 B 1166 GLU GLN LEU MET VAL HIS ALA GLU HIS ILE THR PHE SER
SEQRES 19 B 1166 LEU THR ALA ASP LYS PRO SER TYR GLU ARG GLU PRO HIS
SEQRES 20 B 1166 GLU LEU GLU LEU PHE ARG MET THR GLY LYS THR TYR TYR
SEQRES 21 B 1166 ARG LEU HIS GLN LYS ALA LYS GLU LEU ASN LEU ASP ILE
SEQRES 22 B 1166 THR TYR LYS GLU LEU SER GLY THR GLU ARG HIS THR LYS
SEQRES 23 B 1166 THR PRO GLU LEU ALA HIS LEU GLU ALA GLN TYR GLU ALA
SEQRES 24 B 1166 ARG PRO ALA ILE PRO TYR ALA GLU LYS GLN GLU ALA LEU
SEQRES 25 B 1166 THR VAL MET GLN ALA ALA ASN ARG ARG ALA GLU LEU GLU
SEQRES 26 B 1166 GLY ILE ALA ARG GLU ILE HIS ALA LEU VAL ARG GLU LYS
SEQRES 27 B 1166 GLY TYR ARG TYR LYS ASP VAL ALA ILE LEU ALA ARG GLN
SEQRES 28 B 1166 PRO GLU ASP TYR LYS ASP MET VAL LYS GLU VAL PHE ALA
SEQRES 29 B 1166 ASP TYR GLU ILE PRO TYR PHE ILE ASP GLY LYS ALA SER
SEQRES 30 B 1166 MET LEU ASN HIS PRO LEU ILE GLU PHE ILE ARG SER SER
SEQRES 31 B 1166 LEU ASP VAL LEU LYS GLY ASN TRP ARG TYR GLU ALA VAL
SEQRES 32 B 1166 PHE ARG CYS VAL LYS THR GLU LEU LEU PHE PRO LEU ASN
SEQRES 33 B 1166 GLU PRO LYS ALA LYS VAL ARG GLU GLN VAL ASP GLN LEU
SEQRES 34 B 1166 GLU ASN TYR CYS ILE ALA TYR GLY ILE LYS GLY ASP ARG
SEQRES 35 B 1166 TRP THR LYS GLY ASP ARG PHE GLN TYR ARG ARG PHE VAL
SEQRES 36 B 1166 SER LEU ASP ASP ASP PHE ALA GLN THR ASP GLN GLU ILE
SEQRES 37 B 1166 GLU MET GLU ASN MET LEU ASN ASP THR ARG ASP TRP ILE
SEQRES 38 B 1166 VAL PRO PRO LEU PHE GLN LEU GLN LYS ARG MET LYS LYS
SEQRES 39 B 1166 ALA LYS THR VAL GLN GLU LYS ALA GLU ALA LEU TYR ARG
SEQRES 40 B 1166 TYR LEU GLU GLU THR ASP VAL PRO LEU LYS LEU ASP GLN
SEQRES 41 B 1166 GLU ARG GLN ARG ALA GLU ASP ASP GLY ARG ILE ILE GLU
SEQRES 42 B 1166 ALA GLN GLN HIS GLN GLN ALA TRP ASP ALA VAL ILE GLN
SEQRES 43 B 1166 LEU LEU GLU GLU PHE VAL GLU MET MET GLY ASP ASP GLU
SEQRES 44 B 1166 ILE SER LEU ASP LEU PHE GLN GLN MET ILE GLU ALA GLY
SEQRES 45 B 1166 ALA GLU SER LEU THR PHE SER LEU ILE PRO PRO ALA LEU
SEQRES 46 B 1166 ASP GLN VAL PHE VAL GLY ASN MET ASP LEU SER ARG MET
SEQRES 47 B 1166 TYR GLY THR SER CYS THR PHE VAL LEU GLY ALA ASN ASP
SEQRES 48 B 1166 GLY VAL LEU PRO ALA ARG PRO ASP GLU ASN GLY VAL LEU
SEQRES 49 B 1166 SER ASP ASP ASP ARG GLU TRP LEU LYS THR ILE GLY VAL
SEQRES 50 B 1166 GLU LEU SER SER GLY GLY ARG GLU ARG LEU LEU ASP GLU
SEQRES 51 B 1166 HIS PHE LEU ILE TYR MET ALA PHE SER SER PRO SER ASP
SEQRES 52 B 1166 ARG LEU TYR VAL SER TYR PRO ILE ALA ASP ALA GLU GLY
SEQRES 53 B 1166 LYS THR LEU LEU PRO SER MET ILE VAL LYS ARG LEU GLU
SEQRES 54 B 1166 GLU LEU PHE PRO HIS HIS LYS GLU ARG LEU LEU THR ASN
SEQRES 55 B 1166 GLU PRO GLU GLN VAL SER ASP GLU GLU GLN LEU MET TYR
SEQRES 56 B 1166 VAL VAL ASN LYS SER VAL ALA GLN SER PHE THR ALA SER
SEQRES 57 B 1166 GLN LEU ARG LEU TRP THR ARG GLU TYR ASP ILE SER ASP
SEQRES 58 B 1166 VAL TRP TRP SER THR TYR ASN VAL LEU MET SER GLU GLN
SEQRES 59 B 1166 ASP ARG LEU GLN SER LYS LYS LEU PHE SER SER LEU PHE
SEQRES 60 B 1166 PHE ARG ASN GLU VAL LYS GLN LEU GLU ARG SER VAL SER
SEQRES 61 B 1166 ARG GLN LEU TYR GLY GLU ARG ILE GLN GLY SER VAL SER
SEQRES 62 B 1166 ARG MET GLU THR PHE ASN ALA CYS PRO PHE SER HIS PHE
SEQRES 63 B 1166 ALA SER HIS GLY LEU HIS LEU LYS GLU ARG GLN PHE PHE
SEQRES 64 B 1166 LYS LEU GLU ALA PRO ASP ILE GLY GLN LEU PHE HIS SER
SEQRES 65 B 1166 SER LEU LYS LEU ILE SER ASP ARG LEU ARG ASP GLU LYS
SEQRES 66 B 1166 LEU ASP TRP ARG ASP LEU THR LYS GLU GLN CYS GLU LEU
SEQRES 67 B 1166 PHE SER TYR ASP ALA VAL GLU ARG LEU ALA PRO LYS LEU
SEQRES 68 B 1166 GLN LYS GLU ILE LEU LEU SER SER ASN ARG HIS TYR TYR
SEQRES 69 B 1166 VAL LYS GLU LYS LEU GLN LYS ILE VAL THR ARG VAL SER
SEQRES 70 B 1166 GLY ILE LEU SER GLU HIS ALA LYS ALA SER GLY PHE VAL
SEQRES 71 B 1166 PRO ILE GLY LEU GLU LEU GLY PHE GLY GLY LYS GLY PRO
SEQRES 72 B 1166 LEU PRO PRO LEU THR PHE GLN LEU LYS ASN GLY CYS THR
SEQRES 73 B 1166 MET GLU LEU VAL GLY ARG ILE ASP ARG VAL ASP LYS ALA
SEQRES 74 B 1166 GLU SER SER LYS GLY LEU LEU LEU ARG ILE VAL ALA TYR
SEQRES 75 B 1166 LYS SER SER ASP LYS GLY LEU ASP LEU ALA GLU VAL TYR
SEQRES 76 B 1166 TYR GLY LEU ALA LEU GLN MET LEU THR TYR LEU ASP LEU
SEQRES 77 B 1166 SER ILE THR HIS SER ALA ASP TRP LEU GLY MET ARG ALA
SEQRES 78 B 1166 THR PRO ALA GLY VAL LEU TYR PHE HIS ILE HIS ASP PRO
SEQRES 79 B 1166 MET ILE GLN SER ASN LEU PRO LEU GLY LEU ASP GLU ILE
SEQRES 80 B 1166 GLU GLN GLU ILE PHE LYS LYS PHE LYS MET LYS GLY LEU
SEQRES 81 B 1166 LEU LEU GLY ASP GLN GLU VAL VAL ARG LEU MET ASP THR
SEQRES 82 B 1166 THR LEU GLN GLU GLY ARG SER ASN ILE ILE ASN ALA GLY
SEQRES 83 B 1166 LEU LYS LYS ASP GLY SER LEU ARG SER ASP SER ALA ALA
SEQRES 84 B 1166 VAL GLY GLU LYS GLU PHE ASP LEU LEU THR LYS HIS VAL
SEQRES 85 B 1166 ARG ARG THR PHE GLN GLU ALA GLY GLU GLN ILE THR ASP
SEQRES 86 B 1166 GLY ARG VAL SER ILE GLU PRO TYR LYS MET LYS ASN LYS
SEQRES 87 B 1166 THR PRO CYS THR TYR CYS ALA PHE LYS SER VAL CYS GLN
SEQRES 88 B 1166 PHE ASP GLU SER LEU GLU GLU ASN GLU TYR ARG PRO LEU
SEQRES 89 B 1166 LYS ALA GLU LYS ASP LYS THR ILE LEU GLU TRP ILE LYS
SEQRES 90 B 1166 LYS GLU ALA ASP GLY ASN GLU HIS SER
SEQRES 1 X 48 DT DC DT DA DA DT DG DC DG DA DG DC DA
SEQRES 2 X 48 DC DT DG DC DT DA DT DT DC DC DC DT DA
SEQRES 3 X 48 DG DC DA DG DT DG DC DT DC DG DC DA DT
SEQRES 4 X 48 DT DA DG DA DT DT DT DT DG
HET SO4 B1167 5
HET EDO X 49 4
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 SO4 O4 S 2-
FORMUL 5 EDO C2 H6 O2
FORMUL 6 HOH *189(H2 O)
HELIX 1 1 THR A 12 SER A 21 1 10
HELIX 2 2 GLY A 35 THR A 49 1 15
HELIX 3 3 ASP A 56 ASP A 58 5 3
HELIX 4 4 THR A 66 ARG A 88 1 23
HELIX 5 5 SER A 91 LEU A 101 1 11
HELIX 6 6 THR A 108 TYR A 121 1 14
HELIX 7 7 TYR A 122 ILE A 124 5 3
HELIX 8 8 ASP A 134 GLY A 157 1 24
HELIX 9 9 GLU A 158 THR A 169 1 12
HELIX 10 10 ASP A 174 ARG A 189 1 16
HELIX 11 11 ASN A 193 SER A 200 1 8
HELIX 12 12 PHE A 201 ASP A 206 1 6
HELIX 13 13 PHE A 218 THR A 244 1 27
HELIX 14 14 ASN A 256 HIS A 270 1 15
HELIX 15 15 ASP A 273 VAL A 284 1 12
HELIX 16 16 PRO A 299 ALA A 305 1 7
HELIX 17 17 THR A 306 PHE A 324 1 19
HELIX 18 18 SER A 327 LYS A 363 1 37
HELIX 19 19 ASP A 367 THR A 380 1 14
HELIX 20 20 SER A 391 PHE A 401 1 11
HELIX 21 21 GLU A 408 THR A 412 5 5
HELIX 22 22 ASN A 413 THR A 424 1 12
HELIX 23 23 ASP A 438 SER A 442 5 5
HELIX 24 24 PRO A 451 PHE A 461 1 11
HELIX 25 25 ARG A 481 GLN A 494 1 14
HELIX 26 26 GLY A 497 GLU A 502 1 6
HELIX 27 27 GLU A 546 SER A 564 1 19
HELIX 28 28 TRP A 594 GLN A 605 1 12
HELIX 29 29 ALA A 620 ASN A 635 1 16
HELIX 30 30 GLN A 638 SER A 648 1 11
HELIX 31 31 ASP A 654 LEU A 663 1 10
HELIX 32 32 PRO A 669 GLY A 681 1 13
HELIX 33 33 ASP A 685 HIS A 708 1 24
HELIX 34 34 SER A 709 LYS A 722 1 14
HELIX 35 35 LYS A 722 GLY A 728 1 7
HELIX 36 36 GLY A 732 GLU A 751 1 20
HELIX 37 37 GLY A 757 ARG A 771 1 15
HELIX 38 38 HIS A 794 SER A 796 5 3
HELIX 39 39 THR A 845 ARG A 873 1 29
HELIX 40 40 ASP A 886 ALA A 898 1 13
HELIX 41 41 TYR A 916 ARG A 926 1 11
HELIX 42 42 ALA A 940 HIS A 945 1 6
HELIX 43 43 GLU A 973 ARG A 979 1 7
HELIX 44 44 PHE A 990 TRP A 1000 1 11
HELIX 45 45 HIS A 1004 THR A 1008 5 5
HELIX 46 46 THR A 1056 GLN A 1069 1 14
HELIX 47 47 SER A 1078 LYS A 1092 1 15
HELIX 48 48 THR A 1096 ILE A 1103 1 8
HELIX 49 49 ASP A 1104 GLN A 1110 1 7
HELIX 50 50 PHE A 1111 HIS A 1113 5 3
HELIX 51 51 THR A 1114 GLY A 1122 1 9
HELIX 52 52 LYS A 1139 ILE A 1141 5 3
HELIX 53 53 ALA A 1189 TYR A 1197 1 9
HELIX 54 54 TYR A 1197 LYS A 1213 1 17
HELIX 55 55 GLY B 13 ALA B 29 1 17
HELIX 56 56 PRO B 40 GLN B 42 5 3
HELIX 57 57 MET B 43 ALA B 52 1 10
HELIX 58 58 SER B 67 GLY B 80 1 14
HELIX 59 59 THR B 88 HIS B 103 1 16
HELIX 60 60 LYS B 104 PHE B 107 5 4
HELIX 61 61 SER B 117 TYR B 133 1 17
HELIX 62 62 GLU B 136 GLU B 145 1 10
HELIX 63 63 GLY B 154 LEU B 176 1 23
HELIX 64 64 ASP B 185 ILE B 194 1 10
HELIX 65 65 ALA B 197 LYS B 201 5 5
HELIX 66 66 THR B 214 ALA B 228 1 15
HELIX 67 67 PHE B 252 LEU B 269 1 18
HELIX 68 68 THR B 287 GLN B 296 1 10
HELIX 69 69 ASN B 319 GLU B 337 1 19
HELIX 70 70 ARG B 341 LYS B 343 5 3
HELIX 71 71 GLN B 351 ASP B 354 5 4
HELIX 72 72 TYR B 355 TYR B 366 1 12
HELIX 73 73 HIS B 381 GLY B 396 1 16
HELIX 74 74 ARG B 399 LYS B 408 1 10
HELIX 75 75 PRO B 418 GLY B 437 1 20
HELIX 76 76 GLY B 440 LYS B 445 1 6
HELIX 77 77 ASP B 465 ALA B 495 1 31
HELIX 78 78 THR B 497 THR B 512 1 16
HELIX 79 79 ASP B 513 ASP B 528 1 16
HELIX 80 80 ARG B 530 MET B 555 1 26
HELIX 81 81 SER B 561 LEU B 576 1 16
HELIX 82 82 SER B 625 ILE B 635 1 11
HELIX 83 83 ARG B 644 SER B 659 1 16
HELIX 84 84 SER B 682 PHE B 692 1 11
HELIX 85 85 GLU B 703 VAL B 707 5 5
HELIX 86 86 SER B 708 LEU B 713 1 6
HELIX 87 87 ASN B 718 ARG B 735 1 18
HELIX 88 88 ASP B 741 MET B 751 1 11
HELIX 89 89 ASP B 755 SER B 764 1 10
HELIX 90 90 GLU B 776 TYR B 784 1 9
HELIX 91 91 SER B 791 CYS B 801 1 11
HELIX 92 92 CYS B 801 HIS B 809 1 9
HELIX 93 93 ALA B 823 GLU B 844 1 22
HELIX 94 94 ASP B 847 LEU B 851 5 5
HELIX 95 95 THR B 852 ALA B 868 1 17
HELIX 96 96 PRO B 869 LEU B 871 5 3
HELIX 97 97 GLU B 874 SER B 879 1 6
HELIX 98 98 SER B 879 LYS B 905 1 27
HELIX 99 99 ASP B 970 TYR B 976 1 7
HELIX 100 100 LEU B 980 GLY B 998 1 19
HELIX 101 101 GLY B 1023 LYS B 1034 1 12
HELIX 102 102 ASP B 1044 ASP B 1052 1 9
HELIX 103 103 GLY B 1081 ASP B 1105 1 25
HELIX 104 104 PHE B 1126 GLN B 1131 1 6
HELIX 105 105 LYS B 1148 ALA B 1160 1 13
SHEET 1 A 6 SER A 105 SER A 107 0
SHEET 2 A 6 LEU A 60 VAL A 63 1 N VAL A 62 O SER A 105
SHEET 3 A 6 GLU A 403 VAL A 406 1 O LEU A 405 N VAL A 63
SHEET 4 A 6 LEU A 433 GLY A 437 1 O PHE A 434 N VAL A 406
SHEET 5 A 6 ILE A 26 ALA A 30 1 N VAL A 28 O MET A 435
SHEET 6 A 6 ARG A 470 LEU A 474 1 O ILE A 472 N ALA A 29
SHEET 1 B 2 ARG A 131 ILE A 132 0
SHEET 2 B 2 ILE A 365 ILE A 366 1 O ILE A 366 N ARG A 131
SHEET 1 C 2 LYS A 476 ASN A 477 0
SHEET 2 C 2 LYS A 512 LEU A 513 1 O LYS A 512 N ASN A 477
SHEET 1 D 7 VAL A 609 ALA A 611 0
SHEET 2 D 7 VAL A 788 THR A 792 1 O VAL A 788 N TYR A 610
SHEET 3 D 7 ILE A 585 LEU A 589 1 N LEU A 589 O MET A 791
SHEET 4 D 7 PHE A 801 ALA A 807 1 O PHE A 805 N LEU A 588
SHEET 5 D 7 ALA A 874 SER A 883 1 O PHE A 879 N VAL A 804
SHEET 6 D 7 THR A 525 ILE A 530 1 N GLU A 526 O LEU A 878
SHEET 7 D 7 PHE A 949 ILE A 954 1 O ILE A 954 N LEU A 529
SHEET 1 E 2 TYR A 822 ASP A 825 0
SHEET 2 E 2 GLY A 829 THR A 832 -1 O GLY A 831 N LEU A 823
SHEET 1 F 3 TYR A 834 HIS A 836 0
SHEET 2 F 3 ILE A 841 TYR A 843 -1 O ILE A 841 N HIS A 836
SHEET 3 F 3 ILE B1016 GLN B1017 1 O ILE B1016 N SER A 842
SHEET 1 G 6 SER A1030 GLY A1031 0
SHEET 2 G 6 LYS A1013 VAL A1016 1 N SER A1015 O GLY A1031
SHEET 3 G 6 PRO A1151 GLU A1163 1 O LEU A1153 N GLN A1014
SHEET 4 G 6 LEU A1168 LYS A1174 -1 O LEU A1171 N CYS A1160
SHEET 5 G 6 VAL A1216 PHE A1223 1 O TYR A1222 N LYS A1174
SHEET 6 G 6 HIS A1228 THR A1231 -1 O HIS A1228 N PHE A1223
SHEET 1 H 5 SER A1030 GLY A1031 0
SHEET 2 H 5 LYS A1013 VAL A1016 1 N SER A1015 O GLY A1031
SHEET 3 H 5 PRO A1151 GLU A1163 1 O LEU A1153 N GLN A1014
SHEET 4 H 5 TRP A1125 PRO A1137 -1 N LEU A1136 O LEU A1152
SHEET 5 H 5 GLY B 59 MET B 60 -1 O MET B 60 N SER A1133
SHEET 1 I 6 ALA B 63 PHE B 66 0
SHEET 2 I 6 ILE B 35 LEU B 38 1 N PHE B 37 O GLN B 64
SHEET 3 I 6 HIS B 204 VAL B 207 1 O TYR B 206 N LEU B 38
SHEET 4 I 6 HIS B 230 THR B 236 1 O THR B 232 N ILE B 205
SHEET 5 I 6 ALA B 3 GLY B 8 1 N GLU B 4 O PHE B 233
SHEET 6 I 6 ILE B 273 LEU B 278 1 O THR B 274 N PHE B 5
SHEET 1 J 2 PHE B 86 LEU B 87 0
SHEET 2 J 2 LEU B 181 HIS B 182 1 O LEU B 181 N LEU B 87
SHEET 1 K 7 TYR B 370 ILE B 372 0
SHEET 2 K 7 VAL B 588 ASN B 592 1 O VAL B 590 N PHE B 371
SHEET 3 K 7 VAL B 345 ALA B 349 1 N ILE B 347 O PHE B 589
SHEET 4 K 7 CYS B 603 LEU B 607 1 O PHE B 605 N LEU B 348
SHEET 5 K 7 ARG B 664 PRO B 670 1 O TYR B 666 N VAL B 606
SHEET 6 K 7 LEU B 312 ALA B 317 1 N MET B 315 O VAL B 667
SHEET 7 K 7 ARG B 698 LEU B 700 1 O LEU B 700 N GLN B 316
SHEET 1 L 6 VAL B 910 PHE B 918 0
SHEET 2 L 6 GLY B 941 SER B 951 -1 O GLY B 941 N PHE B 918
SHEET 3 L 6 GLY B 954 LYS B 963 -1 O ARG B 958 N ASP B 947
SHEET 4 L 6 ALA B1001 HIS B1010 1 O PHE B1009 N LYS B 963
SHEET 5 L 6 LYS B1038 LEU B1042 -1 O LEU B1040 N VAL B1006
SHEET 6 L 6 ALA B1079 VAL B1080 1 O VAL B1080 N LEU B1041
SHEET 1 M 2 LEU B 927 LEU B 931 0
SHEET 2 M 2 CYS B 935 LEU B 939 -1 O CYS B 935 N LEU B 931
SHEET 1 N 2 GLY B1058 ARG B1059 0
SHEET 2 N 2 GLY B1066 LEU B1067 -1 O LEU B1067 N GLY B1058
SITE 1 AC1 10 ARG B 9 GLY B 11 SER B 12 GLY B 13
SITE 2 AC1 10 LYS B 14 THR B 15 ARG B 283 HOH B1264
SITE 3 AC1 10 HOH B1265 HOH B1266
SITE 1 AC2 2 DT X 44 DT X 45
CRYST1 100.555 139.714 103.093 90.00 105.54 90.00 P 1 21 1 2
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 0.009945 0.000000 0.002765 0.00000
SCALE2 0.000000 0.007157 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010068 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
