HEADER TRANSFERASE 22-FEB-17 5X6I
TITLE CRYSTAL STRUCTURE OF B. SUBTILIS ADENYLATE KINASE VARIANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLATE KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: I26T;
COMPND 5 SYNONYM: AK,ATP-AMP TRANSPHOSPHORYLASE,ATP:AMP PHOSPHOTRANSFERASE,
COMPND 6 ADENYLATE MONOPHOSPHATE KINASE;
COMPND 7 EC: 2.7.4.3;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: ADK, B4417_1526, SC09_CONTIG26ORF00083;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHOTRANSFERASE ACTIVITY, ATP BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MOON,E.BAE
REVDAT 3 22-NOV-23 5X6I 1 LINK
REVDAT 2 11-SEP-19 5X6I 1 JRNL
REVDAT 1 28-FEB-18 5X6I 0
JRNL AUTH S.MOON,J.KIM,J.KOO,E.BAE
JRNL TITL STRUCTURAL AND MUTATIONAL ANALYSES OF PSYCHROPHILIC AND
JRNL TITL 2 MESOPHILIC ADENYLATE KINASES HIGHLIGHT THE ROLE OF
JRNL TITL 3 HYDROPHOBIC INTERACTIONS IN PROTEIN THERMAL STABILITY.
JRNL REF STRUCT DYN. V. 6 24702 2019
JRNL REFN ESSN 2329-7778
JRNL PMID 31111079
JRNL DOI 10.1063/1.5089707
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 12993
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 679
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) : 874
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2640
REMARK 3 BIN FREE R VALUE SET COUNT : 42
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1654
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 61
REMARK 3 SOLVENT ATOMS : 104
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.94000
REMARK 3 B22 (A**2) : -2.20000
REMARK 3 B33 (A**2) : 1.26000
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): 0.206
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.197
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.161
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.097
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
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): 1741 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1627 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2364 ; 1.874 ; 2.036
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3770 ; 0.890 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 211 ; 6.195 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 81 ;37.976 ;25.556
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 307 ;14.280 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;12.364 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 260 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1928 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 352 ; 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): 847 ; 2.719 ; 3.318
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 846 ; 2.716 ; 3.317
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1057 ; 3.899 ; 4.957
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1058 ; 3.898 ; 4.958
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 894 ; 3.615 ; 3.725
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 895 ; 3.613 ; 3.724
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1308 ; 5.560 ; 5.409
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1998 ; 7.584 ;26.958
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1969 ; 7.574 ;26.769
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 30
REMARK 3 RESIDUE RANGE : A 61 A 126
REMARK 3 RESIDUE RANGE : A 165 A 212
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8833 -3.1452 -11.2145
REMARK 3 T TENSOR
REMARK 3 T11: 0.0581 T22: 0.0555
REMARK 3 T33: 0.0677 T12: 0.0248
REMARK 3 T13: 0.0540 T23: 0.0348
REMARK 3 L TENSOR
REMARK 3 L11: 0.2117 L22: 1.1140
REMARK 3 L33: 0.9902 L12: -0.0252
REMARK 3 L13: -0.2737 L23: -0.1586
REMARK 3 S TENSOR
REMARK 3 S11: -0.1033 S12: -0.0125 S13: -0.0776
REMARK 3 S21: 0.1173 S22: 0.1657 S23: 0.0906
REMARK 3 S31: 0.0601 S32: -0.0908 S33: -0.0623
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 31 A 60
REMARK 3 ORIGIN FOR THE GROUP (A): 14.2141 13.3943 -11.7868
REMARK 3 T TENSOR
REMARK 3 T11: 0.1338 T22: 0.0129
REMARK 3 T33: 0.0475 T12: 0.0089
REMARK 3 T13: 0.0058 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 0.8542 L22: 2.0721
REMARK 3 L33: 0.9048 L12: -0.0566
REMARK 3 L13: -0.5747 L23: -0.6491
REMARK 3 S TENSOR
REMARK 3 S11: 0.0521 S12: 0.0117 S13: 0.1353
REMARK 3 S21: 0.1866 S22: 0.0253 S23: 0.0436
REMARK 3 S31: -0.1092 S32: -0.0432 S33: -0.0774
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 127 A 164
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8176 1.3799 -27.6026
REMARK 3 T TENSOR
REMARK 3 T11: 0.0432 T22: 0.1553
REMARK 3 T33: 0.0940 T12: -0.0551
REMARK 3 T13: -0.0304 T23: -0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 0.2908 L22: 1.3726
REMARK 3 L33: 3.3186 L12: 0.3592
REMARK 3 L13: -0.9481 L23: -1.5586
REMARK 3 S TENSOR
REMARK 3 S11: -0.0589 S12: -0.0301 S13: 0.1037
REMARK 3 S21: -0.1863 S22: 0.3117 S23: 0.0467
REMARK 3 S31: 0.2010 S32: -0.0135 S33: -0.2527
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 303 A 303
REMARK 3 ORIGIN FOR THE GROUP (A): 15.1715 -0.4892 -15.2607
REMARK 3 T TENSOR
REMARK 3 T11: 0.0378 T22: 0.0633
REMARK 3 T33: 0.1065 T12: 0.0129
REMARK 3 T13: 0.0120 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.3266 L22: 2.1823
REMARK 3 L33: 3.5159 L12: -0.5684
REMARK 3 L13: -1.0558 L23: 1.6424
REMARK 3 S TENSOR
REMARK 3 S11: 0.0227 S12: -0.0195 S13: -0.0365
REMARK 3 S21: -0.0566 S22: -0.0574 S23: 0.0452
REMARK 3 S31: -0.1377 S32: 0.0612 S33: 0.0347
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 5X6I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1300002702.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-1A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.96400
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13718
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.0800
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) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.58000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 1P3J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40MM CHLORIDE, 36% POLYETHYLENE GLYCOL
REMARK 280 1500, 50MM CHES PH 9.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 21.86950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.29750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.09000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.29750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.86950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 22.09000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
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 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 213
REMARK 465 GLY A 214
REMARK 465 LEU A 215
REMARK 465 LYS A 216
REMARK 465 LYS A 217
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 A 19 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 88 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 88 NE - CZ - NH2 ANGL. DEV. = -4.1 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 LYS A 105 78.97 -153.48
REMARK 500 ASN A 142 71.12 -160.78
REMARK 500 ASP A 163 31.78 -89.64
REMARK 500 GLN A 198 64.69 -100.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 41 O
REMARK 620 2 GLN A 199 OE1 37.2
REMARK 620 3 HOH A 404 O 80.2 97.8
REMARK 620 4 HOH A 428 O 156.1 124.1 122.7
REMARK 620 5 HOH A 456 O 81.2 70.3 160.4 76.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 116 OD1
REMARK 620 2 ASP A 118 OD2 115.5
REMARK 620 3 GLU A 188 OE1 65.2 140.1
REMARK 620 4 GLU A 188 OE2 63.9 139.0 1.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 130 SG
REMARK 620 2 CYS A 133 SG 109.6
REMARK 620 3 CYS A 150 SG 105.0 115.2
REMARK 620 4 ASP A 153 OD2 107.6 100.1 119.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AP5 A 303 O2B
REMARK 620 2 AP5 A 303 O2G 79.3
REMARK 620 3 HOH A 437 O 103.5 168.5
REMARK 620 4 HOH A 440 O 79.5 95.1 96.4
REMARK 620 5 HOH A 445 O 153.7 82.5 90.9 121.1
REMARK 620 6 HOH A 474 O 80.6 83.8 85.6 160.0 78.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AP5 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5X6J RELATED DB: PDB
REMARK 900 RELATED ID: 5X6K RELATED DB: PDB
REMARK 900 RELATED ID: 5X6L RELATED DB: PDB
DBREF1 5X6I A 1 217 UNP A0A063X902_BACIU
DBREF2 5X6I A A0A063X902 1 217
SEQADV 5X6I THR A 26 UNP A0A063X90 ILE 26 ENGINEERED MUTATION
SEQRES 1 A 217 MET ASN LEU VAL LEU MET GLY LEU PRO GLY ALA GLY LYS
SEQRES 2 A 217 GLY THR GLN GLY GLU ARG ILE VAL GLU ASP TYR GLY THR
SEQRES 3 A 217 PRO HIS ILE SER THR GLY ASP MET PHE ARG ALA ALA MET
SEQRES 4 A 217 LYS GLU GLU THR PRO LEU GLY LEU GLU ALA LYS SER TYR
SEQRES 5 A 217 ILE ASP LYS GLY GLU LEU VAL PRO ASP GLU VAL THR ILE
SEQRES 6 A 217 GLY ILE VAL LYS GLU ARG LEU GLY LYS ASP ASP CYS GLU
SEQRES 7 A 217 ARG GLY PHE LEU LEU ASP GLY PHE PRO ARG THR VAL ALA
SEQRES 8 A 217 GLN ALA GLU ALA LEU GLU GLU ILE LEU GLU GLU TYR GLY
SEQRES 9 A 217 LYS PRO ILE ASP TYR VAL ILE ASN ILE GLU VAL ASP LYS
SEQRES 10 A 217 ASP VAL LEU MET GLU ARG LEU THR GLY ARG ARG ILE CYS
SEQRES 11 A 217 SER VAL CYS GLY THR THR TYR HIS LEU VAL PHE ASN PRO
SEQRES 12 A 217 PRO LYS THR PRO GLY ILE CYS ASP LYS ASP GLY GLY GLU
SEQRES 13 A 217 LEU TYR GLN ARG ALA ASP ASP ASN GLU GLU THR VAL SER
SEQRES 14 A 217 LYS ARG LEU GLU VAL ASN MET LYS GLN THR GLN PRO LEU
SEQRES 15 A 217 LEU ASP PHE TYR SER GLU LYS GLY TYR LEU ALA ASN VAL
SEQRES 16 A 217 ASN GLY GLN GLN ASP ILE GLN ASP VAL TYR ALA ASP VAL
SEQRES 17 A 217 LYS ASP LEU LEU GLY GLY LEU LYS LYS
HET ZN A 301 1
HET MG A 302 1
HET AP5 A 303 57
HET CA A 304 1
HET CA A 305 1
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM AP5 BIS(ADENOSINE)-5'-PENTAPHOSPHATE
HETNAM CA CALCIUM ION
FORMUL 2 ZN ZN 2+
FORMUL 3 MG MG 2+
FORMUL 4 AP5 C20 H29 N10 O22 P5
FORMUL 5 CA 2(CA 2+)
FORMUL 7 HOH *104(H2 O)
HELIX 1 AA1 GLY A 12 GLY A 25 1 14
HELIX 2 AA2 THR A 31 GLU A 42 1 12
HELIX 3 AA3 THR A 43 GLY A 56 1 14
HELIX 4 AA4 PRO A 60 LYS A 74 1 15
HELIX 5 AA5 ASP A 75 GLU A 78 5 4
HELIX 6 AA6 THR A 89 TYR A 103 1 15
HELIX 7 AA7 ASP A 116 ASP A 118 5 3
HELIX 8 AA8 VAL A 119 GLY A 126 1 8
HELIX 9 AA9 ASN A 164 LYS A 189 1 26
HELIX 10 AB1 ASP A 200 LEU A 212 1 13
SHEET 1 AA1 5 HIS A 28 SER A 30 0
SHEET 2 AA1 5 PHE A 81 ASP A 84 1 O LEU A 82 N ILE A 29
SHEET 3 AA1 5 ASN A 2 MET A 6 1 N LEU A 5 O LEU A 83
SHEET 4 AA1 5 TYR A 109 GLU A 114 1 O ILE A 111 N VAL A 4
SHEET 5 AA1 5 LEU A 192 ASN A 196 1 O VAL A 195 N ASN A 112
SHEET 1 AA2 3 THR A 136 HIS A 138 0
SHEET 2 AA2 3 ARG A 127 CYS A 130 -1 N ARG A 128 O TYR A 137
SHEET 3 AA2 3 LEU A 157 TYR A 158 -1 O TYR A 158 N ILE A 129
LINK O GLU A 41 CA CA A 304 1555 1555 2.26
LINK OD1 ASP A 116 CA CA A 305 1555 1555 2.30
LINK OD2 ASP A 118 CA CA A 305 1555 1555 2.22
LINK SG CYS A 130 ZN ZN A 301 1555 1555 2.45
LINK SG CYS A 133 ZN ZN A 301 1555 1555 2.41
LINK SG CYS A 150 ZN ZN A 301 1555 1555 2.25
LINK OD2 ASP A 153 ZN ZN A 301 1555 1555 2.35
LINK OE1 GLU A 188 CA CA A 305 1555 4445 2.63
LINK OE2 GLU A 188 CA CA A 305 1555 4445 2.69
LINK OE1 GLN A 199 CA CA A 304 1555 1545 2.41
LINK MG MG A 302 O2B AP5 A 303 1555 1555 2.42
LINK MG MG A 302 O2G AP5 A 303 1555 1555 2.31
LINK MG MG A 302 O HOH A 437 1555 1555 2.13
LINK MG MG A 302 O HOH A 440 1555 1555 2.31
LINK MG MG A 302 O HOH A 445 1555 1555 2.24
LINK MG MG A 302 O HOH A 474 1555 1555 2.12
LINK CA CA A 304 O HOH A 404 1555 1565 2.36
LINK CA CA A 304 O HOH A 428 1555 1565 2.51
LINK CA CA A 304 O HOH A 456 1555 1555 2.04
CISPEP 1 PHE A 86 PRO A 87 0 -3.22
SITE 1 AC1 4 CYS A 130 CYS A 133 CYS A 150 ASP A 153
SITE 1 AC2 5 AP5 A 303 HOH A 437 HOH A 440 HOH A 445
SITE 2 AC2 5 HOH A 474
SITE 1 AC3 40 PRO A 9 GLY A 10 ALA A 11 GLY A 12
SITE 2 AC3 40 LYS A 13 GLY A 14 THR A 15 THR A 31
SITE 3 AC3 40 GLY A 32 ARG A 36 ILE A 53 GLU A 57
SITE 4 AC3 40 VAL A 59 THR A 64 GLY A 85 PHE A 86
SITE 5 AC3 40 ARG A 88 GLN A 92 ARG A 123 ARG A 127
SITE 6 AC3 40 THR A 136 TYR A 137 HIS A 138 PHE A 141
SITE 7 AC3 40 ARG A 160 ARG A 171 GLY A 197 GLN A 199
SITE 8 AC3 40 ILE A 201 MG A 302 HOH A 413 HOH A 439
SITE 9 AC3 40 HOH A 440 HOH A 443 HOH A 445 HOH A 446
SITE 10 AC3 40 HOH A 453 HOH A 462 HOH A 471 HOH A 474
SITE 1 AC4 6 GLU A 41 GLN A 199 ASP A 207 HOH A 404
SITE 2 AC4 6 HOH A 428 HOH A 456
SITE 1 AC5 3 ASP A 116 ASP A 118 GLU A 188
CRYST1 43.739 44.180 100.595 90.00 90.00 90.00 P 21 21 21 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 0.022863 0.000000 0.000000 0.00000
SCALE2 0.000000 0.022635 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009941 0.00000
(ATOM LINES ARE NOT SHOWN.)
END