HEADER HYDROLASE, LYASE 20-NOV-12 4I14
TITLE CRYSTAL STRUCTURE OF MTB-RIBA2 (RV1415)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOFLAVIN BIOSYNTHESIS PROTEIN RIBBA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE, DHBP
COMPND 5 SYNTHASE, GTP CYCLOHYDROLASE-2, GTP CYCLOHYDROLASE II;
COMPND 6 EC: 4.1.99.12, 3.5.4.25;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 419947;
SOURCE 4 STRAIN: H37RA;
SOURCE 5 GENE: MRA_1424, RIBBA, RV1415;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28C
KEYWDS DHBPS, GCHII, RIBA2, GTP, RIBOFLAVIN, ANTIMICROBIAL, HYDROLASE, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SINGH,P.KUMAR,S.YADAV,R.GAUTAM,N.SHARMA,S.KARTHIKEYAN
REVDAT 3 08-NOV-23 4I14 1 REMARK LINK
REVDAT 2 19-MAR-14 4I14 1 JRNL
REVDAT 1 28-AUG-13 4I14 0
JRNL AUTH M.SINGH,P.KUMAR,S.YADAV,R.GAUTAM,N.SHARMA,S.KARTHIKEYAN
JRNL TITL THE CRYSTAL STRUCTURE REVEALS THE MOLECULAR MECHANISM OF
JRNL TITL 2 BIFUNCTIONAL 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE
JRNL TITL 3 SYNTHASE/GTP CYCLOHYDROLASE II (RV1415) FROM MYCOBACTERIUM
JRNL TITL 4 TUBERCULOSIS
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 69 1633 2013
JRNL REFN ISSN 0907-4449
JRNL PMID 23999287
JRNL DOI 10.1107/S0907444913011402
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 18723
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1010
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1231
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.2860
REMARK 3 BIN FREE R VALUE SET COUNT : 78
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4743
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 7
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.76000
REMARK 3 B22 (A**2) : -4.86000
REMARK 3 B33 (A**2) : 1.10000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.407
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.309
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 36.813
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4817 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6537 ; 1.120 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 635 ; 5.820 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 199 ;33.325 ;22.714
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 745 ;16.659 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;18.134 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 772 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3636 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 208
REMARK 3 ORIGIN FOR THE GROUP (A): -17.4870 -2.7380 39.9560
REMARK 3 T TENSOR
REMARK 3 T11: 0.0097 T22: 0.4988
REMARK 3 T33: 0.0948 T12: -0.0044
REMARK 3 T13: -0.0161 T23: -0.0759
REMARK 3 L TENSOR
REMARK 3 L11: 4.4014 L22: 4.3372
REMARK 3 L33: 3.9407 L12: 0.7112
REMARK 3 L13: 1.0466 L23: 0.5111
REMARK 3 S TENSOR
REMARK 3 S11: 0.1465 S12: -0.2351 S13: 0.0965
REMARK 3 S21: -0.1048 S22: -0.3080 S23: 0.6301
REMARK 3 S31: -0.0245 S32: -0.5015 S33: 0.1615
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 209 A 383
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9120 18.6380 74.1530
REMARK 3 T TENSOR
REMARK 3 T11: 0.3131 T22: 0.7722
REMARK 3 T33: 0.5465 T12: 0.1920
REMARK 3 T13: -0.1785 T23: -0.3342
REMARK 3 L TENSOR
REMARK 3 L11: 5.9416 L22: 4.1150
REMARK 3 L33: 5.1776 L12: 0.8007
REMARK 3 L13: -0.6531 L23: 1.2552
REMARK 3 S TENSOR
REMARK 3 S11: 0.0313 S12: 0.0693 S13: -0.2910
REMARK 3 S21: 0.0328 S22: 0.4796 S23: -0.8775
REMARK 3 S31: 0.3207 S32: 0.7746 S33: -0.5109
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 1 B 202
REMARK 3 ORIGIN FOR THE GROUP (A): -62.1940 11.0230 51.9300
REMARK 3 T TENSOR
REMARK 3 T11: 0.0582 T22: 0.5194
REMARK 3 T33: 0.3117 T12: 0.0342
REMARK 3 T13: -0.0401 T23: 0.1858
REMARK 3 L TENSOR
REMARK 3 L11: 3.3713 L22: 3.1161
REMARK 3 L33: 5.1010 L12: -1.3102
REMARK 3 L13: 1.4420 L23: -1.5140
REMARK 3 S TENSOR
REMARK 3 S11: 0.1188 S12: -0.0649 S13: -0.3118
REMARK 3 S21: 0.0795 S22: -0.2358 S23: -0.0589
REMARK 3 S31: 0.0941 S32: 0.1732 S33: 0.1170
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 203 B 382
REMARK 3 ORIGIN FOR THE GROUP (A): -45.5640 10.2990 81.4630
REMARK 3 T TENSOR
REMARK 3 T11: 0.5327 T22: 0.7019
REMARK 3 T33: 0.2650 T12: 0.1164
REMARK 3 T13: -0.0624 T23: 0.0837
REMARK 3 L TENSOR
REMARK 3 L11: 6.6307 L22: 4.8795
REMARK 3 L33: 2.2906 L12: 4.1930
REMARK 3 L13: 1.9202 L23: 1.9203
REMARK 3 S TENSOR
REMARK 3 S11: 0.2978 S12: -1.1378 S13: 0.2770
REMARK 3 S21: 0.5839 S22: -0.0727 S23: 0.2429
REMARK 3 S31: 0.1648 S32: -0.2988 S33: -0.2250
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: TLS REFINEMENT
REMARK 4
REMARK 4 4I14 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-NOV-12.
REMARK 100 THE DEPOSITION ID IS D_1000076172.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-SEP-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19733
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.36600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1G57 AND 2BZ1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES-NA, PH 7.5, 15% PEG8000,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 84.38200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.41950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 84.38200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.41950
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 76
REMARK 465 VAL A 77
REMARK 465 ASN A 78
REMARK 465 GLN A 79
REMARK 465 ASP A 80
REMARK 465 LYS A 81
REMARK 465 HIS A 82
REMARK 465 GLY A 83
REMARK 465 THR A 84
REMARK 465 PRO A 249
REMARK 465 ASN A 250
REMARK 465 ALA A 251
REMARK 465 GLY A 301
REMARK 465 HIS A 302
REMARK 465 GLU A 303
REMARK 465 GLY A 304
REMARK 465 ARG A 305
REMARK 465 GLY A 306
REMARK 465 ILE A 307
REMARK 465 GLY A 308
REMARK 465 LEU A 309
REMARK 465 MET A 310
REMARK 465 HIS A 311
REMARK 465 LYS A 312
REMARK 465 LEU A 313
REMARK 465 GLN A 314
REMARK 465 ALA A 315
REMARK 465 TYR A 316
REMARK 465 GLN A 317
REMARK 465 LEU A 318
REMARK 465 GLN A 319
REMARK 465 ASP A 320
REMARK 465 ALA A 321
REMARK 465 GLY A 322
REMARK 465 ALA A 323
REMARK 465 ASP A 324
REMARK 465 THR A 325
REMARK 465 VAL A 326
REMARK 465 ASP A 327
REMARK 465 ALA A 328
REMARK 465 ASN A 329
REMARK 465 LEU A 330
REMARK 465 LYS A 331
REMARK 465 LEU A 332
REMARK 465 GLY A 333
REMARK 465 LEU A 334
REMARK 465 PRO A 335
REMARK 465 ALA A 336
REMARK 465 ASP A 337
REMARK 465 ALA A 338
REMARK 465 ARG A 339
REMARK 465 ASP A 340
REMARK 465 ALA A 364
REMARK 465 LYS A 365
REMARK 465 ARG A 366
REMARK 465 VAL A 367
REMARK 465 GLY A 368
REMARK 465 LEU A 369
REMARK 465 VAL A 384
REMARK 465 ARG A 385
REMARK 465 ALA A 386
REMARK 465 ASN A 387
REMARK 465 ALA A 388
REMARK 465 GLU A 389
REMARK 465 ASN A 390
REMARK 465 ILE A 391
REMARK 465 ARG A 392
REMARK 465 TYR A 393
REMARK 465 LEU A 394
REMARK 465 MET A 395
REMARK 465 THR A 396
REMARK 465 LYS A 397
REMARK 465 ARG A 398
REMARK 465 ASP A 399
REMARK 465 LYS A 400
REMARK 465 LEU A 401
REMARK 465 GLY A 402
REMARK 465 HIS A 403
REMARK 465 ASP A 404
REMARK 465 LEU A 405
REMARK 465 ALA A 406
REMARK 465 GLY A 407
REMARK 465 LEU A 408
REMARK 465 ASP A 409
REMARK 465 ASP A 410
REMARK 465 PHE A 411
REMARK 465 HIS A 412
REMARK 465 GLU A 413
REMARK 465 SER A 414
REMARK 465 VAL A 415
REMARK 465 HIS A 416
REMARK 465 LEU A 417
REMARK 465 PRO A 418
REMARK 465 GLY A 419
REMARK 465 GLU A 420
REMARK 465 PHE A 421
REMARK 465 GLY A 422
REMARK 465 GLY A 423
REMARK 465 ALA A 424
REMARK 465 LEU A 425
REMARK 465 TYR B 75
REMARK 465 ALA B 76
REMARK 465 VAL B 77
REMARK 465 ASN B 78
REMARK 465 GLN B 79
REMARK 465 ASP B 80
REMARK 465 LYS B 81
REMARK 465 HIS B 82
REMARK 465 GLY B 83
REMARK 465 THR B 84
REMARK 465 ALA B 85
REMARK 465 ALA B 247
REMARK 465 GLY B 248
REMARK 465 PRO B 249
REMARK 465 ASN B 250
REMARK 465 ALA B 251
REMARK 465 ASP B 252
REMARK 465 GLY B 301
REMARK 465 HIS B 302
REMARK 465 GLU B 303
REMARK 465 GLY B 304
REMARK 465 ARG B 305
REMARK 465 GLY B 306
REMARK 465 ILE B 307
REMARK 465 GLY B 308
REMARK 465 LEU B 309
REMARK 465 MET B 310
REMARK 465 HIS B 311
REMARK 465 LYS B 312
REMARK 465 LEU B 313
REMARK 465 GLN B 314
REMARK 465 ALA B 315
REMARK 465 TYR B 316
REMARK 465 GLN B 317
REMARK 465 LEU B 318
REMARK 465 GLN B 319
REMARK 465 ASP B 320
REMARK 465 ALA B 321
REMARK 465 GLY B 322
REMARK 465 ALA B 323
REMARK 465 ASP B 324
REMARK 465 THR B 325
REMARK 465 VAL B 326
REMARK 465 ASP B 327
REMARK 465 ALA B 328
REMARK 465 ASN B 329
REMARK 465 LEU B 330
REMARK 465 LYS B 331
REMARK 465 LEU B 332
REMARK 465 GLY B 333
REMARK 465 LEU B 334
REMARK 465 PRO B 335
REMARK 465 ALA B 336
REMARK 465 ASP B 337
REMARK 465 ALA B 338
REMARK 465 ARG B 339
REMARK 465 ASP B 340
REMARK 465 LYS B 365
REMARK 465 ARG B 366
REMARK 465 VAL B 367
REMARK 465 GLY B 368
REMARK 465 LEU B 369
REMARK 465 PRO B 383
REMARK 465 VAL B 384
REMARK 465 ARG B 385
REMARK 465 ALA B 386
REMARK 465 ASN B 387
REMARK 465 ALA B 388
REMARK 465 GLU B 389
REMARK 465 ASN B 390
REMARK 465 ILE B 391
REMARK 465 ARG B 392
REMARK 465 TYR B 393
REMARK 465 LEU B 394
REMARK 465 MET B 395
REMARK 465 THR B 396
REMARK 465 LYS B 397
REMARK 465 ARG B 398
REMARK 465 ASP B 399
REMARK 465 LYS B 400
REMARK 465 LEU B 401
REMARK 465 GLY B 402
REMARK 465 HIS B 403
REMARK 465 ASP B 404
REMARK 465 LEU B 405
REMARK 465 ALA B 406
REMARK 465 GLY B 407
REMARK 465 LEU B 408
REMARK 465 ASP B 409
REMARK 465 ASP B 410
REMARK 465 PHE B 411
REMARK 465 HIS B 412
REMARK 465 GLU B 413
REMARK 465 SER B 414
REMARK 465 VAL B 415
REMARK 465 HIS B 416
REMARK 465 LEU B 417
REMARK 465 PRO B 418
REMARK 465 GLY B 419
REMARK 465 GLU B 420
REMARK 465 PHE B 421
REMARK 465 GLY B 422
REMARK 465 GLY B 423
REMARK 465 ALA B 424
REMARK 465 LEU B 425
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 MET A 1 CG SD CE
REMARK 470 LYS A 207 CG CD CE NZ
REMARK 470 ILE A 232 CG1 CG2 CD1
REMARK 470 GLU A 234 CG CD OE1 OE2
REMARK 470 ASP A 235 CG OD1 OD2
REMARK 470 GLU A 237 CG CD OE1 OE2
REMARK 470 ASP A 252 CG OD1 OD2
REMARK 470 ASP A 254 CG OD1 OD2
REMARK 470 ARG A 273 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 276 CG OD1 OD2
REMARK 470 ARG A 290 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 354 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 358 CG CD1 CD2
REMARK 470 ASN A 362 CG OD1 ND2
REMARK 470 HIS A 375 CG ND1 CD2 CE1 NE2
REMARK 470 GLU A 378 CG CD OE1 OE2
REMARK 470 ARG A 379 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 382 CG CD1 CD2
REMARK 470 MET B 1 CG SD CE
REMARK 470 GLU B 26 CG CD OE1 OE2
REMARK 470 ARG B 28 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 93 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 120 CG OD1 OD2
REMARK 470 ARG B 124 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 134 CG CD CE NZ
REMARK 470 GLN B 169 CG CD OE1 NE2
REMARK 470 LYS B 170 CG CD CE NZ
REMARK 470 VAL B 212 CG1 CG2
REMARK 470 ARG B 216 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 217 CG1 CG2 CD1
REMARK 470 ARG B 220 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 245 CG CD OE1 OE2
REMARK 470 ILE B 246 CG1 CG2 CD1
REMARK 470 ASP B 255 CG OD1 OD2
REMARK 470 ARG B 274 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 290 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 354 CG CD NE CZ NH1 NH2
REMARK 470 HIS B 375 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B 377 CG1 CG2 CD1
REMARK 470 VAL B 380 CG1 CG2
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 ASP A 25 -155.54 -153.63
REMARK 500 PRO A 142 46.73 -77.08
REMARK 500 GLU A 234 151.96 176.06
REMARK 500 ASP A 235 77.70 -107.55
REMARK 500 ILE A 377 -60.62 -101.57
REMARK 500 ASP B 25 -168.64 -166.34
REMARK 500 TYR B 56 76.07 -103.15
REMARK 500 LEU B 72 69.77 69.03
REMARK 500 ASP B 120 2.95 -69.69
REMARK 500 PRO B 142 31.35 -68.71
REMARK 500 CYS B 164 145.10 -170.36
REMARK 500 HIS B 208 -18.77 -150.52
REMARK 500 HIS B 221 42.99 -107.31
REMARK 500 ASP B 235 55.72 -109.04
REMARK 500 CYS B 275 -54.75 -127.19
REMARK 500 ASP B 276 -2.01 75.05
REMARK 500 ASN B 361 63.05 -117.75
REMARK 500 ASN B 362 114.71 -167.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 264 SG
REMARK 620 2 CYS A 275 SG 95.9
REMARK 620 3 CYS A 277 SG 98.8 122.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 264 SG
REMARK 620 2 CYS B 277 SG 105.6
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3MIO RELATED DB: PDB
REMARK 900 DHBPS DOMAIN OF MTB-RIBA2
DBREF 4I14 A 1 425 UNP A5U2B7 RIBBA_MYCTA 1 425
DBREF 4I14 B 1 425 UNP A5U2B7 RIBBA_MYCTA 1 425
SEQRES 1 A 425 MET THR ARG LEU ASP SER VAL GLU ARG ALA VAL ALA ASP
SEQRES 2 A 425 ILE ALA ALA GLY LYS ALA VAL ILE VAL ILE ASP ASP GLU
SEQRES 3 A 425 ASP ARG GLU ASN GLU GLY ASP LEU ILE PHE ALA ALA GLU
SEQRES 4 A 425 LYS ALA THR PRO GLU MET VAL ALA PHE MET VAL ARG TYR
SEQRES 5 A 425 THR SER GLY TYR LEU CYS VAL PRO LEU ASP GLY ALA ILE
SEQRES 6 A 425 CYS ASP ARG LEU GLY LEU LEU PRO MET TYR ALA VAL ASN
SEQRES 7 A 425 GLN ASP LYS HIS GLY THR ALA TYR THR VAL THR VAL ASP
SEQRES 8 A 425 ALA ARG ASN GLY ILE GLY THR GLY ILE SER ALA SER ASP
SEQRES 9 A 425 ARG ALA THR THR MET ARG LEU LEU ALA ASP PRO THR SER
SEQRES 10 A 425 VAL ALA ASP ASP PHE THR ARG PRO GLY HIS VAL VAL PRO
SEQRES 11 A 425 LEU ARG ALA LYS ASP GLY GLY VAL LEU ARG ARG PRO GLY
SEQRES 12 A 425 HIS THR GLU ALA ALA VAL ASP LEU ALA ARG MET ALA GLY
SEQRES 13 A 425 LEU GLN PRO ALA GLY ALA ILE CYS GLU ILE VAL SER GLN
SEQRES 14 A 425 LYS ASP GLU GLY SER MET ALA HIS THR ASP GLU LEU ARG
SEQRES 15 A 425 VAL PHE ALA ASP GLU HIS GLY LEU ALA LEU ILE THR ILE
SEQRES 16 A 425 ALA ASP LEU ILE GLU TRP ARG ARG LYS HIS GLU LYS HIS
SEQRES 17 A 425 ILE GLU ARG VAL ALA GLU ALA ARG ILE PRO THR ARG HIS
SEQRES 18 A 425 GLY GLU PHE ARG ALA ILE GLY TYR THR SER ILE TYR GLU
SEQRES 19 A 425 ASP VAL GLU HIS VAL ALA LEU VAL ARG GLY GLU ILE ALA
SEQRES 20 A 425 GLY PRO ASN ALA ASP GLY ASP ASP VAL LEU VAL ARG VAL
SEQRES 21 A 425 HIS SER GLU CYS LEU THR GLY ASP VAL PHE GLY SER ARG
SEQRES 22 A 425 ARG CYS ASP CYS GLY PRO GLN LEU ASP ALA ALA LEU ALA
SEQRES 23 A 425 MET VAL ALA ARG GLU GLY ARG GLY VAL VAL LEU TYR MET
SEQRES 24 A 425 ARG GLY HIS GLU GLY ARG GLY ILE GLY LEU MET HIS LYS
SEQRES 25 A 425 LEU GLN ALA TYR GLN LEU GLN ASP ALA GLY ALA ASP THR
SEQRES 26 A 425 VAL ASP ALA ASN LEU LYS LEU GLY LEU PRO ALA ASP ALA
SEQRES 27 A 425 ARG ASP TYR GLY ILE GLY ALA GLN ILE LEU VAL ASP LEU
SEQRES 28 A 425 GLY VAL ARG SER MET ARG LEU LEU THR ASN ASN PRO ALA
SEQRES 29 A 425 LYS ARG VAL GLY LEU ASP GLY TYR GLY LEU HIS ILE ILE
SEQRES 30 A 425 GLU ARG VAL PRO LEU PRO VAL ARG ALA ASN ALA GLU ASN
SEQRES 31 A 425 ILE ARG TYR LEU MET THR LYS ARG ASP LYS LEU GLY HIS
SEQRES 32 A 425 ASP LEU ALA GLY LEU ASP ASP PHE HIS GLU SER VAL HIS
SEQRES 33 A 425 LEU PRO GLY GLU PHE GLY GLY ALA LEU
SEQRES 1 B 425 MET THR ARG LEU ASP SER VAL GLU ARG ALA VAL ALA ASP
SEQRES 2 B 425 ILE ALA ALA GLY LYS ALA VAL ILE VAL ILE ASP ASP GLU
SEQRES 3 B 425 ASP ARG GLU ASN GLU GLY ASP LEU ILE PHE ALA ALA GLU
SEQRES 4 B 425 LYS ALA THR PRO GLU MET VAL ALA PHE MET VAL ARG TYR
SEQRES 5 B 425 THR SER GLY TYR LEU CYS VAL PRO LEU ASP GLY ALA ILE
SEQRES 6 B 425 CYS ASP ARG LEU GLY LEU LEU PRO MET TYR ALA VAL ASN
SEQRES 7 B 425 GLN ASP LYS HIS GLY THR ALA TYR THR VAL THR VAL ASP
SEQRES 8 B 425 ALA ARG ASN GLY ILE GLY THR GLY ILE SER ALA SER ASP
SEQRES 9 B 425 ARG ALA THR THR MET ARG LEU LEU ALA ASP PRO THR SER
SEQRES 10 B 425 VAL ALA ASP ASP PHE THR ARG PRO GLY HIS VAL VAL PRO
SEQRES 11 B 425 LEU ARG ALA LYS ASP GLY GLY VAL LEU ARG ARG PRO GLY
SEQRES 12 B 425 HIS THR GLU ALA ALA VAL ASP LEU ALA ARG MET ALA GLY
SEQRES 13 B 425 LEU GLN PRO ALA GLY ALA ILE CYS GLU ILE VAL SER GLN
SEQRES 14 B 425 LYS ASP GLU GLY SER MET ALA HIS THR ASP GLU LEU ARG
SEQRES 15 B 425 VAL PHE ALA ASP GLU HIS GLY LEU ALA LEU ILE THR ILE
SEQRES 16 B 425 ALA ASP LEU ILE GLU TRP ARG ARG LYS HIS GLU LYS HIS
SEQRES 17 B 425 ILE GLU ARG VAL ALA GLU ALA ARG ILE PRO THR ARG HIS
SEQRES 18 B 425 GLY GLU PHE ARG ALA ILE GLY TYR THR SER ILE TYR GLU
SEQRES 19 B 425 ASP VAL GLU HIS VAL ALA LEU VAL ARG GLY GLU ILE ALA
SEQRES 20 B 425 GLY PRO ASN ALA ASP GLY ASP ASP VAL LEU VAL ARG VAL
SEQRES 21 B 425 HIS SER GLU CYS LEU THR GLY ASP VAL PHE GLY SER ARG
SEQRES 22 B 425 ARG CYS ASP CYS GLY PRO GLN LEU ASP ALA ALA LEU ALA
SEQRES 23 B 425 MET VAL ALA ARG GLU GLY ARG GLY VAL VAL LEU TYR MET
SEQRES 24 B 425 ARG GLY HIS GLU GLY ARG GLY ILE GLY LEU MET HIS LYS
SEQRES 25 B 425 LEU GLN ALA TYR GLN LEU GLN ASP ALA GLY ALA ASP THR
SEQRES 26 B 425 VAL ASP ALA ASN LEU LYS LEU GLY LEU PRO ALA ASP ALA
SEQRES 27 B 425 ARG ASP TYR GLY ILE GLY ALA GLN ILE LEU VAL ASP LEU
SEQRES 28 B 425 GLY VAL ARG SER MET ARG LEU LEU THR ASN ASN PRO ALA
SEQRES 29 B 425 LYS ARG VAL GLY LEU ASP GLY TYR GLY LEU HIS ILE ILE
SEQRES 30 B 425 GLU ARG VAL PRO LEU PRO VAL ARG ALA ASN ALA GLU ASN
SEQRES 31 B 425 ILE ARG TYR LEU MET THR LYS ARG ASP LYS LEU GLY HIS
SEQRES 32 B 425 ASP LEU ALA GLY LEU ASP ASP PHE HIS GLU SER VAL HIS
SEQRES 33 B 425 LEU PRO GLY GLU PHE GLY GLY ALA LEU
HET ZN A 501 1
HET SO4 A 502 5
HET ZN B 501 1
HET SO4 B 502 5
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 7 HOH *7(H2 O)
HELIX 1 1 SER A 6 ALA A 16 1 11
HELIX 2 2 GLU A 39 ALA A 41 5 3
HELIX 3 3 THR A 42 THR A 53 1 12
HELIX 4 4 GLY A 63 LEU A 69 1 7
HELIX 5 5 SER A 101 ASP A 114 1 14
HELIX 6 6 VAL A 118 ASP A 120 5 3
HELIX 7 7 GLY A 136 ARG A 140 5 5
HELIX 8 8 GLY A 143 ALA A 155 1 13
HELIX 9 9 HIS A 177 HIS A 188 1 12
HELIX 10 10 ILE A 195 GLU A 206 1 12
HELIX 11 11 CYS A 264 VAL A 269 1 6
HELIX 12 12 ASP A 276 GLY A 292 1 17
HELIX 13 13 GLY A 342 LEU A 351 1 10
HELIX 14 14 SER B 6 ALA B 16 1 11
HELIX 15 15 GLU B 39 ALA B 41 5 3
HELIX 16 16 THR B 42 THR B 53 1 12
HELIX 17 17 ASP B 62 GLY B 70 1 9
HELIX 18 18 SER B 101 ASP B 114 1 14
HELIX 19 19 VAL B 118 ASP B 120 5 3
HELIX 20 20 GLY B 136 ARG B 140 5 5
HELIX 21 21 GLY B 143 ALA B 155 1 13
HELIX 22 22 HIS B 177 GLY B 189 1 13
HELIX 23 23 ILE B 195 LYS B 204 1 10
HELIX 24 24 CYS B 264 VAL B 269 1 6
HELIX 25 25 ASP B 276 GLU B 291 1 16
HELIX 26 26 GLY B 342 GLY B 352 1 11
SHEET 1 A 4 GLY A 161 GLU A 165 0
SHEET 2 A 4 ASP A 33 ALA A 37 -1 N LEU A 34 O CYS A 164
SHEET 3 A 4 VAL A 20 ILE A 23 -1 N VAL A 20 O ILE A 35
SHEET 4 A 4 ALA A 191 THR A 194 1 O ALA A 191 N ILE A 21
SHEET 1 B 3 CYS A 58 ASP A 62 0
SHEET 2 B 3 PHE A 122 ALA A 133 1 O LEU A 131 N LEU A 61
SHEET 3 B 3 VAL A 90 ALA A 92 -1 N ASP A 91 O THR A 123
SHEET 1 C 7 ILE A 209 THR A 219 0
SHEET 2 C 7 GLY A 222 SER A 231 -1 O ALA A 226 N ALA A 215
SHEET 3 C 7 GLU A 237 ARG A 243 -1 O HIS A 238 N TYR A 229
SHEET 4 C 7 GLY A 294 MET A 299 -1 O TYR A 298 N VAL A 239
SHEET 5 C 7 VAL A 256 SER A 262 1 N HIS A 261 O LEU A 297
SHEET 6 C 7 SER A 355 LEU A 358 1 O ARG A 357 N VAL A 258
SHEET 7 C 7 HIS A 375 ILE A 376 1 O HIS A 375 N MET A 356
SHEET 1 D 4 GLY B 161 GLU B 165 0
SHEET 2 D 4 ASP B 33 ALA B 37 -1 N LEU B 34 O CYS B 164
SHEET 3 D 4 VAL B 20 ILE B 23 -1 N VAL B 20 O ILE B 35
SHEET 4 D 4 ALA B 191 THR B 194 1 O ALA B 191 N ILE B 21
SHEET 1 E 3 CYS B 58 LEU B 61 0
SHEET 2 E 3 PHE B 122 ARG B 132 1 O LEU B 131 N LEU B 61
SHEET 3 E 3 VAL B 90 ALA B 92 -1 N ASP B 91 O THR B 123
SHEET 1 F 7 ILE B 209 THR B 219 0
SHEET 2 F 7 GLY B 222 SER B 231 -1 O GLY B 228 N VAL B 212
SHEET 3 F 7 GLU B 237 ARG B 243 -1 O HIS B 238 N TYR B 229
SHEET 4 F 7 GLY B 294 MET B 299 -1 O TYR B 298 N VAL B 239
SHEET 5 F 7 VAL B 256 SER B 262 1 N HIS B 261 O LEU B 297
SHEET 6 F 7 SER B 355 LEU B 359 1 O LEU B 359 N VAL B 258
SHEET 7 F 7 HIS B 375 VAL B 380 1 O ILE B 377 N MET B 356
LINK SG CYS A 264 ZN ZN A 501 1555 1555 2.48
LINK SG CYS A 275 ZN ZN A 501 1555 1555 2.59
LINK SG CYS A 277 ZN ZN A 501 1555 1555 2.29
LINK SG CYS B 264 ZN ZN B 501 1555 1555 2.37
LINK SG CYS B 277 ZN ZN B 501 1555 1555 2.29
CISPEP 1 ARG A 124 PRO A 125 0 -1.36
CISPEP 2 ARG B 124 PRO B 125 0 -2.78
SITE 1 AC1 4 CYS A 264 CYS A 275 CYS A 277 HOH A 601
SITE 1 AC2 5 ARG A 141 GLY A 143 HIS A 144 THR A 145
SITE 2 AC2 5 GLU A 146
SITE 1 AC3 4 CYS B 264 CYS B 275 CYS B 277 HOH B 601
SITE 1 AC4 4 ARG B 141 GLY B 143 HIS B 144 THR B 145
CRYST1 168.764 74.839 76.427 90.00 90.00 90.00 P 21 21 2 8
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 0.005925 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013362 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013084 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
