HEADER LIGASE 27-JAN-06 1VS0
TITLE CRYSTAL STRUCTURE OF THE LIGASE DOMAIN FROM M. TUBERCULOSIS LIGD AT
TITLE 2 2.4A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE DNA LIGASE-LIKE PROTEIN RV0938/MT0965;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: LIGD LIGASE DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: ADENYLATED FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: RV0938, MT0965;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAEB1120;
SOURCE 11 OTHER_DETAILS: TEV CLEAVABLE HIS TAG
KEYWDS LIGASE; OB FOLD; NUCLEOTIDYL TRANSFERASE, STRUCTURAL GENOMICS, PSI,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, TB STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 3 TBSGC, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.AKEY,A.MARTINS,J.ANIUKWU,M.S.GLICKMAN,S.SHUMAN,J.M.BERGER,TB
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 4 13-JUL-11 1VS0 1 VERSN
REVDAT 3 24-FEB-09 1VS0 1 VERSN
REVDAT 2 23-MAY-06 1VS0 1 JRNL
REVDAT 1 28-FEB-06 1VS0 0
JRNL AUTH D.AKEY,A.MARTINS,J.ANIUKWU,M.S.GLICKMAN,S.SHUMAN,J.M.BERGER
JRNL TITL CRYSTAL STRUCTURE AND NONHOMOLOGOUS END-JOINING FUNCTION OF
JRNL TITL 2 THE LIGASE COMPONENT OF MYCOBACTERIUM DNA LIGASE D.
JRNL REF J.BIOL.CHEM. V. 281 13412 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16476729
JRNL DOI 10.1074/JBC.M513550200
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 28487
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1453
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1894
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 111
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4777
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 407
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.01000
REMARK 3 B22 (A**2) : 1.01000
REMARK 3 B33 (A**2) : -1.52000
REMARK 3 B12 (A**2) : 0.51000
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): 0.414
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.264
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.190
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.811
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4881 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6636 ; 1.600 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 616 ; 6.814 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 219 ;38.015 ;22.466
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 770 ;18.654 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;19.204 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 706 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3793 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2107 ; 0.233 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3226 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 366 ; 0.213 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 7 ; 0.309 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 131 ; 0.268 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 29 ; 0.352 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 7 ; 0.137 ; 0.200
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): 3090 ; 2.497 ; 3.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4836 ; 3.715 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2060 ; 2.281 ; 3.500
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1799 ; 3.070 ; 3.500
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 453 A 638
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6077 52.9960 125.3335
REMARK 3 T TENSOR
REMARK 3 T11: -0.0623 T22: -0.0758
REMARK 3 T33: -0.0200 T12: 0.0325
REMARK 3 T13: 0.0163 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.1221 L22: 0.7415
REMARK 3 L33: 1.2200 L12: -0.0542
REMARK 3 L13: -0.0150 L23: 0.3666
REMARK 3 S TENSOR
REMARK 3 S11: -0.0183 S12: 0.0440 S13: 0.0243
REMARK 3 S21: 0.0298 S22: -0.0600 S23: 0.0111
REMARK 3 S31: 0.0060 S32: -0.0271 S33: 0.0783
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 639 A 759
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7849 75.2068 154.8358
REMARK 3 T TENSOR
REMARK 3 T11: 0.1044 T22: -0.1325
REMARK 3 T33: -0.0717 T12: -0.0521
REMARK 3 T13: 0.0742 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 1.0544 L22: 2.2426
REMARK 3 L33: 1.9458 L12: -0.3731
REMARK 3 L13: -0.2359 L23: 1.9652
REMARK 3 S TENSOR
REMARK 3 S11: 0.0753 S12: 0.0073 S13: 0.0316
REMARK 3 S21: 0.4854 S22: -0.1455 S23: 0.0148
REMARK 3 S31: 0.3277 S32: 0.0836 S33: 0.0702
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 453 B 638
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6871 55.7937 188.1162
REMARK 3 T TENSOR
REMARK 3 T11: 0.0798 T22: -0.1107
REMARK 3 T33: -0.0869 T12: -0.1443
REMARK 3 T13: 0.0624 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 1.8818 L22: 0.8552
REMARK 3 L33: 1.1395 L12: 1.1439
REMARK 3 L13: -0.6549 L23: -0.0163
REMARK 3 S TENSOR
REMARK 3 S11: 0.1567 S12: -0.0956 S13: 0.0424
REMARK 3 S21: 0.1717 S22: -0.0896 S23: 0.0762
REMARK 3 S31: 0.0074 S32: 0.1108 S33: -0.0671
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 639 B 759
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9281 42.1284 214.3944
REMARK 3 T TENSOR
REMARK 3 T11: -0.0295 T22: -0.0626
REMARK 3 T33: -0.0620 T12: -0.0530
REMARK 3 T13: 0.0234 T23: -0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 0.4184 L22: 1.0467
REMARK 3 L33: 2.8564 L12: 0.3464
REMARK 3 L13: 0.0470 L23: 0.0461
REMARK 3 S TENSOR
REMARK 3 S11: 0.0112 S12: -0.0464 S13: -0.0930
REMARK 3 S21: -0.1261 S22: 0.0697 S23: 0.0411
REMARK 3 S31: -0.1768 S32: 0.0775 S33: -0.0809
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1VS0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-06.
REMARK 100 THE RCSB ID CODE IS RCSB036341.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-SEP-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796, 1.020, 0.9798
REMARK 200 MONOCHROMATOR : ALS BEAMLINE 8.3.1
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BLU-ICE
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28772
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 3000, 25 MM ZNCL2, 100 MM
REMARK 280 SODIUM ACETATE (PH 4.6), VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
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 245.97133
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 122.98567
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 122.98567
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 245.97133
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER. THERE ARE TWO
REMARK 300 MONOMERS IN THE ASYMMETRIC UNIT.
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 GLY A 450
REMARK 465 ALA A 451
REMARK 465 VAL A 452
REMARK 465 GLY A 652
REMARK 465 GLU A 653
REMARK 465 GLY A 654
REMARK 465 GLY A 655
REMARK 465 ARG A 656
REMARK 465 SER A 657
REMARK 465 SER A 658
REMARK 465 GLY A 659
REMARK 465 GLY B 450
REMARK 465 ALA B 451
REMARK 465 VAL B 452
REMARK 465 GLY B 655
REMARK 465 ARG B 656
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 472 CD CE NZ
REMARK 480 ARG A 504 CD NE CZ NH1 NH2
REMARK 480 ARG A 550 CG CD NE CZ NH1 NH2
REMARK 480 ARG A 712 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 715 CD CE NZ
REMARK 480 LYS A 721 CD CE NZ
REMARK 480 GLU B 454 CD OE1 OE2
REMARK 480 LYS B 472 CE NZ
REMARK 480 ARG B 504 NE CZ NH1 NH2
REMARK 480 ARG B 550 CG CD NE CZ NH1 NH2
REMARK 480 ARG B 623 NE CZ NH1 NH2
REMARK 480 ARG B 628 CD NE CZ NH1 NH2
REMARK 480 GLU B 653 CB CG CD OE1 OE2
REMARK 480 GLU B 685 CG CD OE1 OE2
REMARK 480 ARG B 686 NE CZ NH1 NH2
REMARK 480 GLU B 693 CD OE1 OE2
REMARK 480 ARG B 712 CG CD NE CZ NH1 NH2
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 OE2 GLU A 582 O HOH A 9022 1.88
REMARK 500 N PHE B 453 O HOH B 9083 2.08
REMARK 500 ND1 HIS A 524 O HOH A 9220 2.16
REMARK 500 O HOH A 9065 O HOH A 9166 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP A 456 OD2 ASP B 701 2674 1.94
REMARK 500 CL CL B 9008 O HOH B 9178 4456 1.99
REMARK 500 OD2 ASP A 456 OD2 ASP A 750 6655 2.06
REMARK 500 O HOH B 9037 O HOH B 9124 4566 2.16
REMARK 500 CL CL A 9007 O HOH A 9220 6665 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 550 CB ARG A 550 CG 0.262
REMARK 500 GLU B 454 CG GLU B 454 CD -0.136
REMARK 500 LYS B 472 CD LYS B 472 CE -0.444
REMARK 500 ARG B 504 CD ARG B 504 NE -0.530
REMARK 500 ARG B 628 CG ARG B 628 CD -0.210
REMARK 500 ARG B 686 CD ARG B 686 NE 0.179
REMARK 500 GLU B 693 CG GLU B 693 CD -0.184
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 LYS B 472 CG - CD - CE ANGL. DEV. = 36.5 DEGREES
REMARK 500 LYS B 472 CD - CE - NZ ANGL. DEV. = 32.3 DEGREES
REMARK 500 ARG B 504 CG - CD - NE ANGL. DEV. = 40.6 DEGREES
REMARK 500 ARG B 504 CD - NE - CZ ANGL. DEV. = 13.7 DEGREES
REMARK 500 VAL B 679 CB - CA - C ANGL. DEV. = -12.2 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 SER A 731 -75.13 -85.41
REMARK 500 ALA B 473 -27.16 -39.28
REMARK 500 ASP B 535 178.56 -36.19
REMARK 500 ARG B 548 117.49 -36.49
REMARK 500 ARG B 550 24.16 -74.64
REMARK 500 SER B 731 -80.45 -100.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLY A 480 19.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP A 456 24.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A9083 DISTANCE = 5.03 ANGSTROMS
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 A9002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 APK A 481 O1P
REMARK 620 2 ASP A 483 OD1 90.4
REMARK 620 3 ASP A 483 OD2 145.3 55.8
REMARK 620 4 GLU A 613 OE1 137.3 125.4 76.2
REMARK 620 5 GLU A 613 OE2 101.1 99.3 92.9 55.4
REMARK 620 6 ASP A 522 OD2 103.4 101.1 78.5 92.4 147.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A9004 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CL A9007 CL
REMARK 620 2 GLU A 727 OE1 114.2
REMARK 620 3 ASP A 492 OD1 114.0 102.3
REMARK 620 4 HIS A 493 ND1 106.4 122.4 96.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A9009 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 454 OE2
REMARK 620 2 GLU A 454 OE1 58.3
REMARK 620 3 ASP B 701 OD2 87.2 129.0
REMARK 620 4 HIS B 699 NE2 143.7 87.2 126.7
REMARK 620 5 ASP A 750 OD1 123.6 106.0 60.8 73.3
REMARK 620 6 ASP B 701 OD1 94.3 152.3 44.2 118.6 92.1
REMARK 620 7 ASP A 750 OD2 72.5 74.8 58.6 111.5 51.5 102.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B9001 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 APK B 481 O1P
REMARK 620 2 GLU B 613 OE2 84.4
REMARK 620 3 ASP B 483 OD2 99.4 105.1
REMARK 620 4 ASP B 483 OD1 148.2 112.7 51.3
REMARK 620 5 ASP B 522 OD2 106.0 137.2 113.6 80.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B9003 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 727 OE2
REMARK 620 2 GLU B 727 OE1 53.9
REMARK 620 3 CL B9008 CL 87.6 113.2
REMARK 620 4 HIS B 493 ND1 90.4 124.3 104.9
REMARK 620 5 ASP B 492 OD2 161.0 107.1 103.4 101.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 9002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 9003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 9004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 9005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 9006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 9007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 9008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 9009
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV0938 RELATED DB: TARGETDB
DBREF 1VS0 A 452 759 UNP P71571 Y938_MYCTU 452 759
DBREF 1VS0 B 452 759 UNP P71571 Y938_MYCTU 452 759
SEQADV 1VS0 GLY A 450 UNP P71571 CLONING ARTIFACT
SEQADV 1VS0 ALA A 451 UNP P71571 CLONING ARTIFACT
SEQADV 1VS0 MSE A 461 UNP P71571 MET 461 MODIFIED RESIDUE
SEQADV 1VS0 APK A 481 UNP P71571 LYS 481 MODIFIED RESIDUE
SEQADV 1VS0 MSE A 545 UNP P71571 MET 545 MODIFIED RESIDUE
SEQADV 1VS0 MSE A 665 UNP P71571 MET 665 MODIFIED RESIDUE
SEQADV 1VS0 MSE A 694 UNP P71571 MET 694 MODIFIED RESIDUE
SEQADV 1VS0 GLY B 450 UNP P71571 CLONING ARTIFACT
SEQADV 1VS0 ALA B 451 UNP P71571 CLONING ARTIFACT
SEQADV 1VS0 MSE B 461 UNP P71571 MET 461 MODIFIED RESIDUE
SEQADV 1VS0 APK B 481 UNP P71571 LYS 481 MODIFIED RESIDUE
SEQADV 1VS0 MSE B 545 UNP P71571 MET 545 MODIFIED RESIDUE
SEQADV 1VS0 MSE B 665 UNP P71571 MET 665 MODIFIED RESIDUE
SEQADV 1VS0 MSE B 694 UNP P71571 MET 694 MODIFIED RESIDUE
SEQRES 1 A 310 GLY ALA VAL PHE GLU PHE ASP ASN LEU ALA PRO MSE LEU
SEQRES 2 A 310 ALA THR HIS GLY THR VAL ALA GLY LEU LYS ALA SER GLN
SEQRES 3 A 310 TRP ALA PHE GLU GLY APK TRP ASP GLY TYR ARG LEU LEU
SEQRES 4 A 310 VAL GLU ALA ASP HIS GLY ALA VAL ARG LEU ARG SER ARG
SEQRES 5 A 310 SER GLY ARG ASP VAL THR ALA GLU TYR PRO GLN LEU ARG
SEQRES 6 A 310 ALA LEU ALA GLU ASP LEU ALA ASP HIS HIS VAL VAL LEU
SEQRES 7 A 310 ASP GLY GLU ALA VAL VAL LEU ASP SER SER GLY VAL PRO
SEQRES 8 A 310 SER PHE SER GLN MSE GLN ASN ARG GLY ARG ASP THR ARG
SEQRES 9 A 310 VAL GLU PHE TRP ALA PHE ASP LEU LEU TYR LEU ASP GLY
SEQRES 10 A 310 ARG ALA LEU LEU GLY THR ARG TYR GLN ASP ARG ARG LYS
SEQRES 11 A 310 LEU LEU GLU THR LEU ALA ASN ALA THR SER LEU THR VAL
SEQRES 12 A 310 PRO GLU LEU LEU PRO GLY ASP GLY ALA GLN ALA PHE ALA
SEQRES 13 A 310 CYS SER ARG LYS HIS GLY TRP GLU GLY VAL ILE ALA LYS
SEQRES 14 A 310 ARG ARG ASP SER ARG TYR GLN PRO GLY ARG ARG CYS ALA
SEQRES 15 A 310 SER TRP VAL LYS ASP LYS HIS TRP ASN THR GLN GLU VAL
SEQRES 16 A 310 VAL ILE GLY GLY TRP ARG ALA GLY GLU GLY GLY ARG SER
SEQRES 17 A 310 SER GLY VAL GLY SER LEU LEU MSE GLY ILE PRO GLY PRO
SEQRES 18 A 310 GLY GLY LEU GLN PHE ALA GLY ARG VAL GLY THR GLY LEU
SEQRES 19 A 310 SER GLU ARG GLU LEU ALA ASN LEU LYS GLU MSE LEU ALA
SEQRES 20 A 310 PRO LEU HIS THR ASP GLU SER PRO PHE ASP VAL PRO LEU
SEQRES 21 A 310 PRO ALA ARG ASP ALA LYS GLY ILE THR TYR VAL LYS PRO
SEQRES 22 A 310 ALA LEU VAL ALA GLU VAL ARG TYR SER GLU TRP THR PRO
SEQRES 23 A 310 GLU GLY ARG LEU ARG GLN SER SER TRP ARG GLY LEU ARG
SEQRES 24 A 310 PRO ASP LYS LYS PRO SER GLU VAL VAL ARG GLU
SEQRES 1 B 310 GLY ALA VAL PHE GLU PHE ASP ASN LEU ALA PRO MSE LEU
SEQRES 2 B 310 ALA THR HIS GLY THR VAL ALA GLY LEU LYS ALA SER GLN
SEQRES 3 B 310 TRP ALA PHE GLU GLY APK TRP ASP GLY TYR ARG LEU LEU
SEQRES 4 B 310 VAL GLU ALA ASP HIS GLY ALA VAL ARG LEU ARG SER ARG
SEQRES 5 B 310 SER GLY ARG ASP VAL THR ALA GLU TYR PRO GLN LEU ARG
SEQRES 6 B 310 ALA LEU ALA GLU ASP LEU ALA ASP HIS HIS VAL VAL LEU
SEQRES 7 B 310 ASP GLY GLU ALA VAL VAL LEU ASP SER SER GLY VAL PRO
SEQRES 8 B 310 SER PHE SER GLN MSE GLN ASN ARG GLY ARG ASP THR ARG
SEQRES 9 B 310 VAL GLU PHE TRP ALA PHE ASP LEU LEU TYR LEU ASP GLY
SEQRES 10 B 310 ARG ALA LEU LEU GLY THR ARG TYR GLN ASP ARG ARG LYS
SEQRES 11 B 310 LEU LEU GLU THR LEU ALA ASN ALA THR SER LEU THR VAL
SEQRES 12 B 310 PRO GLU LEU LEU PRO GLY ASP GLY ALA GLN ALA PHE ALA
SEQRES 13 B 310 CYS SER ARG LYS HIS GLY TRP GLU GLY VAL ILE ALA LYS
SEQRES 14 B 310 ARG ARG ASP SER ARG TYR GLN PRO GLY ARG ARG CYS ALA
SEQRES 15 B 310 SER TRP VAL LYS ASP LYS HIS TRP ASN THR GLN GLU VAL
SEQRES 16 B 310 VAL ILE GLY GLY TRP ARG ALA GLY GLU GLY GLY ARG SER
SEQRES 17 B 310 SER GLY VAL GLY SER LEU LEU MSE GLY ILE PRO GLY PRO
SEQRES 18 B 310 GLY GLY LEU GLN PHE ALA GLY ARG VAL GLY THR GLY LEU
SEQRES 19 B 310 SER GLU ARG GLU LEU ALA ASN LEU LYS GLU MSE LEU ALA
SEQRES 20 B 310 PRO LEU HIS THR ASP GLU SER PRO PHE ASP VAL PRO LEU
SEQRES 21 B 310 PRO ALA ARG ASP ALA LYS GLY ILE THR TYR VAL LYS PRO
SEQRES 22 B 310 ALA LEU VAL ALA GLU VAL ARG TYR SER GLU TRP THR PRO
SEQRES 23 B 310 GLU GLY ARG LEU ARG GLN SER SER TRP ARG GLY LEU ARG
SEQRES 24 B 310 PRO ASP LYS LYS PRO SER GLU VAL VAL ARG GLU
MODRES 1VS0 MSE A 461 MET SELENOMETHIONINE
MODRES 1VS0 APK A 481 LYS
MODRES 1VS0 MSE A 545 MET SELENOMETHIONINE
MODRES 1VS0 MSE A 665 MET SELENOMETHIONINE
MODRES 1VS0 MSE A 694 MET SELENOMETHIONINE
MODRES 1VS0 MSE B 461 MET SELENOMETHIONINE
MODRES 1VS0 APK B 481 LYS
MODRES 1VS0 MSE B 545 MET SELENOMETHIONINE
MODRES 1VS0 MSE B 665 MET SELENOMETHIONINE
MODRES 1VS0 MSE B 694 MET SELENOMETHIONINE
HET MSE A 461 8
HET APK A 481 31
HET MSE A 545 8
HET MSE A 665 8
HET MSE A 694 8
HET MSE B 461 8
HET APK B 481 31
HET MSE B 545 8
HET MSE B 665 8
HET MSE B 694 16
HET ZN B9001 1
HET ZN A9002 1
HET ZN B9003 1
HET ZN A9004 1
HET CL A9005 1
HET CL B9006 1
HET CL A9007 1
HET CL B9008 1
HET MG A9009 1
HETNAM MSE SELENOMETHIONINE
HETNAM APK 5'-O-[(S)-{[(5S)-5-AMINO-6-OXOHEXYL]AMINO}(HYDROXY)
HETNAM 2 APK PHOSPHORYL]ADENOSINE
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 1 APK 2(C16 H26 N7 O7 P)
FORMUL 3 ZN 4(ZN 2+)
FORMUL 7 CL 4(CL 1-)
FORMUL 11 MG MG 2+
FORMUL 12 HOH *407(H2 O)
HELIX 1 1 GLU A 454 LEU A 458 5 5
HELIX 2 2 VAL A 506 GLN A 512 5 7
HELIX 3 3 LEU A 513 LEU A 520 1 8
HELIX 4 4 SER A 541 ASN A 547 1 7
HELIX 5 5 ARG A 573 THR A 588 1 16
HELIX 6 6 ASP A 599 HIS A 610 1 12
HELIX 7 7 SER A 684 ALA A 696 1 13
HELIX 8 8 PRO A 697 HIS A 699 5 3
HELIX 9 9 PRO A 710 LYS A 715 1 6
HELIX 10 10 LYS A 752 VAL A 756 5 5
HELIX 11 11 GLU B 454 LEU B 458 5 5
HELIX 12 12 VAL B 506 GLN B 512 5 7
HELIX 13 13 LEU B 513 LEU B 520 1 8
HELIX 14 14 SER B 541 ASN B 547 1 7
HELIX 15 15 ARG B 573 THR B 588 1 16
HELIX 16 16 ASP B 599 GLY B 611 1 13
HELIX 17 17 SER B 684 ALA B 696 1 13
HELIX 18 18 PRO B 710 LYS B 715 1 6
HELIX 19 19 LYS B 752 VAL B 756 5 5
SHEET 1 A 4 LEU A 462 HIS A 465 0
SHEET 2 A 4 ARG A 629 LYS A 637 1 O TRP A 633 N THR A 464
SHEET 3 A 4 GLY A 614 ARG A 619 -1 N ALA A 617 O VAL A 634
SHEET 4 A 4 TRP A 476 APK A 481 -1 N GLU A 479 O ILE A 616
SHEET 1 B 5 ALA A 495 SER A 500 0
SHEET 2 B 5 TYR A 485 ASP A 492 -1 N GLU A 490 O ARG A 497
SHEET 3 B 5 HIS A 524 VAL A 532 -1 O ALA A 531 N TYR A 485
SHEET 4 B 5 GLU A 555 LEU A 564 -1 O LEU A 562 N VAL A 526
SHEET 5 B 5 ARG A 567 ALA A 568 -1 O ARG A 567 N LEU A 564
SHEET 1 C 4 GLY A 672 VAL A 679 0
SHEET 2 C 4 SER A 662 GLY A 669 -1 N ILE A 667 O GLN A 674
SHEET 3 C 4 ASN A 640 ARG A 650 -1 N GLY A 647 O LEU A 664
SHEET 4 C 4 ILE A 717 TYR A 719 -1 O THR A 718 N TRP A 649
SHEET 1 D 5 GLY A 672 VAL A 679 0
SHEET 2 D 5 SER A 662 GLY A 669 -1 N ILE A 667 O GLN A 674
SHEET 3 D 5 ASN A 640 ARG A 650 -1 N GLY A 647 O LEU A 664
SHEET 4 D 5 VAL A 725 TYR A 730 -1 O TYR A 730 N ASN A 640
SHEET 5 D 5 SER A 743 LEU A 747 -1 O SER A 743 N ARG A 729
SHEET 1 E 4 LEU B 462 HIS B 465 0
SHEET 2 E 4 ARG B 629 LYS B 637 1 O LYS B 635 N THR B 464
SHEET 3 E 4 GLY B 614 ARG B 619 -1 N ALA B 617 O VAL B 634
SHEET 4 E 4 TRP B 476 GLU B 479 -1 N ALA B 477 O LYS B 618
SHEET 1 F 5 ALA B 495 SER B 500 0
SHEET 2 F 5 TYR B 485 ASP B 492 -1 N GLU B 490 O ARG B 497
SHEET 3 F 5 HIS B 524 VAL B 532 -1 O ALA B 531 N TYR B 485
SHEET 4 F 5 GLU B 555 LEU B 564 -1 O LEU B 562 N VAL B 526
SHEET 5 F 5 ARG B 567 ALA B 568 -1 O ARG B 567 N LEU B 564
SHEET 1 G 5 GLY B 672 VAL B 679 0
SHEET 2 G 5 VAL B 660 GLY B 669 -1 N MSE B 665 O ALA B 676
SHEET 3 G 5 ASN B 640 ALA B 651 -1 N VAL B 645 O GLY B 666
SHEET 4 G 5 ILE B 717 VAL B 720 -1 O THR B 718 N TRP B 649
SHEET 5 G 5 HIS B 699 THR B 700 -1 N THR B 700 O TYR B 719
SHEET 1 H 5 GLY B 672 VAL B 679 0
SHEET 2 H 5 VAL B 660 GLY B 669 -1 N MSE B 665 O ALA B 676
SHEET 3 H 5 ASN B 640 ALA B 651 -1 N VAL B 645 O GLY B 666
SHEET 4 H 5 VAL B 725 TYR B 730 -1 O TYR B 730 N ASN B 640
SHEET 5 H 5 SER B 743 LEU B 747 -1 O GLY B 746 N GLU B 727
LINK C PRO A 460 N MSE A 461 1555 1555 1.33
LINK C MSE A 461 N LEU A 462 1555 1555 1.33
LINK C GLY A 480 N APK A 481 1555 1555 1.57
LINK C APK A 481 N TRP A 482 1555 1555 1.75
LINK O1P APK A 481 ZN ZN A9002 1555 1555 1.97
LINK C GLN A 544 N MSE A 545 1555 1555 1.34
LINK C MSE A 545 N GLN A 546 1555 1555 1.32
LINK C LEU A 664 N MSE A 665 1555 1555 1.33
LINK C MSE A 665 N GLY A 666 1555 1555 1.32
LINK C GLU A 693 N MSE A 694 1555 1555 1.33
LINK C MSE A 694 N LEU A 695 1555 1555 1.33
LINK ZN ZN A9002 OD1 ASP A 483 1555 1555 2.15
LINK ZN ZN A9002 OD2 ASP A 483 1555 1555 2.46
LINK ZN ZN A9002 OE1 GLU A 613 1555 1555 2.30
LINK ZN ZN A9002 OE2 GLU A 613 1555 1555 2.41
LINK ZN ZN A9004 CL CL A9007 1555 1555 2.24
LINK ZN ZN A9004 OE1 GLU A 727 1555 1555 1.91
LINK MG MG A9009 OE2 GLU A 454 1555 1555 2.26
LINK MG MG A9009 OE1 GLU A 454 1555 1555 2.23
LINK C PRO B 460 N MSE B 461 1555 1555 1.33
LINK C MSE B 461 N LEU B 462 1555 1555 1.33
LINK C GLY B 480 N APK B 481 1555 1555 1.81
LINK O1P APK B 481 ZN ZN B9001 1555 1555 1.90
LINK C APK B 481 N TRP B 482 1555 1555 1.71
LINK C GLN B 544 N MSE B 545 1555 1555 1.33
LINK C MSE B 545 N GLN B 546 1555 1555 1.31
LINK C LEU B 664 N MSE B 665 1555 1555 1.33
LINK C MSE B 665 N GLY B 666 1555 1555 1.33
LINK C GLU B 693 N BMSE B 694 1555 1555 1.33
LINK C GLU B 693 N AMSE B 694 1555 1555 1.33
LINK C AMSE B 694 N LEU B 695 1555 1555 1.33
LINK C BMSE B 694 N LEU B 695 1555 1555 1.33
LINK ZN ZN B9001 OE2 GLU B 613 1555 1555 1.69
LINK ZN ZN B9001 OD2 ASP B 483 1555 1555 2.16
LINK ZN ZN B9001 OD1 ASP B 483 1555 1555 2.76
LINK ZN ZN B9003 OE2 GLU B 727 1555 1555 2.61
LINK ZN ZN B9003 OE1 GLU B 727 1555 1555 2.11
LINK ZN ZN B9003 CL CL B9008 1555 1555 1.89
LINK ZN ZN A9002 OD2 ASP A 522 1555 6665 2.00
LINK ZN ZN A9004 OD1 ASP A 492 1555 6665 1.91
LINK ZN ZN A9004 ND1 HIS A 493 1555 6665 2.02
LINK MG MG A9009 OD2 ASP B 701 1555 2674 3.11
LINK MG MG A9009 NE2 HIS B 699 1555 2674 1.97
LINK MG MG A9009 OD1 ASP A 750 1555 6655 2.57
LINK MG MG A9009 OD1 ASP B 701 1555 2674 1.91
LINK MG MG A9009 OD2 ASP A 750 1555 6655 2.43
LINK ZN ZN B9001 OD2 ASP B 522 1555 4456 1.94
LINK ZN ZN B9003 ND1 HIS B 493 1555 4456 2.12
LINK ZN ZN B9003 OD2 ASP B 492 1555 4456 1.93
SITE 1 AC1 4 APK B 481 ASP B 483 ASP B 522 GLU B 613
SITE 1 AC2 4 APK A 481 ASP A 483 ASP A 522 GLU A 613
SITE 1 AC3 4 ASP B 492 HIS B 493 GLU B 727 CL B9008
SITE 1 AC4 4 ASP A 492 HIS A 493 GLU A 727 CL A9007
SITE 1 AC5 4 ALA A 463 APK A 481 LYS A 635 HOH A9163
SITE 1 AC6 4 ALA B 463 APK B 481 HOH B9118 HOH B9188
SITE 1 AC7 6 ASP A 492 HIS A 493 GLU A 727 ARG A 748
SITE 2 AC7 6 ZN A9004 HOH A9220
SITE 1 AC8 7 ASP B 492 HIS B 493 HIS B 524 GLU B 727
SITE 2 AC8 7 ARG B 748 ZN B9003 HOH B9178
SITE 1 AC9 5 GLU A 454 ASP A 456 ASP A 750 HIS B 699
SITE 2 AC9 5 ASP B 701
CRYST1 57.102 57.102 368.957 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 0.017510 0.010110 0.000000 0.00000
SCALE2 0.000000 0.020220 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002710 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
