HEADER OXIDOREDUCTASE 30-JUN-04 1VL0
TITLE CRYSTAL STRUCTURE OF A DTDP-4-DEHYDRORHAMNOSE REDUCTASE, RFBD ORTHOLOG
TITLE 2 (CA_C2315) FROM CLOSTRIDIUM ACETOBUTYLICUM ATCC 824 AT 2.05 A
TITLE 3 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DTDP-4-DEHYDRORHAMNOSE REDUCTASE, RFBD ORTHOLOG;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM ACETOBUTYLICUM;
SOURCE 3 ORGANISM_TAXID: 272562;
SOURCE 4 STRAIN: ATCC 824;
SOURCE 5 GENE: CAC2315;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS DTDP-4-DEHYDRORHAMNOSE REDUCTASE, RFBD ORTHOLOG, STRUCTURAL GENOMICS,
KEYWDS 2 JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, PSI, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 8 25-JAN-23 1VL0 1 REMARK SEQADV LINK
REVDAT 7 11-OCT-17 1VL0 1 REMARK
REVDAT 6 13-JUL-11 1VL0 1 VERSN
REVDAT 5 28-JUL-10 1VL0 1 HEADER TITLE KEYWDS
REVDAT 4 24-FEB-09 1VL0 1 VERSN
REVDAT 3 28-MAR-06 1VL0 1 JRNL
REVDAT 2 18-JAN-05 1VL0 1 AUTHOR KEYWDS REMARK
REVDAT 1 17-AUG-04 1VL0 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF DTDP-4-DEHYDRORHAMNOSE REDUCTASE, RFBD
JRNL TITL 2 ORTHOLOG (CAC2315) FROM CLOSTRIDIUM ACETOBUTYLICUM AT 2.05 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0003
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 63619
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2667
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4678
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 191
REMARK 3 BIN FREE R VALUE : 0.3410
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6583
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 149
REMARK 3 SOLVENT ATOMS : 451
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 40.95
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.66000
REMARK 3 B22 (A**2) : -0.29000
REMARK 3 B33 (A**2) : -2.37000
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): 0.160
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.145
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.121
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.071
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6879 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6157 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9369 ; 1.529 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14372 ; 0.953 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 839 ; 5.811 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 297 ;39.445 ;25.522
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1163 ;14.012 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;21.169 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1084 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7503 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1261 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1272 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5905 ; 0.187 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3399 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3620 ; 0.090 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 397 ; 0.147 ; 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): 8 ; 0.322 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 28 ; 0.279 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.191 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): 1 ; 0.110 ; 0.200
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): 4519 ; 2.181 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1708 ; 0.320 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6818 ; 2.779 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2983 ; 5.138 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2551 ; 6.850 ;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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 279 1
REMARK 3 1 B 1 B 279 1
REMARK 3 1 C 1 C 279 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 4142 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 4142 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 C (A): 4142 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 4142 ; 0.20 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 4142 ; 0.20 ; 0.50
REMARK 3 TIGHT THERMAL 1 C (A**2): 4142 ; 0.19 ; 0.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 0 A 152
REMARK 3 RESIDUE RANGE : A 179 A 212
REMARK 3 RESIDUE RANGE : A 247 A 267
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6110 27.7960 11.5960
REMARK 3 T TENSOR
REMARK 3 T11: -0.0812 T22: 0.0115
REMARK 3 T33: 0.0012 T12: -0.0741
REMARK 3 T13: 0.0173 T23: 0.0214
REMARK 3 L TENSOR
REMARK 3 L11: 0.3562 L22: 0.2724
REMARK 3 L33: 1.1612 L12: 0.0796
REMARK 3 L13: 0.3050 L23: 0.2935
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: -0.0264 S13: -0.0316
REMARK 3 S21: 0.0250 S22: -0.0326 S23: 0.0102
REMARK 3 S31: 0.1643 S32: -0.0896 S33: 0.0075
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 153 A 178
REMARK 3 RESIDUE RANGE : A 213 A 246
REMARK 3 RESIDUE RANGE : A 268 A 280
REMARK 3 ORIGIN FOR THE GROUP (A): 38.6110 24.6090 31.6980
REMARK 3 T TENSOR
REMARK 3 T11: -0.1022 T22: -0.0497
REMARK 3 T33: -0.1084 T12: -0.0018
REMARK 3 T13: 0.0230 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 0.9839 L22: 0.8316
REMARK 3 L33: 2.1822 L12: -0.2002
REMARK 3 L13: -0.3172 L23: -0.4413
REMARK 3 S TENSOR
REMARK 3 S11: -0.0025 S12: -0.0255 S13: -0.1117
REMARK 3 S21: -0.0067 S22: -0.0366 S23: -0.0084
REMARK 3 S31: 0.4025 S32: 0.1768 S33: 0.0392
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 152
REMARK 3 RESIDUE RANGE : B 179 B 212
REMARK 3 RESIDUE RANGE : B 247 B 267
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9790 49.2920 -10.5450
REMARK 3 T TENSOR
REMARK 3 T11: -0.0953 T22: -0.0509
REMARK 3 T33: 0.0362 T12: -0.0069
REMARK 3 T13: 0.0167 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.4276 L22: 0.5868
REMARK 3 L33: 0.8746 L12: 0.2853
REMARK 3 L13: -0.0521 L23: 0.0666
REMARK 3 S TENSOR
REMARK 3 S11: 0.0212 S12: -0.0109 S13: 0.0598
REMARK 3 S21: -0.0717 S22: -0.0125 S23: 0.0106
REMARK 3 S31: -0.0804 S32: -0.0760 S33: -0.0086
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 153 B 178
REMARK 3 RESIDUE RANGE : B 213 B 246
REMARK 3 RESIDUE RANGE : B 268 B 280
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5740 65.8490 -16.5530
REMARK 3 T TENSOR
REMARK 3 T11: -0.0852 T22: -0.1088
REMARK 3 T33: 0.0949 T12: -0.1087
REMARK 3 T13: 0.1139 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 1.2777 L22: 2.6229
REMARK 3 L33: 1.7619 L12: 0.4656
REMARK 3 L13: 0.0943 L23: 0.3417
REMARK 3 S TENSOR
REMARK 3 S11: 0.0212 S12: 0.0872 S13: 0.2604
REMARK 3 S21: -0.3743 S22: 0.0901 S23: -0.3405
REMARK 3 S31: -0.2961 S32: 0.1745 S33: -0.1113
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 0 C 152
REMARK 3 RESIDUE RANGE : C 179 C 212
REMARK 3 RESIDUE RANGE : C 247 C 267
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6810 19.1460 -18.2260
REMARK 3 T TENSOR
REMARK 3 T11: -0.0064 T22: -0.0152
REMARK 3 T33: 0.0130 T12: -0.0455
REMARK 3 T13: 0.0175 T23: -0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 0.5454 L22: 0.9430
REMARK 3 L33: 0.8501 L12: -0.1255
REMARK 3 L13: 0.0580 L23: -0.2363
REMARK 3 S TENSOR
REMARK 3 S11: -0.0183 S12: 0.0123 S13: -0.1018
REMARK 3 S21: -0.1162 S22: -0.0021 S23: -0.0805
REMARK 3 S31: 0.2325 S32: -0.0309 S33: 0.0204
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 153 C 178
REMARK 3 RESIDUE RANGE : C 213 C 246
REMARK 3 RESIDUE RANGE : C 268 C 280
REMARK 3 ORIGIN FOR THE GROUP (A): 42.5760 3.0270 -28.0860
REMARK 3 T TENSOR
REMARK 3 T11: 0.1648 T22: 0.1106
REMARK 3 T33: 0.0945 T12: 0.0787
REMARK 3 T13: 0.1296 T23: -0.0915
REMARK 3 L TENSOR
REMARK 3 L11: 2.6354 L22: 2.4700
REMARK 3 L33: 4.0079 L12: -1.4044
REMARK 3 L13: -0.2671 L23: 0.2325
REMARK 3 S TENSOR
REMARK 3 S11: 0.0607 S12: 0.4555 S13: -0.2238
REMARK 3 S21: -0.2326 S22: -0.1105 S23: -0.2539
REMARK 3 S31: 0.4651 S32: 0.5624 S33: 0.0498
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 : A 300 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 26.5800 20.4710 16.3050
REMARK 3 T TENSOR
REMARK 3 T11: 0.0454 T22: -0.0849
REMARK 3 T33: 0.0918 T12: -0.0529
REMARK 3 T13: -0.0325 T23: 0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 8.2557 L22: 2.5793
REMARK 3 L33: 14.1071 L12: 4.4312
REMARK 3 L13: 8.5026 L23: 3.5270
REMARK 3 S TENSOR
REMARK 3 S11: -0.1051 S12: 0.1016 S13: -0.2085
REMARK 3 S21: 0.4158 S22: 0.4965 S23: 0.2387
REMARK 3 S31: 0.2893 S32: -0.1555 S33: -0.3914
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 : B 300 B 300
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7430 56.7940 -6.3510
REMARK 3 T TENSOR
REMARK 3 T11: 0.0564 T22: -0.0438
REMARK 3 T33: 0.0359 T12: -0.1469
REMARK 3 T13: 0.0032 T23: -0.0444
REMARK 3 L TENSOR
REMARK 3 L11: 8.9175 L22: 10.7274
REMARK 3 L33: 4.9068 L12: 7.7681
REMARK 3 L13: -5.2295 L23: -7.2550
REMARK 3 S TENSOR
REMARK 3 S11: 0.4393 S12: -0.2446 S13: 0.2886
REMARK 3 S21: -0.3723 S22: -0.3355 S23: 0.5652
REMARK 3 S31: -0.7425 S32: 0.1369 S33: -0.1038
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 300 C 300
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2280 18.6230 -26.7230
REMARK 3 T TENSOR
REMARK 3 T11: 0.0395 T22: 0.0498
REMARK 3 T33: 0.1151 T12: -0.0144
REMARK 3 T13: 0.1328 T23: -0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 0.8031 L22: 10.3162
REMARK 3 L33: 2.7407 L12: 2.8784
REMARK 3 L13: 1.4836 L23: 5.3173
REMARK 3 S TENSOR
REMARK 3 S11: 0.1626 S12: 0.3316 S13: 0.3046
REMARK 3 S21: -1.4137 S22: 0.1587 S23: -0.6979
REMARK 3 S31: 0.4936 S32: -0.1702 S33: -0.3213
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 : 1.20
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. AN UNKNOWN ENTITY BOUND TO CHAIN A WAS
REMARK 3 ASSIGNED AS UNKNOWN LIGAND, UNL. 3. OCCUPANCY FOR THE NADH BOUND
REMARK 3 TO CHAIN A WAS SET TO 0.5.
REMARK 4
REMARK 4 1VL0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-04.
REMARK 100 THE DEPOSITION ID IS D_1000001966.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-04; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : ALS; ALS
REMARK 200 BEAMLINE : 8.2.1; 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000; 0.9795,0.9796
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111); NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : ADSC; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA (CCP4 4.2), CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66292
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 19.990
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.57200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE, RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.06M MES, 0.04M MES_NA, 2% NP_PEG MME
REMARK 280 2000 , VAPOR DIFFUSION,SITTING DROP,NANODROP, TEMPERATURE 277K.
REMARK 280 0.06M MES, 0.04M MES_NA, 2% NP_PEG MME 2000 , VAPOR DIFFUSION,
REMARK 280 SITTING DROP,NANODROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.52500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.52500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 53.40000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.33500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 53.40000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.33500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.52500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 53.40000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.33500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 75.52500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 53.40000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.33500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 MSE 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 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 MSE 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 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MSE 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 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
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 LYS A 21 CD CE NZ
REMARK 470 LYS A 23 CE NZ
REMARK 470 LYS A 66 CD CE NZ
REMARK 470 GLU A 171 CD OE1 OE2
REMARK 470 LYS A 230 CD CE NZ
REMARK 470 GLU A 237 CD OE1 OE2
REMARK 470 LYS A 244 CE NZ
REMARK 470 LYS B 21 CD CE NZ
REMARK 470 ASN B 24 CG OD1 ND2
REMARK 470 LYS B 66 CE NZ
REMARK 470 GLU B 171 CD OE1 OE2
REMARK 470 GLU B 238 CG CD OE1 OE2
REMARK 470 PHE B 239 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 241 NE CZ NH1 NH2
REMARK 470 LYS B 244 CE NZ
REMARK 470 LYS B 247 CD CE NZ
REMARK 470 LYS B 272 CE NZ
REMARK 470 HIS C 0 ND1 CD2 CE1 NE2
REMARK 470 LYS C 21 CD CE NZ
REMARK 470 LYS C 66 CE NZ
REMARK 470 GLU C 69 CD OE1 OE2
REMARK 470 LYS C 167 CD CE NZ
REMARK 470 ASP C 170 CG OD1 OD2
REMARK 470 ASP C 228 CG OD1 OD2
REMARK 470 LYS C 230 CG CD CE NZ
REMARK 470 PHE C 239 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG C 241 CD NE CZ NH1 NH2
REMARK 470 LYS C 247 CD CE NZ
REMARK 470 LYS C 272 CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 262 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 31 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP B 117 CB - CG - OD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ARG B 147 NE - CZ - NH1 ANGL. DEV. = 3.2 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 ALA A 63 95.73 -63.17
REMARK 500 ASN A 120 61.32 -168.93
REMARK 500 THR A 259 -101.88 -118.06
REMARK 500 ASP B 31 -169.17 -127.49
REMARK 500 ALA B 63 98.13 -66.50
REMARK 500 GLN B 70 54.48 -113.56
REMARK 500 SER B 100 -159.99 -131.69
REMARK 500 ASN B 120 64.36 -168.30
REMARK 500 THR B 259 -100.66 -118.15
REMARK 500 ALA C 63 94.26 -64.20
REMARK 500 ASN C 120 62.26 -166.39
REMARK 500 THR C 259 -99.61 -118.13
REMARK 500 GLN C 279 49.39 -87.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI C 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 355809 RELATED DB: TARGETDB
DBREF 1VL0 A 1 280 UNP Q97GQ1 Q97GQ1_CLOAB 1 280
DBREF 1VL0 B 1 280 UNP Q97GQ1 Q97GQ1_CLOAB 1 280
DBREF 1VL0 C 1 280 UNP Q97GQ1 Q97GQ1_CLOAB 1 280
SEQADV 1VL0 MSE A -11 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 GLY A -10 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 SER A -9 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 ASP A -8 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 LYS A -7 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 ILE A -6 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS A -5 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS A -4 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS A -3 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS A -2 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS A -1 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS A 0 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 MSE A 1 UNP Q97GQ1 MET 1 MODIFIED RESIDUE
SEQADV 1VL0 MSE A 162 UNP Q97GQ1 MET 162 MODIFIED RESIDUE
SEQADV 1VL0 MSE A 255 UNP Q97GQ1 MET 255 MODIFIED RESIDUE
SEQADV 1VL0 MSE A 280 UNP Q97GQ1 MET 280 MODIFIED RESIDUE
SEQADV 1VL0 MSE B -11 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 GLY B -10 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 SER B -9 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 ASP B -8 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 LYS B -7 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 ILE B -6 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS B -5 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS B -4 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS B -3 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS B -2 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS B -1 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS B 0 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 MSE B 1 UNP Q97GQ1 MET 1 MODIFIED RESIDUE
SEQADV 1VL0 MSE B 162 UNP Q97GQ1 MET 162 MODIFIED RESIDUE
SEQADV 1VL0 MSE B 255 UNP Q97GQ1 MET 255 MODIFIED RESIDUE
SEQADV 1VL0 MSE B 280 UNP Q97GQ1 MET 280 MODIFIED RESIDUE
SEQADV 1VL0 MSE C -11 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 GLY C -10 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 SER C -9 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 ASP C -8 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 LYS C -7 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 ILE C -6 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS C -5 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS C -4 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS C -3 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS C -2 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS C -1 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 HIS C 0 UNP Q97GQ1 EXPRESSION TAG
SEQADV 1VL0 MSE C 1 UNP Q97GQ1 MET 1 MODIFIED RESIDUE
SEQADV 1VL0 MSE C 162 UNP Q97GQ1 MET 162 MODIFIED RESIDUE
SEQADV 1VL0 MSE C 255 UNP Q97GQ1 MET 255 MODIFIED RESIDUE
SEQADV 1VL0 MSE C 280 UNP Q97GQ1 MET 280 MODIFIED RESIDUE
SEQRES 1 A 292 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 A 292 LYS ILE LEU ILE THR GLY ALA ASN GLY GLN LEU GLY ARG
SEQRES 3 A 292 GLU ILE GLN LYS GLN LEU LYS GLY LYS ASN VAL GLU VAL
SEQRES 4 A 292 ILE PRO THR ASP VAL GLN ASP LEU ASP ILE THR ASN VAL
SEQRES 5 A 292 LEU ALA VAL ASN LYS PHE PHE ASN GLU LYS LYS PRO ASN
SEQRES 6 A 292 VAL VAL ILE ASN CYS ALA ALA HIS THR ALA VAL ASP LYS
SEQRES 7 A 292 CYS GLU GLU GLN TYR ASP LEU ALA TYR LYS ILE ASN ALA
SEQRES 8 A 292 ILE GLY PRO LYS ASN LEU ALA ALA ALA ALA TYR SER VAL
SEQRES 9 A 292 GLY ALA GLU ILE VAL GLN ILE SER THR ASP TYR VAL PHE
SEQRES 10 A 292 ASP GLY GLU ALA LYS GLU PRO ILE THR GLU PHE ASP GLU
SEQRES 11 A 292 VAL ASN PRO GLN SER ALA TYR GLY LYS THR LYS LEU GLU
SEQRES 12 A 292 GLY GLU ASN PHE VAL LYS ALA LEU ASN PRO LYS TYR TYR
SEQRES 13 A 292 ILE VAL ARG THR ALA TRP LEU TYR GLY ASP GLY ASN ASN
SEQRES 14 A 292 PHE VAL LYS THR MSE ILE ASN LEU GLY LYS THR HIS ASP
SEQRES 15 A 292 GLU LEU LYS VAL VAL HIS ASP GLN VAL GLY THR PRO THR
SEQRES 16 A 292 SER THR VAL ASP LEU ALA ARG VAL VAL LEU LYS VAL ILE
SEQRES 17 A 292 ASP GLU LYS ASN TYR GLY THR PHE HIS CYS THR CYS LYS
SEQRES 18 A 292 GLY ILE CYS SER TRP TYR ASP PHE ALA VAL GLU ILE PHE
SEQRES 19 A 292 ARG LEU THR GLY ILE ASP VAL LYS VAL THR PRO CYS THR
SEQRES 20 A 292 THR GLU GLU PHE PRO ARG PRO ALA LYS ARG PRO LYS TYR
SEQRES 21 A 292 SER VAL LEU ARG ASN TYR MSE LEU GLU LEU THR THR GLY
SEQRES 22 A 292 ASP ILE THR ARG GLU TRP LYS GLU SER LEU LYS GLU TYR
SEQRES 23 A 292 ILE ASP LEU LEU GLN MSE
SEQRES 1 B 292 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 B 292 LYS ILE LEU ILE THR GLY ALA ASN GLY GLN LEU GLY ARG
SEQRES 3 B 292 GLU ILE GLN LYS GLN LEU LYS GLY LYS ASN VAL GLU VAL
SEQRES 4 B 292 ILE PRO THR ASP VAL GLN ASP LEU ASP ILE THR ASN VAL
SEQRES 5 B 292 LEU ALA VAL ASN LYS PHE PHE ASN GLU LYS LYS PRO ASN
SEQRES 6 B 292 VAL VAL ILE ASN CYS ALA ALA HIS THR ALA VAL ASP LYS
SEQRES 7 B 292 CYS GLU GLU GLN TYR ASP LEU ALA TYR LYS ILE ASN ALA
SEQRES 8 B 292 ILE GLY PRO LYS ASN LEU ALA ALA ALA ALA TYR SER VAL
SEQRES 9 B 292 GLY ALA GLU ILE VAL GLN ILE SER THR ASP TYR VAL PHE
SEQRES 10 B 292 ASP GLY GLU ALA LYS GLU PRO ILE THR GLU PHE ASP GLU
SEQRES 11 B 292 VAL ASN PRO GLN SER ALA TYR GLY LYS THR LYS LEU GLU
SEQRES 12 B 292 GLY GLU ASN PHE VAL LYS ALA LEU ASN PRO LYS TYR TYR
SEQRES 13 B 292 ILE VAL ARG THR ALA TRP LEU TYR GLY ASP GLY ASN ASN
SEQRES 14 B 292 PHE VAL LYS THR MSE ILE ASN LEU GLY LYS THR HIS ASP
SEQRES 15 B 292 GLU LEU LYS VAL VAL HIS ASP GLN VAL GLY THR PRO THR
SEQRES 16 B 292 SER THR VAL ASP LEU ALA ARG VAL VAL LEU LYS VAL ILE
SEQRES 17 B 292 ASP GLU LYS ASN TYR GLY THR PHE HIS CYS THR CYS LYS
SEQRES 18 B 292 GLY ILE CYS SER TRP TYR ASP PHE ALA VAL GLU ILE PHE
SEQRES 19 B 292 ARG LEU THR GLY ILE ASP VAL LYS VAL THR PRO CYS THR
SEQRES 20 B 292 THR GLU GLU PHE PRO ARG PRO ALA LYS ARG PRO LYS TYR
SEQRES 21 B 292 SER VAL LEU ARG ASN TYR MSE LEU GLU LEU THR THR GLY
SEQRES 22 B 292 ASP ILE THR ARG GLU TRP LYS GLU SER LEU LYS GLU TYR
SEQRES 23 B 292 ILE ASP LEU LEU GLN MSE
SEQRES 1 C 292 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 C 292 LYS ILE LEU ILE THR GLY ALA ASN GLY GLN LEU GLY ARG
SEQRES 3 C 292 GLU ILE GLN LYS GLN LEU LYS GLY LYS ASN VAL GLU VAL
SEQRES 4 C 292 ILE PRO THR ASP VAL GLN ASP LEU ASP ILE THR ASN VAL
SEQRES 5 C 292 LEU ALA VAL ASN LYS PHE PHE ASN GLU LYS LYS PRO ASN
SEQRES 6 C 292 VAL VAL ILE ASN CYS ALA ALA HIS THR ALA VAL ASP LYS
SEQRES 7 C 292 CYS GLU GLU GLN TYR ASP LEU ALA TYR LYS ILE ASN ALA
SEQRES 8 C 292 ILE GLY PRO LYS ASN LEU ALA ALA ALA ALA TYR SER VAL
SEQRES 9 C 292 GLY ALA GLU ILE VAL GLN ILE SER THR ASP TYR VAL PHE
SEQRES 10 C 292 ASP GLY GLU ALA LYS GLU PRO ILE THR GLU PHE ASP GLU
SEQRES 11 C 292 VAL ASN PRO GLN SER ALA TYR GLY LYS THR LYS LEU GLU
SEQRES 12 C 292 GLY GLU ASN PHE VAL LYS ALA LEU ASN PRO LYS TYR TYR
SEQRES 13 C 292 ILE VAL ARG THR ALA TRP LEU TYR GLY ASP GLY ASN ASN
SEQRES 14 C 292 PHE VAL LYS THR MSE ILE ASN LEU GLY LYS THR HIS ASP
SEQRES 15 C 292 GLU LEU LYS VAL VAL HIS ASP GLN VAL GLY THR PRO THR
SEQRES 16 C 292 SER THR VAL ASP LEU ALA ARG VAL VAL LEU LYS VAL ILE
SEQRES 17 C 292 ASP GLU LYS ASN TYR GLY THR PHE HIS CYS THR CYS LYS
SEQRES 18 C 292 GLY ILE CYS SER TRP TYR ASP PHE ALA VAL GLU ILE PHE
SEQRES 19 C 292 ARG LEU THR GLY ILE ASP VAL LYS VAL THR PRO CYS THR
SEQRES 20 C 292 THR GLU GLU PHE PRO ARG PRO ALA LYS ARG PRO LYS TYR
SEQRES 21 C 292 SER VAL LEU ARG ASN TYR MSE LEU GLU LEU THR THR GLY
SEQRES 22 C 292 ASP ILE THR ARG GLU TRP LYS GLU SER LEU LYS GLU TYR
SEQRES 23 C 292 ILE ASP LEU LEU GLN MSE
MODRES 1VL0 MSE A 1 MET SELENOMETHIONINE
MODRES 1VL0 MSE A 162 MET SELENOMETHIONINE
MODRES 1VL0 MSE A 255 MET SELENOMETHIONINE
MODRES 1VL0 MSE A 280 MET SELENOMETHIONINE
MODRES 1VL0 MSE B 1 MET SELENOMETHIONINE
MODRES 1VL0 MSE B 162 MET SELENOMETHIONINE
MODRES 1VL0 MSE B 255 MET SELENOMETHIONINE
MODRES 1VL0 MSE B 280 MET SELENOMETHIONINE
MODRES 1VL0 MSE C 1 MET SELENOMETHIONINE
MODRES 1VL0 MSE C 162 MET SELENOMETHIONINE
MODRES 1VL0 MSE C 255 MET SELENOMETHIONINE
MODRES 1VL0 MSE C 280 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 162 8
HET MSE A 255 8
HET MSE A 280 9
HET MSE B 1 8
HET MSE B 162 8
HET MSE B 255 8
HET MSE B 280 8
HET MSE C 1 8
HET MSE C 162 8
HET MSE C 255 8
HET MSE C 280 8
HET NAI A 300 44
HET UNL A 301 17
HET NAI B 300 44
HET NAI C 300 44
HETNAM MSE SELENOMETHIONINE
HETNAM NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
HETNAM UNL UNKNOWN LIGAND
HETSYN NAI NADH
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 4 NAI 3(C21 H29 N7 O14 P2)
FORMUL 8 HOH *451(H2 O)
HELIX 1 1 GLY A 10 LYS A 21 1 12
HELIX 2 2 ASN A 39 LYS A 51 1 13
HELIX 3 3 ALA A 63 GLN A 70 1 8
HELIX 4 4 GLN A 70 ALA A 79 1 10
HELIX 5 5 ALA A 79 VAL A 92 1 14
HELIX 6 6 TYR A 103 PHE A 105 5 3
HELIX 7 7 SER A 123 ASN A 140 1 18
HELIX 8 8 ASN A 157 HIS A 169 1 13
HELIX 9 9 THR A 185 LYS A 199 1 15
HELIX 10 10 TRP A 214 GLY A 226 1 13
HELIX 11 11 ASN A 253 THR A 259 1 7
HELIX 12 12 GLU A 266 GLN A 279 1 14
HELIX 13 13 GLY B 10 LYS B 21 1 12
HELIX 14 14 ASN B 39 LYS B 51 1 13
HELIX 15 15 ALA B 63 GLN B 70 1 8
HELIX 16 16 GLN B 70 ALA B 79 1 10
HELIX 17 17 ALA B 79 VAL B 92 1 14
HELIX 18 18 TYR B 103 PHE B 105 5 3
HELIX 19 19 SER B 123 ASN B 140 1 18
HELIX 20 20 ASN B 157 HIS B 169 1 13
HELIX 21 21 THR B 185 LYS B 199 1 15
HELIX 22 22 TRP B 214 GLY B 226 1 13
HELIX 23 23 THR B 235 PHE B 239 5 5
HELIX 24 24 ASN B 253 THR B 259 1 7
HELIX 25 25 GLU B 266 GLN B 279 1 14
HELIX 26 26 GLY C 10 LYS C 21 1 12
HELIX 27 27 ASN C 39 LYS C 51 1 13
HELIX 28 28 ALA C 63 GLN C 70 1 8
HELIX 29 29 GLN C 70 ALA C 79 1 10
HELIX 30 30 ALA C 79 VAL C 92 1 14
HELIX 31 31 TYR C 103 PHE C 105 5 3
HELIX 32 32 SER C 123 ASN C 140 1 18
HELIX 33 33 ASN C 157 HIS C 169 1 13
HELIX 34 34 THR C 185 LYS C 199 1 15
HELIX 35 35 TRP C 214 GLY C 226 1 13
HELIX 36 36 THR C 235 PHE C 239 5 5
HELIX 37 37 ASN C 253 THR C 259 1 7
HELIX 38 38 GLU C 266 GLN C 279 1 14
SHEET 1 A 6 VAL A 25 THR A 30 0
SHEET 2 A 6 MSE A 1 THR A 6 1 N MSE A 1 O GLU A 26
SHEET 3 A 6 VAL A 54 ASN A 57 1 O ILE A 56 N LEU A 4
SHEET 4 A 6 GLU A 95 THR A 101 1 O VAL A 97 N VAL A 55
SHEET 5 A 6 TYR A 143 THR A 148 1 O TYR A 144 N GLN A 98
SHEET 6 A 6 GLY A 202 HIS A 205 1 O PHE A 204 N ILE A 145
SHEET 1 B 2 LEU A 151 TYR A 152 0
SHEET 2 B 2 THR A 183 SER A 184 1 O THR A 183 N TYR A 152
SHEET 1 C 2 GLU A 171 VAL A 175 0
SHEET 2 C 2 LYS A 230 CYS A 234 1 O THR A 232 N LEU A 172
SHEET 1 D 2 VAL A 179 GLY A 180 0
SHEET 2 D 2 CYS A 212 SER A 213 -1 O CYS A 212 N GLY A 180
SHEET 1 E 6 GLU B 26 THR B 30 0
SHEET 2 E 6 LYS B 2 THR B 6 1 N ILE B 3 O ILE B 28
SHEET 3 E 6 VAL B 54 ASN B 57 1 O ILE B 56 N LEU B 4
SHEET 4 E 6 GLU B 95 THR B 101 1 O VAL B 97 N VAL B 55
SHEET 5 E 6 TYR B 143 THR B 148 1 O TYR B 144 N GLN B 98
SHEET 6 E 6 GLY B 202 HIS B 205 1 O PHE B 204 N ILE B 145
SHEET 1 F 2 LEU B 151 TYR B 152 0
SHEET 2 F 2 THR B 183 SER B 184 1 O THR B 183 N TYR B 152
SHEET 1 G 2 GLU B 171 VAL B 175 0
SHEET 2 G 2 LYS B 230 CYS B 234 1 O THR B 232 N LEU B 172
SHEET 1 H 2 VAL B 179 GLY B 180 0
SHEET 2 H 2 CYS B 212 SER B 213 -1 O CYS B 212 N GLY B 180
SHEET 1 I 6 VAL C 25 THR C 30 0
SHEET 2 I 6 MSE C 1 THR C 6 1 N MSE C 1 O GLU C 26
SHEET 3 I 6 VAL C 54 ASN C 57 1 O ILE C 56 N LEU C 4
SHEET 4 I 6 GLU C 95 THR C 101 1 O VAL C 97 N VAL C 55
SHEET 5 I 6 TYR C 143 THR C 148 1 O TYR C 144 N GLN C 98
SHEET 6 I 6 GLY C 202 HIS C 205 1 O PHE C 204 N ILE C 145
SHEET 1 J 2 LEU C 151 TYR C 152 0
SHEET 2 J 2 THR C 183 SER C 184 1 O THR C 183 N TYR C 152
SHEET 1 K 2 GLU C 171 VAL C 175 0
SHEET 2 K 2 LYS C 230 CYS C 234 1 O THR C 232 N LEU C 172
SHEET 1 L 2 VAL C 179 GLY C 180 0
SHEET 2 L 2 CYS C 212 SER C 213 -1 O CYS C 212 N GLY C 180
LINK C HIS A 0 N MSE A 1 1555 1555 1.32
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C THR A 161 N MSE A 162 1555 1555 1.33
LINK C MSE A 162 N ILE A 163 1555 1555 1.33
LINK C TYR A 254 N MSE A 255 1555 1555 1.31
LINK C MSE A 255 N LEU A 256 1555 1555 1.33
LINK C GLN A 279 N MSE A 280 1555 1555 1.31
LINK C MSE B 1 N LYS B 2 1555 1555 1.32
LINK C THR B 161 N MSE B 162 1555 1555 1.33
LINK C MSE B 162 N ILE B 163 1555 1555 1.32
LINK C TYR B 254 N MSE B 255 1555 1555 1.31
LINK C MSE B 255 N LEU B 256 1555 1555 1.33
LINK C GLN B 279 N MSE B 280 1555 1555 1.33
LINK C HIS C 0 N MSE C 1 1555 1555 1.34
LINK C MSE C 1 N LYS C 2 1555 1555 1.32
LINK C THR C 161 N MSE C 162 1555 1555 1.33
LINK C MSE C 162 N ILE C 163 1555 1555 1.33
LINK C TYR C 254 N MSE C 255 1555 1555 1.32
LINK C MSE C 255 N LEU C 256 1555 1555 1.32
LINK C GLN C 279 N MSE C 280 1555 1555 1.33
SITE 1 AC1 21 GLY A 10 GLN A 11 LEU A 12 ASP A 31
SITE 2 AC1 21 LEU A 35 ASP A 36 ILE A 37 CYS A 58
SITE 3 AC1 21 ALA A 59 ALA A 60 THR A 62 ILE A 99
SITE 4 AC1 21 SER A 100 THR A 101 TYR A 125 LYS A 129
SITE 5 AC1 21 THR A 148 TRP A 150 LEU A 151 HOH A 313
SITE 6 AC1 21 HOH A 383
SITE 1 AC2 10 THR A 207 CYS A 208 GLY A 210 ILE A 211
SITE 2 AC2 10 LEU A 251 ARG A 252 ASN A 253 HOH A 309
SITE 3 AC2 10 HOH A 324 HOH A 337
SITE 1 AC3 25 GLY B 10 GLN B 11 LEU B 12 ASP B 31
SITE 2 AC3 25 VAL B 32 LEU B 35 ASP B 36 ILE B 37
SITE 3 AC3 25 CYS B 58 ALA B 59 ALA B 60 THR B 62
SITE 4 AC3 25 ILE B 77 ILE B 99 SER B 100 THR B 101
SITE 5 AC3 25 TYR B 125 LYS B 129 THR B 148 LEU B 151
SITE 6 AC3 25 HOH B 306 HOH B 309 HOH B 349 HOH B 360
SITE 7 AC3 25 HOH B 445
SITE 1 AC4 24 GLY C 10 GLN C 11 LEU C 12 ASP C 31
SITE 2 AC4 24 VAL C 32 LEU C 35 ASP C 36 ILE C 37
SITE 3 AC4 24 CYS C 58 ALA C 59 ALA C 60 THR C 62
SITE 4 AC4 24 ILE C 99 SER C 100 THR C 101 TYR C 125
SITE 5 AC4 24 LYS C 129 THR C 148 TRP C 150 LEU C 151
SITE 6 AC4 24 HOH C 306 HOH C 310 HOH C 318 HOH C 394
CRYST1 106.800 130.670 151.050 90.00 90.00 90.00 C 2 2 21 24
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 0.009363 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007653 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006620 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
