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HEADER OXIDOREDUCTASE 26-JAN-12 4DGQ
TITLE CRYSTAL STRUCTURE OF NON-HEME CHLOROPEROXIDASE FROM BURKHOLDERIA
TITLE 2 CENOCEPACIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-HEME CHLOROPEROXIDASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 1.11.1.10;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CENOCEPACIA;
SOURCE 3 ORGANISM_TAXID: 216591;
SOURCE 4 STRAIN: J2315 / LMG 16656;
SOURCE 5 GENE: CPO, BCEJ2315_07640, BCAL0771;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: AVA0421
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.GARDBERG,T.E.EDWARDS,J.A.ABENDROTH,B.STAKER,L.STEWART,SEATTLE
AUTHOR 2 STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 1 07-MAR-12 4DGQ 0
JRNL AUTH A.S.GARDBERG,T.E.EDWARDS,J.A.ABENDROTH,B.STAKER,L.STEWART
JRNL TITL CRYSTAL STRUCTURE OF NON-HEME CHLOROPEROXIDASE FROM
JRNL TITL 2 BURKHOLDERIA CENOCEPACIA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.59
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 84695
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) : 0.136
REMARK 3 R VALUE (WORKING SET) : 0.135
REMARK 3 FREE R VALUE : 0.163
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4223
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5786
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE SET COUNT : 276
REMARK 3 BIN FREE R VALUE : 0.2430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6394
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 858
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.59
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.01000
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): 0.092
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.056
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.610
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6639 ; 0.016 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 4350 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9044 ; 1.595 ; 1.919
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10566 ; 0.970 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 840 ; 5.571 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 310 ;33.278 ;23.742
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 974 ;12.404 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;22.121 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 955 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7601 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1427 ; 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): 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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 9
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 23
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5370 1.5280 -26.2990
REMARK 3 T TENSOR
REMARK 3 T11: 0.0435 T22: 0.0696
REMARK 3 T33: 0.0656 T12: 0.0050
REMARK 3 T13: -0.0355 T23: 0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 1.1876 L22: 0.9968
REMARK 3 L33: 2.6505 L12: -0.3997
REMARK 3 L13: -1.4292 L23: 0.8199
REMARK 3 S TENSOR
REMARK 3 S11: 0.0494 S12: 0.1399 S13: 0.1418
REMARK 3 S21: -0.1889 S22: 0.0388 S23: 0.1570
REMARK 3 S31: -0.0904 S32: -0.1130 S33: -0.0882
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 24 A 149
REMARK 3 ORIGIN FOR THE GROUP (A): -22.9180 -10.8590 -18.4650
REMARK 3 T TENSOR
REMARK 3 T11: 0.0203 T22: 0.0322
REMARK 3 T33: 0.0365 T12: -0.0029
REMARK 3 T13: -0.0221 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.3226 L22: 0.3540
REMARK 3 L33: 0.3832 L12: 0.1038
REMARK 3 L13: 0.0419 L23: 0.0965
REMARK 3 S TENSOR
REMARK 3 S11: 0.0330 S12: 0.0429 S13: -0.0160
REMARK 3 S21: -0.0251 S22: -0.0313 S23: 0.0740
REMARK 3 S31: 0.0334 S32: -0.0563 S33: -0.0017
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 150 A 276
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1360 -17.4980 -16.3100
REMARK 3 T TENSOR
REMARK 3 T11: 0.0260 T22: 0.0092
REMARK 3 T33: 0.0263 T12: -0.0039
REMARK 3 T13: -0.0118 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.5113 L22: 0.4585
REMARK 3 L33: 0.3387 L12: 0.1062
REMARK 3 L13: 0.0307 L23: -0.0363
REMARK 3 S TENSOR
REMARK 3 S11: 0.0130 S12: 0.0183 S13: -0.0501
REMARK 3 S21: -0.0076 S22: -0.0075 S23: 0.0129
REMARK 3 S31: 0.0798 S32: -0.0001 S33: -0.0055
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 1 B 23
REMARK 3 ORIGIN FOR THE GROUP (A): -24.3230 11.6470 -4.1100
REMARK 3 T TENSOR
REMARK 3 T11: 0.0261 T22: 0.0883
REMARK 3 T33: 0.0738 T12: 0.0177
REMARK 3 T13: -0.0125 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 2.1737 L22: 2.2385
REMARK 3 L33: 1.2311 L12: 1.2616
REMARK 3 L13: -0.6289 L23: -1.3087
REMARK 3 S TENSOR
REMARK 3 S11: -0.0371 S12: 0.1264 S13: 0.0989
REMARK 3 S21: -0.0259 S22: 0.0412 S23: 0.1591
REMARK 3 S31: -0.0550 S32: -0.1995 S33: -0.0041
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 24 B 149
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5510 15.8230 4.9740
REMARK 3 T TENSOR
REMARK 3 T11: 0.0246 T22: 0.0130
REMARK 3 T33: 0.0369 T12: 0.0009
REMARK 3 T13: 0.0098 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 0.3754 L22: 0.3331
REMARK 3 L33: 0.2991 L12: 0.2451
REMARK 3 L13: -0.0585 L23: 0.1037
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: -0.0190 S13: 0.0469
REMARK 3 S21: 0.0206 S22: -0.0142 S23: 0.0336
REMARK 3 S31: -0.0427 S32: -0.0259 S33: -0.0109
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 150 B 276
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1560 9.3500 9.3180
REMARK 3 T TENSOR
REMARK 3 T11: 0.0125 T22: 0.0189
REMARK 3 T33: 0.0088 T12: -0.0029
REMARK 3 T13: -0.0035 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.5888 L22: 0.5008
REMARK 3 L33: 0.5645 L12: 0.0079
REMARK 3 L13: -0.1735 L23: 0.1912
REMARK 3 S TENSOR
REMARK 3 S11: 0.0120 S12: -0.0787 S13: 0.0184
REMARK 3 S21: 0.0568 S22: 0.0080 S23: -0.0232
REMARK 3 S31: 0.0073 S32: 0.0822 S33: -0.0199
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 : C 1 C 23
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1780 21.8810 -20.8810
REMARK 3 T TENSOR
REMARK 3 T11: 0.0933 T22: 0.0353
REMARK 3 T33: 0.0833 T12: 0.0348
REMARK 3 T13: 0.0260 T23: 0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 2.1411 L22: 2.4507
REMARK 3 L33: 1.4989 L12: 1.3535
REMARK 3 L13: 1.0233 L23: 1.1918
REMARK 3 S TENSOR
REMARK 3 S11: 0.0717 S12: 0.0658 S13: 0.1714
REMARK 3 S21: -0.0358 S22: -0.0302 S23: 0.1813
REMARK 3 S31: -0.1903 S32: -0.0981 S33: -0.0415
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 : C 24 C 149
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1590 14.9080 -28.8440
REMARK 3 T TENSOR
REMARK 3 T11: 0.0413 T22: 0.0523
REMARK 3 T33: 0.0289 T12: -0.0068
REMARK 3 T13: 0.0042 T23: 0.0350
REMARK 3 L TENSOR
REMARK 3 L11: 0.2671 L22: 0.2290
REMARK 3 L33: 0.5125 L12: 0.0644
REMARK 3 L13: -0.2904 L23: 0.0145
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: 0.0601 S13: 0.0693
REMARK 3 S21: -0.0400 S22: 0.0090 S23: 0.0192
REMARK 3 S31: -0.0718 S32: 0.0120 S33: -0.0341
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 150 C 276
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7580 10.2140 -25.1640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0143 T22: 0.0535
REMARK 3 T33: 0.0229 T12: -0.0104
REMARK 3 T13: 0.0098 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.3866 L22: 0.3472
REMARK 3 L33: 0.6584 L12: 0.0534
REMARK 3 L13: -0.1826 L23: -0.1488
REMARK 3 S TENSOR
REMARK 3 S11: 0.0177 S12: 0.0435 S13: -0.0022
REMARK 3 S21: -0.0475 S22: -0.0038 S23: -0.0597
REMARK 3 S31: -0.0344 S32: 0.1004 S33: -0.0140
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES WITH TLS ADDED. HYDROGENS HAVE
REMARK 3 BEEN ADDED IN THE RIDING POSITIONS.
REMARK 4
REMARK 4 4DGQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-12.
REMARK 100 THE RCSB ID CODE IS RCSB070307.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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 FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.541780
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84726
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY : 11.100
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.7700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.50400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
REMARK 200 SOFTWARE USED: PHASER_MR
REMARK 200 STARTING MODEL: PDB ENTRY 1ZOI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: INTERNAL TRACKING NUMBER 228044H10.
REMARK 280 WIZARD III/IV SCREEN CONDITION H10: 30% 2-PROPANOL, 30% PEG3350,
REMARK 280 0.1 M TRIS, PH 8.5. BUCEA00095HA1 PS01264 AT 21.88MG/ML IN A
REMARK 280 STABILIZING BUFFER OF 25 MM HEPES, PH 7.0, 500 MM NACL, 2 MM DTT,
REMARK 280 0.025% SODIUM AZIDE, 5% GLYCEROL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 55.92500
REMARK 290 SMTRY3 2 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: 6070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 GLY B -3
REMARK 465 PRO B -2
REMARK 465 GLY B -1
REMARK 465 GLY C -3
REMARK 465 PRO C -2
REMARK 465 GLY C -1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 113 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 175 CG CD CE NZ
REMARK 470 LYS B 7 CG CD CE NZ
REMARK 470 LYS B 175 CG CD CE NZ
REMARK 470 LYS B 244 CG CD CE NZ
REMARK 470 LYS B 247 CG CD CE NZ
REMARK 470 SER C 0 OG
REMARK 470 LYS C 7 CG CD CE NZ
REMARK 470 ARG C 113 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 175 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU A 178 OH TYR C 182 1.90
REMARK 500 OH TYR B 182 OE2 GLU C 178 1.90
REMARK 500 OD1 ASP B 39 O HOH B 552 2.01
REMARK 500 O HOH B 637 O HOH B 675 2.11
REMARK 500 O HOH B 557 O HOH B 644 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 26 CG HIS A 26 CD2 0.100
REMARK 500 HIS A 262 CG HIS A 262 CD2 0.061
REMARK 500 HIS B 26 CG HIS B 26 CD2 0.076
REMARK 500 ASP B 234 CB ASP B 234 CG 0.132
REMARK 500 HIS C 26 CG HIS C 26 CD2 0.074
REMARK 500 HIS C 55 CG HIS C 55 CD2 0.061
REMARK 500 HIS C 96 CG HIS C 96 CD2 0.056
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 8 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 264 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 57 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 57 NE - CZ - NH2 ANGL. DEV. = -3.8 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 PRO A 32 45.46 -105.02
REMARK 500 LEU A 33 -142.52 -96.46
REMARK 500 SER A 97 -121.37 64.09
REMARK 500 LEU A 127 108.66 -170.16
REMARK 500 ASN A 153 82.39 -163.83
REMARK 500 SER A 235 -94.28 -136.24
REMARK 500 PRO B 32 49.07 -102.15
REMARK 500 LEU B 33 -143.70 -102.66
REMARK 500 SER B 97 -124.92 63.46
REMARK 500 ASN B 153 77.40 -164.99
REMARK 500 SER B 235 -96.20 -136.33
REMARK 500 PRO C 32 48.48 -102.72
REMARK 500 LEU C 33 -141.90 -101.19
REMARK 500 SER C 97 -124.36 61.77
REMARK 500 LEU C 127 118.66 -164.33
REMARK 500 ASN C 153 79.41 -164.11
REMARK 500 SER C 235 -94.67 -137.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ILE C 258 24.7 L L OUTSIDE RANGE
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 EDO A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: BUCEA.00095.H RELATED DB: TARGETTRACK
DBREF 4DGQ A 1 276 UNP B4EA96 B4EA96_BURCJ 1 276
DBREF 4DGQ B 1 276 UNP B4EA96 B4EA96_BURCJ 1 276
DBREF 4DGQ C 1 276 UNP B4EA96 B4EA96_BURCJ 1 276
SEQADV 4DGQ GLY A -3 UNP B4EA96 EXPRESSION TAG
SEQADV 4DGQ PRO A -2 UNP B4EA96 EXPRESSION TAG
SEQADV 4DGQ GLY A -1 UNP B4EA96 EXPRESSION TAG
SEQADV 4DGQ SER A 0 UNP B4EA96 EXPRESSION TAG
SEQADV 4DGQ GLY B -3 UNP B4EA96 EXPRESSION TAG
SEQADV 4DGQ PRO B -2 UNP B4EA96 EXPRESSION TAG
SEQADV 4DGQ GLY B -1 UNP B4EA96 EXPRESSION TAG
SEQADV 4DGQ SER B 0 UNP B4EA96 EXPRESSION TAG
SEQADV 4DGQ GLY C -3 UNP B4EA96 EXPRESSION TAG
SEQADV 4DGQ PRO C -2 UNP B4EA96 EXPRESSION TAG
SEQADV 4DGQ GLY C -1 UNP B4EA96 EXPRESSION TAG
SEQADV 4DGQ SER C 0 UNP B4EA96 EXPRESSION TAG
SEQRES 1 A 280 GLY PRO GLY SER MET GLY THR VAL THR THR LYS ASP GLY
SEQRES 2 A 280 VAL GLU ILE PHE TYR LYS ASP TRP GLY PRO ARG ASP ALA
SEQRES 3 A 280 LYS VAL ILE HIS PHE HIS HIS GLY TRP PRO LEU SER SER
SEQRES 4 A 280 ASP ASP TRP ASP ALA GLN LEU LEU PHE PHE VAL ASN LYS
SEQRES 5 A 280 GLY PHE ARG VAL VAL ALA HIS ASP ARG ARG GLY HIS GLY
SEQRES 6 A 280 ARG SER SER GLN VAL TRP ASP GLY HIS ASP MET ASP HIS
SEQRES 7 A 280 TYR ALA ASP ASP ALA ALA ALA VAL VAL GLU LYS LEU GLY
SEQRES 8 A 280 THR HIS GLY ALA MET HIS VAL GLY HIS SER THR GLY GLY
SEQRES 9 A 280 GLY GLU VAL VAL ARG TYR ILE ALA ARG HIS GLY GLU ARG
SEQRES 10 A 280 ASN VAL SER LYS ALA VAL LEU ILE SER SER VAL PRO PRO
SEQRES 11 A 280 LEU MET VAL LYS THR SER SER ASN PRO ASN GLY THR PRO
SEQRES 12 A 280 LYS SER VAL PHE ASP ASP PHE GLN ALA HIS VAL ALA ALA
SEQRES 13 A 280 ASN ARG ALA GLN PHE TYR LEU ASP VAL PRO ALA GLY PRO
SEQRES 14 A 280 PHE TYR GLY TYR ASN ARG PRO GLY ALA LYS PRO SER GLU
SEQRES 15 A 280 GLY VAL ILE TYR ASN TRP TRP ARG GLN GLY MET MET GLY
SEQRES 16 A 280 SER THR LYS ALA GLN TYR ASP GLY ILE VAL ALA PHE SER
SEQRES 17 A 280 GLN THR ASP PHE THR ASN ASP LEU LYS GLY ILE THR ILE
SEQRES 18 A 280 PRO VAL LEU VAL ILE HIS GLY ASP ASP ASP GLN VAL VAL
SEQRES 19 A 280 PRO TYR ALA ASP SER GLY VAL LEU SER ALA LYS LEU VAL
SEQRES 20 A 280 LYS ASN GLY LYS LEU ILE THR TYR LYS GLY ALA PRO HIS
SEQRES 21 A 280 GLY ILE PRO THR THR HIS ALA ASP LYS VAL ASN ALA ASP
SEQRES 22 A 280 LEU LEU GLU PHE LEU GLN SER
SEQRES 1 B 280 GLY PRO GLY SER MET GLY THR VAL THR THR LYS ASP GLY
SEQRES 2 B 280 VAL GLU ILE PHE TYR LYS ASP TRP GLY PRO ARG ASP ALA
SEQRES 3 B 280 LYS VAL ILE HIS PHE HIS HIS GLY TRP PRO LEU SER SER
SEQRES 4 B 280 ASP ASP TRP ASP ALA GLN LEU LEU PHE PHE VAL ASN LYS
SEQRES 5 B 280 GLY PHE ARG VAL VAL ALA HIS ASP ARG ARG GLY HIS GLY
SEQRES 6 B 280 ARG SER SER GLN VAL TRP ASP GLY HIS ASP MET ASP HIS
SEQRES 7 B 280 TYR ALA ASP ASP ALA ALA ALA VAL VAL GLU LYS LEU GLY
SEQRES 8 B 280 THR HIS GLY ALA MET HIS VAL GLY HIS SER THR GLY GLY
SEQRES 9 B 280 GLY GLU VAL VAL ARG TYR ILE ALA ARG HIS GLY GLU ARG
SEQRES 10 B 280 ASN VAL SER LYS ALA VAL LEU ILE SER SER VAL PRO PRO
SEQRES 11 B 280 LEU MET VAL LYS THR SER SER ASN PRO ASN GLY THR PRO
SEQRES 12 B 280 LYS SER VAL PHE ASP ASP PHE GLN ALA HIS VAL ALA ALA
SEQRES 13 B 280 ASN ARG ALA GLN PHE TYR LEU ASP VAL PRO ALA GLY PRO
SEQRES 14 B 280 PHE TYR GLY TYR ASN ARG PRO GLY ALA LYS PRO SER GLU
SEQRES 15 B 280 GLY VAL ILE TYR ASN TRP TRP ARG GLN GLY MET MET GLY
SEQRES 16 B 280 SER THR LYS ALA GLN TYR ASP GLY ILE VAL ALA PHE SER
SEQRES 17 B 280 GLN THR ASP PHE THR ASN ASP LEU LYS GLY ILE THR ILE
SEQRES 18 B 280 PRO VAL LEU VAL ILE HIS GLY ASP ASP ASP GLN VAL VAL
SEQRES 19 B 280 PRO TYR ALA ASP SER GLY VAL LEU SER ALA LYS LEU VAL
SEQRES 20 B 280 LYS ASN GLY LYS LEU ILE THR TYR LYS GLY ALA PRO HIS
SEQRES 21 B 280 GLY ILE PRO THR THR HIS ALA ASP LYS VAL ASN ALA ASP
SEQRES 22 B 280 LEU LEU GLU PHE LEU GLN SER
SEQRES 1 C 280 GLY PRO GLY SER MET GLY THR VAL THR THR LYS ASP GLY
SEQRES 2 C 280 VAL GLU ILE PHE TYR LYS ASP TRP GLY PRO ARG ASP ALA
SEQRES 3 C 280 LYS VAL ILE HIS PHE HIS HIS GLY TRP PRO LEU SER SER
SEQRES 4 C 280 ASP ASP TRP ASP ALA GLN LEU LEU PHE PHE VAL ASN LYS
SEQRES 5 C 280 GLY PHE ARG VAL VAL ALA HIS ASP ARG ARG GLY HIS GLY
SEQRES 6 C 280 ARG SER SER GLN VAL TRP ASP GLY HIS ASP MET ASP HIS
SEQRES 7 C 280 TYR ALA ASP ASP ALA ALA ALA VAL VAL GLU LYS LEU GLY
SEQRES 8 C 280 THR HIS GLY ALA MET HIS VAL GLY HIS SER THR GLY GLY
SEQRES 9 C 280 GLY GLU VAL VAL ARG TYR ILE ALA ARG HIS GLY GLU ARG
SEQRES 10 C 280 ASN VAL SER LYS ALA VAL LEU ILE SER SER VAL PRO PRO
SEQRES 11 C 280 LEU MET VAL LYS THR SER SER ASN PRO ASN GLY THR PRO
SEQRES 12 C 280 LYS SER VAL PHE ASP ASP PHE GLN ALA HIS VAL ALA ALA
SEQRES 13 C 280 ASN ARG ALA GLN PHE TYR LEU ASP VAL PRO ALA GLY PRO
SEQRES 14 C 280 PHE TYR GLY TYR ASN ARG PRO GLY ALA LYS PRO SER GLU
SEQRES 15 C 280 GLY VAL ILE TYR ASN TRP TRP ARG GLN GLY MET MET GLY
SEQRES 16 C 280 SER THR LYS ALA GLN TYR ASP GLY ILE VAL ALA PHE SER
SEQRES 17 C 280 GLN THR ASP PHE THR ASN ASP LEU LYS GLY ILE THR ILE
SEQRES 18 C 280 PRO VAL LEU VAL ILE HIS GLY ASP ASP ASP GLN VAL VAL
SEQRES 19 C 280 PRO TYR ALA ASP SER GLY VAL LEU SER ALA LYS LEU VAL
SEQRES 20 C 280 LYS ASN GLY LYS LEU ILE THR TYR LYS GLY ALA PRO HIS
SEQRES 21 C 280 GLY ILE PRO THR THR HIS ALA ASP LYS VAL ASN ALA ASP
SEQRES 22 C 280 LEU LEU GLU PHE LEU GLN SER
HET EDO A 301 4
HET EDO B 301 4
HET EDO C 301 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 EDO 3(C2 H6 O2)
FORMUL 7 HOH *858(H2 O)
HELIX 1 1 SER A 34 ASP A 37 5 4
HELIX 2 2 TRP A 38 LYS A 48 1 11
HELIX 3 3 ASP A 71 GLY A 87 1 17
HELIX 4 4 THR A 98 GLY A 111 1 14
HELIX 5 5 GLU A 112 VAL A 115 5 4
HELIX 6 6 PRO A 139 GLY A 164 1 26
HELIX 7 7 SER A 177 GLY A 191 1 15
HELIX 8 8 SER A 192 THR A 206 1 15
HELIX 9 9 PHE A 208 GLY A 214 1 7
HELIX 10 10 PRO A 231 ASP A 234 5 4
HELIX 11 11 SER A 235 VAL A 243 1 9
HELIX 12 12 GLY A 257 HIS A 262 1 6
HELIX 13 13 HIS A 262 SER A 276 1 15
HELIX 14 14 SER B 34 ASP B 37 5 4
HELIX 15 15 TRP B 38 LYS B 48 1 11
HELIX 16 16 ASP B 71 GLY B 87 1 17
HELIX 17 17 THR B 98 GLY B 111 1 14
HELIX 18 18 PRO B 139 GLY B 164 1 26
HELIX 19 19 SER B 177 GLY B 191 1 15
HELIX 20 20 SER B 192 GLN B 205 1 14
HELIX 21 21 PHE B 208 GLY B 214 1 7
HELIX 22 22 PRO B 231 ASP B 234 5 4
HELIX 23 23 SER B 235 VAL B 243 1 9
HELIX 24 24 GLY B 257 HIS B 262 1 6
HELIX 25 25 HIS B 262 SER B 276 1 15
HELIX 26 26 SER C 34 ASP C 37 5 4
HELIX 27 27 TRP C 38 LYS C 48 1 11
HELIX 28 28 ASP C 71 GLY C 87 1 17
HELIX 29 29 THR C 98 GLY C 111 1 14
HELIX 30 30 GLU C 112 VAL C 115 5 4
HELIX 31 31 PRO C 139 GLY C 164 1 26
HELIX 32 32 SER C 177 GLY C 191 1 15
HELIX 33 33 SER C 192 THR C 206 1 15
HELIX 34 34 PHE C 208 GLY C 214 1 7
HELIX 35 35 PRO C 231 ASP C 234 5 4
HELIX 36 36 SER C 235 VAL C 243 1 9
HELIX 37 37 GLY C 257 HIS C 262 1 6
HELIX 38 38 HIS C 262 SER C 276 1 15
SHEET 1 A 8 THR A 3 THR A 5 0
SHEET 2 A 8 GLU A 11 TRP A 17 -1 O ILE A 12 N VAL A 4
SHEET 3 A 8 ARG A 51 HIS A 55 -1 O VAL A 52 N TRP A 17
SHEET 4 A 8 VAL A 24 HIS A 28 1 N PHE A 27 O VAL A 53
SHEET 5 A 8 MET A 92 HIS A 96 1 O VAL A 94 N HIS A 26
SHEET 6 A 8 LYS A 117 ILE A 121 1 O ILE A 121 N GLY A 95
SHEET 7 A 8 VAL A 219 GLY A 224 1 O LEU A 220 N LEU A 120
SHEET 8 A 8 GLY A 246 TYR A 251 1 O LYS A 247 N VAL A 221
SHEET 1 B 8 THR B 3 THR B 5 0
SHEET 2 B 8 GLU B 11 TRP B 17 -1 O ILE B 12 N VAL B 4
SHEET 3 B 8 ARG B 51 HIS B 55 -1 O VAL B 52 N TRP B 17
SHEET 4 B 8 VAL B 24 HIS B 28 1 N PHE B 27 O VAL B 53
SHEET 5 B 8 ALA B 91 HIS B 96 1 O VAL B 94 N HIS B 26
SHEET 6 B 8 VAL B 115 ILE B 121 1 O ILE B 121 N GLY B 95
SHEET 7 B 8 VAL B 219 GLY B 224 1 O LEU B 220 N LEU B 120
SHEET 8 B 8 GLY B 246 TYR B 251 1 O ILE B 249 N VAL B 221
SHEET 1 C 8 THR C 3 THR C 5 0
SHEET 2 C 8 GLU C 11 TRP C 17 -1 O ILE C 12 N VAL C 4
SHEET 3 C 8 ARG C 51 HIS C 55 -1 O VAL C 52 N TRP C 17
SHEET 4 C 8 VAL C 24 HIS C 28 1 N PHE C 27 O VAL C 53
SHEET 5 C 8 MET C 92 HIS C 96 1 O VAL C 94 N HIS C 26
SHEET 6 C 8 LYS C 117 ILE C 121 1 O ILE C 121 N GLY C 95
SHEET 7 C 8 VAL C 219 GLY C 224 1 O ILE C 222 N LEU C 120
SHEET 8 C 8 GLY C 246 TYR C 251 1 O ILE C 249 N VAL C 221
CISPEP 1 TRP A 31 PRO A 32 0 -5.55
CISPEP 2 PRO A 125 PRO A 126 0 3.88
CISPEP 3 TRP B 31 PRO B 32 0 -9.82
CISPEP 4 PRO B 125 PRO B 126 0 7.56
CISPEP 5 TRP C 31 PRO C 32 0 -10.65
CISPEP 6 PRO C 125 PRO C 126 0 4.12
SITE 1 AC1 4 TRP A 31 SER A 97 THR A 98 VAL A 229
SITE 1 AC2 5 TRP B 31 SER B 97 THR B 98 PHE B 203
SITE 2 AC2 5 VAL B 229
SITE 1 AC3 4 TRP C 31 SER C 97 THR C 98 VAL C 229
CRYST1 60.770 111.850 80.210 90.00 111.65 90.00 P 1 21 1 6
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 0.016455 0.000000 0.006533 0.00000
SCALE2 0.000000 0.008941 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013414 0.00000
TER 2150 SER A 276
TER 4295 SER B 276
TER 6435 SER C 276
MASTER 552 0 3 38 24 0 4 6 7264 3 12 66
END |