HEADER TRANSFERASE 30-OCT-13 4NF2
TITLE CRYSTAL STRUCTURE OF ANABOLIC ORNITHINE CARBAMOYLTRANSFERASE FROM
TITLE 2 BACILLUS ANTHRACIS IN COMPLEX WITH CARBAMOYL PHOSPHATE AND L-
TITLE 3 NORVALINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ORNITHINE CARBAMOYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: OTCASE;
COMPND 5 EC: 2.1.3.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_COMMON: ANTHRAX, ANTHRAX BACTERIUM;
SOURCE 4 ORGANISM_TAXID: 261594;
SOURCE 5 STRAIN: AMES ANCESTOR;
SOURCE 6 GENE: ARGF, BAS4036, BA_4351, GBAA_4351;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, NIAID, NATIONAL INSTITUTE OF ALLERGY AND
KEYWDS 2 INFECTIOUS DISEASES, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS 3 DISEASES, CSGID, CARBAMOYL PHOSPHATE, L-ORNITHINE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.G.SHABALIN,K.HANDING,M.T.CYMBOROWSKI,J.STAM,J.WINSOR,L.SHUVALOVA,
AUTHOR 2 W.F.ANDERSON,W.MINOR,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
AUTHOR 3 DISEASES (CSGID)
REVDAT 3 20-SEP-23 4NF2 1 REMARK
REVDAT 2 13-APR-22 4NF2 1 AUTHOR JRNL REMARK SEQADV
REVDAT 1 13-NOV-13 4NF2 0
JRNL AUTH I.G.SHABALIN,K.HANDING,M.T.CYMBOROWSKI,J.STAM,J.WINSOR,
JRNL AUTH 2 L.SHUVALOVA,W.F.ANDERSON,W.MINOR
JRNL TITL CRYSTAL STRUCTURES AND KINETIC PROPERTIES OF ANABOLIC
JRNL TITL 2 ORNITHINE CARBAMOYLTRANSFERASE FROM HUMAN PATHOGENS VIBRIO
JRNL TITL 3 VULNIFICUS AND BACILLUS ANTHRACIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 104782
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) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.170
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5231
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) : 1.74
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7294
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 387
REMARK 3 BIN FREE R VALUE : 0.2460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7212
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 846
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.36000
REMARK 3 B22 (A**2) : -1.41000
REMARK 3 B33 (A**2) : 1.05000
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): 0.091
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.087
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.480
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.971
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7521 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7266 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10193 ; 1.695 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16776 ; 1.278 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 954 ; 5.735 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 346 ;40.069 ;25.578
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1365 ;13.616 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;14.904 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1159 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8519 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1666 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 3
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 5 311 B 5 311 19819 0.070 0.050
REMARK 3 2 A 5 311 C 5 311 19630 0.090 0.050
REMARK 3 3 B 5 311 C 5 311 19558 0.090 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 5 A 134
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7530 11.0900 10.8770
REMARK 3 T TENSOR
REMARK 3 T11: 0.0338 T22: 0.0833
REMARK 3 T33: 0.0848 T12: 0.0064
REMARK 3 T13: -0.0199 T23: -0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 0.8002 L22: 1.4318
REMARK 3 L33: 0.5640 L12: 0.1530
REMARK 3 L13: 0.0780 L23: -0.0166
REMARK 3 S TENSOR
REMARK 3 S11: -0.0282 S12: -0.0822 S13: 0.1364
REMARK 3 S21: 0.0230 S22: -0.0602 S23: 0.2437
REMARK 3 S31: -0.0105 S32: -0.1197 S33: 0.0884
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 135 A 237
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6210 31.3120 0.3280
REMARK 3 T TENSOR
REMARK 3 T11: 0.1133 T22: 0.0786
REMARK 3 T33: 0.2590 T12: 0.0124
REMARK 3 T13: -0.1061 T23: 0.0815
REMARK 3 L TENSOR
REMARK 3 L11: 2.5302 L22: 1.2466
REMARK 3 L33: 1.5272 L12: -0.9749
REMARK 3 L13: 0.7117 L23: -0.8920
REMARK 3 S TENSOR
REMARK 3 S11: -0.1311 S12: 0.2974 S13: 0.6677
REMARK 3 S21: 0.0340 S22: -0.1020 S23: -0.1445
REMARK 3 S31: -0.2569 S32: -0.0911 S33: 0.2331
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 : A 238 A 250
REMARK 3 ORIGIN FOR THE GROUP (A): 31.4280 26.3500 -11.7180
REMARK 3 T TENSOR
REMARK 3 T11: 0.4263 T22: 0.4319
REMARK 3 T33: 0.3843 T12: 0.0576
REMARK 3 T13: 0.1380 T23: 0.2769
REMARK 3 L TENSOR
REMARK 3 L11: 6.2817 L22: 17.9888
REMARK 3 L33: 5.8908 L12: 6.0406
REMARK 3 L13: 0.1004 L23: 1.4107
REMARK 3 S TENSOR
REMARK 3 S11: -0.4893 S12: 0.7872 S13: -0.2519
REMARK 3 S21: -1.5604 S22: -0.0061 S23: -1.4983
REMARK 3 S31: 0.6986 S32: 0.7067 S33: 0.4954
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 : A 251 A 311
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0710 29.5120 8.9260
REMARK 3 T TENSOR
REMARK 3 T11: 0.0941 T22: 0.0144
REMARK 3 T33: 0.2786 T12: -0.0176
REMARK 3 T13: -0.1334 T23: 0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 2.8517 L22: 1.7681
REMARK 3 L33: 1.5859 L12: 0.1283
REMARK 3 L13: 0.3680 L23: -0.4970
REMARK 3 S TENSOR
REMARK 3 S11: -0.1941 S12: 0.0336 S13: 0.7108
REMARK 3 S21: 0.0647 S22: -0.1378 S23: -0.1059
REMARK 3 S31: -0.3006 S32: 0.0865 S33: 0.3319
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 : B 5 B 66
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9730 5.1470 30.5870
REMARK 3 T TENSOR
REMARK 3 T11: 0.1486 T22: 0.0967
REMARK 3 T33: 0.0209 T12: 0.0192
REMARK 3 T13: -0.0158 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 1.2119 L22: 1.5552
REMARK 3 L33: 1.2532 L12: -0.1046
REMARK 3 L13: 0.0550 L23: -0.0452
REMARK 3 S TENSOR
REMARK 3 S11: -0.0720 S12: -0.2045 S13: 0.1358
REMARK 3 S21: 0.3298 S22: 0.0206 S23: 0.0129
REMARK 3 S31: -0.0746 S32: -0.0924 S33: 0.0514
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 : B 67 B 190
REMARK 3 ORIGIN FOR THE GROUP (A): 45.7020 5.9620 21.7580
REMARK 3 T TENSOR
REMARK 3 T11: 0.0996 T22: 0.0807
REMARK 3 T33: 0.0498 T12: 0.0081
REMARK 3 T13: -0.0331 T23: -0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 1.3679 L22: 1.0643
REMARK 3 L33: 0.2585 L12: -0.2250
REMARK 3 L13: 0.2468 L23: 0.0122
REMARK 3 S TENSOR
REMARK 3 S11: -0.0667 S12: -0.0317 S13: 0.1903
REMARK 3 S21: 0.1288 S22: -0.0010 S23: -0.1445
REMARK 3 S31: -0.0210 S32: 0.0161 S33: 0.0677
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 : B 191 B 304
REMARK 3 ORIGIN FOR THE GROUP (A): 57.0900 -7.2910 22.2750
REMARK 3 T TENSOR
REMARK 3 T11: 0.0963 T22: 0.0844
REMARK 3 T33: 0.0804 T12: 0.0285
REMARK 3 T13: -0.0383 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 1.1814 L22: 1.3294
REMARK 3 L33: 0.8958 L12: 0.0914
REMARK 3 L13: -0.0802 L23: 0.1091
REMARK 3 S TENSOR
REMARK 3 S11: -0.0228 S12: -0.0265 S13: -0.0347
REMARK 3 S21: 0.1163 S22: 0.0107 S23: -0.3195
REMARK 3 S31: 0.0547 S32: 0.1415 S33: 0.0121
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 305 B 311
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8070 11.3690 33.5250
REMARK 3 T TENSOR
REMARK 3 T11: 0.2442 T22: 0.1159
REMARK 3 T33: 0.1485 T12: 0.0518
REMARK 3 T13: 0.0438 T23: -0.1000
REMARK 3 L TENSOR
REMARK 3 L11: 16.4595 L22: 14.6225
REMARK 3 L33: 6.3856 L12: 7.9328
REMARK 3 L13: 0.0601 L23: -7.5148
REMARK 3 S TENSOR
REMARK 3 S11: 0.2896 S12: -0.6178 S13: 1.1907
REMARK 3 S21: 1.0144 S22: -0.0345 S23: 0.6567
REMARK 3 S31: -0.7716 S32: -0.1084 S33: -0.2551
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 5 C 148
REMARK 3 ORIGIN FOR THE GROUP (A): 21.5470 -14.5110 18.4380
REMARK 3 T TENSOR
REMARK 3 T11: 0.1305 T22: 0.0996
REMARK 3 T33: 0.0274 T12: -0.0419
REMARK 3 T13: 0.0112 T23: 0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 1.3789 L22: 0.5405
REMARK 3 L33: 0.6868 L12: 0.2748
REMARK 3 L13: 0.6102 L23: 0.3026
REMARK 3 S TENSOR
REMARK 3 S11: 0.0487 S12: -0.2083 S13: -0.0915
REMARK 3 S21: 0.1630 S22: -0.0391 S23: 0.0759
REMARK 3 S31: 0.1117 S32: -0.1381 S33: -0.0096
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 149 C 232
REMARK 3 ORIGIN FOR THE GROUP (A): 10.1900 -29.2120 4.0320
REMARK 3 T TENSOR
REMARK 3 T11: 0.1056 T22: 0.0627
REMARK 3 T33: 0.0940 T12: -0.0724
REMARK 3 T13: -0.0157 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 1.3268 L22: 1.5310
REMARK 3 L33: 1.7462 L12: 0.0076
REMARK 3 L13: 0.1193 L23: 0.5831
REMARK 3 S TENSOR
REMARK 3 S11: 0.0601 S12: -0.1047 S13: -0.2127
REMARK 3 S21: 0.1600 S22: -0.0395 S23: 0.1528
REMARK 3 S31: 0.2865 S32: -0.1289 S33: -0.0206
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 233 C 248
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8090 -18.6230 -8.9500
REMARK 3 T TENSOR
REMARK 3 T11: 0.1062 T22: 0.1592
REMARK 3 T33: 0.0672 T12: -0.0820
REMARK 3 T13: 0.0430 T23: -0.0546
REMARK 3 L TENSOR
REMARK 3 L11: 5.8812 L22: 6.0886
REMARK 3 L33: 13.8112 L12: 3.4252
REMARK 3 L13: 7.1509 L23: 7.9945
REMARK 3 S TENSOR
REMARK 3 S11: -0.1766 S12: 0.7872 S13: -0.3341
REMARK 3 S21: -0.4860 S22: 0.7822 S23: -0.5334
REMARK 3 S31: -0.4766 S32: 1.2919 S33: -0.6056
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 249 C 311
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3090 -15.6370 4.3790
REMARK 3 T TENSOR
REMARK 3 T11: 0.0374 T22: 0.0981
REMARK 3 T33: 0.0671 T12: -0.0378
REMARK 3 T13: -0.0041 T23: -0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 0.7906 L22: 1.4508
REMARK 3 L33: 1.5552 L12: 0.1533
REMARK 3 L13: 0.3878 L23: 0.6716
REMARK 3 S TENSOR
REMARK 3 S11: 0.0033 S12: -0.1314 S13: -0.0015
REMARK 3 S21: 0.0268 S22: -0.1085 S23: 0.2825
REMARK 3 S31: -0.0040 S32: -0.2527 S33: 0.1052
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: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 4NF2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000083121.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : BE-LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105149
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : 0.04400
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) : 1.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.60200
REMARK 200 R SYM FOR SHELL (I) : 0.60200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGT
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP, HKL-3000, CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 4H31
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 10 MG/ML IN 10 MM TRIS-HCL PH
REMARK 280 8.3, 20 MM CARBAMOYL PHOSPHATE, 20 MM L-NORVALINE, 500 MM NACL
REMARK 280 AND 5 MM B-MERCAPTOETHANOL. CRYSTALLIZATION CONDITION: INDEX #79
REMARK 280 (0.1 M BIS-TRIS PH 6.5, 0.2 M NH4 ACETATE,25% W/V PEG 3350).
REMARK 280 MIXED AS 0.2 UL + 0.2 UL., VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
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 42.94650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.49450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.94650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.49450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 42.94650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.94650
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 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 MET A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 TYR A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 THR A 3
REMARK 465 VAL A 4
REMARK 465 VAL A 312
REMARK 465 GLU A 313
REMARK 465 GLU A 314
REMARK 465 LEU A 315
REMARK 465 SER A 316
REMARK 465 MET B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 VAL B -13
REMARK 465 ASP B -12
REMARK 465 LEU B -11
REMARK 465 GLY B -10
REMARK 465 THR B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 THR B 3
REMARK 465 VAL B 4
REMARK 465 VAL B 312
REMARK 465 GLU B 313
REMARK 465 GLU B 314
REMARK 465 LEU B 315
REMARK 465 SER B 316
REMARK 465 MET C -23
REMARK 465 HIS C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 SER C -16
REMARK 465 SER C -15
REMARK 465 GLY C -14
REMARK 465 VAL C -13
REMARK 465 ASP C -12
REMARK 465 LEU C -11
REMARK 465 GLY C -10
REMARK 465 THR C -9
REMARK 465 GLU C -8
REMARK 465 ASN C -7
REMARK 465 LEU C -6
REMARK 465 TYR C -5
REMARK 465 PHE C -4
REMARK 465 GLN C -3
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 ALA C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 THR C 3
REMARK 465 VAL C 4
REMARK 465 VAL C 312
REMARK 465 GLU C 313
REMARK 465 GLU C 314
REMARK 465 LEU C 315
REMARK 465 SER C 316
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 39 CG CD CE NZ
REMARK 470 GLU A 241 CG CD OE1 OE2
REMARK 470 LYS A 254 CD CE NZ
REMARK 470 LYS A 310 CG CD CE NZ
REMARK 470 LYS B 8 CE NZ
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 GLU B 240 CG CD OE1 OE2
REMARK 470 GLU B 242 CG CD OE1 OE2
REMARK 470 LYS C 8 CD CE NZ
REMARK 470 LYS C 39 CD CE NZ
REMARK 470 LYS C 205 CE NZ
REMARK 470 GLU C 241 CG CD OE1 OE2
REMARK 470 LYS C 310 NZ
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 ASN A 10 39.07 -87.69
REMARK 500 ASN A 10 38.80 -87.32
REMARK 500 LEU A 17 -13.74 89.08
REMARK 500 THR A 58 -61.41 -109.31
REMARK 500 LEU A 130 129.42 130.06
REMARK 500 ASN A 165 -167.54 -117.01
REMARK 500 LEU A 270 151.70 69.74
REMARK 500 GLU A 276 -98.55 -104.13
REMARK 500 ASN B 10 39.61 -89.43
REMARK 500 LEU B 17 -15.39 89.81
REMARK 500 LEU B 130 134.55 130.35
REMARK 500 LEU B 270 149.97 70.13
REMARK 500 GLU B 276 -94.08 -106.08
REMARK 500 ASN C 10 40.92 -90.85
REMARK 500 LEU C 17 -14.53 89.09
REMARK 500 PHE C 110 -64.00 -91.42
REMARK 500 LEU C 130 135.20 133.29
REMARK 500 ASN C 151 19.83 58.11
REMARK 500 LEU C 270 153.11 67.10
REMARK 500 GLU C 276 -101.24 -105.19
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 CP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NVA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NVA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CP B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CP C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NVA C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EP1 RELATED DB: PDB
REMARK 900 APO-FORM
REMARK 900 RELATED ID: CSGID-IDP02525 RELATED DB: TARGETTRACK
DBREF 4NF2 A 1 316 UNP Q81M99 OTC_BACAN 1 316
DBREF 4NF2 B 1 316 UNP Q81M99 OTC_BACAN 1 316
DBREF 4NF2 C 1 316 UNP Q81M99 OTC_BACAN 1 316
SEQADV 4NF2 MET A -23 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS A -22 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS A -21 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS A -20 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS A -19 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS A -18 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS A -17 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 SER A -16 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 SER A -15 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLY A -14 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 VAL A -13 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 ASP A -12 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 LEU A -11 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLY A -10 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 THR A -9 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLU A -8 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 ASN A -7 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 LEU A -6 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 TYR A -5 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 PHE A -4 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLN A -3 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 SER A -2 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 ASN A -1 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 ALA A 0 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLN A 86 UNP Q81M99 GLY 86 ENGINEERED MUTATION
SEQADV 4NF2 ARG A 191 UNP Q81M99 LYS 191 ENGINEERED MUTATION
SEQADV 4NF2 MET B -23 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS B -22 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS B -21 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS B -20 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS B -19 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS B -18 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS B -17 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 SER B -16 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 SER B -15 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLY B -14 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 VAL B -13 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 ASP B -12 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 LEU B -11 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLY B -10 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 THR B -9 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLU B -8 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 ASN B -7 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 LEU B -6 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 TYR B -5 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 PHE B -4 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLN B -3 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 SER B -2 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 ASN B -1 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 ALA B 0 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLN B 86 UNP Q81M99 GLY 86 ENGINEERED MUTATION
SEQADV 4NF2 ARG B 191 UNP Q81M99 LYS 191 ENGINEERED MUTATION
SEQADV 4NF2 MET C -23 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS C -22 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS C -21 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS C -20 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS C -19 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS C -18 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 HIS C -17 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 SER C -16 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 SER C -15 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLY C -14 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 VAL C -13 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 ASP C -12 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 LEU C -11 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLY C -10 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 THR C -9 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLU C -8 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 ASN C -7 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 LEU C -6 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 TYR C -5 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 PHE C -4 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLN C -3 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 SER C -2 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 ASN C -1 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 ALA C 0 UNP Q81M99 EXPRESSION TAG
SEQADV 4NF2 GLN C 86 UNP Q81M99 GLY 86 ENGINEERED MUTATION
SEQADV 4NF2 ARG C 191 UNP Q81M99 LYS 191 ENGINEERED MUTATION
SEQRES 1 A 340 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 340 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 A 340 THR VAL GLN VAL PRO LYS LEU ASN THR LYS ASP LEU LEU
SEQRES 4 A 340 THR LEU GLU GLU LEU THR GLN GLU GLU ILE ILE SER LEU
SEQRES 5 A 340 ILE GLU PHE ALA ILE TYR LEU LYS LYS ASN LYS GLN GLU
SEQRES 6 A 340 PRO LEU LEU GLN GLY LYS ILE LEU GLY LEU ILE PHE ASP
SEQRES 7 A 340 LYS HIS SER THR ARG THR ARG VAL SER PHE GLU ALA GLY
SEQRES 8 A 340 MET VAL GLN LEU GLY GLY HIS GLY MET PHE LEU ASN GLY
SEQRES 9 A 340 LYS GLU MET GLN MET GLN ARG GLY GLU THR VAL SER ASP
SEQRES 10 A 340 THR ALA LYS VAL LEU SER HIS TYR ILE ASP GLY ILE MET
SEQRES 11 A 340 ILE ARG THR PHE SER HIS ALA ASP VAL GLU GLU LEU ALA
SEQRES 12 A 340 LYS GLU SER SER ILE PRO VAL ILE ASN GLY LEU THR ASP
SEQRES 13 A 340 ASP HIS HIS PRO CYS GLN ALA LEU ALA ASP LEU MET THR
SEQRES 14 A 340 ILE TYR GLU GLU THR ASN THR PHE LYS GLY ILE LYS LEU
SEQRES 15 A 340 ALA TYR VAL GLY ASP GLY ASN ASN VAL CYS HIS SER LEU
SEQRES 16 A 340 LEU LEU ALA SER ALA LYS VAL GLY MET HIS MET THR VAL
SEQRES 17 A 340 ALA THR PRO VAL GLY TYR ARG PRO ASN GLU GLU ILE VAL
SEQRES 18 A 340 LYS LYS ALA LEU ALA ILE ALA LYS GLU THR GLY ALA GLU
SEQRES 19 A 340 ILE GLU ILE LEU HIS ASN PRO GLU LEU ALA VAL ASN GLU
SEQRES 20 A 340 ALA ASP PHE ILE TYR THR ASP VAL TRP MET SER MET GLY
SEQRES 21 A 340 GLN GLU GLY GLU GLU GLU LYS TYR THR LEU PHE GLN PRO
SEQRES 22 A 340 TYR GLN ILE ASN LYS GLU LEU VAL LYS HIS ALA LYS GLN
SEQRES 23 A 340 THR TYR HIS PHE LEU HIS CYS LEU PRO ALA HIS ARG GLU
SEQRES 24 A 340 GLU GLU VAL THR GLY GLU ILE ILE ASP GLY PRO GLN SER
SEQRES 25 A 340 ILE VAL PHE GLU GLN ALA GLY ASN ARG LEU HIS ALA GLN
SEQRES 26 A 340 LYS ALA LEU LEU VAL SER LEU PHE LYS ASN VAL GLU GLU
SEQRES 27 A 340 LEU SER
SEQRES 1 B 340 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 340 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 B 340 THR VAL GLN VAL PRO LYS LEU ASN THR LYS ASP LEU LEU
SEQRES 4 B 340 THR LEU GLU GLU LEU THR GLN GLU GLU ILE ILE SER LEU
SEQRES 5 B 340 ILE GLU PHE ALA ILE TYR LEU LYS LYS ASN LYS GLN GLU
SEQRES 6 B 340 PRO LEU LEU GLN GLY LYS ILE LEU GLY LEU ILE PHE ASP
SEQRES 7 B 340 LYS HIS SER THR ARG THR ARG VAL SER PHE GLU ALA GLY
SEQRES 8 B 340 MET VAL GLN LEU GLY GLY HIS GLY MET PHE LEU ASN GLY
SEQRES 9 B 340 LYS GLU MET GLN MET GLN ARG GLY GLU THR VAL SER ASP
SEQRES 10 B 340 THR ALA LYS VAL LEU SER HIS TYR ILE ASP GLY ILE MET
SEQRES 11 B 340 ILE ARG THR PHE SER HIS ALA ASP VAL GLU GLU LEU ALA
SEQRES 12 B 340 LYS GLU SER SER ILE PRO VAL ILE ASN GLY LEU THR ASP
SEQRES 13 B 340 ASP HIS HIS PRO CYS GLN ALA LEU ALA ASP LEU MET THR
SEQRES 14 B 340 ILE TYR GLU GLU THR ASN THR PHE LYS GLY ILE LYS LEU
SEQRES 15 B 340 ALA TYR VAL GLY ASP GLY ASN ASN VAL CYS HIS SER LEU
SEQRES 16 B 340 LEU LEU ALA SER ALA LYS VAL GLY MET HIS MET THR VAL
SEQRES 17 B 340 ALA THR PRO VAL GLY TYR ARG PRO ASN GLU GLU ILE VAL
SEQRES 18 B 340 LYS LYS ALA LEU ALA ILE ALA LYS GLU THR GLY ALA GLU
SEQRES 19 B 340 ILE GLU ILE LEU HIS ASN PRO GLU LEU ALA VAL ASN GLU
SEQRES 20 B 340 ALA ASP PHE ILE TYR THR ASP VAL TRP MET SER MET GLY
SEQRES 21 B 340 GLN GLU GLY GLU GLU GLU LYS TYR THR LEU PHE GLN PRO
SEQRES 22 B 340 TYR GLN ILE ASN LYS GLU LEU VAL LYS HIS ALA LYS GLN
SEQRES 23 B 340 THR TYR HIS PHE LEU HIS CYS LEU PRO ALA HIS ARG GLU
SEQRES 24 B 340 GLU GLU VAL THR GLY GLU ILE ILE ASP GLY PRO GLN SER
SEQRES 25 B 340 ILE VAL PHE GLU GLN ALA GLY ASN ARG LEU HIS ALA GLN
SEQRES 26 B 340 LYS ALA LEU LEU VAL SER LEU PHE LYS ASN VAL GLU GLU
SEQRES 27 B 340 LEU SER
SEQRES 1 C 340 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 340 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 C 340 THR VAL GLN VAL PRO LYS LEU ASN THR LYS ASP LEU LEU
SEQRES 4 C 340 THR LEU GLU GLU LEU THR GLN GLU GLU ILE ILE SER LEU
SEQRES 5 C 340 ILE GLU PHE ALA ILE TYR LEU LYS LYS ASN LYS GLN GLU
SEQRES 6 C 340 PRO LEU LEU GLN GLY LYS ILE LEU GLY LEU ILE PHE ASP
SEQRES 7 C 340 LYS HIS SER THR ARG THR ARG VAL SER PHE GLU ALA GLY
SEQRES 8 C 340 MET VAL GLN LEU GLY GLY HIS GLY MET PHE LEU ASN GLY
SEQRES 9 C 340 LYS GLU MET GLN MET GLN ARG GLY GLU THR VAL SER ASP
SEQRES 10 C 340 THR ALA LYS VAL LEU SER HIS TYR ILE ASP GLY ILE MET
SEQRES 11 C 340 ILE ARG THR PHE SER HIS ALA ASP VAL GLU GLU LEU ALA
SEQRES 12 C 340 LYS GLU SER SER ILE PRO VAL ILE ASN GLY LEU THR ASP
SEQRES 13 C 340 ASP HIS HIS PRO CYS GLN ALA LEU ALA ASP LEU MET THR
SEQRES 14 C 340 ILE TYR GLU GLU THR ASN THR PHE LYS GLY ILE LYS LEU
SEQRES 15 C 340 ALA TYR VAL GLY ASP GLY ASN ASN VAL CYS HIS SER LEU
SEQRES 16 C 340 LEU LEU ALA SER ALA LYS VAL GLY MET HIS MET THR VAL
SEQRES 17 C 340 ALA THR PRO VAL GLY TYR ARG PRO ASN GLU GLU ILE VAL
SEQRES 18 C 340 LYS LYS ALA LEU ALA ILE ALA LYS GLU THR GLY ALA GLU
SEQRES 19 C 340 ILE GLU ILE LEU HIS ASN PRO GLU LEU ALA VAL ASN GLU
SEQRES 20 C 340 ALA ASP PHE ILE TYR THR ASP VAL TRP MET SER MET GLY
SEQRES 21 C 340 GLN GLU GLY GLU GLU GLU LYS TYR THR LEU PHE GLN PRO
SEQRES 22 C 340 TYR GLN ILE ASN LYS GLU LEU VAL LYS HIS ALA LYS GLN
SEQRES 23 C 340 THR TYR HIS PHE LEU HIS CYS LEU PRO ALA HIS ARG GLU
SEQRES 24 C 340 GLU GLU VAL THR GLY GLU ILE ILE ASP GLY PRO GLN SER
SEQRES 25 C 340 ILE VAL PHE GLU GLN ALA GLY ASN ARG LEU HIS ALA GLN
SEQRES 26 C 340 LYS ALA LEU LEU VAL SER LEU PHE LYS ASN VAL GLU GLU
SEQRES 27 C 340 LEU SER
HET CP A 401 8
HET NVA A 402 8
HET CL A 403 1
HET CL A 404 1
HET CL B 401 1
HET NVA B 402 8
HET CP B 403 8
HET CL B 404 1
HET CP C 401 8
HET NVA C 402 8
HET CL C 403 1
HETNAM CP PHOSPHORIC ACID MONO(FORMAMIDE)ESTER
HETNAM NVA NORVALINE
HETNAM CL CHLORIDE ION
FORMUL 4 CP 3(C H4 N O5 P)
FORMUL 5 NVA 3(C5 H11 N O2)
FORMUL 6 CL 5(CL 1-)
FORMUL 15 HOH *846(H2 O)
HELIX 1 1 THR A 21 ASN A 38 1 18
HELIX 2 2 THR A 58 LEU A 71 1 14
HELIX 3 3 LYS A 81 GLY A 88 5 8
HELIX 4 4 THR A 90 SER A 99 1 10
HELIX 5 5 SER A 111 SER A 122 1 12
HELIX 6 6 HIS A 135 ASN A 151 1 17
HELIX 7 7 ASN A 165 GLY A 179 1 15
HELIX 8 8 ASN A 193 GLY A 208 1 16
HELIX 9 9 ASN A 216 ASN A 222 1 7
HELIX 10 10 GLU A 240 GLN A 248 1 9
HELIX 11 11 PRO A 249 GLN A 251 5 3
HELIX 12 12 ASN A 253 LYS A 258 1 6
HELIX 13 13 THR A 279 ASP A 284 1 6
HELIX 14 14 ILE A 289 ASN A 311 1 23
HELIX 15 15 THR B 21 ASN B 38 1 18
HELIX 16 16 THR B 58 LEU B 71 1 14
HELIX 17 17 LYS B 81 GLY B 88 5 8
HELIX 18 18 THR B 90 SER B 99 1 10
HELIX 19 19 SER B 111 SER B 122 1 12
HELIX 20 20 HIS B 135 ASN B 151 1 17
HELIX 21 21 ASN B 165 GLY B 179 1 15
HELIX 22 22 ASN B 193 GLY B 208 1 16
HELIX 23 23 ASN B 216 ASN B 222 1 7
HELIX 24 24 GLU B 241 GLN B 248 1 8
HELIX 25 25 PRO B 249 GLN B 251 5 3
HELIX 26 26 ASN B 253 LYS B 258 1 6
HELIX 27 27 THR B 279 ASP B 284 1 6
HELIX 28 28 ILE B 289 ASN B 311 1 23
HELIX 29 29 THR C 21 ASN C 38 1 18
HELIX 30 30 THR C 58 LEU C 71 1 14
HELIX 31 31 LYS C 81 GLY C 88 5 8
HELIX 32 32 THR C 90 SER C 99 1 10
HELIX 33 33 SER C 111 SER C 122 1 12
HELIX 34 34 HIS C 135 ASN C 151 1 17
HELIX 35 35 ASN C 165 GLY C 179 1 15
HELIX 36 36 ASN C 193 GLY C 208 1 16
HELIX 37 37 ASN C 216 ASN C 222 1 7
HELIX 38 38 SER C 234 GLU C 238 5 5
HELIX 39 39 GLU C 242 GLN C 248 1 7
HELIX 40 40 PRO C 249 GLN C 251 5 3
HELIX 41 41 ASN C 253 LYS C 258 1 6
HELIX 42 42 THR C 279 ASP C 284 1 6
HELIX 43 43 ILE C 289 ASN C 311 1 23
SHEET 1 A 4 HIS A 74 ASN A 79 0
SHEET 2 A 4 ILE A 48 PHE A 53 1 N LEU A 51 O MET A 76
SHEET 3 A 4 GLY A 104 ARG A 108 1 O MET A 106 N GLY A 50
SHEET 4 A 4 VAL A 126 ASN A 128 1 O ILE A 127 N ILE A 107
SHEET 1 B 5 ILE A 211 LEU A 214 0
SHEET 2 B 5 HIS A 181 ALA A 185 1 N VAL A 184 O LEU A 214
SHEET 3 B 5 LYS A 157 VAL A 161 1 N TYR A 160 O THR A 183
SHEET 4 B 5 PHE A 226 THR A 229 1 O PHE A 226 N ALA A 159
SHEET 5 B 5 HIS A 265 HIS A 268 1 O LEU A 267 N ILE A 227
SHEET 1 C 4 HIS B 74 ASN B 79 0
SHEET 2 C 4 ILE B 48 PHE B 53 1 N LEU B 51 O LEU B 78
SHEET 3 C 4 GLY B 104 ARG B 108 1 O MET B 106 N GLY B 50
SHEET 4 C 4 VAL B 126 ASN B 128 1 O ILE B 127 N ILE B 107
SHEET 1 D 5 ILE B 211 LEU B 214 0
SHEET 2 D 5 HIS B 181 ALA B 185 1 N VAL B 184 O LEU B 214
SHEET 3 D 5 LYS B 157 VAL B 161 1 N TYR B 160 O THR B 183
SHEET 4 D 5 PHE B 226 THR B 229 1 O PHE B 226 N ALA B 159
SHEET 5 D 5 HIS B 265 HIS B 268 1 O LEU B 267 N ILE B 227
SHEET 1 E 4 HIS C 74 ASN C 79 0
SHEET 2 E 4 ILE C 48 PHE C 53 1 N LEU C 51 O LEU C 78
SHEET 3 E 4 GLY C 104 ARG C 108 1 O MET C 106 N GLY C 50
SHEET 4 E 4 VAL C 126 ASN C 128 1 O ILE C 127 N ILE C 107
SHEET 1 F 5 ILE C 211 LEU C 214 0
SHEET 2 F 5 HIS C 181 ALA C 185 1 N VAL C 184 O LEU C 214
SHEET 3 F 5 LYS C 157 VAL C 161 1 N TYR C 160 O THR C 183
SHEET 4 F 5 PHE C 226 THR C 229 1 O PHE C 226 N ALA C 159
SHEET 5 F 5 HIS C 265 HIS C 268 1 O LEU C 267 N ILE C 227
CISPEP 1 LEU A 270 PRO A 271 0 1.81
CISPEP 2 LEU B 270 PRO B 271 0 1.31
CISPEP 3 LEU C 270 PRO C 271 0 -1.00
SITE 1 AC1 12 SER A 57 THR A 58 ARG A 59 THR A 60
SITE 2 AC1 12 ARG A 108 HIS A 135 GLN A 138 CYS A 269
SITE 3 AC1 12 LEU A 270 ARG A 297 NVA A 402 GLN B 84
SITE 1 AC2 9 ASN A 165 ASN A 166 ASP A 230 SER A 234
SITE 2 AC2 9 MET A 235 LEU A 270 CP A 401 HOH A 513
SITE 3 AC2 9 HOH A 601
SITE 1 AC3 4 ILE A 289 VAL A 290 PHE A 291 GLU A 292
SITE 1 AC4 4 SER A 234 GLY A 236 HOH A 513 HOH A 540
SITE 1 AC5 4 ILE B 289 PHE B 291 GLU B 292 HOH B 619
SITE 1 AC6 10 LEU B 130 ASN B 165 ASN B 166 ASP B 230
SITE 2 AC6 10 SER B 234 MET B 235 LEU B 270 CP B 403
SITE 3 AC6 10 HOH B 645 HOH B 666
SITE 1 AC7 12 SER B 57 THR B 58 ARG B 59 THR B 60
SITE 2 AC7 12 ARG B 108 HIS B 135 GLN B 138 CYS B 269
SITE 3 AC7 12 LEU B 270 ARG B 297 NVA B 402 GLN C 84
SITE 1 AC8 4 SER B 234 GLY B 236 HOH B 666 HOH B 667
SITE 1 AC9 12 GLN A 84 SER C 57 THR C 58 ARG C 59
SITE 2 AC9 12 THR C 60 ARG C 108 HIS C 135 GLN C 138
SITE 3 AC9 12 CYS C 269 LEU C 270 ARG C 297 NVA C 402
SITE 1 BC1 10 HOH A 520 LEU C 130 ASN C 165 ASN C 166
SITE 2 BC1 10 ASP C 230 SER C 234 MET C 235 LEU C 270
SITE 3 BC1 10 CP C 401 HOH C 517
SITE 1 BC2 5 HOH A 689 ILE C 289 PHE C 291 GLU C 292
SITE 2 BC2 5 HOH C 632
CRYST1 85.893 99.893 118.989 90.00 90.00 90.00 P 21 21 21 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 0.011642 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010011 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008404 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
