HEADER TRANSFERASE 14-FEB-05 1VR6
TITLE CRYSTAL STRUCTURE OF PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE (DAHP
TITLE 2 SYNTHASE) (TM0343) FROM THERMOTOGA MARITIMA AT 1.92 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PHOSPHO-2-KETO-3-DEOXYHEPTONATE ALDOLASE, DAHP SYNTHETASE,
COMPND 5 3-DEOXY-D-ARABINO-HEPTULOSONATE 7-PHOSPHATE SYNTHASE;
COMPND 6 EC: 2.5.1.54;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: TM0343;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS TM0343, PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE (EC 2.5.1.54)
KEYWDS 2 (DAHP SYNTHASE), STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 5 20-SEP-23 1VR6 1 REMARK
REVDAT 4 25-JAN-23 1VR6 1 SEQADV
REVDAT 3 13-JUL-11 1VR6 1 VERSN
REVDAT 2 24-FEB-09 1VR6 1 VERSN
REVDAT 1 08-MAR-05 1VR6 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE
JRNL TITL 2 ALDOLASE (DAHP SYNTHASE) (TM0343) FROM THERMOTOGA MARITIMA
JRNL TITL 3 AT 1.92 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.92 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.92
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 97241
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5111
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) : 1.92
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6387
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE SET COUNT : 321
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10375
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 615
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 44.73
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : -0.29000
REMARK 3 B33 (A**2) : 0.28000
REMARK 3 B12 (A**2) : 0.00000
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): 0.153
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.142
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.386
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10573 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 9954 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14297 ; 1.516 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): 23062 ; 0.842 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1353 ; 5.943 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 438 ;35.389 ;23.858
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1853 ;14.676 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 69 ;20.190 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1655 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11752 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2053 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2051 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 10028 ; 0.192 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5162 ; 0.172 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 6179 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 591 ; 0.180 ; 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): 21 ; 0.271 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 68 ; 0.298 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.179 ; 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): 6915 ; 2.113 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2786 ; 0.604 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10835 ; 3.095 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4023 ; 5.247 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3462 ; 7.058 ;11.000
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A -4 A 70 6
REMARK 3 1 B -3 B 70 6
REMARK 3 1 C -4 C 70 6
REMARK 3 1 D -2 D 70 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 1026 ; 0.62 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 1026 ; 0.62 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 1026 ; 0.66 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 D (A): 1026 ; 0.67 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1026 ; 2.05 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 1026 ; 2.22 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 1026 ; 2.73 ; 10.00
REMARK 3 LOOSE THERMAL 1 D (A**2): 1026 ; 2.39 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 71 A 338 6
REMARK 3 1 B 71 B 338 6
REMARK 3 1 C 71 C 338 6
REMARK 3 1 D 71 D 338 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 2 A (A): 3784 ; 0.49 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 B (A): 3784 ; 0.53 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 C (A): 3784 ; 0.49 ; 5.00
REMARK 3 LOOSE POSITIONAL 2 D (A): 3784 ; 0.48 ; 5.00
REMARK 3 LOOSE THERMAL 2 A (A**2): 3784 ; 3.48 ; 10.00
REMARK 3 LOOSE THERMAL 2 B (A**2): 3784 ; 2.84 ; 10.00
REMARK 3 LOOSE THERMAL 2 C (A**2): 3784 ; 2.60 ; 10.00
REMARK 3 LOOSE THERMAL 2 D (A**2): 3784 ; 2.57 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
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 -4 A 70
REMARK 3 ORIGIN FOR THE GROUP (A): -38.1290 -17.6880 38.3190
REMARK 3 T TENSOR
REMARK 3 T11: -0.1122 T22: 0.0785
REMARK 3 T33: 0.0528 T12: 0.0711
REMARK 3 T13: -0.0268 T23: 0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 7.2752 L22: 3.4076
REMARK 3 L33: 1.4194 L12: 0.4146
REMARK 3 L13: 2.1389 L23: 1.7575
REMARK 3 S TENSOR
REMARK 3 S11: -0.0864 S12: -0.5558 S13: 0.0864
REMARK 3 S21: 0.2051 S22: 0.0570 S23: 0.2715
REMARK 3 S31: -0.0737 S32: -0.3104 S33: 0.0294
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 71 A 338
REMARK 3 ORIGIN FOR THE GROUP (A): -1.6510 -30.8880 51.0910
REMARK 3 T TENSOR
REMARK 3 T11: -0.2787 T22: -0.1489
REMARK 3 T33: -0.2117 T12: 0.0049
REMARK 3 T13: -0.0086 T23: -0.0426
REMARK 3 L TENSOR
REMARK 3 L11: 1.9343 L22: 1.4756
REMARK 3 L33: 1.7715 L12: -0.1985
REMARK 3 L13: 0.6319 L23: -0.3890
REMARK 3 S TENSOR
REMARK 3 S11: 0.0154 S12: -0.2259 S13: -0.0134
REMARK 3 S21: 0.0176 S22: -0.0584 S23: -0.1058
REMARK 3 S31: 0.0726 S32: -0.0381 S33: 0.0430
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 -3 B 70
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7380 -64.8750 24.0340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0681 T22: -0.1533
REMARK 3 T33: -0.0535 T12: 0.0084
REMARK 3 T13: 0.0743 T23: -0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 5.0641 L22: 6.3550
REMARK 3 L33: 1.7910 L12: 2.5242
REMARK 3 L13: -0.7374 L23: 0.7950
REMARK 3 S TENSOR
REMARK 3 S11: -0.0821 S12: 0.3050 S13: -0.1858
REMARK 3 S21: -0.7356 S22: 0.1480 S23: -0.2934
REMARK 3 S31: -0.3286 S32: -0.0731 S33: -0.0660
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 71 B 338
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4460 -24.6820 16.6900
REMARK 3 T TENSOR
REMARK 3 T11: -0.0412 T22: -0.1817
REMARK 3 T33: -0.2064 T12: -0.0261
REMARK 3 T13: 0.0602 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 1.3398 L22: 2.9019
REMARK 3 L33: 2.1186 L12: 0.1374
REMARK 3 L13: -0.4672 L23: -0.4827
REMARK 3 S TENSOR
REMARK 3 S11: -0.1000 S12: 0.2663 S13: 0.0787
REMARK 3 S21: -0.6367 S22: 0.0396 S23: -0.0938
REMARK 3 S31: 0.0433 S32: -0.1146 S33: 0.0604
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C -4 C 70
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8590 -58.8510 40.2380
REMARK 3 T TENSOR
REMARK 3 T11: -0.1148 T22: -0.0468
REMARK 3 T33: -0.0277 T12: 0.0190
REMARK 3 T13: 0.0437 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 5.4116 L22: 3.6391
REMARK 3 L33: 1.7045 L12: 1.8828
REMARK 3 L13: -0.1802 L23: -0.1948
REMARK 3 S TENSOR
REMARK 3 S11: 0.0495 S12: -0.3733 S13: -0.3409
REMARK 3 S21: 0.0435 S22: 0.0483 S23: -0.2844
REMARK 3 S31: -0.0262 S32: 0.0349 S33: -0.0977
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 71 C 338
REMARK 3 ORIGIN FOR THE GROUP (A): -33.2340 -46.9040 47.3740
REMARK 3 T TENSOR
REMARK 3 T11: -0.2603 T22: -0.0417
REMARK 3 T33: -0.0930 T12: -0.0320
REMARK 3 T13: 0.0029 T23: 0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 2.7520 L22: 1.4718
REMARK 3 L33: 2.3699 L12: -0.2207
REMARK 3 L13: -0.5042 L23: 0.1032
REMARK 3 S TENSOR
REMARK 3 S11: -0.0441 S12: -0.2089 S13: -0.0631
REMARK 3 S21: 0.0171 S22: -0.0193 S23: 0.2766
REMARK 3 S31: -0.0460 S32: -0.2965 S33: 0.0634
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D -2 D 70
REMARK 3 ORIGIN FOR THE GROUP (A): -26.8590 -9.8380 25.3190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0066 T22: -0.0359
REMARK 3 T33: 0.0746 T12: 0.0606
REMARK 3 T13: -0.0582 T23: 0.0545
REMARK 3 L TENSOR
REMARK 3 L11: 4.3290 L22: 6.0154
REMARK 3 L33: 2.0994 L12: 1.2707
REMARK 3 L13: 0.9366 L23: 1.1819
REMARK 3 S TENSOR
REMARK 3 S11: 0.0509 S12: 0.2680 S13: 0.4192
REMARK 3 S21: -0.5847 S22: -0.0383 S23: 0.2790
REMARK 3 S31: -0.3094 S32: -0.1106 S33: -0.0126
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 71 D 338
REMARK 3 ORIGIN FOR THE GROUP (A): -28.1240 -49.5130 13.2610
REMARK 3 T TENSOR
REMARK 3 T11: 0.0722 T22: -0.0489
REMARK 3 T33: -0.1207 T12: -0.0549
REMARK 3 T13: -0.1198 T23: -0.0582
REMARK 3 L TENSOR
REMARK 3 L11: 1.3216 L22: 2.7022
REMARK 3 L33: 3.0486 L12: -0.1667
REMARK 3 L13: 0.3319 L23: 0.6457
REMARK 3 S TENSOR
REMARK 3 S11: -0.0147 S12: 0.2993 S13: -0.1375
REMARK 3 S21: -0.6461 S22: -0.0550 S23: 0.1675
REMARK 3 S31: 0.1886 S32: -0.1286 S33: 0.0697
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS 2. THERE IS A LARGE POSITIVE PEAK BETWEEN
REMARK 3 RESIDUE 211 OF CHAINS A AND C AND B AND D.
REMARK 4
REMARK 4 1VR6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000002078.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-AUG-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL SI(111)
REMARK 200 OPTICS : FIXED-HEIGHT EXIT BEAM, TOROIDAL
REMARK 200 FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 102464
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.920
REMARK 200 RESOLUTION RANGE LOW (A) : 47.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.570
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.63
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.65900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.490
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1RZM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35.0% ETHYLENE-GLYCOL, 0.1M ACETATE,
REMARK 280 PH 5.5, VAPOR DIFFUSION, SITTING DROP, NANODROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 36.57550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 124.77000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.11300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 124.77000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.57550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.11300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 MET B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 ASP B -8
REMARK 465 LYS B -7
REMARK 465 ILE B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 THR B 134
REMARK 465 SER B 135
REMARK 465 PRO B 136
REMARK 465 TYR B 137
REMARK 465 MET C -11
REMARK 465 GLY C -10
REMARK 465 SER C -9
REMARK 465 ASP C -8
REMARK 465 LYS C -7
REMARK 465 ILE C -6
REMARK 465 HIS C -5
REMARK 465 SER C 135
REMARK 465 PRO C 136
REMARK 465 TYR C 137
REMARK 465 SER C 138
REMARK 465 MET D -11
REMARK 465 GLY D -10
REMARK 465 SER D -9
REMARK 465 ASP D -8
REMARK 465 LYS D -7
REMARK 465 ILE D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 TYR D 137
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 12 CD OE1 OE2
REMARK 470 LYS A 19 CG CD CE NZ
REMARK 470 LYS A 27 CG CD CE NZ
REMARK 470 LYS A 32 CE NZ
REMARK 470 GLN A 34 CG CD OE1 NE2
REMARK 470 ASP A 45 CG OD1 OD2
REMARK 470 TYR A 47 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN A 92 CB CG OD1 ND2
REMARK 470 LYS B 19 CE NZ
REMARK 470 LYS B 27 CD CE NZ
REMARK 470 TYR B 47 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 70 CG CD CE NZ
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 GLU B 168 CG CD OE1 OE2
REMARK 470 ARG B 192 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 196 CD CE NZ
REMARK 470 LYS B 260 CE NZ
REMARK 470 LYS B 305 CE NZ
REMARK 470 LYS C 19 CG CD CE NZ
REMARK 470 LYS C 27 CG CD CE NZ
REMARK 470 GLN C 34 CB CG CD OE1 NE2
REMARK 470 GLU C 79 CD OE1 OE2
REMARK 470 ASN C 92 CG OD1 ND2
REMARK 470 ARG C 133 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 140 CB CG CD OE1 NE2
REMARK 470 LYS C 145 CG CD CE NZ
REMARK 470 LYS C 156 CG CD CE NZ
REMARK 470 ARG C 186 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 260 CD CE NZ
REMARK 470 LYS C 336 CD CE NZ
REMARK 470 GLU D 11 CG CD OE1 OE2
REMARK 470 GLU D 12 CG CD OE1 OE2
REMARK 470 ARG D 15 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 46 CG CD NE CZ NH1 NH2
REMARK 470 TYR D 47 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP D 51 CG OD1 OD2
REMARK 470 LYS D 52 CG CD CE NZ
REMARK 470 LYS D 70 CG CD CE NZ
REMARK 470 GLU D 79 CG CD OE1 OE2
REMARK 470 ASP D 87 CG OD1 OD2
REMARK 470 ASN D 92 CG OD1 ND2
REMARK 470 GLU D 108 CG CD OE1 OE2
REMARK 470 GLU D 119 CD OE1 OE2
REMARK 470 LYS D 123 CD CE NZ
REMARK 470 LYS D 131 CE NZ
REMARK 470 ARG D 133 CG CD NE CZ NH1 NH2
REMARK 470 THR D 134 OG1 CG2
REMARK 470 SER D 135 CB OG
REMARK 470 GLN D 140 CG CD OE1 NE2
REMARK 470 LEU D 142 CG CD1 CD2
REMARK 470 LYS D 145 CG CD CE NZ
REMARK 470 ASP D 169 CG OD1 OD2
REMARK 470 LYS D 173 CD CE NZ
REMARK 470 ARG D 186 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 192 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 196 CD CE NZ
REMARK 470 LYS D 260 CD CE NZ
REMARK 470 LYS D 305 CE NZ
REMARK 470 LYS D 311 CE NZ
REMARK 470 LYS D 327 CE NZ
REMARK 470 LYS D 328 CD CE NZ
REMARK 470 LYS D 336 CG CD CE NZ
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 298 OG SER A 313 2.03
REMARK 500 O HOH A 452 O HOH A 531 2.04
REMARK 500 SG CYS D 102 OE2 GLU D 298 2.05
REMARK 500 O HOH D 435 O HOH D 436 2.08
REMARK 500 O HOH A 438 O HOH A 521 2.12
REMARK 500 O HOH C 488 O HOH D 437 2.12
REMARK 500 O HOH A 499 O HOH A 529 2.13
REMARK 500 O HOH A 398 O HOH A 526 2.13
REMARK 500 O HOH A 375 O HOH A 532 2.16
REMARK 500 CD GLU A 298 OG SER A 313 2.17
REMARK 500 O HOH A 408 O HOH C 483 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 TYR D 157 C TYR D 157 O 0.128
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 ARG A 240 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 240 NE - CZ - NH2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 285 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 285 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ARG B 285 NE - CZ - NH1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG B 285 NE - CZ - NH2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ARG D 285 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG D 285 NE - CZ - NH2 ANGL. DEV. = -3.6 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 LYS A 70 -52.35 -129.57
REMARK 500 ASN A 92 120.37 -38.07
REMARK 500 ASP A 251 78.89 -101.76
REMARK 500 LYS B 70 -47.69 -136.28
REMARK 500 LYS C 70 -51.63 -132.12
REMARK 500 ASN C 92 118.17 -32.58
REMARK 500 LYS D 70 -43.56 -138.49
REMARK 500 HIS D 77 78.20 -150.56
REMARK 500 THR D 134 -143.00 -114.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS A -4 HIS A -3 148.79
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 282218 RELATED DB: TARGETDB
DBREF 1VR6 A 1 338 UNP Q9WYH8 AROF_THEMA 1 338
DBREF 1VR6 B 1 338 UNP Q9WYH8 AROF_THEMA 1 338
DBREF 1VR6 C 1 338 UNP Q9WYH8 AROF_THEMA 1 338
DBREF 1VR6 D 1 338 UNP Q9WYH8 AROF_THEMA 1 338
SEQADV 1VR6 MET A -11 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 GLY A -10 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 SER A -9 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 ASP A -8 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 LYS A -7 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 ILE A -6 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS A -5 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS A -4 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS A -3 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS A -2 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS A -1 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS A 0 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 MET B -11 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 GLY B -10 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 SER B -9 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 ASP B -8 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 LYS B -7 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 ILE B -6 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS B -5 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS B -4 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS B -3 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS B -2 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS B -1 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS B 0 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 MET C -11 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 GLY C -10 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 SER C -9 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 ASP C -8 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 LYS C -7 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 ILE C -6 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS C -5 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS C -4 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS C -3 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS C -2 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS C -1 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS C 0 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 MET D -11 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 GLY D -10 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 SER D -9 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 ASP D -8 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 LYS D -7 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 ILE D -6 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS D -5 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS D -4 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS D -3 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS D -2 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS D -1 UNP Q9WYH8 EXPRESSION TAG
SEQADV 1VR6 HIS D 0 UNP Q9WYH8 EXPRESSION TAG
SEQRES 1 A 350 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 A 350 ILE VAL VAL LEU LYS PRO GLY SER THR GLU GLU ASP ILE
SEQRES 3 A 350 ARG LYS VAL VAL LYS LEU ALA GLU SER TYR ASN LEU LYS
SEQRES 4 A 350 CYS HIS ILE SER LYS GLY GLN GLU ARG THR VAL ILE GLY
SEQRES 5 A 350 ILE ILE GLY ASP ASP ARG TYR VAL VAL ALA ASP LYS PHE
SEQRES 6 A 350 GLU SER LEU ASP CYS VAL GLU SER VAL VAL ARG VAL LEU
SEQRES 7 A 350 LYS PRO TYR LYS LEU VAL SER ARG GLU PHE HIS PRO GLU
SEQRES 8 A 350 ASP THR VAL ILE ASP LEU GLY ASP VAL LYS ILE GLY ASN
SEQRES 9 A 350 GLY TYR PHE THR ILE ILE ALA GLY PRO CYS SER VAL GLU
SEQRES 10 A 350 GLY ARG GLU MET LEU MET GLU THR ALA HIS PHE LEU SER
SEQRES 11 A 350 GLU LEU GLY VAL LYS VAL LEU ARG GLY GLY ALA TYR LYS
SEQRES 12 A 350 PRO ARG THR SER PRO TYR SER PHE GLN GLY LEU GLY GLU
SEQRES 13 A 350 LYS GLY LEU GLU TYR LEU ARG GLU ALA ALA ASP LYS TYR
SEQRES 14 A 350 GLY MET TYR VAL VAL THR GLU ALA LEU GLY GLU ASP ASP
SEQRES 15 A 350 LEU PRO LYS VAL ALA GLU TYR ALA ASP ILE ILE GLN ILE
SEQRES 16 A 350 GLY ALA ARG ASN ALA GLN ASN PHE ARG LEU LEU SER LYS
SEQRES 17 A 350 ALA GLY SER TYR ASN LYS PRO VAL LEU LEU LYS ARG GLY
SEQRES 18 A 350 PHE MET ASN THR ILE GLU GLU PHE LEU LEU SER ALA GLU
SEQRES 19 A 350 TYR ILE ALA ASN SER GLY ASN THR LYS ILE ILE LEU CYS
SEQRES 20 A 350 GLU ARG GLY ILE ARG THR PHE GLU LYS ALA THR ARG ASN
SEQRES 21 A 350 THR LEU ASP ILE SER ALA VAL PRO ILE ILE ARG LYS GLU
SEQRES 22 A 350 SER HIS LEU PRO ILE LEU VAL ASP PRO SER HIS SER GLY
SEQRES 23 A 350 GLY ARG ARG ASP LEU VAL ILE PRO LEU SER ARG ALA ALA
SEQRES 24 A 350 ILE ALA VAL GLY ALA HIS GLY ILE ILE VAL GLU VAL HIS
SEQRES 25 A 350 PRO GLU PRO GLU LYS ALA LEU SER ASP GLY LYS GLN SER
SEQRES 26 A 350 LEU ASP PHE GLU LEU PHE LYS GLU LEU VAL GLN GLU MET
SEQRES 27 A 350 LYS LYS LEU ALA ASP ALA LEU GLY VAL LYS VAL ASN
SEQRES 1 B 350 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 B 350 ILE VAL VAL LEU LYS PRO GLY SER THR GLU GLU ASP ILE
SEQRES 3 B 350 ARG LYS VAL VAL LYS LEU ALA GLU SER TYR ASN LEU LYS
SEQRES 4 B 350 CYS HIS ILE SER LYS GLY GLN GLU ARG THR VAL ILE GLY
SEQRES 5 B 350 ILE ILE GLY ASP ASP ARG TYR VAL VAL ALA ASP LYS PHE
SEQRES 6 B 350 GLU SER LEU ASP CYS VAL GLU SER VAL VAL ARG VAL LEU
SEQRES 7 B 350 LYS PRO TYR LYS LEU VAL SER ARG GLU PHE HIS PRO GLU
SEQRES 8 B 350 ASP THR VAL ILE ASP LEU GLY ASP VAL LYS ILE GLY ASN
SEQRES 9 B 350 GLY TYR PHE THR ILE ILE ALA GLY PRO CYS SER VAL GLU
SEQRES 10 B 350 GLY ARG GLU MET LEU MET GLU THR ALA HIS PHE LEU SER
SEQRES 11 B 350 GLU LEU GLY VAL LYS VAL LEU ARG GLY GLY ALA TYR LYS
SEQRES 12 B 350 PRO ARG THR SER PRO TYR SER PHE GLN GLY LEU GLY GLU
SEQRES 13 B 350 LYS GLY LEU GLU TYR LEU ARG GLU ALA ALA ASP LYS TYR
SEQRES 14 B 350 GLY MET TYR VAL VAL THR GLU ALA LEU GLY GLU ASP ASP
SEQRES 15 B 350 LEU PRO LYS VAL ALA GLU TYR ALA ASP ILE ILE GLN ILE
SEQRES 16 B 350 GLY ALA ARG ASN ALA GLN ASN PHE ARG LEU LEU SER LYS
SEQRES 17 B 350 ALA GLY SER TYR ASN LYS PRO VAL LEU LEU LYS ARG GLY
SEQRES 18 B 350 PHE MET ASN THR ILE GLU GLU PHE LEU LEU SER ALA GLU
SEQRES 19 B 350 TYR ILE ALA ASN SER GLY ASN THR LYS ILE ILE LEU CYS
SEQRES 20 B 350 GLU ARG GLY ILE ARG THR PHE GLU LYS ALA THR ARG ASN
SEQRES 21 B 350 THR LEU ASP ILE SER ALA VAL PRO ILE ILE ARG LYS GLU
SEQRES 22 B 350 SER HIS LEU PRO ILE LEU VAL ASP PRO SER HIS SER GLY
SEQRES 23 B 350 GLY ARG ARG ASP LEU VAL ILE PRO LEU SER ARG ALA ALA
SEQRES 24 B 350 ILE ALA VAL GLY ALA HIS GLY ILE ILE VAL GLU VAL HIS
SEQRES 25 B 350 PRO GLU PRO GLU LYS ALA LEU SER ASP GLY LYS GLN SER
SEQRES 26 B 350 LEU ASP PHE GLU LEU PHE LYS GLU LEU VAL GLN GLU MET
SEQRES 27 B 350 LYS LYS LEU ALA ASP ALA LEU GLY VAL LYS VAL ASN
SEQRES 1 C 350 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 C 350 ILE VAL VAL LEU LYS PRO GLY SER THR GLU GLU ASP ILE
SEQRES 3 C 350 ARG LYS VAL VAL LYS LEU ALA GLU SER TYR ASN LEU LYS
SEQRES 4 C 350 CYS HIS ILE SER LYS GLY GLN GLU ARG THR VAL ILE GLY
SEQRES 5 C 350 ILE ILE GLY ASP ASP ARG TYR VAL VAL ALA ASP LYS PHE
SEQRES 6 C 350 GLU SER LEU ASP CYS VAL GLU SER VAL VAL ARG VAL LEU
SEQRES 7 C 350 LYS PRO TYR LYS LEU VAL SER ARG GLU PHE HIS PRO GLU
SEQRES 8 C 350 ASP THR VAL ILE ASP LEU GLY ASP VAL LYS ILE GLY ASN
SEQRES 9 C 350 GLY TYR PHE THR ILE ILE ALA GLY PRO CYS SER VAL GLU
SEQRES 10 C 350 GLY ARG GLU MET LEU MET GLU THR ALA HIS PHE LEU SER
SEQRES 11 C 350 GLU LEU GLY VAL LYS VAL LEU ARG GLY GLY ALA TYR LYS
SEQRES 12 C 350 PRO ARG THR SER PRO TYR SER PHE GLN GLY LEU GLY GLU
SEQRES 13 C 350 LYS GLY LEU GLU TYR LEU ARG GLU ALA ALA ASP LYS TYR
SEQRES 14 C 350 GLY MET TYR VAL VAL THR GLU ALA LEU GLY GLU ASP ASP
SEQRES 15 C 350 LEU PRO LYS VAL ALA GLU TYR ALA ASP ILE ILE GLN ILE
SEQRES 16 C 350 GLY ALA ARG ASN ALA GLN ASN PHE ARG LEU LEU SER LYS
SEQRES 17 C 350 ALA GLY SER TYR ASN LYS PRO VAL LEU LEU LYS ARG GLY
SEQRES 18 C 350 PHE MET ASN THR ILE GLU GLU PHE LEU LEU SER ALA GLU
SEQRES 19 C 350 TYR ILE ALA ASN SER GLY ASN THR LYS ILE ILE LEU CYS
SEQRES 20 C 350 GLU ARG GLY ILE ARG THR PHE GLU LYS ALA THR ARG ASN
SEQRES 21 C 350 THR LEU ASP ILE SER ALA VAL PRO ILE ILE ARG LYS GLU
SEQRES 22 C 350 SER HIS LEU PRO ILE LEU VAL ASP PRO SER HIS SER GLY
SEQRES 23 C 350 GLY ARG ARG ASP LEU VAL ILE PRO LEU SER ARG ALA ALA
SEQRES 24 C 350 ILE ALA VAL GLY ALA HIS GLY ILE ILE VAL GLU VAL HIS
SEQRES 25 C 350 PRO GLU PRO GLU LYS ALA LEU SER ASP GLY LYS GLN SER
SEQRES 26 C 350 LEU ASP PHE GLU LEU PHE LYS GLU LEU VAL GLN GLU MET
SEQRES 27 C 350 LYS LYS LEU ALA ASP ALA LEU GLY VAL LYS VAL ASN
SEQRES 1 D 350 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 D 350 ILE VAL VAL LEU LYS PRO GLY SER THR GLU GLU ASP ILE
SEQRES 3 D 350 ARG LYS VAL VAL LYS LEU ALA GLU SER TYR ASN LEU LYS
SEQRES 4 D 350 CYS HIS ILE SER LYS GLY GLN GLU ARG THR VAL ILE GLY
SEQRES 5 D 350 ILE ILE GLY ASP ASP ARG TYR VAL VAL ALA ASP LYS PHE
SEQRES 6 D 350 GLU SER LEU ASP CYS VAL GLU SER VAL VAL ARG VAL LEU
SEQRES 7 D 350 LYS PRO TYR LYS LEU VAL SER ARG GLU PHE HIS PRO GLU
SEQRES 8 D 350 ASP THR VAL ILE ASP LEU GLY ASP VAL LYS ILE GLY ASN
SEQRES 9 D 350 GLY TYR PHE THR ILE ILE ALA GLY PRO CYS SER VAL GLU
SEQRES 10 D 350 GLY ARG GLU MET LEU MET GLU THR ALA HIS PHE LEU SER
SEQRES 11 D 350 GLU LEU GLY VAL LYS VAL LEU ARG GLY GLY ALA TYR LYS
SEQRES 12 D 350 PRO ARG THR SER PRO TYR SER PHE GLN GLY LEU GLY GLU
SEQRES 13 D 350 LYS GLY LEU GLU TYR LEU ARG GLU ALA ALA ASP LYS TYR
SEQRES 14 D 350 GLY MET TYR VAL VAL THR GLU ALA LEU GLY GLU ASP ASP
SEQRES 15 D 350 LEU PRO LYS VAL ALA GLU TYR ALA ASP ILE ILE GLN ILE
SEQRES 16 D 350 GLY ALA ARG ASN ALA GLN ASN PHE ARG LEU LEU SER LYS
SEQRES 17 D 350 ALA GLY SER TYR ASN LYS PRO VAL LEU LEU LYS ARG GLY
SEQRES 18 D 350 PHE MET ASN THR ILE GLU GLU PHE LEU LEU SER ALA GLU
SEQRES 19 D 350 TYR ILE ALA ASN SER GLY ASN THR LYS ILE ILE LEU CYS
SEQRES 20 D 350 GLU ARG GLY ILE ARG THR PHE GLU LYS ALA THR ARG ASN
SEQRES 21 D 350 THR LEU ASP ILE SER ALA VAL PRO ILE ILE ARG LYS GLU
SEQRES 22 D 350 SER HIS LEU PRO ILE LEU VAL ASP PRO SER HIS SER GLY
SEQRES 23 D 350 GLY ARG ARG ASP LEU VAL ILE PRO LEU SER ARG ALA ALA
SEQRES 24 D 350 ILE ALA VAL GLY ALA HIS GLY ILE ILE VAL GLU VAL HIS
SEQRES 25 D 350 PRO GLU PRO GLU LYS ALA LEU SER ASP GLY LYS GLN SER
SEQRES 26 D 350 LEU ASP PHE GLU LEU PHE LYS GLU LEU VAL GLN GLU MET
SEQRES 27 D 350 LYS LYS LEU ALA ASP ALA LEU GLY VAL LYS VAL ASN
FORMUL 5 HOH *615(H2 O)
HELIX 1 1 THR A 10 TYR A 24 1 15
HELIX 2 2 VAL A 49 SER A 55 1 7
HELIX 3 3 GLY A 106 LEU A 120 1 15
HELIX 4 4 GLY A 143 GLY A 158 1 16
HELIX 5 5 GLY A 167 ASP A 169 5 3
HELIX 6 6 ASP A 170 ALA A 178 1 9
HELIX 7 7 GLY A 184 ALA A 188 5 5
HELIX 8 8 ASN A 190 SER A 199 1 10
HELIX 9 9 THR A 213 SER A 227 1 15
HELIX 10 10 SER A 253 SER A 262 1 10
HELIX 11 11 ASP A 269 GLY A 275 1 7
HELIX 12 12 ARG A 276 ASP A 278 5 3
HELIX 13 13 LEU A 279 GLY A 291 1 13
HELIX 14 14 GLU A 302 ALA A 306 5 5
HELIX 15 15 ASP A 309 SER A 313 5 5
HELIX 16 16 ASP A 315 GLY A 334 1 20
HELIX 17 17 THR B 10 TYR B 24 1 15
HELIX 18 18 VAL B 49 SER B 55 1 7
HELIX 19 19 GLY B 106 LEU B 120 1 15
HELIX 20 20 GLY B 143 GLY B 158 1 16
HELIX 21 21 ASP B 170 ALA B 178 1 9
HELIX 22 22 ALA B 185 ALA B 188 5 4
HELIX 23 23 ASN B 190 TYR B 200 1 11
HELIX 24 24 THR B 213 ASN B 226 1 14
HELIX 25 25 SER B 253 SER B 262 1 10
HELIX 26 26 ARG B 276 ASP B 278 5 3
HELIX 27 27 LEU B 279 GLY B 291 1 13
HELIX 28 28 GLU B 302 ALA B 306 5 5
HELIX 29 29 ASP B 309 SER B 313 5 5
HELIX 30 30 ASP B 315 GLY B 334 1 20
HELIX 31 31 THR C 10 TYR C 24 1 15
HELIX 32 32 VAL C 49 SER C 55 1 7
HELIX 33 33 GLY C 106 LEU C 120 1 15
HELIX 34 34 GLY C 143 GLY C 158 1 16
HELIX 35 35 GLY C 167 ASP C 169 5 3
HELIX 36 36 ASP C 170 ALA C 178 1 9
HELIX 37 37 GLY C 184 ALA C 188 5 5
HELIX 38 38 ASN C 190 SER C 199 1 10
HELIX 39 39 THR C 213 ASN C 226 1 14
HELIX 40 40 SER C 253 SER C 262 1 10
HELIX 41 41 ASP C 269 GLY C 275 1 7
HELIX 42 42 ARG C 276 ASP C 278 5 3
HELIX 43 43 LEU C 279 GLY C 291 1 13
HELIX 44 44 GLU C 302 ALA C 306 5 5
HELIX 45 45 ASP C 309 SER C 313 5 5
HELIX 46 46 ASP C 315 GLY C 334 1 20
HELIX 47 47 THR D 10 TYR D 24 1 15
HELIX 48 48 VAL D 49 SER D 55 1 7
HELIX 49 49 GLY D 106 LEU D 120 1 15
HELIX 50 50 GLY D 143 TYR D 157 1 15
HELIX 51 51 ASP D 170 ALA D 178 1 9
HELIX 52 52 GLY D 184 ALA D 188 5 5
HELIX 53 53 ASN D 190 SER D 199 1 10
HELIX 54 54 THR D 213 SER D 227 1 15
HELIX 55 55 SER D 253 SER D 262 1 10
HELIX 56 56 ARG D 276 ASP D 278 5 3
HELIX 57 57 LEU D 279 GLY D 291 1 13
HELIX 58 58 GLU D 302 ALA D 306 5 5
HELIX 59 59 ASP D 309 SER D 313 5 5
HELIX 60 60 ASP D 315 GLY D 334 1 20
SHEET 1 A 4 LEU A 26 LYS A 32 0
SHEET 2 A 4 THR A 37 ASP A 45 -1 O ILE A 42 N LYS A 27
SHEET 3 A 4 HIS A -3 LEU A 5 -1 N HIS A -1 O GLY A 43
SHEET 4 A 4 VAL A 59 ARG A 64 -1 O VAL A 63 N ILE A 2
SHEET 1 B 2 ILE A 83 ASP A 84 0
SHEET 2 B 2 LYS A 89 ILE A 90 -1 O ILE A 90 N ILE A 83
SHEET 1 C10 LYS A 336 ASN A 338 0
SHEET 2 C10 TYR A 94 GLY A 100 1 N ILE A 97 O ASN A 338
SHEET 3 C10 GLY A 294 GLU A 298 1 O VAL A 297 N ILE A 98
SHEET 4 C10 ILE A 266 VAL A 268 1 N VAL A 268 O GLY A 294
SHEET 5 C10 ILE A 232 GLU A 236 1 N LEU A 234 O LEU A 267
SHEET 6 C10 VAL A 204 LYS A 207 1 N LEU A 206 O ILE A 233
SHEET 7 C10 ILE A 180 ILE A 183 1 N ILE A 183 O LEU A 205
SHEET 8 C10 TYR A 160 GLU A 164 1 N THR A 163 O GLN A 182
SHEET 9 C10 VAL A 124 ARG A 126 1 N LEU A 125 O TYR A 160
SHEET 10 C10 TYR A 94 GLY A 100 1 N ALA A 99 O VAL A 124
SHEET 1 D 4 LEU B 26 LYS B 32 0
SHEET 2 D 4 THR B 37 ASP B 44 -1 O ILE B 42 N LYS B 27
SHEET 3 D 4 HIS B -2 LEU B 5 -1 N VAL B 3 O ILE B 39
SHEET 4 D 4 VAL B 59 ARG B 64 -1 O VAL B 63 N ILE B 2
SHEET 1 E 2 ILE B 83 ASP B 84 0
SHEET 2 E 2 LYS B 89 ILE B 90 -1 O ILE B 90 N ILE B 83
SHEET 1 F10 LYS B 336 ASN B 338 0
SHEET 2 F10 TYR B 94 GLY B 100 1 N PHE B 95 O ASN B 338
SHEET 3 F10 GLY B 294 GLU B 298 1 O ILE B 295 N ILE B 98
SHEET 4 F10 ILE B 266 VAL B 268 1 N VAL B 268 O GLY B 294
SHEET 5 F10 ILE B 232 GLU B 236 1 N LEU B 234 O LEU B 267
SHEET 6 F10 VAL B 204 LYS B 207 1 N VAL B 204 O ILE B 233
SHEET 7 F10 ILE B 180 ILE B 183 1 N ILE B 183 O LEU B 205
SHEET 8 F10 TYR B 160 ALA B 165 1 N ALA B 165 O GLN B 182
SHEET 9 F10 VAL B 124 ARG B 126 1 N LEU B 125 O TYR B 160
SHEET 10 F10 TYR B 94 GLY B 100 1 N ALA B 99 O VAL B 124
SHEET 1 G 4 LYS C 27 LYS C 32 0
SHEET 2 G 4 THR C 37 ASP C 44 -1 O ILE C 42 N LYS C 27
SHEET 3 G 4 HIS C -2 LEU C 5 -1 N HIS C -1 O GLY C 43
SHEET 4 G 4 VAL C 59 ARG C 64 -1 O VAL C 63 N ILE C 2
SHEET 1 H 2 ILE C 83 ASP C 84 0
SHEET 2 H 2 LYS C 89 ILE C 90 -1 O ILE C 90 N ILE C 83
SHEET 1 I10 LYS C 336 ASN C 338 0
SHEET 2 I10 TYR C 94 GLY C 100 1 N ILE C 97 O ASN C 338
SHEET 3 I10 GLY C 294 GLU C 298 1 O ILE C 295 N ILE C 98
SHEET 4 I10 ILE C 266 VAL C 268 1 N VAL C 268 O GLY C 294
SHEET 5 I10 ILE C 232 GLU C 236 1 N LEU C 234 O LEU C 267
SHEET 6 I10 VAL C 204 LYS C 207 1 N LEU C 206 O ILE C 233
SHEET 7 I10 ILE C 180 ILE C 183 1 N ILE C 183 O LEU C 205
SHEET 8 I10 TYR C 160 GLU C 164 1 N THR C 163 O GLN C 182
SHEET 9 I10 VAL C 124 ARG C 126 1 N LEU C 125 O TYR C 160
SHEET 10 I10 TYR C 94 GLY C 100 1 N ALA C 99 O ARG C 126
SHEET 1 J 4 LYS D 27 LYS D 32 0
SHEET 2 J 4 THR D 37 GLY D 43 -1 O VAL D 38 N SER D 31
SHEET 3 J 4 HIS D -1 LEU D 5 -1 N MET D 1 O ILE D 41
SHEET 4 J 4 VAL D 59 ARG D 64 -1 O VAL D 63 N ILE D 2
SHEET 1 K 2 ILE D 83 ASP D 84 0
SHEET 2 K 2 LYS D 89 ILE D 90 -1 O ILE D 90 N ILE D 83
SHEET 1 L10 LYS D 336 ASN D 338 0
SHEET 2 L10 TYR D 94 GLY D 100 1 N ILE D 97 O ASN D 338
SHEET 3 L10 GLY D 294 GLU D 298 1 O VAL D 297 N ILE D 98
SHEET 4 L10 ILE D 266 VAL D 268 1 N VAL D 268 O ILE D 296
SHEET 5 L10 ILE D 232 GLU D 236 1 N LEU D 234 O LEU D 267
SHEET 6 L10 VAL D 204 LYS D 207 1 N LEU D 206 O ILE D 233
SHEET 7 L10 ILE D 180 ILE D 183 1 N ILE D 183 O LEU D 205
SHEET 8 L10 TYR D 160 GLU D 164 1 N THR D 163 O GLN D 182
SHEET 9 L10 VAL D 124 ARG D 126 1 N LEU D 125 O TYR D 160
SHEET 10 L10 TYR D 94 GLY D 100 1 N ALA D 99 O VAL D 124
CRYST1 73.151 74.226 249.540 90.00 90.00 90.00 P 21 21 21 16
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 0.013670 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013472 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004007 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
