HEADER LIGASE 05-NOV-12 4HV4
TITLE 2.25 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF UDP-N-ACETYLMURAMATE--L-
TITLE 2 ALANINE LIGASE (MURC) FROM YERSINIA PESTIS CO92 IN COMPLEX WITH AMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: UDP-N-ACETYLMURAMOYL-L-ALANINE SYNTHETASE;
COMPND 5 EC: 6.3.2.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YERSINIA PESTIS;
SOURCE 3 ORGANISM_TAXID: 214092;
SOURCE 4 STRAIN: CO92;
SOURCE 5 GENE: MURC, Y3625, YPO0556, YP_3628;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE, MURC, YERSINIA PESTIS CO92,
KEYWDS 2 PEPTIDOGLYCAN SYNTHESIS, CENTER FOR STRUCTURAL GENOMICS OF
KEYWDS 3 INFECTIOUS DISEASES (CSGID), NIAID, NATIONAL INSTITUTE OF ALLERGY
KEYWDS 4 AND INFECTIOUS DISEASES, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.HALAVATY,G.MINASOV,I.DUBROVSKA,J.WINSOR,L.SHUVALOVA,S.PETERSON,
AUTHOR 2 W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID)
REVDAT 3 20-SEP-23 4HV4 1 REMARK SEQADV LINK
REVDAT 2 15-NOV-17 4HV4 1 REMARK
REVDAT 1 21-NOV-12 4HV4 0
JRNL AUTH A.S.HALAVATY,G.MINASOV,I.DUBROVSKA,J.WINSOR,L.SHUVALOVA,
JRNL AUTH 2 S.PETERSON,W.F.ANDERSON,
JRNL AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 4 (CSGID)
JRNL TITL 2.25 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF
JRNL TITL 2 UDP-N-ACETYLMURAMATE--L-ALANINE LIGASE (MURC) FROM YERSINIA
JRNL TITL 3 PESTIS CO92 IN COMPLEX WITH AMP
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 43511
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2317
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3150
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 179
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7099
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 282
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.41000
REMARK 3 B22 (A**2) : -1.10000
REMARK 3 B33 (A**2) : 2.50000
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): 0.314
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.215
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.150
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.240
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7474 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5011 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10175 ; 1.589 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12161 ; 0.867 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 955 ; 2.503 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 354 ;27.795 ;23.277
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1190 ;10.753 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 69 ;12.677 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1135 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8538 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1551 ; 0.001 ; 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): 4696 ; 0.915 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1915 ; 0.248 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7554 ; 1.691 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2778 ; 2.881 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2621 ; 4.480 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 19 A 108
REMARK 3 ORIGIN FOR THE GROUP (A): 9.8299 36.4926 33.3843
REMARK 3 T TENSOR
REMARK 3 T11: 0.0776 T22: 0.1793
REMARK 3 T33: 0.1205 T12: 0.0193
REMARK 3 T13: 0.0093 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 3.1314 L22: 4.1121
REMARK 3 L33: 1.8839 L12: -0.1355
REMARK 3 L13: -0.0244 L23: 1.3149
REMARK 3 S TENSOR
REMARK 3 S11: 0.0120 S12: -0.2031 S13: 0.3010
REMARK 3 S21: 0.1363 S22: 0.0169 S23: 0.2266
REMARK 3 S31: -0.1742 S32: -0.1245 S33: -0.0288
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 109 A 325
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0960 27.9620 13.0233
REMARK 3 T TENSOR
REMARK 3 T11: 0.0609 T22: 0.0376
REMARK 3 T33: 0.0185 T12: 0.0361
REMARK 3 T13: -0.0133 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 1.2372 L22: 1.0499
REMARK 3 L33: 1.5917 L12: 0.0242
REMARK 3 L13: 0.1607 L23: -0.1908
REMARK 3 S TENSOR
REMARK 3 S11: -0.0026 S12: 0.0173 S13: -0.0646
REMARK 3 S21: -0.2089 S22: -0.0527 S23: -0.0128
REMARK 3 S31: 0.0358 S32: 0.0486 S33: 0.0552
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 326 A 483
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7039 46.9682 0.5694
REMARK 3 T TENSOR
REMARK 3 T11: 0.1462 T22: 0.0756
REMARK 3 T33: 0.0205 T12: 0.0128
REMARK 3 T13: -0.0443 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 1.2255 L22: 1.2497
REMARK 3 L33: 1.5096 L12: 0.2643
REMARK 3 L13: 0.9202 L23: 0.4552
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: 0.0101 S13: 0.0664
REMARK 3 S21: -0.0302 S22: -0.0148 S23: -0.0180
REMARK 3 S31: -0.0285 S32: -0.0379 S33: 0.0139
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 15 B 107
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1096 59.2460 60.0237
REMARK 3 T TENSOR
REMARK 3 T11: 0.0228 T22: 0.0494
REMARK 3 T33: 0.0730 T12: -0.0291
REMARK 3 T13: 0.0128 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 4.1006 L22: 2.5282
REMARK 3 L33: 3.4571 L12: -0.5716
REMARK 3 L13: -0.9453 L23: 0.8874
REMARK 3 S TENSOR
REMARK 3 S11: 0.0062 S12: -0.1423 S13: -0.1378
REMARK 3 S21: -0.0073 S22: -0.0315 S23: 0.1604
REMARK 3 S31: 0.0666 S32: -0.0546 S33: 0.0253
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 108 B 305
REMARK 3 ORIGIN FOR THE GROUP (A): 31.4082 68.9234 38.9709
REMARK 3 T TENSOR
REMARK 3 T11: 0.0109 T22: 0.0273
REMARK 3 T33: 0.0047 T12: 0.0147
REMARK 3 T13: 0.0044 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 0.7121 L22: 0.8769
REMARK 3 L33: 1.8232 L12: 0.1786
REMARK 3 L13: 0.1257 L23: -0.0675
REMARK 3 S TENSOR
REMARK 3 S11: 0.0096 S12: -0.0106 S13: 0.0238
REMARK 3 S21: -0.0345 S22: -0.0660 S23: -0.0371
REMARK 3 S31: 0.0104 S32: 0.1205 S33: 0.0564
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 306 B 483
REMARK 3 ORIGIN FOR THE GROUP (A): 8.6287 73.1041 27.2686
REMARK 3 T TENSOR
REMARK 3 T11: 0.0465 T22: 0.1107
REMARK 3 T33: 0.0674 T12: 0.0006
REMARK 3 T13: -0.0202 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 1.6341 L22: 1.7634
REMARK 3 L33: 1.2626 L12: -0.9567
REMARK 3 L13: 0.0086 L23: -0.0251
REMARK 3 S TENSOR
REMARK 3 S11: -0.0529 S12: -0.0318 S13: -0.1520
REMARK 3 S21: -0.0626 S22: 0.0331 S23: 0.3393
REMARK 3 S31: -0.0386 S32: -0.3214 S33: 0.0197
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 501 A 501
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0543 36.3699 6.5723
REMARK 3 T TENSOR
REMARK 3 T11: 0.2755 T22: 0.3104
REMARK 3 T33: 0.1411 T12: -0.0440
REMARK 3 T13: -0.1376 T23: -0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 2.8261 L22: 33.0681
REMARK 3 L33: 28.8711 L12: 6.3640
REMARK 3 L13: -8.8987 L23: -24.0277
REMARK 3 S TENSOR
REMARK 3 S11: 0.0461 S12: -0.0002 S13: 0.1218
REMARK 3 S21: -0.4590 S22: 0.5444 S23: 1.2375
REMARK 3 S31: -0.0083 S32: -0.1346 S33: -0.5905
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 501 B 501
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7713 72.5034 32.8934
REMARK 3 T TENSOR
REMARK 3 T11: 0.1816 T22: 0.1826
REMARK 3 T33: 0.2799 T12: 0.0124
REMARK 3 T13: 0.0402 T23: -0.0487
REMARK 3 L TENSOR
REMARK 3 L11: 4.2610 L22: 14.8419
REMARK 3 L33: 1.2424 L12: 7.9522
REMARK 3 L13: -2.3007 L23: -4.2936
REMARK 3 S TENSOR
REMARK 3 S11: -0.1921 S12: 0.0979 S13: -0.0398
REMARK 3 S21: -0.3527 S22: 0.1843 S23: -0.0813
REMARK 3 S31: 0.0988 S32: -0.0510 S33: 0.0079
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4HV4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-12.
REMARK 100 THE DEPOSITION ID IS D_1000075958.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : DIAMOND(111)
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-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45997
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.80
REMARK 200 R MERGE FOR SHELL (I) : 0.55400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.680
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 2F00
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN 7.4 MG/ML IN 10 MM TRIS-HCL
REMARK 280 PH8.3 0.5 M NACL 5 MM BME, 1 MM ADP, 1 MM MGCL2 CRYSTALLIZATION:
REMARK 280 THE PACT SUITE (G7) - 0.2 M SODIUM ACETATE 0.1 M BIS TRIS
REMARK 280 PROPANE PH 7.5 20% (W/V) PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
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 33.26700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 91.64800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.01050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 91.64800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.26700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.01050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 THR A 3
REMARK 465 GLN A 4
REMARK 465 GLN A 5
REMARK 465 LEU A 6
REMARK 465 ALA A 7
REMARK 465 LYS A 8
REMARK 465 LEU A 9
REMARK 465 ARG A 10
REMARK 465 THR A 11
REMARK 465 ILE A 12
REMARK 465 VAL A 13
REMARK 465 PRO A 14
REMARK 465 GLU A 15
REMARK 465 MET A 16
REMARK 465 ARG A 17
REMARK 465 ARG A 18
REMARK 465 LEU A 484
REMARK 465 LYS A 485
REMARK 465 ASP A 486
REMARK 465 GLU A 487
REMARK 465 GLU A 488
REMARK 465 HIS A 489
REMARK 465 HIS A 490
REMARK 465 GLY A 491
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 THR B 3
REMARK 465 GLN B 4
REMARK 465 GLN B 5
REMARK 465 LEU B 6
REMARK 465 ALA B 7
REMARK 465 LYS B 8
REMARK 465 LEU B 9
REMARK 465 ARG B 10
REMARK 465 THR B 11
REMARK 465 ILE B 12
REMARK 465 VAL B 13
REMARK 465 PRO B 14
REMARK 465 HIS B 199
REMARK 465 MET B 200
REMARK 465 ASP B 201
REMARK 465 THR B 202
REMARK 465 TYR B 203
REMARK 465 GLN B 204
REMARK 465 GLY B 205
REMARK 465 LEU B 484
REMARK 465 LYS B 485
REMARK 465 ASP B 486
REMARK 465 GLU B 487
REMARK 465 GLU B 488
REMARK 465 HIS B 489
REMARK 465 HIS B 490
REMARK 465 GLY B 491
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 326 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 ASP A 50 140.53 -170.21
REMARK 500 PHE A 69 40.99 -100.30
REMARK 500 ASP A 147 73.65 18.88
REMARK 500 GLN A 186 79.69 -119.54
REMARK 500 ASN A 194 163.32 175.04
REMARK 500 HIS A 199 161.00 175.44
REMARK 500 HIS A 199 154.52 177.31
REMARK 500 PHE A 328 62.86 37.52
REMARK 500 ASN A 340 11.36 -144.61
REMARK 500 ARG A 383 142.55 74.46
REMARK 500 PHE B 69 59.81 -106.22
REMARK 500 ILE B 88 123.63 -27.51
REMARK 500 ASP B 147 75.02 8.63
REMARK 500 ASN B 194 162.77 175.60
REMARK 500 ASN B 340 22.06 -141.43
REMARK 500 ARG B 383 141.84 74.99
REMARK 500 LYS B 434 -56.95 -130.65
REMARK 500 GLU B 457 31.69 75.97
REMARK 500 ALA B 465 -155.93 -103.24
REMARK 500 LEU B 480 -17.64 72.24
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 AMP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP90657 RELATED DB: TARGETTRACK
DBREF 4HV4 A 1 491 UNP Q8ZIE8 MURC_YERPE 1 491
DBREF 4HV4 B 1 491 UNP Q8ZIE8 MURC_YERPE 1 491
SEQADV 4HV4 SER A -2 UNP Q8ZIE8 EXPRESSION TAG
SEQADV 4HV4 ASN A -1 UNP Q8ZIE8 EXPRESSION TAG
SEQADV 4HV4 ALA A 0 UNP Q8ZIE8 EXPRESSION TAG
SEQADV 4HV4 SER B -2 UNP Q8ZIE8 EXPRESSION TAG
SEQADV 4HV4 ASN B -1 UNP Q8ZIE8 EXPRESSION TAG
SEQADV 4HV4 ALA B 0 UNP Q8ZIE8 EXPRESSION TAG
SEQRES 1 A 494 SER ASN ALA MET ASN THR GLN GLN LEU ALA LYS LEU ARG
SEQRES 2 A 494 THR ILE VAL PRO GLU MET ARG ARG VAL ARG HIS ILE HIS
SEQRES 3 A 494 PHE VAL GLY ILE GLY GLY ALA GLY MET GLY GLY ILE ALA
SEQRES 4 A 494 GLU VAL LEU ALA ASN GLU GLY TYR GLN ILE SER GLY SER
SEQRES 5 A 494 ASP LEU ALA PRO ASN SER VAL THR GLN HIS LEU THR ALA
SEQRES 6 A 494 LEU GLY ALA GLN ILE TYR PHE HIS HIS ARG PRO GLU ASN
SEQRES 7 A 494 VAL LEU ASP ALA SER VAL VAL VAL VAL SER THR ALA ILE
SEQRES 8 A 494 SER ALA ASP ASN PRO GLU ILE VAL ALA ALA ARG GLU ALA
SEQRES 9 A 494 ARG ILE PRO VAL ILE ARG ARG ALA GLU MET LEU ALA GLU
SEQRES 10 A 494 LEU MET ARG TYR ARG HIS GLY ILE ALA VAL ALA GLY THR
SEQRES 11 A 494 HIS GLY LYS THR THR THR THR ALA MET LEU SER SER ILE
SEQRES 12 A 494 TYR ALA GLU ALA GLY LEU ASP PRO THR PHE VAL ASN GLY
SEQRES 13 A 494 GLY LEU VAL LYS ALA ALA GLY THR HIS ALA ARG LEU GLY
SEQRES 14 A 494 SER SER ARG TYR LEU ILE ALA GLU ALA ASP GLU SER ASP
SEQRES 15 A 494 ALA SER PHE LEU HIS LEU GLN PRO MET VAL ALA ILE VAL
SEQRES 16 A 494 THR ASN ILE GLU ALA ASP HIS MET ASP THR TYR GLN GLY
SEQRES 17 A 494 ASP PHE GLU ASN LEU LYS GLN THR PHE ILE ASN PHE LEU
SEQRES 18 A 494 HIS ASN LEU PRO PHE TYR GLY ARG ALA VAL MET CYS ILE
SEQRES 19 A 494 ASP ASP PRO VAL VAL ARG GLU LEU LEU PRO ARG VAL GLY
SEQRES 20 A 494 ARG HIS ILE THR THR TYR GLY PHE SER ASP ASP ALA ASP
SEQRES 21 A 494 VAL GLN ILE ALA SER TYR ARG GLN GLU GLY PRO GLN GLY
SEQRES 22 A 494 HIS PHE THR LEU ARG ARG GLN ASP LYS PRO LEU ILE GLU
SEQRES 23 A 494 VAL THR LEU ASN ALA PRO GLY ARG HIS ASN ALA LEU ASN
SEQRES 24 A 494 ALA ALA ALA ALA VAL ALA VAL ALA THR GLU GLU GLY ILE
SEQRES 25 A 494 GLU ASP GLU ASP ILE LEU ARG ALA LEU VAL GLY PHE GLN
SEQRES 26 A 494 GLY THR GLY ARG ARG PHE ASP PHE LEU GLY ASN PHE PRO
SEQRES 27 A 494 LEU ALA PRO VAL ASN GLY LYS GLU GLY SER ALA MET LEU
SEQRES 28 A 494 VAL ASP ASP TYR GLY HIS HIS PRO THR GLU VAL ASP ALA
SEQRES 29 A 494 THR ILE LYS ALA ALA ARG ALA GLY TRP PRO ASP LYS ARG
SEQRES 30 A 494 ILE VAL MET LEU PHE GLN PRO HIS ARG TYR THR ARG THR
SEQRES 31 A 494 ARG ASP LEU TYR ASP ASP PHE ALA ASN VAL LEU SER GLN
SEQRES 32 A 494 VAL ASP VAL LEU LEU MET LEU ASP VAL TYR ALA ALA GLY
SEQRES 33 A 494 GLU PRO PRO ILE PRO GLY ALA ASP SER ARG ALA LEU CYS
SEQRES 34 A 494 ARG THR ILE ARG ASN ARG GLY LYS LEU ASP PRO ILE LEU
SEQRES 35 A 494 VAL PRO ASP SER GLU SER ALA PRO GLU MET LEU ALA GLN
SEQRES 36 A 494 ILE LEU ASN GLY GLU ASP LEU ILE LEU VAL GLN GLY ALA
SEQRES 37 A 494 GLY ASN ILE GLY LYS ILE ALA ARG LYS LEU ALA GLU HIS
SEQRES 38 A 494 LYS LEU GLN PRO GLN LEU LYS ASP GLU GLU HIS HIS GLY
SEQRES 1 B 494 SER ASN ALA MET ASN THR GLN GLN LEU ALA LYS LEU ARG
SEQRES 2 B 494 THR ILE VAL PRO GLU MET ARG ARG VAL ARG HIS ILE HIS
SEQRES 3 B 494 PHE VAL GLY ILE GLY GLY ALA GLY MET GLY GLY ILE ALA
SEQRES 4 B 494 GLU VAL LEU ALA ASN GLU GLY TYR GLN ILE SER GLY SER
SEQRES 5 B 494 ASP LEU ALA PRO ASN SER VAL THR GLN HIS LEU THR ALA
SEQRES 6 B 494 LEU GLY ALA GLN ILE TYR PHE HIS HIS ARG PRO GLU ASN
SEQRES 7 B 494 VAL LEU ASP ALA SER VAL VAL VAL VAL SER THR ALA ILE
SEQRES 8 B 494 SER ALA ASP ASN PRO GLU ILE VAL ALA ALA ARG GLU ALA
SEQRES 9 B 494 ARG ILE PRO VAL ILE ARG ARG ALA GLU MET LEU ALA GLU
SEQRES 10 B 494 LEU MET ARG TYR ARG HIS GLY ILE ALA VAL ALA GLY THR
SEQRES 11 B 494 HIS GLY LYS THR THR THR THR ALA MET LEU SER SER ILE
SEQRES 12 B 494 TYR ALA GLU ALA GLY LEU ASP PRO THR PHE VAL ASN GLY
SEQRES 13 B 494 GLY LEU VAL LYS ALA ALA GLY THR HIS ALA ARG LEU GLY
SEQRES 14 B 494 SER SER ARG TYR LEU ILE ALA GLU ALA ASP GLU SER ASP
SEQRES 15 B 494 ALA SER PHE LEU HIS LEU GLN PRO MET VAL ALA ILE VAL
SEQRES 16 B 494 THR ASN ILE GLU ALA ASP HIS MET ASP THR TYR GLN GLY
SEQRES 17 B 494 ASP PHE GLU ASN LEU LYS GLN THR PHE ILE ASN PHE LEU
SEQRES 18 B 494 HIS ASN LEU PRO PHE TYR GLY ARG ALA VAL MET CYS ILE
SEQRES 19 B 494 ASP ASP PRO VAL VAL ARG GLU LEU LEU PRO ARG VAL GLY
SEQRES 20 B 494 ARG HIS ILE THR THR TYR GLY PHE SER ASP ASP ALA ASP
SEQRES 21 B 494 VAL GLN ILE ALA SER TYR ARG GLN GLU GLY PRO GLN GLY
SEQRES 22 B 494 HIS PHE THR LEU ARG ARG GLN ASP LYS PRO LEU ILE GLU
SEQRES 23 B 494 VAL THR LEU ASN ALA PRO GLY ARG HIS ASN ALA LEU ASN
SEQRES 24 B 494 ALA ALA ALA ALA VAL ALA VAL ALA THR GLU GLU GLY ILE
SEQRES 25 B 494 GLU ASP GLU ASP ILE LEU ARG ALA LEU VAL GLY PHE GLN
SEQRES 26 B 494 GLY THR GLY ARG ARG PHE ASP PHE LEU GLY ASN PHE PRO
SEQRES 27 B 494 LEU ALA PRO VAL ASN GLY LYS GLU GLY SER ALA MET LEU
SEQRES 28 B 494 VAL ASP ASP TYR GLY HIS HIS PRO THR GLU VAL ASP ALA
SEQRES 29 B 494 THR ILE LYS ALA ALA ARG ALA GLY TRP PRO ASP LYS ARG
SEQRES 30 B 494 ILE VAL MET LEU PHE GLN PRO HIS ARG TYR THR ARG THR
SEQRES 31 B 494 ARG ASP LEU TYR ASP ASP PHE ALA ASN VAL LEU SER GLN
SEQRES 32 B 494 VAL ASP VAL LEU LEU MET LEU ASP VAL TYR ALA ALA GLY
SEQRES 33 B 494 GLU PRO PRO ILE PRO GLY ALA ASP SER ARG ALA LEU CYS
SEQRES 34 B 494 ARG THR ILE ARG ASN ARG GLY LYS LEU ASP PRO ILE LEU
SEQRES 35 B 494 VAL PRO ASP SER GLU SER ALA PRO GLU MET LEU ALA GLN
SEQRES 36 B 494 ILE LEU ASN GLY GLU ASP LEU ILE LEU VAL GLN GLY ALA
SEQRES 37 B 494 GLY ASN ILE GLY LYS ILE ALA ARG LYS LEU ALA GLU HIS
SEQRES 38 B 494 LYS LEU GLN PRO GLN LEU LYS ASP GLU GLU HIS HIS GLY
HET AMP A 501 23
HET BME A 502 4
HET AMP B 501 23
HET BME B 502 4
HETNAM AMP ADENOSINE MONOPHOSPHATE
HETNAM BME BETA-MERCAPTOETHANOL
FORMUL 3 AMP 2(C10 H14 N5 O7 P)
FORMUL 4 BME 2(C2 H6 O S)
FORMUL 7 HOH *282(H2 O)
HELIX 1 1 GLY A 31 GLU A 42 1 12
HELIX 2 2 ASN A 54 LEU A 63 1 10
HELIX 3 3 ARG A 72 LEU A 77 5 6
HELIX 4 4 ASN A 92 ALA A 101 1 10
HELIX 5 5 ARG A 108 ARG A 117 1 10
HELIX 6 6 GLY A 129 ALA A 144 1 16
HELIX 7 7 GLU A 177 LEU A 185 5 9
HELIX 8 8 GLY A 205 HIS A 219 1 15
HELIX 9 9 ASP A 233 LEU A 240 1 8
HELIX 10 10 PRO A 241 VAL A 243 5 3
HELIX 11 11 GLY A 290 GLY A 308 1 19
HELIX 12 12 GLU A 310 PHE A 321 1 12
HELIX 13 13 LEU A 336 GLY A 341 1 6
HELIX 14 14 HIS A 355 TRP A 370 1 16
HELIX 15 15 ARG A 383 LEU A 390 1 8
HELIX 16 16 LEU A 390 SER A 399 1 10
HELIX 17 17 ASP A 421 ASN A 431 1 11
HELIX 18 18 SER A 445 LEU A 454 1 10
HELIX 19 19 ASN A 467 HIS A 478 1 12
HELIX 20 20 GLU B 15 VAL B 19 5 5
HELIX 21 21 GLY B 29 GLY B 43 1 15
HELIX 22 22 ASN B 54 LEU B 63 1 10
HELIX 23 23 ARG B 72 LEU B 77 5 6
HELIX 24 24 ASN B 92 ALA B 101 1 10
HELIX 25 25 ARG B 108 ARG B 117 1 10
HELIX 26 26 GLY B 129 ALA B 144 1 16
HELIX 27 27 GLU B 177 LEU B 185 5 9
HELIX 28 28 PHE B 207 HIS B 219 1 13
HELIX 29 29 ASP B 233 LEU B 240 1 8
HELIX 30 30 PRO B 241 VAL B 243 5 3
HELIX 31 31 GLY B 290 GLY B 308 1 19
HELIX 32 32 GLU B 310 PHE B 321 1 12
HELIX 33 33 LEU B 336 GLY B 341 1 6
HELIX 34 34 HIS B 355 TRP B 370 1 16
HELIX 35 35 ARG B 383 LEU B 390 1 8
HELIX 36 36 LEU B 390 SER B 399 1 10
HELIX 37 37 ASP B 421 ARG B 432 1 12
HELIX 38 38 SER B 445 LEU B 454 1 10
HELIX 39 39 ASN B 467 HIS B 478 1 12
SHEET 1 A 5 GLN A 66 TYR A 68 0
SHEET 2 A 5 GLN A 45 SER A 49 1 N GLY A 48 O GLN A 66
SHEET 3 A 5 HIS A 21 VAL A 25 1 N ILE A 22 O GLN A 45
SHEET 4 A 5 VAL A 81 VAL A 84 1 O VAL A 83 N HIS A 23
SHEET 5 A 5 VAL A 105 ARG A 107 1 O ILE A 106 N VAL A 84
SHEET 1 B10 THR A 161 ARG A 164 0
SHEET 2 B10 THR A 149 VAL A 156 -1 N ASN A 152 O HIS A 162
SHEET 3 B10 TYR A 170 GLU A 174 1 O TYR A 170 N THR A 149
SHEET 4 B10 HIS A 120 ALA A 125 1 N ILE A 122 O ALA A 173
SHEET 5 B10 VAL A 189 VAL A 192 1 O ILE A 191 N ALA A 125
SHEET 6 B10 ARG A 226 CYS A 230 1 O VAL A 228 N ALA A 190
SHEET 7 B10 ILE A 247 GLY A 251 1 O THR A 248 N ALA A 227
SHEET 8 B10 VAL A 258 GLU A 266 1 O ILE A 260 N GLY A 251
SHEET 9 B10 GLN A 269 ARG A 275 -1 O GLN A 269 N GLU A 266
SHEET 10 B10 ILE A 282 LEU A 286 -1 O LEU A 286 N GLY A 270
SHEET 1 C 6 ASP A 329 PRO A 335 0
SHEET 2 C 6 SER A 345 ASP A 351 -1 O LEU A 348 N GLY A 332
SHEET 3 C 6 ASP A 458 GLN A 463 1 O ILE A 460 N MET A 347
SHEET 4 C 6 ARG A 374 PHE A 379 1 N ARG A 374 O LEU A 459
SHEET 5 C 6 VAL A 403 LEU A 407 1 O LEU A 405 N MET A 377
SHEET 6 C 6 ILE A 438 VAL A 440 1 O VAL A 440 N MET A 406
SHEET 1 D 5 GLN B 66 TYR B 68 0
SHEET 2 D 5 GLN B 45 SER B 49 1 N GLY B 48 O TYR B 68
SHEET 3 D 5 HIS B 21 VAL B 25 1 N ILE B 22 O GLN B 45
SHEET 4 D 5 VAL B 81 VAL B 84 1 O VAL B 83 N VAL B 25
SHEET 5 D 5 VAL B 105 ARG B 107 1 O ILE B 106 N VAL B 82
SHEET 1 E10 ALA B 163 ARG B 164 0
SHEET 2 E10 THR B 149 VAL B 151 -1 N PHE B 150 O ARG B 164
SHEET 3 E10 TYR B 170 GLU B 174 1 O ILE B 172 N THR B 149
SHEET 4 E10 HIS B 120 ALA B 125 1 N ILE B 122 O LEU B 171
SHEET 5 E10 VAL B 189 VAL B 192 1 O ILE B 191 N ALA B 125
SHEET 6 E10 ARG B 226 CYS B 230 1 O VAL B 228 N ALA B 190
SHEET 7 E10 HIS B 246 GLY B 251 1 O HIS B 246 N ALA B 227
SHEET 8 E10 VAL B 258 GLU B 266 1 O ILE B 260 N GLY B 251
SHEET 9 E10 GLN B 269 ARG B 276 -1 O GLN B 269 N GLU B 266
SHEET 10 E10 ILE B 282 LEU B 286 -1 O VAL B 284 N PHE B 272
SHEET 1 F 6 ASP B 329 PRO B 335 0
SHEET 2 F 6 SER B 345 ASP B 351 -1 O LEU B 348 N LEU B 331
SHEET 3 F 6 ASP B 458 GLN B 463 1 O ILE B 460 N MET B 347
SHEET 4 F 6 ARG B 374 PHE B 379 1 N LEU B 378 O GLN B 463
SHEET 5 F 6 VAL B 403 LEU B 407 1 O LEU B 405 N MET B 377
SHEET 6 F 6 ILE B 438 VAL B 440 1 O VAL B 440 N MET B 406
LINK SG ACYS A 426 S2 ABME A 502 1555 1555 2.14
LINK SG ACYS B 426 S2 ABME B 502 1555 1555 1.91
SITE 1 AC1 18 HIS A 128 GLY A 129 LYS A 130 THR A 131
SITE 2 AC1 18 THR A 132 ASN A 194 HIS A 292 ASN A 296
SITE 3 AC1 18 ARG A 327 ASP A 351 TYR A 352 GLY A 353
SITE 4 AC1 18 GLU A 358 ALA A 361 THR A 362 HOH A 662
SITE 5 AC1 18 HOH A 683 HOH A 706
SITE 1 AC2 2 CYS A 426 ARG A 427
SITE 1 AC3 18 HIS B 128 GLY B 129 LYS B 130 THR B 131
SITE 2 AC3 18 THR B 132 ASN B 194 HIS B 292 ASN B 296
SITE 3 AC3 18 ARG B 327 ASP B 351 TYR B 352 GLY B 353
SITE 4 AC3 18 GLU B 358 THR B 362 HOH B 664 HOH B 701
SITE 5 AC3 18 HOH B 703 HOH B 727
SITE 1 AC4 2 CYS B 426 ARG B 430
CRYST1 66.534 78.021 183.296 90.00 90.00 90.00 P 21 21 21 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 0.015030 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012817 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005456 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
