HEADER REPLICATION 31-JAN-03 1NUI
TITLE CRYSTAL STRUCTURE OF THE PRIMASE FRAGMENT OF BACTERIOPHAGE T7 PRIMASE-
TITLE 2 HELICASE PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA PRIMASE/HELICASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-255;
COMPND 5 EC: 2.7.7.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE T7;
SOURCE 3 ORGANISM_TAXID: 10760;
SOURCE 4 GENE: 4;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET17B
KEYWDS ZINC-BIDING DOMAIN, TOPRIM FOLD, DNA REPLICATION, DNA-DIRECTED RNA
KEYWDS 2 POLYMERASE, PRIMOSOME, LATE PROTEIN, ATP-BINDING, TRANSFERASE,
KEYWDS 3 REPLICATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KATO,T.ITO,G.WAGNER,C.C.RICHARDSON,T.ELLENBERGER
REVDAT 5 14-FEB-24 1NUI 1 REMARK
REVDAT 4 27-OCT-21 1NUI 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 1NUI 1 VERSN
REVDAT 2 24-FEB-09 1NUI 1 VERSN
REVDAT 1 27-MAY-03 1NUI 0
JRNL AUTH M.KATO,T.ITO,G.WAGNER,C.C.RICHARDSON,T.ELLENBERGER
JRNL TITL MODULAR ARCHITECTURE OF THE BACTERIOPHAGE T7 PRIMASE COUPLES
JRNL TITL 2 RNA PRIMER SYNTHESIS TO DNA SYNTHESIS
JRNL REF MOL.CELL V. 11 1349 2003
JRNL REFN ISSN 1097-2765
JRNL PMID 12769857
JRNL DOI 10.1016/S1097-2765(03)00195-3
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 19053
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) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1029
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1303
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE SET COUNT : 65
REMARK 3 BIN FREE R VALUE : 0.3640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3763
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 14
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) : 19.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.10000
REMARK 3 B22 (A**2) : 2.10000
REMARK 3 B33 (A**2) : -3.14000
REMARK 3 B12 (A**2) : 1.05000
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): 0.680
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.364
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.284
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.135
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.905
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.859
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3843 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5173 ; 1.464 ; 1.929
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 477 ; 1.173 ; 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): 537 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2940 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2014 ; 0.293 ; 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): 153 ; 0.204 ; 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): 81 ; 0.368 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.090 ; 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): 2371 ; 1.037 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3779 ; 2.025 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1472 ; 3.191 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1394 ; 5.324 ; 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 : 1
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 10 A 40 6
REMARK 3 1 B 10 B 40 6
REMARK 3 2 A 57 A 255 5
REMARK 3 2 B 57 B 255 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1551 ; 0.44 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 238 ; 5.37 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1551 ; 1.57 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 238 ; 3.00 ; 10.00
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 10 A 44
REMARK 3 ORIGIN FOR THE GROUP (A): 90.1725 49.0973 21.9643
REMARK 3 T TENSOR
REMARK 3 T11: 0.5033 T22: 0.5322
REMARK 3 T33: 0.4874 T12: -0.1964
REMARK 3 T13: -0.0843 T23: 0.0801
REMARK 3 L TENSOR
REMARK 3 L11: 14.9892 L22: 11.7408
REMARK 3 L33: 19.8698 L12: -12.0978
REMARK 3 L13: -8.2518 L23: 10.1938
REMARK 3 S TENSOR
REMARK 3 S11: -0.8520 S12: 0.0913 S13: -0.8933
REMARK 3 S21: 1.2635 S22: -0.2976 S23: 0.2412
REMARK 3 S31: 1.0375 S32: 0.9240 S33: 1.1496
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 49 A 255
REMARK 3 ORIGIN FOR THE GROUP (A): 49.7047 69.8542 19.5145
REMARK 3 T TENSOR
REMARK 3 T11: 0.1451 T22: 0.5387
REMARK 3 T33: 0.3389 T12: -0.0390
REMARK 3 T13: -0.0857 T23: 0.1444
REMARK 3 L TENSOR
REMARK 3 L11: 9.6441 L22: 1.9050
REMARK 3 L33: 4.3323 L12: 0.6644
REMARK 3 L13: 3.4306 L23: -0.3648
REMARK 3 S TENSOR
REMARK 3 S11: -0.3447 S12: 0.7708 S13: 0.9336
REMARK 3 S21: -0.1935 S22: 0.1510 S23: 0.1340
REMARK 3 S31: -0.3736 S32: 0.2607 S33: 0.1937
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 10 B 42
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3843 53.7531 39.8301
REMARK 3 T TENSOR
REMARK 3 T11: 0.5678 T22: 0.6547
REMARK 3 T33: 0.4406 T12: 0.0876
REMARK 3 T13: -0.0657 T23: -0.1457
REMARK 3 L TENSOR
REMARK 3 L11: 26.4016 L22: 11.5727
REMARK 3 L33: 11.8456 L12: 14.9794
REMARK 3 L13: -11.5948 L23: -15.3116
REMARK 3 S TENSOR
REMARK 3 S11: -1.1775 S12: 0.3064 S13: -0.4971
REMARK 3 S21: -0.2842 S22: 0.4254 S23: 0.2149
REMARK 3 S31: -0.4126 S32: -0.2590 S33: 0.7521
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 50 B 255
REMARK 3 ORIGIN FOR THE GROUP (A): 82.5700 64.7157 41.4902
REMARK 3 T TENSOR
REMARK 3 T11: 0.0368 T22: 0.2587
REMARK 3 T33: 0.1651 T12: -0.0778
REMARK 3 T13: -0.0269 T23: -0.0601
REMARK 3 L TENSOR
REMARK 3 L11: 4.5707 L22: 1.4009
REMARK 3 L33: 4.1364 L12: 0.1449
REMARK 3 L13: 1.3257 L23: -0.0359
REMARK 3 S TENSOR
REMARK 3 S11: -0.0712 S12: 0.1234 S13: -0.0803
REMARK 3 S21: -0.1411 S22: 0.0668 S23: 0.1447
REMARK 3 S31: -0.0217 S32: -0.2824 S33: 0.0044
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 1NUI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018217.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9474, 0.9797, 0.9795, 0.9300,
REMARK 200 1.5418
REMARK 200 MONOCHROMATOR : HORIZONTAL FOCUSSING 5.05 DEGREE
REMARK 200 ASYMMETRIC CUT SI(111)
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 : 28599
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 65.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.24100
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: MAD
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, MES, DTT, ATP, PH 6.3,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500004 -0.866019 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866032 -0.499996 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.48167
REMARK 290 SMTRY1 3 -0.499996 0.866019 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866032 -0.500004 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 56.96333
REMARK 290 SMTRY1 4 -0.500004 0.866015 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866032 0.500004 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 56.96333
REMARK 290 SMTRY1 6 -0.499996 -0.866023 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866032 0.499996 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 28.48167
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMELECULE:1, 2
REMARK 300 THE AUTHOR INDICATES THAT THE PROTEIN CAN
REMARK 300 FUNCTION AS A MONOMER BUT APPEARS TO FORM A
REMARK 300 DIMER IN THE CRYSTAL POSSIBLY DUE TO CRYSTAL
REMARK 300 PACKING FORCES. SEE REMARK 350 FOR INFORMATION
REMARK 300 ON GENERATING THE BIOLOGICAL MOLECULE(S).
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 MET A 1
REMARK 465 ASP A 2
REMARK 465 ASN A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 ASP A 6
REMARK 465 SER A 7
REMARK 465 ASP A 8
REMARK 465 SER A 9
REMARK 465 GLY A 45
REMARK 465 ASN A 46
REMARK 465 GLU A 47
REMARK 465 ASP A 48
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 ASN B 3
REMARK 465 SER B 4
REMARK 465 HIS B 5
REMARK 465 ASP B 6
REMARK 465 SER B 7
REMARK 465 ASP B 8
REMARK 465 SER B 9
REMARK 465 THR B 43
REMARK 465 ALA B 44
REMARK 465 GLY B 45
REMARK 465 ASN B 46
REMARK 465 GLU B 47
REMARK 465 ASP B 48
REMARK 465 THR B 49
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 CB SER B 22 CB SER B 22 4556 2.11
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 TYR A 13 161.59 174.89
REMARK 500 ASN A 19 -84.53 -108.23
REMARK 500 SER A 22 -158.41 -77.58
REMARK 500 ASP A 31 -46.87 -23.90
REMARK 500 VAL A 38 -77.56 -52.72
REMARK 500 GLU A 40 35.91 74.81
REMARK 500 LYS A 55 10.87 -50.98
REMARK 500 SER A 59 -152.25 -160.31
REMARK 500 ASP A 125 -169.10 -120.14
REMARK 500 LYS A 128 65.01 70.61
REMARK 500 ASN A 148 44.54 -92.97
REMARK 500 CYS A 171 28.90 43.81
REMARK 500 HIS A 180 47.39 -107.69
REMARK 500 ALA A 185 -51.57 -28.11
REMARK 500 PHE A 196 -12.71 -43.20
REMARK 500 LEU A 204 94.29 -56.30
REMARK 500 MET A 205 67.48 -101.34
REMARK 500 ASP A 207 154.28 -43.74
REMARK 500 MET A 208 62.38 -101.09
REMARK 500 VAL A 228 173.16 -57.14
REMARK 500 ARG A 229 137.73 -176.79
REMARK 500 ASN A 244 38.67 -140.86
REMARK 500 SER B 22 103.49 163.39
REMARK 500 ASP B 24 72.33 -110.43
REMARK 500 PHE B 35 124.96 179.91
REMARK 500 VAL B 38 -70.72 -42.76
REMARK 500 GLU B 40 45.64 38.18
REMARK 500 LYS B 55 25.54 -76.98
REMARK 500 SER B 59 -168.77 -174.37
REMARK 500 GLU B 73 0.30 -67.78
REMARK 500 LEU B 81 78.09 -104.41
REMARK 500 ARG B 84 -10.29 -142.28
REMARK 500 VAL B 104 145.10 -33.39
REMARK 500 ASP B 125 -167.93 -111.56
REMARK 500 ASP B 127 25.69 -69.88
REMARK 500 LYS B 128 71.45 40.00
REMARK 500 CYS B 171 13.26 54.47
REMARK 500 TYR B 193 -71.06 -43.88
REMARK 500 MET B 208 54.77 -91.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR B 66 0.06 SIDE CHAIN
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 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 17 SG
REMARK 620 2 CYS A 20 SG 118.0
REMARK 620 3 CYS A 36 SG 104.1 94.7
REMARK 620 4 CYS A 39 SG 113.0 126.9 86.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 157 OE2
REMARK 620 2 ASP A 207 OD1 74.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 237 OD2
REMARK 620 2 HOH A 807 O 162.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 17 SG
REMARK 620 2 CYS B 20 SG 80.5
REMARK 620 3 CYS B 36 SG 85.8 137.9
REMARK 620 4 CYS B 39 SG 95.8 117.0 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 157 OE2
REMARK 620 2 ASP B 207 OD1 73.7
REMARK 620 3 HOH B 805 O 74.4 68.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 604 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 237 OD2
REMARK 620 2 HOH B 804 O 168.7
REMARK 620 N 1
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 604
DBREF 1NUI A 1 255 UNP P03692 PRIM_BPT7 1 255
DBREF 1NUI B 1 255 UNP P03692 PRIM_BPT7 1 255
SEQADV 1NUI GLY A 64 UNP P03692 MET 64 ENGINEERED MUTATION
SEQADV 1NUI GLY B 64 UNP P03692 MET 64 ENGINEERED MUTATION
SEQRES 1 A 255 MET ASP ASN SER HIS ASP SER ASP SER VAL PHE LEU TYR
SEQRES 2 A 255 HIS ILE PRO CYS ASP ASN CYS GLY SER SER ASP GLY ASN
SEQRES 3 A 255 SER LEU PHE SER ASP GLY HIS THR PHE CYS TYR VAL CYS
SEQRES 4 A 255 GLU LYS TRP THR ALA GLY ASN GLU ASP THR LYS GLU ARG
SEQRES 5 A 255 ALA SER LYS ARG LYS PRO SER GLY GLY LYS PRO GLY THR
SEQRES 6 A 255 TYR ASN VAL TRP ASN PHE GLY GLU SER ASN GLY ARG TYR
SEQRES 7 A 255 SER ALA LEU THR ALA ARG GLY ILE SER LYS GLU THR CYS
SEQRES 8 A 255 GLN LYS ALA GLY TYR TRP ILE ALA LYS VAL ASP GLY VAL
SEQRES 9 A 255 MET TYR GLN VAL ALA ASP TYR ARG ASP GLN ASN GLY ASN
SEQRES 10 A 255 ILE VAL SER GLN LYS VAL ARG ASP LYS ASP LYS ASN PHE
SEQRES 11 A 255 LYS THR THR GLY SER HIS LYS SER ASP ALA LEU PHE GLY
SEQRES 12 A 255 LYS HIS LEU TRP ASN GLY GLY LYS LYS ILE VAL VAL THR
SEQRES 13 A 255 GLU GLY GLU ILE ASP MET LEU THR VAL MET GLU LEU GLN
SEQRES 14 A 255 ASP CYS LYS TYR PRO VAL VAL SER LEU GLY HIS GLY ALA
SEQRES 15 A 255 SER ALA ALA LYS LYS THR CYS ALA ALA ASN TYR GLU TYR
SEQRES 16 A 255 PHE ASP GLN PHE GLU GLN ILE ILE LEU MET PHE ASP MET
SEQRES 17 A 255 ASP GLU ALA GLY ARG LYS ALA VAL GLU GLU ALA ALA GLN
SEQRES 18 A 255 VAL LEU PRO ALA GLY LYS VAL ARG VAL ALA VAL LEU PRO
SEQRES 19 A 255 CYS LYS ASP ALA ASN GLU CYS HIS LEU ASN GLY HIS ASP
SEQRES 20 A 255 ARG GLU ILE MET GLU GLN VAL TRP
SEQRES 1 B 255 MET ASP ASN SER HIS ASP SER ASP SER VAL PHE LEU TYR
SEQRES 2 B 255 HIS ILE PRO CYS ASP ASN CYS GLY SER SER ASP GLY ASN
SEQRES 3 B 255 SER LEU PHE SER ASP GLY HIS THR PHE CYS TYR VAL CYS
SEQRES 4 B 255 GLU LYS TRP THR ALA GLY ASN GLU ASP THR LYS GLU ARG
SEQRES 5 B 255 ALA SER LYS ARG LYS PRO SER GLY GLY LYS PRO GLY THR
SEQRES 6 B 255 TYR ASN VAL TRP ASN PHE GLY GLU SER ASN GLY ARG TYR
SEQRES 7 B 255 SER ALA LEU THR ALA ARG GLY ILE SER LYS GLU THR CYS
SEQRES 8 B 255 GLN LYS ALA GLY TYR TRP ILE ALA LYS VAL ASP GLY VAL
SEQRES 9 B 255 MET TYR GLN VAL ALA ASP TYR ARG ASP GLN ASN GLY ASN
SEQRES 10 B 255 ILE VAL SER GLN LYS VAL ARG ASP LYS ASP LYS ASN PHE
SEQRES 11 B 255 LYS THR THR GLY SER HIS LYS SER ASP ALA LEU PHE GLY
SEQRES 12 B 255 LYS HIS LEU TRP ASN GLY GLY LYS LYS ILE VAL VAL THR
SEQRES 13 B 255 GLU GLY GLU ILE ASP MET LEU THR VAL MET GLU LEU GLN
SEQRES 14 B 255 ASP CYS LYS TYR PRO VAL VAL SER LEU GLY HIS GLY ALA
SEQRES 15 B 255 SER ALA ALA LYS LYS THR CYS ALA ALA ASN TYR GLU TYR
SEQRES 16 B 255 PHE ASP GLN PHE GLU GLN ILE ILE LEU MET PHE ASP MET
SEQRES 17 B 255 ASP GLU ALA GLY ARG LYS ALA VAL GLU GLU ALA ALA GLN
SEQRES 18 B 255 VAL LEU PRO ALA GLY LYS VAL ARG VAL ALA VAL LEU PRO
SEQRES 19 B 255 CYS LYS ASP ALA ASN GLU CYS HIS LEU ASN GLY HIS ASP
SEQRES 20 B 255 ARG GLU ILE MET GLU GLN VAL TRP
HET ZN A 501 1
HET MG A 601 1
HET MG A 602 1
HET ZN B 502 1
HET MG B 603 1
HET MG B 604 1
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 MG 4(MG 2+)
FORMUL 9 HOH *14(H2 O)
HELIX 1 1 THR A 49 LYS A 55 1 7
HELIX 2 2 ASN A 70 SER A 74 5 5
HELIX 3 3 LEU A 81 GLY A 85 5 5
HELIX 4 4 SER A 87 GLY A 95 1 9
HELIX 5 5 GLY A 143 TRP A 147 5 5
HELIX 6 6 GLY A 158 ASP A 170 1 13
HELIX 7 7 ALA A 184 ASN A 192 1 9
HELIX 8 8 ASN A 192 ASP A 197 1 6
HELIX 9 9 ASP A 209 LEU A 223 1 15
HELIX 10 10 ASP A 237 LEU A 243 1 7
HELIX 11 11 HIS A 246 TRP A 255 1 10
HELIX 12 12 LYS B 50 LYS B 55 1 6
HELIX 13 13 PHE B 71 ASN B 75 5 5
HELIX 14 14 LEU B 81 GLY B 85 5 5
HELIX 15 15 SER B 87 GLY B 95 1 9
HELIX 16 16 GLY B 143 TRP B 147 5 5
HELIX 17 17 GLY B 158 GLN B 169 1 12
HELIX 18 18 GLY B 181 SER B 183 5 3
HELIX 19 19 ALA B 184 ASN B 192 1 9
HELIX 20 20 ASN B 192 ASP B 197 1 6
HELIX 21 21 ASP B 209 LEU B 223 1 15
HELIX 22 22 ASP B 237 ASN B 244 1 8
HELIX 23 23 HIS B 246 TRP B 255 1 10
SHEET 1 A 4 PHE A 11 ILE A 15 0
SHEET 2 A 4 ASN A 26 PHE A 29 -1 O ASN A 26 N ILE A 15
SHEET 3 A 4 THR A 34 CYS A 36 -1 O PHE A 35 N SER A 27
SHEET 4 A 4 TRP A 42 THR A 43 -1 O THR A 43 N THR A 34
SHEET 1 B 4 TYR A 96 VAL A 101 0
SHEET 2 B 4 VAL A 104 ARG A 112 -1 O VAL A 108 N TRP A 97
SHEET 3 B 4 ILE A 118 ARG A 124 -1 O SER A 120 N TYR A 111
SHEET 4 B 4 LYS A 131 GLY A 134 -1 O LYS A 131 N VAL A 123
SHEET 1 C 4 VAL A 175 VAL A 176 0
SHEET 2 C 4 VAL A 154 THR A 156 1 N VAL A 154 O VAL A 176
SHEET 3 C 4 ILE A 202 MET A 205 1 O MET A 205 N VAL A 155
SHEET 4 C 4 VAL A 228 VAL A 230 1 N ARG A 229 O LEU A 204
SHEET 1 D 3 PHE B 11 TYR B 13 0
SHEET 2 D 3 ASN B 26 PHE B 29 -1 O LEU B 28 N TYR B 13
SHEET 3 D 3 THR B 34 CYS B 36 -1 O PHE B 35 N SER B 27
SHEET 1 E 4 TYR B 96 LYS B 100 0
SHEET 2 E 4 MET B 105 ARG B 112 -1 O VAL B 108 N TRP B 97
SHEET 3 E 4 ILE B 118 ARG B 124 -1 O SER B 120 N TYR B 111
SHEET 4 E 4 THR B 132 GLY B 134 -1 O THR B 133 N GLN B 121
SHEET 1 F 5 LEU B 141 PHE B 142 0
SHEET 2 F 5 VAL B 175 LEU B 178 -1 O SER B 177 N PHE B 142
SHEET 3 F 5 GLY B 150 THR B 156 1 N THR B 156 O VAL B 176
SHEET 4 F 5 PHE B 199 MET B 205 1 O ILE B 203 N VAL B 155
SHEET 5 F 5 VAL B 228 VAL B 230 1 O ARG B 229 N LEU B 204
LINK SG CYS A 17 ZN ZN A 501 1555 1555 2.46
LINK SG CYS A 20 ZN ZN A 501 1555 1555 2.23
LINK SG CYS A 36 ZN ZN A 501 1555 1555 2.31
LINK SG CYS A 39 ZN ZN A 501 1555 1555 2.40
LINK OE2 GLU A 157 MG MG A 601 1555 1555 2.46
LINK OD1 ASP A 207 MG MG A 601 1555 1555 2.24
LINK OD2 ASP A 237 MG MG A 602 1555 1555 2.55
LINK MG MG A 602 O HOH A 807 1555 1555 2.77
LINK SG CYS B 17 ZN ZN B 502 1555 1555 2.59
LINK SG CYS B 20 ZN ZN B 502 1555 1555 2.39
LINK SG CYS B 36 ZN ZN B 502 1555 1555 2.25
LINK SG CYS B 39 ZN ZN B 502 1555 1555 2.55
LINK OE2 GLU B 157 MG MG B 603 1555 1555 2.14
LINK OD1 ASP B 207 MG MG B 603 1555 1555 2.04
LINK OD2 ASP B 237 MG MG B 604 1555 1555 2.32
LINK MG MG B 603 O HOH B 805 1555 1555 2.31
LINK MG MG B 604 O HOH B 804 1555 1555 3.13
SITE 1 AC1 4 CYS A 17 CYS A 20 CYS A 36 CYS A 39
SITE 1 AC2 4 CYS B 17 CYS B 20 CYS B 36 CYS B 39
SITE 1 AC3 2 GLU A 157 ASP A 207
SITE 1 AC4 3 ARG A 84 ASP A 237 HOH A 807
SITE 1 AC5 4 GLU B 157 ASP B 207 ASP B 209 HOH B 805
SITE 1 AC6 1 ASP B 237
CRYST1 136.459 136.460 85.445 90.00 90.00 120.00 P 31 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 0.007328 0.004231 0.000000 0.00000
SCALE2 0.000000 0.008462 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011703 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
