HEADER DNA EXCISION REPAIR 04-MAY-04 1T5L
TITLE CRYSTAL STRUCTURE OF THE DNA REPAIR PROTEIN UVRB POINT MUTANT Y96A
TITLE 2 REVEALING A NOVEL FOLD FOR DOMAIN 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UVRABC SYSTEM PROTEIN B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: UVRB PROTEIN, EXCINUCLEASE ABC SUBUNIT B;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CALDOTENAX;
SOURCE 3 ORGANISM_TAXID: 1395;
SOURCE 4 GENE: UVRB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA DAMAGE, DNA REPAIR, NUCLEOTIDE EXCISION REPAIR, UVRB, UVRA, UVRC,
KEYWDS 2 NER, MFD, TRCF, DNA EXCISION REPAIR
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.TRUGLIO,D.L.CROTEAU,M.SKORVAGA,M.J.DELLAVECCHIA,K.THEIS,
AUTHOR 2 B.S.MANDAVILLI,B.VAN HOUTEN,C.KISKER
REVDAT 4 14-FEB-24 1T5L 1 REMARK LINK
REVDAT 3 24-FEB-09 1T5L 1 VERSN
REVDAT 2 17-AUG-04 1T5L 1 JRNL
REVDAT 1 22-JUN-04 1T5L 0
JRNL AUTH J.J.TRUGLIO,D.L.CROTEAU,M.SKORVAGA,M.J.DELLAVECCHIA,K.THEIS,
JRNL AUTH 2 B.S.MANDAVILLI,B.VAN HOUTEN,C.KISKER
JRNL TITL INTERACTIONS BETWEEN UVRA AND UVRB: THE ROLE OF UVRB'S
JRNL TITL 2 DOMAIN 2 IN NUCLEOTIDE EXCISION REPAIR
JRNL REF EMBO J. V. 23 2498 2004
JRNL REFN ISSN 0261-4189
JRNL PMID 15192705
JRNL DOI 10.1038/SJ.EMBOJ.7600263
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 61362
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3277
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4421
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3370
REMARK 3 BIN FREE R VALUE SET COUNT : 252
REMARK 3 BIN FREE R VALUE : 0.3980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9612
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 196
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.82000
REMARK 3 B22 (A**2) : 1.82000
REMARK 3 B33 (A**2) : -2.73000
REMARK 3 B12 (A**2) : 0.91000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.405
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.304
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.236
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.316
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9774 ; 0.019 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13208 ; 1.868 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1188 ; 3.584 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1486 ; 0.130 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7432 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4294 ; 0.239 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 385 ; 0.171 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 66 ; 0.208 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.133 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5926 ; 0.899 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9624 ; 1.735 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3848 ; 2.629 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3584 ; 4.522 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 5
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 90 4
REMARK 3 1 B 3 B 90 4
REMARK 3 2 A 131 A 157 4
REMARK 3 2 B 131 B 157 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 900 ; 0.29 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 900 ; 0.90 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 245 A 414 4
REMARK 3 1 B 245 B 414 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 1392 ; 0.31 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 1392 ; 2.07 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 91 A 117 4
REMARK 3 1 B 91 B 117 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 226 ; 0.48 ; 0.50
REMARK 3 MEDIUM THERMAL 3 A (A**2): 226 ; 0.67 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 158 A 244 4
REMARK 3 1 B 158 B 244 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 4 A (A): 720 ; 0.49 ; 0.50
REMARK 3 MEDIUM THERMAL 4 A (A**2): 720 ; 0.57 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 415 A 595 4
REMARK 3 1 B 415 B 595 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 5 A (A): 1452 ; 0.31 ; 0.50
REMARK 3 MEDIUM THERMAL 5 A (A**2): 1452 ; 1.15 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T5L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022340.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X26C
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61397
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: COMO
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, TRIS, ZNCL2, PH 8.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 106.55467
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 53.27733
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 53.27733
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 106.55467
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ILE A 596
REMARK 465 ARG A 597
REMARK 465 ALA A 598
REMARK 465 THR A 599
REMARK 465 TYR A 600
REMARK 465 ALA A 601
REMARK 465 ALA A 602
REMARK 465 GLU A 603
REMARK 465 GLU A 604
REMARK 465 THR A 605
REMARK 465 GLU A 606
REMARK 465 MET A 607
REMARK 465 TYR A 608
REMARK 465 GLU A 609
REMARK 465 ALA A 610
REMARK 465 LYS A 611
REMARK 465 PRO A 612
REMARK 465 ALA A 613
REMARK 465 ALA A 614
REMARK 465 ALA A 615
REMARK 465 MET A 616
REMARK 465 THR A 617
REMARK 465 LYS A 618
REMARK 465 GLN A 619
REMARK 465 GLU A 620
REMARK 465 ARG A 621
REMARK 465 GLU A 622
REMARK 465 GLU A 623
REMARK 465 LEU A 624
REMARK 465 ILE A 625
REMARK 465 ARG A 626
REMARK 465 THR A 627
REMARK 465 LEU A 628
REMARK 465 GLU A 629
REMARK 465 ALA A 630
REMARK 465 GLU A 631
REMARK 465 MET A 632
REMARK 465 LYS A 633
REMARK 465 GLU A 634
REMARK 465 ALA A 635
REMARK 465 ALA A 636
REMARK 465 LYS A 637
REMARK 465 ALA A 638
REMARK 465 LEU A 639
REMARK 465 ASP A 640
REMARK 465 PHE A 641
REMARK 465 GLU A 642
REMARK 465 ARG A 643
REMARK 465 ALA A 644
REMARK 465 ALA A 645
REMARK 465 GLN A 646
REMARK 465 LEU A 647
REMARK 465 ARG A 648
REMARK 465 ASP A 649
REMARK 465 ILE A 650
REMARK 465 ILE A 651
REMARK 465 PHE A 652
REMARK 465 GLU A 653
REMARK 465 LEU A 654
REMARK 465 LYS A 655
REMARK 465 ALA A 656
REMARK 465 GLU A 657
REMARK 465 GLY A 658
REMARK 465 ILE B 596
REMARK 465 ARG B 597
REMARK 465 ALA B 598
REMARK 465 THR B 599
REMARK 465 TYR B 600
REMARK 465 ALA B 601
REMARK 465 ALA B 602
REMARK 465 GLU B 603
REMARK 465 GLU B 604
REMARK 465 THR B 605
REMARK 465 GLU B 606
REMARK 465 MET B 607
REMARK 465 TYR B 608
REMARK 465 GLU B 609
REMARK 465 ALA B 610
REMARK 465 LYS B 611
REMARK 465 PRO B 612
REMARK 465 ALA B 613
REMARK 465 ALA B 614
REMARK 465 ALA B 615
REMARK 465 MET B 616
REMARK 465 THR B 617
REMARK 465 LYS B 618
REMARK 465 GLN B 619
REMARK 465 GLU B 620
REMARK 465 ARG B 621
REMARK 465 GLU B 622
REMARK 465 GLU B 623
REMARK 465 LEU B 624
REMARK 465 ILE B 625
REMARK 465 ARG B 626
REMARK 465 THR B 627
REMARK 465 LEU B 628
REMARK 465 GLU B 629
REMARK 465 ALA B 630
REMARK 465 GLU B 631
REMARK 465 MET B 632
REMARK 465 LYS B 633
REMARK 465 GLU B 634
REMARK 465 ALA B 635
REMARK 465 ALA B 636
REMARK 465 LYS B 637
REMARK 465 ALA B 638
REMARK 465 LEU B 639
REMARK 465 ASP B 640
REMARK 465 PHE B 641
REMARK 465 GLU B 642
REMARK 465 ARG B 643
REMARK 465 ALA B 644
REMARK 465 ALA B 645
REMARK 465 GLN B 646
REMARK 465 LEU B 647
REMARK 465 ARG B 648
REMARK 465 ASP B 649
REMARK 465 ILE B 650
REMARK 465 ILE B 651
REMARK 465 PHE B 652
REMARK 465 GLU B 653
REMARK 465 LEU B 654
REMARK 465 LYS B 655
REMARK 465 ALA B 656
REMARK 465 GLU B 657
REMARK 465 GLY B 658
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 A 130 O HOH A 729 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 26 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 94 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP A 185 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 LEU A 281 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 ASP A 423 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 432 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 LEU A 520 CA - CB - CG ANGL. DEV. = -14.2 DEGREES
REMARK 500 ARG A 569 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ASP B 94 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG B 134 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ASP B 185 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP B 208 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 219 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 270 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG B 270 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG B 291 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 MET B 350 CG - SD - CE ANGL. DEV. = 10.0 DEGREES
REMARK 500 ASP B 432 CB - CG - OD2 ANGL. DEV. = 6.3 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 PHE A 81 57.45 -141.38
REMARK 500 TYR A 95 39.39 -165.67
REMARK 500 ASP A 112 -54.93 -4.03
REMARK 500 ALA A 113 92.83 -40.60
REMARK 500 LYS A 114 133.33 -31.44
REMARK 500 ILE A 115 97.56 -68.20
REMARK 500 VAL A 142 -1.22 -58.39
REMARK 500 CYS A 144 0.66 -69.16
REMARK 500 GLU A 166 46.68 -72.51
REMARK 500 ASN A 184 86.54 -154.29
REMARK 500 ASP A 187 85.02 -168.25
REMARK 500 ASP A 208 -75.48 -95.50
REMARK 500 PHE A 217 77.12 -157.91
REMARK 500 GLU A 222 -82.72 -93.70
REMARK 500 THR A 231 -44.31 -141.81
REMARK 500 GLU A 237 48.82 -175.83
REMARK 500 MET A 300 22.70 -140.90
REMARK 500 ASP A 332 41.81 -91.32
REMARK 500 ASN A 387 -70.84 -89.27
REMARK 500 SER A 477 -16.75 -43.82
REMARK 500 GLU A 507 157.78 -47.37
REMARK 500 ASP A 594 -127.93 -129.81
REMARK 500 TYR B 95 -4.80 -146.00
REMARK 500 ASP B 112 -99.81 -143.23
REMARK 500 ALA B 113 94.66 -9.16
REMARK 500 LYS B 114 100.81 -35.23
REMARK 500 ILE B 115 102.42 -23.23
REMARK 500 VAL B 142 -6.32 -59.11
REMARK 500 GLN B 180 31.57 71.52
REMARK 500 ILE B 186 -92.07 -64.33
REMARK 500 ARG B 190 131.74 -34.49
REMARK 500 LEU B 230 -62.11 -92.02
REMARK 500 THR B 231 -78.74 -60.84
REMARK 500 ASN B 387 -73.55 -97.41
REMARK 500 SER B 393 148.63 -172.93
REMARK 500 GLU B 507 139.94 -37.45
REMARK 500 ASP B 594 -61.01 -102.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 659 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 403 NE2
REMARK 620 2 HOH A 708 O 101.1
REMARK 620 3 HOH A 726 O 137.3 64.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 659
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 659
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 660
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 660
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1D9X RELATED DB: PDB
REMARK 900 RELATED ID: 1D9Z RELATED DB: PDB
REMARK 900 RELATED ID: 1C40 RELATED DB: PDB
REMARK 900 RELATED ID: 1D2M RELATED DB: PDB
REMARK 900 RELATED ID: 1E52 RELATED DB: PDB
REMARK 900 RELATED ID: 1QOJ RELATED DB: PDB
REMARK 999
REMARK 999 AUTHORS INFORMED THAT THE SEQUENCE THEY PROVIDED
REMARK 999 IS CORRECT AND THAT THE SEQUENCE IN THE SWISS PROT
REMARK 999 ENTRY IS INCORRECT.
DBREF 1T5L A 1 658 UNP P56981 UVRB_BACCA 1 657
DBREF 1T5L B 1 658 UNP P56981 UVRB_BACCA 1 657
SEQADV 1T5L ARG A 190 UNP P56981 190 SEE REMARK 999
SEQADV 1T5L GLU A 233 UNP P56981 LYS 232 SEE REMARK 999
SEQADV 1T5L ARG B 190 UNP P56981 190 SEE REMARK 999
SEQADV 1T5L GLU B 233 UNP P56981 LYS 232 SEE REMARK 999
SEQRES 1 A 658 VAL GLU GLY ARG PHE GLN LEU VAL ALA PRO TYR GLU PRO
SEQRES 2 A 658 GLN GLY ASP GLN PRO GLN ALA ILE ALA LYS LEU VAL ASP
SEQRES 3 A 658 GLY LEU ARG ARG GLY VAL LYS HIS GLN THR LEU LEU GLY
SEQRES 4 A 658 ALA THR GLY THR GLY LYS THR PHE THR ILE SER ASN VAL
SEQRES 5 A 658 ILE ALA GLN VAL ASN LYS PRO THR LEU VAL ILE ALA HIS
SEQRES 6 A 658 ASN LYS THR LEU ALA GLY GLN LEU TYR SER GLU LEU LYS
SEQRES 7 A 658 GLU PHE PHE PRO HIS ASN ALA VAL GLU TYR PHE VAL SER
SEQRES 8 A 658 TYR TYR ASP TYR ALA GLN PRO GLU ALA TYR VAL PRO GLN
SEQRES 9 A 658 THR ASP THR TYR ILE GLU LYS ASP ALA LYS ILE ASN ASP
SEQRES 10 A 658 GLU ILE ASP LYS LEU ARG HIS SER ALA THR SER ALA LEU
SEQRES 11 A 658 PHE GLU ARG ARG ASP VAL ILE ILE VAL ALA SER VAL SER
SEQRES 12 A 658 CYS ILE TYR GLY LEU GLY SER PRO GLU GLU TYR ARG GLU
SEQRES 13 A 658 LEU VAL VAL SER LEU ARG VAL GLY MET GLU ILE GLU ARG
SEQRES 14 A 658 ASN ALA LEU LEU ARG ARG LEU VAL ASP ILE GLN TYR ASP
SEQRES 15 A 658 ARG ASN ASP ILE ASP PHE ARG ARG GLY THR PHE ARG VAL
SEQRES 16 A 658 ARG GLY ASP VAL VAL GLU ILE PHE PRO ALA SER ARG ASP
SEQRES 17 A 658 GLU HIS CYS ILE ARG VAL GLU PHE PHE GLY ASP GLU ILE
SEQRES 18 A 658 GLU ARG ILE ARG GLU VAL ASP ALA LEU THR GLY GLU VAL
SEQRES 19 A 658 LEU GLY GLU ARG GLU HIS VAL ALA ILE PHE PRO ALA SER
SEQRES 20 A 658 HIS PHE VAL THR ARG GLU GLU LYS MET ARG LEU ALA ILE
SEQRES 21 A 658 GLN ASN ILE GLU GLN GLU LEU GLU GLU ARG LEU ALA GLU
SEQRES 22 A 658 LEU ARG ALA GLN GLY LYS LEU LEU GLU ALA GLN ARG LEU
SEQRES 23 A 658 GLU GLN ARG THR ARG TYR ASP LEU GLU MET MET ARG GLU
SEQRES 24 A 658 MET GLY PHE CYS SER GLY ILE GLU ASN TYR SER ARG HIS
SEQRES 25 A 658 LEU ALA LEU ARG PRO PRO GLY SER THR PRO TYR THR LEU
SEQRES 26 A 658 LEU ASP TYR PHE PRO ASP ASP PHE LEU ILE ILE VAL ASP
SEQRES 27 A 658 GLU SER HIS VAL THR LEU PRO GLN LEU ARG GLY MET TYR
SEQRES 28 A 658 ASN GLY ASP ARG ALA ARG LYS GLN VAL LEU VAL ASP HIS
SEQRES 29 A 658 GLY PHE ARG LEU PRO SER ALA LEU ASP ASN ARG PRO LEU
SEQRES 30 A 658 THR PHE GLU GLU PHE GLU GLN LYS ILE ASN GLN ILE ILE
SEQRES 31 A 658 TYR VAL SER ALA THR PRO GLY PRO TYR GLU LEU GLU HIS
SEQRES 32 A 658 SER PRO GLY VAL VAL GLU GLN ILE ILE ARG PRO THR GLY
SEQRES 33 A 658 LEU LEU ASP PRO THR ILE ASP VAL ARG PRO THR LYS GLY
SEQRES 34 A 658 GLN ILE ASP ASP LEU ILE GLY GLU ILE ARG GLU ARG VAL
SEQRES 35 A 658 GLU ARG ASN GLU ARG THR LEU VAL THR THR LEU THR LYS
SEQRES 36 A 658 LYS MET ALA GLU ASP LEU THR ASP TYR LEU LYS GLU ALA
SEQRES 37 A 658 GLY ILE LYS VAL ALA TYR LEU HIS SER GLU ILE LYS THR
SEQRES 38 A 658 LEU GLU ARG ILE GLU ILE ILE ARG ASP LEU ARG LEU GLY
SEQRES 39 A 658 LYS TYR ASP VAL LEU VAL GLY ILE ASN LEU LEU ARG GLU
SEQRES 40 A 658 GLY LEU ASP ILE PRO GLU VAL SER LEU VAL ALA ILE LEU
SEQRES 41 A 658 ASP ALA ASP LYS GLU GLY PHE LEU ARG SER GLU ARG SER
SEQRES 42 A 658 LEU ILE GLN THR ILE GLY ARG ALA ALA ARG ASN ALA ASN
SEQRES 43 A 658 GLY HIS VAL ILE MET TYR ALA ASP THR ILE THR LYS SER
SEQRES 44 A 658 MET GLU ILE ALA ILE GLN GLU THR LYS ARG ARG ARG ALA
SEQRES 45 A 658 ILE GLN GLU GLU TYR ASN ARG LYS HIS GLY ILE VAL PRO
SEQRES 46 A 658 ARG THR VAL LYS LYS GLU ILE ARG ASP VAL ILE ARG ALA
SEQRES 47 A 658 THR TYR ALA ALA GLU GLU THR GLU MET TYR GLU ALA LYS
SEQRES 48 A 658 PRO ALA ALA ALA MET THR LYS GLN GLU ARG GLU GLU LEU
SEQRES 49 A 658 ILE ARG THR LEU GLU ALA GLU MET LYS GLU ALA ALA LYS
SEQRES 50 A 658 ALA LEU ASP PHE GLU ARG ALA ALA GLN LEU ARG ASP ILE
SEQRES 51 A 658 ILE PHE GLU LEU LYS ALA GLU GLY
SEQRES 1 B 658 VAL GLU GLY ARG PHE GLN LEU VAL ALA PRO TYR GLU PRO
SEQRES 2 B 658 GLN GLY ASP GLN PRO GLN ALA ILE ALA LYS LEU VAL ASP
SEQRES 3 B 658 GLY LEU ARG ARG GLY VAL LYS HIS GLN THR LEU LEU GLY
SEQRES 4 B 658 ALA THR GLY THR GLY LYS THR PHE THR ILE SER ASN VAL
SEQRES 5 B 658 ILE ALA GLN VAL ASN LYS PRO THR LEU VAL ILE ALA HIS
SEQRES 6 B 658 ASN LYS THR LEU ALA GLY GLN LEU TYR SER GLU LEU LYS
SEQRES 7 B 658 GLU PHE PHE PRO HIS ASN ALA VAL GLU TYR PHE VAL SER
SEQRES 8 B 658 TYR TYR ASP TYR ALA GLN PRO GLU ALA TYR VAL PRO GLN
SEQRES 9 B 658 THR ASP THR TYR ILE GLU LYS ASP ALA LYS ILE ASN ASP
SEQRES 10 B 658 GLU ILE ASP LYS LEU ARG HIS SER ALA THR SER ALA LEU
SEQRES 11 B 658 PHE GLU ARG ARG ASP VAL ILE ILE VAL ALA SER VAL SER
SEQRES 12 B 658 CYS ILE TYR GLY LEU GLY SER PRO GLU GLU TYR ARG GLU
SEQRES 13 B 658 LEU VAL VAL SER LEU ARG VAL GLY MET GLU ILE GLU ARG
SEQRES 14 B 658 ASN ALA LEU LEU ARG ARG LEU VAL ASP ILE GLN TYR ASP
SEQRES 15 B 658 ARG ASN ASP ILE ASP PHE ARG ARG GLY THR PHE ARG VAL
SEQRES 16 B 658 ARG GLY ASP VAL VAL GLU ILE PHE PRO ALA SER ARG ASP
SEQRES 17 B 658 GLU HIS CYS ILE ARG VAL GLU PHE PHE GLY ASP GLU ILE
SEQRES 18 B 658 GLU ARG ILE ARG GLU VAL ASP ALA LEU THR GLY GLU VAL
SEQRES 19 B 658 LEU GLY GLU ARG GLU HIS VAL ALA ILE PHE PRO ALA SER
SEQRES 20 B 658 HIS PHE VAL THR ARG GLU GLU LYS MET ARG LEU ALA ILE
SEQRES 21 B 658 GLN ASN ILE GLU GLN GLU LEU GLU GLU ARG LEU ALA GLU
SEQRES 22 B 658 LEU ARG ALA GLN GLY LYS LEU LEU GLU ALA GLN ARG LEU
SEQRES 23 B 658 GLU GLN ARG THR ARG TYR ASP LEU GLU MET MET ARG GLU
SEQRES 24 B 658 MET GLY PHE CYS SER GLY ILE GLU ASN TYR SER ARG HIS
SEQRES 25 B 658 LEU ALA LEU ARG PRO PRO GLY SER THR PRO TYR THR LEU
SEQRES 26 B 658 LEU ASP TYR PHE PRO ASP ASP PHE LEU ILE ILE VAL ASP
SEQRES 27 B 658 GLU SER HIS VAL THR LEU PRO GLN LEU ARG GLY MET TYR
SEQRES 28 B 658 ASN GLY ASP ARG ALA ARG LYS GLN VAL LEU VAL ASP HIS
SEQRES 29 B 658 GLY PHE ARG LEU PRO SER ALA LEU ASP ASN ARG PRO LEU
SEQRES 30 B 658 THR PHE GLU GLU PHE GLU GLN LYS ILE ASN GLN ILE ILE
SEQRES 31 B 658 TYR VAL SER ALA THR PRO GLY PRO TYR GLU LEU GLU HIS
SEQRES 32 B 658 SER PRO GLY VAL VAL GLU GLN ILE ILE ARG PRO THR GLY
SEQRES 33 B 658 LEU LEU ASP PRO THR ILE ASP VAL ARG PRO THR LYS GLY
SEQRES 34 B 658 GLN ILE ASP ASP LEU ILE GLY GLU ILE ARG GLU ARG VAL
SEQRES 35 B 658 GLU ARG ASN GLU ARG THR LEU VAL THR THR LEU THR LYS
SEQRES 36 B 658 LYS MET ALA GLU ASP LEU THR ASP TYR LEU LYS GLU ALA
SEQRES 37 B 658 GLY ILE LYS VAL ALA TYR LEU HIS SER GLU ILE LYS THR
SEQRES 38 B 658 LEU GLU ARG ILE GLU ILE ILE ARG ASP LEU ARG LEU GLY
SEQRES 39 B 658 LYS TYR ASP VAL LEU VAL GLY ILE ASN LEU LEU ARG GLU
SEQRES 40 B 658 GLY LEU ASP ILE PRO GLU VAL SER LEU VAL ALA ILE LEU
SEQRES 41 B 658 ASP ALA ASP LYS GLU GLY PHE LEU ARG SER GLU ARG SER
SEQRES 42 B 658 LEU ILE GLN THR ILE GLY ARG ALA ALA ARG ASN ALA ASN
SEQRES 43 B 658 GLY HIS VAL ILE MET TYR ALA ASP THR ILE THR LYS SER
SEQRES 44 B 658 MET GLU ILE ALA ILE GLN GLU THR LYS ARG ARG ARG ALA
SEQRES 45 B 658 ILE GLN GLU GLU TYR ASN ARG LYS HIS GLY ILE VAL PRO
SEQRES 46 B 658 ARG THR VAL LYS LYS GLU ILE ARG ASP VAL ILE ARG ALA
SEQRES 47 B 658 THR TYR ALA ALA GLU GLU THR GLU MET TYR GLU ALA LYS
SEQRES 48 B 658 PRO ALA ALA ALA MET THR LYS GLN GLU ARG GLU GLU LEU
SEQRES 49 B 658 ILE ARG THR LEU GLU ALA GLU MET LYS GLU ALA ALA LYS
SEQRES 50 B 658 ALA LEU ASP PHE GLU ARG ALA ALA GLN LEU ARG ASP ILE
SEQRES 51 B 658 ILE PHE GLU LEU LYS ALA GLU GLY
HET ZN A 659 1
HET ZN A 660 1
HET ZN B 659 1
HET ZN B 660 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 4(ZN 2+)
FORMUL 7 HOH *196(H2 O)
HELIX 1 1 ASP A 16 GLY A 31 1 16
HELIX 2 2 GLY A 44 ASN A 57 1 14
HELIX 3 3 ASN A 66 PHE A 81 1 16
HELIX 4 4 SER A 91 TYR A 95 5 5
HELIX 5 5 ASN A 116 ARG A 133 1 18
HELIX 6 6 VAL A 142 TYR A 146 5 5
HELIX 7 7 SER A 150 LEU A 157 1 8
HELIX 8 8 GLU A 168 ILE A 179 1 12
HELIX 9 9 ARG A 252 GLN A 277 1 26
HELIX 10 10 LYS A 279 GLY A 301 1 23
HELIX 11 11 GLY A 305 ASN A 308 5 4
HELIX 12 12 TYR A 309 LEU A 315 1 7
HELIX 13 13 THR A 324 PHE A 329 1 6
HELIX 14 14 GLU A 339 HIS A 364 1 26
HELIX 15 15 LEU A 368 ASN A 374 5 7
HELIX 16 16 THR A 378 ILE A 386 1 9
HELIX 17 17 GLY A 397 SER A 404 1 8
HELIX 18 18 GLY A 429 ARG A 444 1 16
HELIX 19 19 THR A 454 GLU A 467 1 14
HELIX 20 20 LYS A 480 LEU A 493 1 14
HELIX 21 21 GLY A 526 ARG A 529 5 4
HELIX 22 22 SER A 530 GLY A 539 1 10
HELIX 23 23 ARG A 540 ALA A 542 5 3
HELIX 24 24 THR A 557 GLY A 582 1 26
HELIX 25 25 ASP B 16 ARG B 30 1 15
HELIX 26 26 GLY B 44 ASN B 57 1 14
HELIX 27 27 ASN B 66 PHE B 81 1 16
HELIX 28 28 SER B 91 TYR B 95 5 5
HELIX 29 29 ASN B 116 ARG B 133 1 18
HELIX 30 30 VAL B 142 TYR B 146 5 5
HELIX 31 31 SER B 150 LEU B 157 1 8
HELIX 32 32 GLU B 168 ASP B 178 1 11
HELIX 33 33 ARG B 252 GLN B 277 1 26
HELIX 34 34 LYS B 279 GLY B 301 1 23
HELIX 35 35 GLY B 305 ASN B 308 5 4
HELIX 36 36 TYR B 309 ALA B 314 1 6
HELIX 37 37 THR B 324 PHE B 329 5 6
HELIX 38 38 GLU B 339 GLY B 349 1 11
HELIX 39 39 GLY B 349 HIS B 364 1 16
HELIX 40 40 LEU B 368 ASN B 374 5 7
HELIX 41 41 THR B 378 ILE B 386 1 9
HELIX 42 42 GLY B 397 SER B 404 1 8
HELIX 43 43 GLY B 429 ARG B 444 1 16
HELIX 44 44 THR B 454 GLU B 467 1 14
HELIX 45 45 LYS B 480 LEU B 493 1 14
HELIX 46 46 GLY B 526 ARG B 529 5 4
HELIX 47 47 SER B 530 GLY B 539 1 10
HELIX 48 48 ARG B 540 ALA B 542 5 3
HELIX 49 49 THR B 557 GLY B 582 1 26
SHEET 1 A 7 ALA A 85 PHE A 89 0
SHEET 2 A 7 VAL A 136 ALA A 140 1 O ILE A 137 N GLU A 87
SHEET 3 A 7 THR A 60 ILE A 63 1 N VAL A 62 O ALA A 140
SHEET 4 A 7 LEU A 334 ASP A 338 1 O LEU A 334 N LEU A 61
SHEET 5 A 7 GLN A 388 SER A 393 1 O ILE A 390 N VAL A 337
SHEET 6 A 7 HIS A 34 GLY A 39 1 N LEU A 37 O TYR A 391
SHEET 7 A 7 VAL A 408 GLN A 410 1 O VAL A 408 N THR A 36
SHEET 1 B 2 ALA A 100 VAL A 102 0
SHEET 2 B 2 THR A 107 ILE A 109 -1 O ILE A 109 N ALA A 100
SHEET 1 C 2 VAL A 159 ARG A 162 0
SHEET 2 C 2 HIS A 240 ILE A 243 -1 O VAL A 241 N LEU A 161
SHEET 1 D 5 ASP A 182 ARG A 183 0
SHEET 2 D 5 THR A 192 VAL A 195 1 O PHE A 193 N ASP A 182
SHEET 3 D 5 VAL A 199 ILE A 202 -1 O GLU A 201 N ARG A 194
SHEET 4 D 5 HIS A 210 PHE A 216 -1 O ILE A 212 N ILE A 202
SHEET 5 D 5 ILE A 221 ASP A 228 -1 O GLU A 222 N GLU A 215
SHEET 1 E 6 THR A 421 ARG A 425 0
SHEET 2 E 6 HIS A 548 TYR A 552 1 O MET A 551 N ASP A 423
SHEET 3 E 6 VAL A 514 ILE A 519 1 N ILE A 519 O ILE A 550
SHEET 4 E 6 ARG A 447 THR A 451 1 N LEU A 449 O ALA A 518
SHEET 5 E 6 VAL A 498 GLY A 501 1 O GLY A 501 N VAL A 450
SHEET 6 E 6 VAL A 472 LEU A 475 1 N LEU A 475 O VAL A 500
SHEET 1 F 7 ALA B 85 PHE B 89 0
SHEET 2 F 7 VAL B 136 ALA B 140 1 O ILE B 137 N GLU B 87
SHEET 3 F 7 THR B 60 ILE B 63 1 N VAL B 62 O ALA B 140
SHEET 4 F 7 LEU B 334 ASP B 338 1 O ILE B 336 N LEU B 61
SHEET 5 F 7 GLN B 388 SER B 393 1 O ILE B 390 N ILE B 335
SHEET 6 F 7 HIS B 34 GLY B 39 1 N LEU B 37 O TYR B 391
SHEET 7 F 7 VAL B 408 GLN B 410 1 O VAL B 408 N THR B 36
SHEET 1 G 2 ALA B 100 VAL B 102 0
SHEET 2 G 2 THR B 107 ILE B 109 -1 O ILE B 109 N ALA B 100
SHEET 1 H 2 VAL B 159 ARG B 162 0
SHEET 2 H 2 HIS B 240 ILE B 243 -1 O VAL B 241 N LEU B 161
SHEET 1 I 6 ASP B 182 ARG B 183 0
SHEET 2 I 6 THR B 192 ARG B 196 1 O PHE B 193 N ASP B 182
SHEET 3 I 6 VAL B 199 ILE B 202 -1 O GLU B 201 N ARG B 194
SHEET 4 I 6 HIS B 210 PHE B 216 -1 O VAL B 214 N VAL B 200
SHEET 5 I 6 ILE B 221 ASP B 228 -1 O GLU B 222 N GLU B 215
SHEET 6 I 6 VAL B 234 GLU B 237 -1 O LEU B 235 N GLU B 226
SHEET 1 J 6 THR B 421 ARG B 425 0
SHEET 2 J 6 HIS B 548 TYR B 552 1 O MET B 551 N ARG B 425
SHEET 3 J 6 VAL B 514 ILE B 519 1 N ILE B 519 O TYR B 552
SHEET 4 J 6 ARG B 447 THR B 451 1 N LEU B 449 O ALA B 518
SHEET 5 J 6 VAL B 498 GLY B 501 1 O GLY B 501 N VAL B 450
SHEET 6 J 6 TYR B 474 LEU B 475 1 N LEU B 475 O VAL B 500
LINK NE2 HIS A 403 ZN ZN A 659 1555 1555 2.13
LINK NE2 HIS A 581 ZN ZN A 660 1555 1555 2.24
LINK ZN ZN A 659 O HOH A 708 1555 1555 2.69
LINK ZN ZN A 659 O HOH A 726 1555 1555 2.69
LINK NE2 HIS B 403 ZN ZN B 659 1555 1555 2.21
LINK NE2 HIS B 581 ZN ZN B 660 1555 1555 2.22
SITE 1 AC1 3 HIS A 403 HOH A 708 HOH A 726
SITE 1 AC2 1 HIS B 403
SITE 1 AC3 2 GLU B 295 HIS B 581
SITE 1 AC4 1 HIS A 581
CRYST1 150.815 150.815 159.832 90.00 90.00 120.00 P 32 2 1 12
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 0.006631 0.003828 0.000000 0.00000
SCALE2 0.000000 0.007656 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006257 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
