HEADER TRANSFERASE 18-JAN-07 2OLC
TITLE CRYSTAL STRUCTURE OF 5-METHYLTHIORIBOSE KINASE IN COMPLEX WITH ADP-2HO
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLTHIORIBOSE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MTR KINASE;
COMPND 5 EC: 2.7.1.100;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: MTNK;
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: PTRCHIS2
KEYWDS KINASE ADP-2HO COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.Y.KU,G.D.SMITH,P.L.HOWELL
REVDAT 4 27-DEC-23 2OLC 1 REMARK
REVDAT 3 13-JUL-11 2OLC 1 VERSN
REVDAT 2 24-FEB-09 2OLC 1 VERSN
REVDAT 1 22-MAY-07 2OLC 0
JRNL AUTH S.Y.KU,G.D.SMITH,P.L.HOWELL
JRNL TITL ADP-2HO AS A PHASING TOOL FOR NUCLEOTIDE-CONTAINING
JRNL TITL 2 PROTEINS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 63 493 2007
JRNL REFN ISSN 0907-4449
JRNL PMID 17372354
JRNL DOI 10.1107/S0907444907006592
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 107.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 63173
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3148
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4352
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.2800
REMARK 3 BIN FREE R VALUE SET COUNT : 209
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5917
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 87
REMARK 3 SOLVENT ATOMS : 434
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) : 27.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.53000
REMARK 3 B22 (A**2) : -0.23000
REMARK 3 B33 (A**2) : 1.76000
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): 0.189
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.167
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.138
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.094
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6145 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8361 ; 1.324 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 744 ; 5.723 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 278 ;36.241 ;24.029
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 989 ;14.560 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;15.694 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 961 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4608 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2979 ; 0.196 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4305 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 479 ; 0.159 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 9 ; 0.165 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 34 ; 0.204 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.258 ; 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): 3831 ; 0.495 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6027 ; 0.841 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2592 ; 1.558 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2334 ; 2.270 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 5 A 396 3
REMARK 3 1 B 7 B 396 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1436 ; 0.040 ; 0.050
REMARK 3 LOOSE POSITIONAL 1 A (A): 1405 ; 0.290 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 1436 ; 0.100 ; 0.500
REMARK 3 LOOSE THERMAL 1 A (A**2): 1405 ; 0.970 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 5 A 120
REMARK 3 ORIGIN FOR THE GROUP (A): 63.2020 27.5569 20.8721
REMARK 3 T TENSOR
REMARK 3 T11: -0.1170 T22: -0.0892
REMARK 3 T33: 0.1478 T12: 0.0396
REMARK 3 T13: 0.0569 T23: 0.0510
REMARK 3 L TENSOR
REMARK 3 L11: 2.5995 L22: 1.2183
REMARK 3 L33: 1.2241 L12: 0.0624
REMARK 3 L13: 0.3710 L23: -0.0756
REMARK 3 S TENSOR
REMARK 3 S11: -0.0474 S12: 0.0571 S13: 0.2370
REMARK 3 S21: 0.0418 S22: -0.0001 S23: 0.4026
REMARK 3 S31: 0.0372 S32: -0.0513 S33: 0.0475
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 : B 7 B 120
REMARK 3 ORIGIN FOR THE GROUP (A): 60.5708 -19.5267 4.2206
REMARK 3 T TENSOR
REMARK 3 T11: -0.0939 T22: -0.0355
REMARK 3 T33: 0.0590 T12: 0.0065
REMARK 3 T13: -0.0168 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 2.9367 L22: 1.6280
REMARK 3 L33: 1.4040 L12: -0.1162
REMARK 3 L13: -0.5471 L23: 1.1233
REMARK 3 S TENSOR
REMARK 3 S11: -0.0280 S12: 0.1728 S13: -0.2582
REMARK 3 S21: -0.0283 S22: -0.1688 S23: 0.4576
REMARK 3 S31: 0.1067 S32: -0.0184 S33: 0.1968
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 121 A 396
REMARK 3 ORIGIN FOR THE GROUP (A): 87.8823 20.0204 16.5730
REMARK 3 T TENSOR
REMARK 3 T11: -0.0386 T22: -0.0030
REMARK 3 T33: -0.0334 T12: 0.0256
REMARK 3 T13: 0.0258 T23: 0.0812
REMARK 3 L TENSOR
REMARK 3 L11: 0.8221 L22: 1.0472
REMARK 3 L33: 0.3191 L12: 0.1717
REMARK 3 L13: 0.0426 L23: 0.1479
REMARK 3 S TENSOR
REMARK 3 S11: -0.0561 S12: 0.0698 S13: 0.1707
REMARK 3 S21: -0.0486 S22: 0.0975 S23: -0.0021
REMARK 3 S31: 0.0173 S32: 0.0330 S33: -0.0413
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 121 B 396
REMARK 3 ORIGIN FOR THE GROUP (A): 85.9864 -14.7135 10.6240
REMARK 3 T TENSOR
REMARK 3 T11: -0.0344 T22: 0.0232
REMARK 3 T33: -0.0815 T12: 0.0177
REMARK 3 T13: 0.0163 T23: 0.0442
REMARK 3 L TENSOR
REMARK 3 L11: 0.7334 L22: 0.6075
REMARK 3 L33: 0.3089 L12: -0.2092
REMARK 3 L13: 0.1335 L23: -0.0681
REMARK 3 S TENSOR
REMARK 3 S11: -0.0252 S12: 0.1519 S13: -0.0388
REMARK 3 S21: -0.0086 S22: 0.0307 S23: 0.0044
REMARK 3 S31: -0.0140 S32: 0.0312 S33: -0.0054
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2OLC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000041278.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-AUG-03; 01-SEP-04
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; N
REMARK 200 RADIATION SOURCE : NSLS; ROTATING ANODE
REMARK 200 BEAMLINE : X8C; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5362; 1.5418
REMARK 200 MONOCHROMATOR : SI(111); NI FILTER
REMARK 200 OPTICS : MIRRORS; OSMIC
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4R; RIGAKU RAXIS
REMARK 200 IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK 9.5L
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63253
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 71.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 26.94
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 26.57
REMARK 200 R MERGE FOR SHELL (I) : 0.43400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX, RESOLVE 2.06, SHELXDE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22%(W/V) PEG2000MME, 0.1M TRISHCL PH
REMARK 280 7.5 AND 0.3M SODIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 107.60000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.80000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 107.60000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.80000
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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER IN THE ASSYMETRIC UNIT
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: 6750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -174.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 215.20000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 GLY A 2
REMARK 465 VAL A 3
REMARK 465 THR A 4
REMARK 465 PHE A 27
REMARK 465 PRO A 28
REMARK 465 SER A 29
REMARK 465 LYS A 30
REMARK 465 SER A 31
REMARK 465 GLN A 52
REMARK 465 GLU A 53
REMARK 465 HIS A 54
REMARK 465 ASP A 55
REMARK 465 ALA A 67
REMARK 465 LYS A 68
REMARK 465 VAL A 69
REMARK 465 VAL A 70
REMARK 465 GLY A 71
REMARK 465 GLU A 72
REMARK 465 SER A 73
REMARK 465 GLU A 397
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 VAL B 3
REMARK 465 THR B 4
REMARK 465 LYS B 5
REMARK 465 THR B 6
REMARK 465 LYS B 30
REMARK 465 SER B 31
REMARK 465 ASP B 51
REMARK 465 GLN B 52
REMARK 465 GLU B 53
REMARK 465 HIS B 54
REMARK 465 ASP B 55
REMARK 465 LYS B 68
REMARK 465 VAL B 69
REMARK 465 VAL B 70
REMARK 465 GLY B 71
REMARK 465 GLU B 72
REMARK 465 SER B 73
REMARK 465 TRP B 74
REMARK 465 GLU B 397
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 5 CG CD CE NZ
REMARK 470 PRO A 7 CG CD
REMARK 470 LEU A 8 CG CD1 CD2
REMARK 470 GLU A 10 CG CD OE1 OE2
REMARK 470 LEU A 20 CG CD1 CD2
REMARK 470 LYS A 23 CG CD CE NZ
REMARK 470 GLN A 36 CG CD OE1 NE2
REMARK 470 ARG A 56 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 66 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 108 CG CD OE1 OE2
REMARK 470 ASP A 190 CG OD1 OD2
REMARK 470 GLU A 196 CG CD OE1 OE2
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 GLU A 302 CG CD OE1 OE2
REMARK 470 GLN A 305 CG CD OE1 NE2
REMARK 470 LYS A 306 CG CD CE NZ
REMARK 470 ASN A 314 CG OD1 ND2
REMARK 470 ASP A 316 CG OD1 OD2
REMARK 470 GLU A 369 CG CD OE1 OE2
REMARK 470 LEU B 8 CG CD1 CD2
REMARK 470 GLU B 10 CG CD OE1 OE2
REMARK 470 LYS B 23 CG CD CE NZ
REMARK 470 LEU B 26 CG CD1 CD2
REMARK 470 SER B 29 OG
REMARK 470 GLN B 36 CG CD OE1 NE2
REMARK 470 ASN B 42 CG OD1 ND2
REMARK 470 ARG B 56 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 66 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 108 CG CD OE1 OE2
REMARK 470 GLN B 138 CG CD OE1 NE2
REMARK 470 ASP B 190 CG OD1 OD2
REMARK 470 GLU B 298 CG CD OE1 OE2
REMARK 470 GLU B 302 CG CD OE1 OE2
REMARK 470 LYS B 306 CG CD CE NZ
REMARK 470 LYS B 382 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 HO HO A 400 O HOH A 1001 1.98
REMARK 500 HO HO B 401 O HOH B 1002 2.03
REMARK 500 O HOH B 1106 O HOH B 1155 2.12
REMARK 500 HO HO A 400 O HOH A 1002 2.17
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 PRO A 7 N - CA - CB ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG B 340 NE - CZ - NH1 ANGL. DEV. = -3.4 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 TYR A 133 77.92 45.63
REMARK 500 THR A 183 -60.02 -126.19
REMARK 500 ASP A 233 48.39 -158.95
REMARK 500 PRO A 251 43.77 -79.10
REMARK 500 TYR B 66 79.25 74.16
REMARK 500 TYR B 133 76.53 48.65
REMARK 500 THR B 183 -59.97 -127.93
REMARK 500 ASP B 233 45.27 -155.19
REMARK 500 PRO B 251 49.71 -83.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CPS A 777
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HO A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPS A 777
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HO B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 999
DBREF 2OLC A 1 397 UNP O31663 MTNK_BACSU 1 397
DBREF 2OLC B 1 397 UNP O31663 MTNK_BACSU 1 397
SEQRES 1 A 397 MET GLY VAL THR LYS THR PRO LEU TYR GLU THR LEU ASN
SEQRES 2 A 397 GLU SER SER ALA VAL ALA LEU ALA VAL LYS LEU GLY LEU
SEQRES 3 A 397 PHE PRO SER LYS SER THR LEU THR CYS GLN GLU ILE GLY
SEQRES 4 A 397 ASP GLY ASN LEU ASN TYR VAL PHE HIS ILE TYR ASP GLN
SEQRES 5 A 397 GLU HIS ASP ARG ALA LEU ILE ILE LYS GLN ALA VAL PRO
SEQRES 6 A 397 TYR ALA LYS VAL VAL GLY GLU SER TRP PRO LEU THR ILE
SEQRES 7 A 397 ASP ARG ALA ARG ILE GLU SER SER ALA LEU ILE ARG GLN
SEQRES 8 A 397 GLY GLU HIS VAL PRO HIS LEU VAL PRO ARG VAL PHE TYR
SEQRES 9 A 397 SER ASP THR GLU MET ALA VAL THR VAL MET GLU ASP LEU
SEQRES 10 A 397 SER HIS LEU LYS ILE ALA ARG LYS GLY LEU ILE GLU GLY
SEQRES 11 A 397 GLU ASN TYR PRO HIS LEU SER GLN HIS ILE GLY GLU PHE
SEQRES 12 A 397 LEU GLY LYS THR LEU PHE TYR SER SER ASP TYR ALA LEU
SEQRES 13 A 397 GLU PRO LYS VAL LYS LYS GLN LEU VAL LYS GLN PHE THR
SEQRES 14 A 397 ASN PRO GLU LEU CYS ASP ILE THR GLU ARG LEU VAL PHE
SEQRES 15 A 397 THR ASP PRO PHE PHE ASP HIS ASP THR ASN ASP PHE GLU
SEQRES 16 A 397 GLU GLU LEU ARG PRO PHE VAL GLU LYS LEU TRP ASN ASN
SEQRES 17 A 397 ASP SER VAL LYS ILE GLU ALA ALA LYS LEU LYS LYS SER
SEQRES 18 A 397 PHE LEU THR SER ALA GLU THR LEU ILE HIS GLY ASP LEU
SEQRES 19 A 397 HIS THR GLY SER ILE PHE ALA SER GLU HIS GLU THR LYS
SEQRES 20 A 397 VAL ILE ASP PRO GLU PHE ALA PHE TYR GLY PRO ILE GLY
SEQRES 21 A 397 PHE ASP VAL GLY GLN PHE ILE ALA ASN LEU PHE LEU ASN
SEQRES 22 A 397 ALA LEU SER ARG ASP GLY ALA ASP ARG GLU PRO LEU TYR
SEQRES 23 A 397 GLU HIS VAL ASN GLN VAL TRP GLU THR PHE GLU GLU THR
SEQRES 24 A 397 PHE SER GLU ALA TRP GLN LYS ASP SER LEU ASP VAL TYR
SEQRES 25 A 397 ALA ASN ILE ASP GLY TYR LEU THR ASP THR LEU SER HIS
SEQRES 26 A 397 ILE PHE GLU GLU ALA ILE GLY PHE ALA GLY CYS GLU LEU
SEQRES 27 A 397 ILE ARG ARG THR ILE GLY LEU ALA HIS VAL ALA ASP LEU
SEQRES 28 A 397 ASP THR ILE VAL PRO PHE ASP LYS ARG ILE GLY ARG LYS
SEQRES 29 A 397 ARG LEU ALA LEU GLU THR GLY THR ALA PHE ILE GLU LYS
SEQRES 30 A 397 ARG SER GLU PHE LYS THR ILE THR ASP VAL ILE GLU LEU
SEQRES 31 A 397 PHE LYS LEU LEU VAL LYS GLU
SEQRES 1 B 397 MET GLY VAL THR LYS THR PRO LEU TYR GLU THR LEU ASN
SEQRES 2 B 397 GLU SER SER ALA VAL ALA LEU ALA VAL LYS LEU GLY LEU
SEQRES 3 B 397 PHE PRO SER LYS SER THR LEU THR CYS GLN GLU ILE GLY
SEQRES 4 B 397 ASP GLY ASN LEU ASN TYR VAL PHE HIS ILE TYR ASP GLN
SEQRES 5 B 397 GLU HIS ASP ARG ALA LEU ILE ILE LYS GLN ALA VAL PRO
SEQRES 6 B 397 TYR ALA LYS VAL VAL GLY GLU SER TRP PRO LEU THR ILE
SEQRES 7 B 397 ASP ARG ALA ARG ILE GLU SER SER ALA LEU ILE ARG GLN
SEQRES 8 B 397 GLY GLU HIS VAL PRO HIS LEU VAL PRO ARG VAL PHE TYR
SEQRES 9 B 397 SER ASP THR GLU MET ALA VAL THR VAL MET GLU ASP LEU
SEQRES 10 B 397 SER HIS LEU LYS ILE ALA ARG LYS GLY LEU ILE GLU GLY
SEQRES 11 B 397 GLU ASN TYR PRO HIS LEU SER GLN HIS ILE GLY GLU PHE
SEQRES 12 B 397 LEU GLY LYS THR LEU PHE TYR SER SER ASP TYR ALA LEU
SEQRES 13 B 397 GLU PRO LYS VAL LYS LYS GLN LEU VAL LYS GLN PHE THR
SEQRES 14 B 397 ASN PRO GLU LEU CYS ASP ILE THR GLU ARG LEU VAL PHE
SEQRES 15 B 397 THR ASP PRO PHE PHE ASP HIS ASP THR ASN ASP PHE GLU
SEQRES 16 B 397 GLU GLU LEU ARG PRO PHE VAL GLU LYS LEU TRP ASN ASN
SEQRES 17 B 397 ASP SER VAL LYS ILE GLU ALA ALA LYS LEU LYS LYS SER
SEQRES 18 B 397 PHE LEU THR SER ALA GLU THR LEU ILE HIS GLY ASP LEU
SEQRES 19 B 397 HIS THR GLY SER ILE PHE ALA SER GLU HIS GLU THR LYS
SEQRES 20 B 397 VAL ILE ASP PRO GLU PHE ALA PHE TYR GLY PRO ILE GLY
SEQRES 21 B 397 PHE ASP VAL GLY GLN PHE ILE ALA ASN LEU PHE LEU ASN
SEQRES 22 B 397 ALA LEU SER ARG ASP GLY ALA ASP ARG GLU PRO LEU TYR
SEQRES 23 B 397 GLU HIS VAL ASN GLN VAL TRP GLU THR PHE GLU GLU THR
SEQRES 24 B 397 PHE SER GLU ALA TRP GLN LYS ASP SER LEU ASP VAL TYR
SEQRES 25 B 397 ALA ASN ILE ASP GLY TYR LEU THR ASP THR LEU SER HIS
SEQRES 26 B 397 ILE PHE GLU GLU ALA ILE GLY PHE ALA GLY CYS GLU LEU
SEQRES 27 B 397 ILE ARG ARG THR ILE GLY LEU ALA HIS VAL ALA ASP LEU
SEQRES 28 B 397 ASP THR ILE VAL PRO PHE ASP LYS ARG ILE GLY ARG LYS
SEQRES 29 B 397 ARG LEU ALA LEU GLU THR GLY THR ALA PHE ILE GLU LYS
SEQRES 30 B 397 ARG SER GLU PHE LYS THR ILE THR ASP VAL ILE GLU LEU
SEQRES 31 B 397 PHE LYS LEU LEU VAL LYS GLU
HET HO A 400 1
HET HO A 401 1
HET CPS A 777 29
HET ADP A 999 27
HET HO B 400 1
HET HO B 401 1
HET ADP B 999 27
HETNAM HO HOLMIUM ATOM
HETNAM CPS 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-
HETNAM 2 CPS PROPANESULFONATE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETSYN CPS CHAPS
FORMUL 3 HO 4(HO)
FORMUL 5 CPS C32 H58 N2 O7 S
FORMUL 6 ADP 2(C10 H15 N5 O10 P2)
FORMUL 10 HOH *434(H2 O)
HELIX 1 1 ASN A 13 LEU A 24 1 12
HELIX 2 2 ASP A 79 GLU A 93 1 15
HELIX 3 3 VAL A 95 VAL A 99 5 5
HELIX 4 4 ALA A 123 GLU A 129 1 7
HELIX 5 5 HIS A 135 SER A 151 1 17
HELIX 6 6 GLU A 157 PHE A 168 1 12
HELIX 7 7 ASN A 170 VAL A 181 1 12
HELIX 8 8 THR A 183 PHE A 187 5 5
HELIX 9 9 GLU A 195 GLU A 197 5 3
HELIX 10 10 LEU A 198 ASN A 207 1 10
HELIX 11 11 ASN A 208 SER A 225 1 18
HELIX 12 12 HIS A 235 GLY A 237 5 3
HELIX 13 13 ILE A 259 ARG A 277 1 19
HELIX 14 14 ASP A 278 ASP A 281 5 4
HELIX 15 15 ARG A 282 SER A 308 1 27
HELIX 16 16 GLY A 317 GLY A 344 1 28
HELIX 17 17 VAL A 348 THR A 353 1 6
HELIX 18 18 PRO A 356 ARG A 378 1 23
HELIX 19 19 THR A 383 VAL A 395 1 13
HELIX 20 20 ASN B 13 LEU B 24 1 12
HELIX 21 21 ASP B 79 VAL B 95 1 17
HELIX 22 22 PRO B 96 VAL B 99 5 4
HELIX 23 23 ALA B 123 GLY B 130 1 8
HELIX 24 24 HIS B 135 SER B 151 1 17
HELIX 25 25 GLU B 157 PHE B 168 1 12
HELIX 26 26 ASN B 170 VAL B 181 1 12
HELIX 27 27 THR B 183 PHE B 187 5 5
HELIX 28 28 GLU B 195 GLU B 197 5 3
HELIX 29 29 LEU B 198 ASN B 207 1 10
HELIX 30 30 ASN B 208 SER B 225 1 18
HELIX 31 31 HIS B 235 GLY B 237 5 3
HELIX 32 32 ILE B 259 ARG B 277 1 19
HELIX 33 33 ASP B 278 ASP B 281 5 4
HELIX 34 34 ARG B 282 SER B 308 1 27
HELIX 35 35 GLY B 317 GLY B 344 1 28
HELIX 36 36 VAL B 348 THR B 353 1 6
HELIX 37 37 PRO B 356 ARG B 378 1 23
HELIX 38 38 THR B 383 LYS B 396 1 14
SHEET 1 A 5 THR A 34 GLU A 37 0
SHEET 2 A 5 ASN A 44 TYR A 50 -1 O HIS A 48 N GLN A 36
SHEET 3 A 5 LEU A 58 ALA A 63 -1 O ILE A 60 N PHE A 47
SHEET 4 A 5 VAL A 111 MET A 114 -1 O THR A 112 N LYS A 61
SHEET 5 A 5 VAL A 102 ASP A 106 -1 N TYR A 104 O VAL A 113
SHEET 1 B 3 LYS A 121 ILE A 122 0
SHEET 2 B 3 ILE A 239 ALA A 241 -1 O ALA A 241 N LYS A 121
SHEET 3 B 3 THR A 246 VAL A 248 -1 O LYS A 247 N PHE A 240
SHEET 1 C 2 THR A 228 ILE A 230 0
SHEET 2 C 2 PHE A 255 GLY A 257 -1 O PHE A 255 N ILE A 230
SHEET 1 D 5 THR B 34 GLU B 37 0
SHEET 2 D 5 ASN B 44 TYR B 50 -1 O HIS B 48 N GLN B 36
SHEET 3 D 5 LEU B 58 ALA B 63 -1 O ILE B 60 N PHE B 47
SHEET 4 D 5 VAL B 111 MET B 114 -1 O MET B 114 N ILE B 59
SHEET 5 D 5 VAL B 102 ASP B 106 -1 N TYR B 104 O VAL B 113
SHEET 1 E 3 LYS B 121 ILE B 122 0
SHEET 2 E 3 ILE B 239 ALA B 241 -1 O ALA B 241 N LYS B 121
SHEET 3 E 3 THR B 246 VAL B 248 -1 O LYS B 247 N PHE B 240
SHEET 1 F 2 THR B 228 ILE B 230 0
SHEET 2 F 2 PHE B 255 GLY B 257 -1 O PHE B 255 N ILE B 230
CISPEP 1 VAL A 355 PRO A 356 0 -5.55
CISPEP 2 PRO B 28 SER B 29 0 -13.23
CISPEP 3 VAL B 355 PRO B 356 0 -2.69
SITE 1 AC1 4 ASP A 250 ADP A 999 HOH A1001 HOH A1002
SITE 1 AC2 5 ASP A 250 GLU A 252 ADP A 999 HOH A1000
SITE 2 AC2 5 HOH A1001
SITE 1 AC3 11 LYS A 377 ASP A 386 GLU A 389 LEU A 390
SITE 2 AC3 11 LYS B 377 GLU B 380 LEU B 393 LEU B 394
SITE 3 AC3 11 HOH B1118 HOH B1140 HOH B1186
SITE 1 AC4 18 ASP A 40 ASN A 44 ILE A 59 LYS A 61
SITE 2 AC4 18 MET A 114 GLU A 115 ASP A 116 LEU A 117
SITE 3 AC4 18 SER A 118 PHE A 240 ASP A 250 GLU A 252
SITE 4 AC4 18 HO A 400 HO A 401 HOH A1001 HOH A1002
SITE 5 AC4 18 HOH A1024 HOH A1048
SITE 1 AC5 4 ASP B 250 ADP B 999 HOH B1000 HOH B1001
SITE 1 AC6 4 ASP B 250 GLU B 252 ADP B 999 HOH B1002
SITE 1 AC7 18 ASP B 40 ASN B 44 ILE B 59 LYS B 61
SITE 2 AC7 18 MET B 114 GLU B 115 ASP B 116 LEU B 117
SITE 3 AC7 18 ILE B 122 PHE B 240 ASP B 250 GLU B 252
SITE 4 AC7 18 HO B 400 HO B 401 HOH B1000 HOH B1001
SITE 5 AC7 18 HOH B1099 HOH B1196
CRYST1 215.200 83.600 51.600 90.00 90.00 90.00 P 21 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004647 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011962 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019380 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
