HEADER TRANSFERASE 03-APR-06 2GKS
TITLE CRYSTAL STRUCTURE OF THE BI-FUNCTIONAL ATP SULFURYLASE-APS KINASE FROM
TITLE 2 AQUIFEX AEOLICUS, A CHEMOLITHOTROPHIC THERMOPHILE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL SAT/APS KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.7.7.4, 2.7.1.25;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 GENE: SAT/CYSC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET23A
KEYWDS TRANSFERASE, KINASE, SULFURYLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.YU,I.J.MACREA,E.B.LANSDON,I.H.SEGEL,A.J.FISHER
REVDAT 4 30-AUG-23 2GKS 1 REMARK
REVDAT 3 13-JUL-11 2GKS 1 VERSN
REVDAT 2 24-FEB-09 2GKS 1 VERSN
REVDAT 1 06-MAR-07 2GKS 0
JRNL AUTH Z.YU,E.B.LANSDON,I.H.SEGEL,A.J.FISHER
JRNL TITL CRYSTAL STRUCTURE OF THE BIFUNCTIONAL ATP SULFURYLASE-APS
JRNL TITL 2 KINASE FROM THE CHEMOLITHOTROPHIC THERMOPHILE AQUIFEX
JRNL TITL 3 AEOLICUS.
JRNL REF J.MOL.BIOL. V. 365 732 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17095009
JRNL DOI 10.1016/J.JMB.2006.10.035
REMARK 2
REMARK 2 RESOLUTION. 2.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.31
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 47281
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2475
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) : 2.31
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.37
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3244
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 154
REMARK 3 BIN FREE R VALUE : 0.2810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8446
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 108
REMARK 3 SOLVENT ATOMS : 299
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : -0.07000
REMARK 3 B33 (A**2) : 0.23000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.400
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.245
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.183
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.548
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8755 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11859 ; 1.235 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1046 ; 5.378 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 379 ;35.169 ;23.483
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1582 ;15.629 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 63 ;19.868 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1301 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6495 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3995 ; 0.188 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5870 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 439 ; 0.134 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 62 ; 0.176 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.195 ; 0.200
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): 5445 ; 0.430 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8507 ; 0.712 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3830 ; 1.190 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3352 ; 1.876 ; 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 4 A 140
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3240 0.1640 68.9570
REMARK 3 T TENSOR
REMARK 3 T11: -0.1424 T22: -0.2073
REMARK 3 T33: -0.1658 T12: 0.0778
REMARK 3 T13: -0.0733 T23: -0.0766
REMARK 3 L TENSOR
REMARK 3 L11: 3.5171 L22: 3.2758
REMARK 3 L33: 2.5248 L12: -0.0059
REMARK 3 L13: -1.3133 L23: 0.3131
REMARK 3 S TENSOR
REMARK 3 S11: -0.0862 S12: 0.2074 S13: -0.1995
REMARK 3 S21: -0.3734 S22: -0.0792 S23: 0.3261
REMARK 3 S31: 0.0736 S32: -0.0008 S33: 0.1654
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 141 A 321
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1470 3.8690 93.7320
REMARK 3 T TENSOR
REMARK 3 T11: -0.0479 T22: 0.0324
REMARK 3 T33: -0.1782 T12: 0.1545
REMARK 3 T13: 0.0892 T23: 0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 2.6847 L22: 3.7544
REMARK 3 L33: 2.5058 L12: -0.8577
REMARK 3 L13: -0.3045 L23: 0.6445
REMARK 3 S TENSOR
REMARK 3 S11: -0.3265 S12: -0.7132 S13: -0.4286
REMARK 3 S21: 0.6503 S22: 0.1266 S23: 0.5656
REMARK 3 S31: 0.3073 S32: 0.1295 S33: 0.1999
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 337 A 370
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6340 15.7740 94.6200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0825 T22: 0.1440
REMARK 3 T33: 0.0806 T12: 0.1543
REMARK 3 T13: 0.0599 T23: -0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 25.3483 L22: 3.2006
REMARK 3 L33: 15.6437 L12: -7.4717
REMARK 3 L13: 16.8075 L23: -7.0735
REMARK 3 S TENSOR
REMARK 3 S11: 0.3341 S12: -1.7708 S13: -1.9074
REMARK 3 S21: 0.2782 S22: 0.8971 S23: 1.0933
REMARK 3 S31: 0.5866 S32: -1.0787 S33: -1.2311
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 371 A 546
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2100 21.6020 67.4700
REMARK 3 T TENSOR
REMARK 3 T11: -0.0528 T22: -0.1338
REMARK 3 T33: -0.0227 T12: -0.0597
REMARK 3 T13: -0.0396 T23: -0.0591
REMARK 3 L TENSOR
REMARK 3 L11: 6.9584 L22: 2.5458
REMARK 3 L33: 2.0378 L12: 0.4053
REMARK 3 L13: -1.0611 L23: 0.5958
REMARK 3 S TENSOR
REMARK 3 S11: -0.3179 S12: 0.7222 S13: -0.1495
REMARK 3 S21: -0.2945 S22: 0.0999 S23: 0.4045
REMARK 3 S31: 0.1987 S32: -0.4062 S33: 0.2180
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 3 B 140
REMARK 3 ORIGIN FOR THE GROUP (A): -35.0240 56.8950 71.6640
REMARK 3 T TENSOR
REMARK 3 T11: -0.1519 T22: -0.1927
REMARK 3 T33: -0.2558 T12: 0.0326
REMARK 3 T13: -0.0377 T23: -0.0462
REMARK 3 L TENSOR
REMARK 3 L11: 3.3372 L22: 3.1314
REMARK 3 L33: 4.4967 L12: -1.0223
REMARK 3 L13: 2.1770 L23: -1.2071
REMARK 3 S TENSOR
REMARK 3 S11: -0.2487 S12: -0.0814 S13: 0.2808
REMARK 3 S21: -0.1425 S22: 0.0712 S23: -0.1781
REMARK 3 S31: -0.3891 S32: -0.2054 S33: 0.1774
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 141 B 321
REMARK 3 ORIGIN FOR THE GROUP (A): -29.3050 49.5420 95.7260
REMARK 3 T TENSOR
REMARK 3 T11: -0.0265 T22: 0.1862
REMARK 3 T33: -0.3048 T12: 0.1484
REMARK 3 T13: -0.0066 T23: -0.0555
REMARK 3 L TENSOR
REMARK 3 L11: 3.6269 L22: 3.9588
REMARK 3 L33: 4.3868 L12: -0.9302
REMARK 3 L13: 2.0265 L23: -0.7175
REMARK 3 S TENSOR
REMARK 3 S11: -0.3644 S12: -1.0544 S13: 0.1945
REMARK 3 S21: 0.7345 S22: 0.2000 S23: -0.0851
REMARK 3 S31: -0.3929 S32: -0.6243 S33: 0.1644
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 337 B 370
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6190 39.0150 96.3620
REMARK 3 T TENSOR
REMARK 3 T11: 0.0076 T22: 0.1684
REMARK 3 T33: -0.0273 T12: 0.0628
REMARK 3 T13: -0.0938 T23: -0.0338
REMARK 3 L TENSOR
REMARK 3 L11: 18.1283 L22: 7.1552
REMARK 3 L33: 21.4636 L12: -2.9092
REMARK 3 L13: -9.4876 L23: 8.2140
REMARK 3 S TENSOR
REMARK 3 S11: 0.6898 S12: -0.4920 S13: 0.3104
REMARK 3 S21: 0.1204 S22: 0.5420 S23: -1.2704
REMARK 3 S31: -0.4541 S32: 1.9300 S33: -1.2318
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 371 B 546
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2870 34.7620 68.0490
REMARK 3 T TENSOR
REMARK 3 T11: -0.0824 T22: -0.2502
REMARK 3 T33: 0.0331 T12: -0.0059
REMARK 3 T13: -0.0320 T23: -0.0827
REMARK 3 L TENSOR
REMARK 3 L11: 4.1417 L22: 1.0338
REMARK 3 L33: 2.6754 L12: 0.1910
REMARK 3 L13: -1.8501 L23: -0.5935
REMARK 3 S TENSOR
REMARK 3 S11: 0.1441 S12: -0.0187 S13: 0.8794
REMARK 3 S21: -0.0512 S22: 0.1727 S23: 0.1068
REMARK 3 S31: -0.2716 S32: 0.1374 S33: -0.3168
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GKS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037241.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-02
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 : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49813
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 99.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.32800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.010
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: PDB ENTRY 1I2D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% ETHANOL, 1.0% PEG 6000, 50 MM
REMARK 280 NAAC, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
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 33.64150
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER IN THE ASYMMETRIC
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: 6420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 MET A 1
REMARK 465 GLU A 2
REMARK 465 LYS A 3
REMARK 465 ALA A 322
REMARK 465 LYS A 323
REMARK 465 LYS A 324
REMARK 465 ARG A 325
REMARK 465 ASN A 326
REMARK 465 LEU A 327
REMARK 465 LYS A 328
REMARK 465 TYR A 329
REMARK 465 ILE A 330
REMARK 465 ASN A 331
REMARK 465 ILE A 332
REMARK 465 SER A 333
REMARK 465 GLY A 334
REMARK 465 THR A 335
REMARK 465 GLU A 336
REMARK 465 LYS A 496
REMARK 465 GLU A 497
REMARK 465 GLY A 498
REMARK 465 LEU A 499
REMARK 465 ILE A 500
REMARK 465 LYS A 501
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ALA B 322
REMARK 465 LYS B 323
REMARK 465 LYS B 324
REMARK 465 ARG B 325
REMARK 465 ASN B 326
REMARK 465 LEU B 327
REMARK 465 LYS B 328
REMARK 465 TYR B 329
REMARK 465 ILE B 330
REMARK 465 ASN B 331
REMARK 465 ILE B 332
REMARK 465 SER B 333
REMARK 465 GLY B 334
REMARK 465 THR B 335
REMARK 465 GLU B 336
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 TYR A 6 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASN A 320 CG OD1 ND2
REMARK 470 GLU A 321 CG CD OE1 OE2
REMARK 470 ILE A 337 CG1 CG2 CD1
REMARK 470 ARG A 338 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 426 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 485 CG CD OE1 OE2
REMARK 470 LYS A 489 CG CD CE NZ
REMARK 470 LYS A 493 CG CD CE NZ
REMARK 470 LYS A 494 CG CD CE NZ
REMARK 470 LYS B 3 CG CD CE NZ
REMARK 470 ILE B 319 CG1 CG2 CD1
REMARK 470 ASN B 320 CG OD1 ND2
REMARK 470 GLU B 321 CG CD OE1 OE2
REMARK 470 ILE B 337 CG1 CG2 CD1
REMARK 470 ARG B 338 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 344 CG CD OE1 NE2
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 GLU A 339 CD GLU A 339 OE1 0.116
REMARK 500 GLU A 339 CD GLU A 339 OE2 0.116
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 SER A 46 16.70 -140.65
REMARK 500 PRO A 82 -7.66 -54.83
REMARK 500 ASP A 143 -77.14 -101.06
REMARK 500 THR A 203 -108.96 -119.68
REMARK 500 GLU A 318 32.27 -81.01
REMARK 500 ILE A 319 97.37 60.64
REMARK 500 CYS A 382 -3.80 71.76
REMARK 500 SER A 453 73.94 27.64
REMARK 500 THR B 29 127.25 -38.55
REMARK 500 ASP B 143 -82.11 -99.32
REMARK 500 HIS B 176 -167.21 -100.37
REMARK 500 THR B 203 -108.22 -117.14
REMARK 500 LYS B 343 -149.83 -70.36
REMARK 500 ARG B 346 -158.98 -140.32
REMARK 500 SER B 453 72.77 30.18
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 ADP A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 904
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS INDICATE THAT POSITION 21 IS A GLU. SEQUENCE IN
REMARK 999 THE DATABASE COULD BE A VARIANT
DBREF 2GKS A 1 546 UNP O67174 SATC_AQUAE 1 546
DBREF 2GKS B 1 546 UNP O67174 SATC_AQUAE 1 546
SEQADV 2GKS GLU A 21 UNP O67174 LYS 21 SEE REMARK 999
SEQADV 2GKS GLU B 21 UNP O67174 LYS 21 SEE REMARK 999
SEQRES 1 A 546 MET GLU LYS ILE LYS TYR LEU LYS SER ILE GLN ILE SER
SEQRES 2 A 546 GLN ARG SER VAL LEU ASP LEU GLU LEU LEU ALA VAL GLY
SEQRES 3 A 546 ALA PHE THR PRO LEU ASP ARG PHE MET GLY GLU GLU ASP
SEQRES 4 A 546 TYR ARG ASN VAL VAL GLU SER MET ARG LEU LYS SER GLY
SEQRES 5 A 546 THR LEU PHE PRO ILE PRO ILE THR LEU PRO MET GLU LYS
SEQRES 6 A 546 GLU ILE ALA LYS ASP LEU LYS GLU GLY GLU TRP ILE VAL
SEQRES 7 A 546 LEU ARG ASP PRO LYS ASN VAL PRO LEU ALA ILE MET ARG
SEQRES 8 A 546 VAL GLU GLU VAL TYR LYS TRP ASN LEU GLU TYR GLU ALA
SEQRES 9 A 546 LYS ASN VAL LEU GLY THR THR ASP PRO ARG HIS PRO LEU
SEQRES 10 A 546 VAL ALA GLU MET HIS THR TRP GLY GLU TYR TYR ILE SER
SEQRES 11 A 546 GLY GLU LEU LYS VAL ILE GLN LEU PRO LYS TYR TYR ASP
SEQRES 12 A 546 PHE PRO GLU TYR ARG LYS THR PRO LYS GLN VAL ARG GLU
SEQRES 13 A 546 GLU ILE LYS SER LEU GLY LEU ASP LYS ILE VAL ALA PHE
SEQRES 14 A 546 GLN THR ARG ASN PRO MET HIS ARG VAL HIS GLU GLU LEU
SEQRES 15 A 546 THR LYS ARG ALA MET GLU LYS VAL GLY GLY GLY LEU LEU
SEQRES 16 A 546 LEU HIS PRO VAL VAL GLY LEU THR LYS PRO GLY ASP VAL
SEQRES 17 A 546 ASP VAL TYR THR ARG MET ARG ILE TYR LYS VAL LEU TYR
SEQRES 18 A 546 GLU LYS TYR TYR ASP LYS LYS LYS THR ILE LEU ALA PHE
SEQRES 19 A 546 LEU PRO LEU ALA MET ARG MET ALA GLY PRO ARG GLU ALA
SEQRES 20 A 546 LEU TRP HIS GLY ILE ILE ARG ARG ASN TYR GLY ALA THR
SEQRES 21 A 546 HIS PHE ILE VAL GLY ARG ASP HIS ALA SER PRO GLY LYS
SEQRES 22 A 546 ASP SER LYS GLY LYS PRO PHE TYR ASP PRO TYR GLU ALA
SEQRES 23 A 546 GLN GLU LEU PHE LYS LYS TYR GLU ASP GLU ILE GLY ILE
SEQRES 24 A 546 LYS MET VAL PRO PHE GLU GLU LEU VAL TYR VAL PRO GLU
SEQRES 25 A 546 LEU ASP GLN TYR VAL GLU ILE ASN GLU ALA LYS LYS ARG
SEQRES 26 A 546 ASN LEU LYS TYR ILE ASN ILE SER GLY THR GLU ILE ARG
SEQRES 27 A 546 GLU ASN PHE LEU LYS GLN GLY ARG LYS LEU PRO GLU TRP
SEQRES 28 A 546 PHE THR ARG PRO GLU VAL ALA GLU ILE LEU ALA GLU THR
SEQRES 29 A 546 TYR VAL PRO LYS HIS LYS GLN GLY PHE CYS VAL TRP LEU
SEQRES 30 A 546 THR GLY LEU PRO CYS ALA GLY LYS SER THR ILE ALA GLU
SEQRES 31 A 546 ILE LEU ALA THR MET LEU GLN ALA ARG GLY ARG LYS VAL
SEQRES 32 A 546 THR LEU LEU ASP GLY ASP VAL VAL ARG THR HIS LEU SER
SEQRES 33 A 546 ARG GLY LEU GLY PHE SER LYS GLU ASP ARG ILE THR ASN
SEQRES 34 A 546 ILE LEU ARG VAL GLY PHE VAL ALA SER GLU ILE VAL LYS
SEQRES 35 A 546 HIS ASN GLY VAL VAL ILE CYS ALA LEU VAL SER PRO TYR
SEQRES 36 A 546 ARG SER ALA ARG ASN GLN VAL ARG ASN MET MET GLU GLU
SEQRES 37 A 546 GLY LYS PHE ILE GLU VAL PHE VAL ASP ALA PRO VAL GLU
SEQRES 38 A 546 VAL CYS GLU GLU ARG ASP VAL LYS GLY LEU TYR LYS LYS
SEQRES 39 A 546 ALA LYS GLU GLY LEU ILE LYS GLY PHE THR GLY VAL ASP
SEQRES 40 A 546 ASP PRO TYR GLU PRO PRO VAL ALA PRO GLU VAL ARG VAL
SEQRES 41 A 546 ASP THR THR LYS LEU THR PRO GLU GLU SER ALA LEU LYS
SEQRES 42 A 546 ILE LEU GLU PHE LEU LYS LYS GLU GLY PHE ILE LYS ASP
SEQRES 1 B 546 MET GLU LYS ILE LYS TYR LEU LYS SER ILE GLN ILE SER
SEQRES 2 B 546 GLN ARG SER VAL LEU ASP LEU GLU LEU LEU ALA VAL GLY
SEQRES 3 B 546 ALA PHE THR PRO LEU ASP ARG PHE MET GLY GLU GLU ASP
SEQRES 4 B 546 TYR ARG ASN VAL VAL GLU SER MET ARG LEU LYS SER GLY
SEQRES 5 B 546 THR LEU PHE PRO ILE PRO ILE THR LEU PRO MET GLU LYS
SEQRES 6 B 546 GLU ILE ALA LYS ASP LEU LYS GLU GLY GLU TRP ILE VAL
SEQRES 7 B 546 LEU ARG ASP PRO LYS ASN VAL PRO LEU ALA ILE MET ARG
SEQRES 8 B 546 VAL GLU GLU VAL TYR LYS TRP ASN LEU GLU TYR GLU ALA
SEQRES 9 B 546 LYS ASN VAL LEU GLY THR THR ASP PRO ARG HIS PRO LEU
SEQRES 10 B 546 VAL ALA GLU MET HIS THR TRP GLY GLU TYR TYR ILE SER
SEQRES 11 B 546 GLY GLU LEU LYS VAL ILE GLN LEU PRO LYS TYR TYR ASP
SEQRES 12 B 546 PHE PRO GLU TYR ARG LYS THR PRO LYS GLN VAL ARG GLU
SEQRES 13 B 546 GLU ILE LYS SER LEU GLY LEU ASP LYS ILE VAL ALA PHE
SEQRES 14 B 546 GLN THR ARG ASN PRO MET HIS ARG VAL HIS GLU GLU LEU
SEQRES 15 B 546 THR LYS ARG ALA MET GLU LYS VAL GLY GLY GLY LEU LEU
SEQRES 16 B 546 LEU HIS PRO VAL VAL GLY LEU THR LYS PRO GLY ASP VAL
SEQRES 17 B 546 ASP VAL TYR THR ARG MET ARG ILE TYR LYS VAL LEU TYR
SEQRES 18 B 546 GLU LYS TYR TYR ASP LYS LYS LYS THR ILE LEU ALA PHE
SEQRES 19 B 546 LEU PRO LEU ALA MET ARG MET ALA GLY PRO ARG GLU ALA
SEQRES 20 B 546 LEU TRP HIS GLY ILE ILE ARG ARG ASN TYR GLY ALA THR
SEQRES 21 B 546 HIS PHE ILE VAL GLY ARG ASP HIS ALA SER PRO GLY LYS
SEQRES 22 B 546 ASP SER LYS GLY LYS PRO PHE TYR ASP PRO TYR GLU ALA
SEQRES 23 B 546 GLN GLU LEU PHE LYS LYS TYR GLU ASP GLU ILE GLY ILE
SEQRES 24 B 546 LYS MET VAL PRO PHE GLU GLU LEU VAL TYR VAL PRO GLU
SEQRES 25 B 546 LEU ASP GLN TYR VAL GLU ILE ASN GLU ALA LYS LYS ARG
SEQRES 26 B 546 ASN LEU LYS TYR ILE ASN ILE SER GLY THR GLU ILE ARG
SEQRES 27 B 546 GLU ASN PHE LEU LYS GLN GLY ARG LYS LEU PRO GLU TRP
SEQRES 28 B 546 PHE THR ARG PRO GLU VAL ALA GLU ILE LEU ALA GLU THR
SEQRES 29 B 546 TYR VAL PRO LYS HIS LYS GLN GLY PHE CYS VAL TRP LEU
SEQRES 30 B 546 THR GLY LEU PRO CYS ALA GLY LYS SER THR ILE ALA GLU
SEQRES 31 B 546 ILE LEU ALA THR MET LEU GLN ALA ARG GLY ARG LYS VAL
SEQRES 32 B 546 THR LEU LEU ASP GLY ASP VAL VAL ARG THR HIS LEU SER
SEQRES 33 B 546 ARG GLY LEU GLY PHE SER LYS GLU ASP ARG ILE THR ASN
SEQRES 34 B 546 ILE LEU ARG VAL GLY PHE VAL ALA SER GLU ILE VAL LYS
SEQRES 35 B 546 HIS ASN GLY VAL VAL ILE CYS ALA LEU VAL SER PRO TYR
SEQRES 36 B 546 ARG SER ALA ARG ASN GLN VAL ARG ASN MET MET GLU GLU
SEQRES 37 B 546 GLY LYS PHE ILE GLU VAL PHE VAL ASP ALA PRO VAL GLU
SEQRES 38 B 546 VAL CYS GLU GLU ARG ASP VAL LYS GLY LEU TYR LYS LYS
SEQRES 39 B 546 ALA LYS GLU GLY LEU ILE LYS GLY PHE THR GLY VAL ASP
SEQRES 40 B 546 ASP PRO TYR GLU PRO PRO VAL ALA PRO GLU VAL ARG VAL
SEQRES 41 B 546 ASP THR THR LYS LEU THR PRO GLU GLU SER ALA LEU LYS
SEQRES 42 B 546 ILE LEU GLU PHE LEU LYS LYS GLU GLY PHE ILE LYS ASP
HET ADP A 900 27
HET ADP A 902 27
HET ADP B 906 27
HET ADP B 904 27
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 3 ADP 4(C10 H15 N5 O10 P2)
FORMUL 7 HOH *299(H2 O)
HELIX 1 1 SER A 13 VAL A 25 1 13
HELIX 2 2 GLY A 36 MET A 47 1 12
HELIX 3 3 GLU A 64 LYS A 69 1 6
HELIX 4 4 ASN A 99 GLY A 109 1 11
HELIX 5 5 HIS A 115 HIS A 122 1 8
HELIX 6 6 PHE A 144 ARG A 148 5 5
HELIX 7 7 THR A 150 GLY A 162 1 13
HELIX 8 8 HIS A 176 GLY A 191 1 16
HELIX 9 9 ASP A 209 TYR A 225 1 17
HELIX 10 10 GLY A 243 TYR A 257 1 15
HELIX 11 11 TYR A 284 GLY A 298 1 15
HELIX 12 12 ARG A 338 LYS A 343 1 6
HELIX 13 13 ARG A 354 TYR A 365 1 12
HELIX 14 14 PRO A 367 GLN A 371 5 5
HELIX 15 15 GLY A 384 ARG A 399 1 16
HELIX 16 16 ASP A 407 LEU A 415 1 9
HELIX 17 17 SER A 422 HIS A 443 1 22
HELIX 18 18 TYR A 455 ASN A 464 1 10
HELIX 19 19 PRO A 479 GLU A 481 5 3
HELIX 20 20 VAL A 482 ASP A 487 1 6
HELIX 21 21 GLY A 490 ALA A 495 1 6
HELIX 22 22 THR A 526 GLU A 541 1 16
HELIX 23 23 LYS B 3 LEU B 7 5 5
HELIX 24 24 SER B 13 VAL B 25 1 13
HELIX 25 25 GLY B 36 MET B 47 1 12
HELIX 26 26 GLU B 64 LYS B 69 1 6
HELIX 27 27 ASN B 99 LEU B 108 1 10
HELIX 28 28 HIS B 115 HIS B 122 1 8
HELIX 29 29 PHE B 144 ARG B 148 5 5
HELIX 30 30 THR B 150 LEU B 161 1 12
HELIX 31 31 HIS B 176 GLY B 191 1 16
HELIX 32 32 ASP B 209 TYR B 225 1 17
HELIX 33 33 ALA B 242 TYR B 257 1 16
HELIX 34 34 TYR B 284 GLY B 298 1 15
HELIX 35 35 ARG B 354 TYR B 365 1 12
HELIX 36 36 PRO B 367 GLN B 371 5 5
HELIX 37 37 GLY B 384 ARG B 399 1 16
HELIX 38 38 GLY B 408 LEU B 415 1 8
HELIX 39 39 SER B 422 HIS B 443 1 22
HELIX 40 40 TYR B 455 ASN B 464 1 10
HELIX 41 41 LYS B 489 GLY B 498 1 10
HELIX 42 42 GLY B 498 GLY B 505 1 8
HELIX 43 43 THR B 526 GLU B 541 1 16
SHEET 1 A 4 LYS A 8 GLN A 11 0
SHEET 2 A 4 TRP A 76 ARG A 80 1 O ARG A 80 N ILE A 10
SHEET 3 A 4 PRO A 86 ARG A 91 -1 O ALA A 88 N LEU A 79
SHEET 4 A 4 LEU A 133 VAL A 135 -1 O LYS A 134 N ILE A 89
SHEET 1 B 3 LEU A 61 MET A 63 0
SHEET 2 B 3 TYR A 127 SER A 130 -1 O TYR A 127 N MET A 63
SHEET 3 B 3 GLU A 94 LYS A 97 -1 N TYR A 96 O TYR A 128
SHEET 1 C 5 THR A 230 LEU A 232 0
SHEET 2 C 5 GLY A 193 LEU A 196 1 N LEU A 194 O ILE A 231
SHEET 3 C 5 ILE A 166 PHE A 169 1 N VAL A 167 O LEU A 195
SHEET 4 C 5 HIS A 261 VAL A 264 1 O HIS A 261 N ALA A 168
SHEET 5 C 5 LYS A 300 PRO A 303 1 O VAL A 302 N PHE A 262
SHEET 1 D 2 VAL A 308 TYR A 309 0
SHEET 2 D 2 TYR A 316 VAL A 317 -1 O VAL A 317 N VAL A 308
SHEET 1 E 5 VAL A 403 LEU A 406 0
SHEET 2 E 5 VAL A 446 ALA A 450 1 O ILE A 448 N LEU A 406
SHEET 3 E 5 PHE A 373 THR A 378 1 N LEU A 377 O CYS A 449
SHEET 4 E 5 PHE A 471 ASP A 477 1 O ILE A 472 N CYS A 374
SHEET 5 E 5 VAL A 518 ASP A 521 1 O VAL A 520 N ASP A 477
SHEET 1 F 4 LYS B 8 GLN B 11 0
SHEET 2 F 4 TRP B 76 ARG B 80 1 O VAL B 78 N ILE B 10
SHEET 3 F 4 PRO B 86 ARG B 91 -1 O ALA B 88 N LEU B 79
SHEET 4 F 4 LEU B 133 VAL B 135 -1 O LYS B 134 N ILE B 89
SHEET 1 G 3 LEU B 61 MET B 63 0
SHEET 2 G 3 TYR B 127 SER B 130 -1 O ILE B 129 N LEU B 61
SHEET 3 G 3 GLU B 94 LYS B 97 -1 N TYR B 96 O TYR B 128
SHEET 1 H 5 THR B 230 LEU B 232 0
SHEET 2 H 5 GLY B 193 PRO B 198 1 N LEU B 196 O ILE B 231
SHEET 3 H 5 ILE B 166 THR B 171 1 N VAL B 167 O LEU B 195
SHEET 4 H 5 HIS B 261 VAL B 264 1 O ILE B 263 N ALA B 168
SHEET 5 H 5 LYS B 300 PRO B 303 1 O LYS B 300 N PHE B 262
SHEET 1 I 2 LEU B 307 VAL B 310 0
SHEET 2 I 2 GLN B 315 GLU B 318 -1 O VAL B 317 N VAL B 308
SHEET 1 J 5 VAL B 403 ASP B 407 0
SHEET 2 J 5 VAL B 446 ALA B 450 1 O ILE B 448 N LEU B 406
SHEET 3 J 5 PHE B 373 THR B 378 1 N LEU B 377 O CYS B 449
SHEET 4 J 5 PHE B 471 ASP B 477 1 O VAL B 474 N TRP B 376
SHEET 5 J 5 VAL B 518 ASP B 521 1 O VAL B 520 N PHE B 475
SSBOND 1 CYS B 382 CYS B 483 1555 1555 2.09
CISPEP 1 THR A 29 PRO A 30 0 6.49
CISPEP 2 THR B 29 PRO B 30 0 13.38
SITE 1 AC1 10 CYS A 382 ALA A 383 GLY A 384 LYS A 385
SITE 2 AC1 10 SER A 386 THR A 387 ARG A 486 THR A 522
SITE 3 AC1 10 LEU A 525 HOH A 920
SITE 1 AC2 14 PHE A 169 GLN A 170 THR A 171 ARG A 172
SITE 2 AC2 14 ASN A 173 MET A 239 GLY A 265 ARG A 266
SITE 3 AC2 14 HIS A 268 ALA A 269 GLU A 305 GLU A 306
SITE 4 AC2 14 LEU A 307 HOH A 989
SITE 1 AC3 15 PHE B 169 GLN B 170 THR B 171 ARG B 172
SITE 2 AC3 15 ASN B 173 HIS B 179 LEU B 182 GLY B 265
SITE 3 AC3 15 ARG B 266 HIS B 268 ALA B 269 GLU B 305
SITE 4 AC3 15 GLU B 306 LEU B 307 HOH B 984
SITE 1 AC4 14 LEU B 380 CYS B 382 ALA B 383 GLY B 384
SITE 2 AC4 14 LYS B 385 SER B 386 THR B 387 ARG B 486
SITE 3 AC4 14 LYS B 496 THR B 522 LEU B 525 HOH B 970
SITE 4 AC4 14 HOH B 974 HOH B1030
CRYST1 82.228 67.283 108.728 90.00 105.43 90.00 P 1 21 1 4
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 0.012161 0.000000 0.003356 0.00000
SCALE2 0.000000 0.014863 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009541 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
