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HEADER HYDROLASE 15-JUN-20 6XFO
TITLE ORTHORHOMBIC CRYSTAL FORM OF STRIGA HERMONTHICA DWARF14 (SHD14)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D14;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;
SOURCE 3 ORGANISM_COMMON: PURPLE WITCHWEED;
SOURCE 4 ORGANISM_TAXID: 68872;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA GAMI2
KEYWDS STRIGOLACTONE RECEPTOR, ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.HAMIAUX,K.C.SNOWDEN
REVDAT 1 24-JUN-20 6XFO 0
JRNL AUTH C.HAMIAUX,Y.ZHANG,K.C.SNOWDEN,H.J.BOUWMEESTER
JRNL TITL TO BE PUBLISHED
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
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) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 68492
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3564
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) : 1.58
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5005
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 270
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4104
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 434
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.34000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : 0.73000
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): 0.085
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.779
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4230 ; 0.017 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4010 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5761 ; 2.074 ; 1.631
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9217 ; 1.607 ; 1.570
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 540 ; 6.465 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 228 ;27.222 ;20.088
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 676 ;12.509 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;15.549 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 540 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4809 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 966 ; 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 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 2
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 2 A 266
REMARK 3 ORIGIN FOR THE GROUP (A): 30.3780 26.8200 101.4160
REMARK 3 T TENSOR
REMARK 3 T11: 0.0432 T22: 0.0101
REMARK 3 T33: 0.0668 T12: 0.0048
REMARK 3 T13: -0.0381 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 2.0095 L22: 2.4325
REMARK 3 L33: 0.5993 L12: -0.9819
REMARK 3 L13: -0.1387 L23: -0.1580
REMARK 3 S TENSOR
REMARK 3 S11: 0.1381 S12: -0.0526 S13: -0.0691
REMARK 3 S21: -0.1541 S22: -0.0957 S23: 0.1418
REMARK 3 S31: 0.0448 S32: 0.0429 S33: -0.0424
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 3 B 266
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5260 26.0870 58.3080
REMARK 3 T TENSOR
REMARK 3 T11: 0.0219 T22: 0.0106
REMARK 3 T33: 0.0828 T12: 0.0067
REMARK 3 T13: -0.0040 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.9249 L22: 4.1254
REMARK 3 L33: 1.0538 L12: -1.1888
REMARK 3 L13: -0.2176 L23: -0.4696
REMARK 3 S TENSOR
REMARK 3 S11: 0.0489 S12: -0.0751 S13: 0.1562
REMARK 3 S21: 0.0059 S22: -0.0431 S23: -0.4191
REMARK 3 S31: -0.0080 S32: 0.0466 S33: -0.0059
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
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 6XFO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-20.
REMARK 100 THE DEPOSITION ID IS D_1000249998.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.6
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72148
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 46.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.20
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 21.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.20
REMARK 200 R MERGE FOR SHELL (I) : 1.03900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.6
REMARK 200 STARTING MODEL: 4DNP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS/ACETATE PH 8.5, 0.2 M
REMARK 280 MGCL2, 20% PEG 8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 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 36.11500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.31000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.66500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.31000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.11500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.66500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 VAL A 2
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 O HOH A 401 O HOH A 439 2.00
REMARK 500 O HOH A 401 O HOH A 437 2.04
REMARK 500 O HOH A 419 O HOH A 554 2.05
REMARK 500 O GLY B 233 O ACT B 301 2.06
REMARK 500 OH TYR B 40 OD1 ASN B 254 2.08
REMARK 500 O HOH A 618 O HOH A 625 2.13
REMARK 500 OH TYR A 40 OD1 ASN A 254 2.13
REMARK 500 O GLY B 233 C ACT B 301 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD2 ASP B 61 O ACT B 301 3656 2.07
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 ASP A 61 CG ASP A 61 OD2 -0.146
REMARK 500 HIS A 95 CE1 HIS A 95 NE2 -0.076
REMARK 500 MET A 192 CB MET A 192 CG 0.311
REMARK 500 GLU B 169 CD GLU B 169 OE1 0.067
REMARK 500 HIS B 246 CE1 HIS B 246 NE2 -0.068
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 ARG A 43 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 PHE A 74 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 108 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 176 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 12 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 176 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG B 235 CG - CD - NE ANGL. DEV. = -18.9 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 68 59.10 -92.83
REMARK 500 SER A 96 -118.00 54.29
REMARK 500 LYS A 129 107.30 -49.68
REMARK 500 ASN A 150 80.84 -166.16
REMARK 500 ASP A 242 42.03 -97.35
REMARK 500 PRO A 265 -168.94 -75.45
REMARK 500 ASP B 44 18.34 -144.45
REMARK 500 SER B 96 -113.31 50.39
REMARK 500 ARG B 124 129.22 -172.14
REMARK 500 LYS B 129 109.85 -37.60
REMARK 500 ASN B 150 79.55 -161.22
REMARK 500 ASP B 242 43.74 -96.16
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 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 233 O
REMARK 620 2 HOH A 407 O 74.1
REMARK 620 3 HOH A 459 O 83.0 88.2
REMARK 620 4 HOH A 545 O 101.4 174.5 94.5
REMARK 620 5 ASP A 61 OD2 41.5 115.6 82.7 60.2
REMARK 620 6 HOH A 442 O 168.8 94.7 95.7 89.8 149.5
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 MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 301
DBREF1 6XFO A 1 266 UNP A0A2U8XQ45_STRHE
DBREF2 6XFO A A0A2U8XQ45 1 266
DBREF1 6XFO B 1 266 UNP A0A2U8XQ45_STRHE
DBREF2 6XFO B A0A2U8XQ45 1 266
SEQRES 1 A 266 MET VAL GLN SER LEU LEU GLU ALA LEU ASN VAL ARG VAL
SEQRES 2 A 266 VAL GLY SER GLY GLU LYS VAL LEU VAL LEU ALA HIS GLY
SEQRES 3 A 266 VAL GLY THR ASP GLN SER ALA TRP GLN ARG ILE LEU PRO
SEQRES 4 A 266 TYR PHE VAL ARG ASP HIS ARG VAL VAL LEU TYR ASP LEU
SEQRES 5 A 266 VAL CYS ALA GLY SER VAL ASN PRO ASP TYR PHE ASP PHE
SEQRES 6 A 266 ARG ARG TYR THR SER LEU ASP ALA PHE VAL ASP ASP LEU
SEQRES 7 A 266 LEU ALA ILE LEU ASP ALA LEU ARG LEU GLY ARG CYS THR
SEQRES 8 A 266 TYR VAL GLY HIS SER VAL SER ALA SER ILE GLY ILE LEU
SEQRES 9 A 266 ALA SER ILE ARG ARG PRO ASP LEU PHE ALA LYS LEU ILE
SEQRES 10 A 266 LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP LYS ASN
SEQRES 11 A 266 TYR HIS GLY GLY PHE ALA ASP GLY GLU ILE ASP THR VAL
SEQRES 12 A 266 PHE ALA ALA MET GLU ALA ASN TYR ALA ALA TRP VAL SER
SEQRES 13 A 266 GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO GLU
SEQRES 14 A 266 ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES 15 A 266 PRO ASP ILE THR LEU PHE VAL SER ARG MET VAL PHE ASN
SEQRES 16 A 266 SER ASP LEU ARG GLY VAL LEU GLY LEU VAL THR VAL PRO
SEQRES 17 A 266 CYS SER VAL LEU GLN THR SER LYS ASP HIS SER VAL PRO
SEQRES 18 A 266 GLU SER MET ALA ALA TYR LEU LYS GLU ASN LEU GLY GLY
SEQRES 19 A 266 ARG THR THR VAL HIS MET LEU ASP ILE GLU GLY HIS LEU
SEQRES 20 A 266 PRO HIS LEU SER ALA PRO ASN LEU LEU ALA GLN GLU LEU
SEQRES 21 A 266 ARG ARG ALA LEU PRO ARG
SEQRES 1 B 266 MET VAL GLN SER LEU LEU GLU ALA LEU ASN VAL ARG VAL
SEQRES 2 B 266 VAL GLY SER GLY GLU LYS VAL LEU VAL LEU ALA HIS GLY
SEQRES 3 B 266 VAL GLY THR ASP GLN SER ALA TRP GLN ARG ILE LEU PRO
SEQRES 4 B 266 TYR PHE VAL ARG ASP HIS ARG VAL VAL LEU TYR ASP LEU
SEQRES 5 B 266 VAL CYS ALA GLY SER VAL ASN PRO ASP TYR PHE ASP PHE
SEQRES 6 B 266 ARG ARG TYR THR SER LEU ASP ALA PHE VAL ASP ASP LEU
SEQRES 7 B 266 LEU ALA ILE LEU ASP ALA LEU ARG LEU GLY ARG CYS THR
SEQRES 8 B 266 TYR VAL GLY HIS SER VAL SER ALA SER ILE GLY ILE LEU
SEQRES 9 B 266 ALA SER ILE ARG ARG PRO ASP LEU PHE ALA LYS LEU ILE
SEQRES 10 B 266 LEU ILE GLY ALA SER PRO ARG PHE LEU ASN ASP LYS ASN
SEQRES 11 B 266 TYR HIS GLY GLY PHE ALA ASP GLY GLU ILE ASP THR VAL
SEQRES 12 B 266 PHE ALA ALA MET GLU ALA ASN TYR ALA ALA TRP VAL SER
SEQRES 13 B 266 GLY PHE ALA PRO LEU ALA VAL GLY ALA ASP VAL PRO GLU
SEQRES 14 B 266 ALA VAL ARG GLU PHE SER ARG THR LEU PHE ASN MET ARG
SEQRES 15 B 266 PRO ASP ILE THR LEU PHE VAL SER ARG MET VAL PHE ASN
SEQRES 16 B 266 SER ASP LEU ARG GLY VAL LEU GLY LEU VAL THR VAL PRO
SEQRES 17 B 266 CYS SER VAL LEU GLN THR SER LYS ASP HIS SER VAL PRO
SEQRES 18 B 266 GLU SER MET ALA ALA TYR LEU LYS GLU ASN LEU GLY GLY
SEQRES 19 B 266 ARG THR THR VAL HIS MET LEU ASP ILE GLU GLY HIS LEU
SEQRES 20 B 266 PRO HIS LEU SER ALA PRO ASN LEU LEU ALA GLN GLU LEU
SEQRES 21 B 266 ARG ARG ALA LEU PRO ARG
HET MG A 301 1
HET ACT B 301 4
HETNAM MG MAGNESIUM ION
HETNAM ACT ACETATE ION
FORMUL 3 MG MG 2+
FORMUL 4 ACT C2 H3 O2 1-
FORMUL 5 HOH *434(H2 O)
HELIX 1 AA1 SER A 4 LEU A 9 1 6
HELIX 2 AA2 ASP A 30 GLN A 35 5 6
HELIX 3 AA3 ILE A 37 PHE A 41 5 5
HELIX 4 AA4 ASN A 59 PHE A 63 5 5
HELIX 5 AA5 SER A 70 ARG A 86 1 17
HELIX 6 AA6 SER A 96 ARG A 109 1 14
HELIX 7 AA7 ILE A 140 ASN A 150 1 11
HELIX 8 AA8 ASN A 150 GLY A 164 1 15
HELIX 9 AA9 VAL A 167 ASN A 180 1 14
HELIX 10 AB1 ARG A 182 ASN A 195 1 14
HELIX 11 AB2 LEU A 198 VAL A 205 5 8
HELIX 12 AB3 SER A 223 LEU A 232 1 10
HELIX 13 AB4 LEU A 247 ALA A 252 1 6
HELIX 14 AB5 ALA A 252 ALA A 263 1 12
HELIX 15 AB6 VAL B 2 LEU B 9 1 8
HELIX 16 AB7 ASP B 30 GLN B 35 5 6
HELIX 17 AB8 ILE B 37 PHE B 41 5 5
HELIX 18 AB9 ASN B 59 PHE B 63 5 5
HELIX 19 AC1 SER B 70 ARG B 86 1 17
HELIX 20 AC2 SER B 96 ARG B 109 1 14
HELIX 21 AC3 ILE B 140 ASN B 150 1 11
HELIX 22 AC4 ASN B 150 GLY B 164 1 15
HELIX 23 AC5 VAL B 167 ASN B 180 1 14
HELIX 24 AC6 ARG B 182 ASN B 195 1 14
HELIX 25 AC7 LEU B 198 VAL B 205 5 8
HELIX 26 AC8 SER B 223 LEU B 232 1 10
HELIX 27 AC9 LEU B 247 ALA B 252 1 6
HELIX 28 AD1 ALA B 252 LEU B 264 1 13
SHEET 1 AA1 7 ARG A 12 VAL A 14 0
SHEET 2 AA1 7 HIS A 45 LEU A 49 -1 O VAL A 47 N VAL A 14
SHEET 3 AA1 7 LYS A 19 ALA A 24 1 N LEU A 21 O VAL A 48
SHEET 4 AA1 7 CYS A 90 HIS A 95 1 O VAL A 93 N VAL A 22
SHEET 5 AA1 7 PHE A 113 ILE A 119 1 O ILE A 117 N TYR A 92
SHEET 6 AA1 7 CYS A 209 SER A 215 1 O SER A 210 N LEU A 118
SHEET 7 AA1 7 THR A 236 GLU A 244 1 O THR A 237 N VAL A 211
SHEET 1 AA2 7 ARG B 12 GLY B 15 0
SHEET 2 AA2 7 HIS B 45 LEU B 49 -1 O VAL B 47 N VAL B 14
SHEET 3 AA2 7 LYS B 19 ALA B 24 1 N LEU B 21 O VAL B 48
SHEET 4 AA2 7 CYS B 90 HIS B 95 1 O VAL B 93 N VAL B 22
SHEET 5 AA2 7 PHE B 113 ILE B 119 1 O ILE B 119 N GLY B 94
SHEET 6 AA2 7 CYS B 209 SER B 215 1 O SER B 210 N LEU B 118
SHEET 7 AA2 7 THR B 236 GLU B 244 1 O THR B 237 N VAL B 211
LINK O GLY A 233 MG MG A 301 1555 1555 2.06
LINK MG MG A 301 O HOH A 407 1555 1555 2.02
LINK MG MG A 301 O HOH A 459 1555 1555 1.98
LINK MG MG A 301 O HOH A 545 1555 1555 1.73
LINK OD2 ASP A 61 MG MG A 301 1555 3657 2.22
LINK MG MG A 301 O HOH A 442 1555 3647 2.18
SITE 1 AC1 6 ASP A 61 GLY A 233 HOH A 407 HOH A 442
SITE 2 AC1 6 HOH A 459 HOH A 545
SITE 1 AC2 4 ASP B 61 GLY B 233 HOH B 468 HOH B 495
CRYST1 72.230 83.330 86.620 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013845 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011545 0.00000
TER 2061 ARG A 266
TER 4135 ARG B 266
MASTER 424 0 2 28 14 0 3 6 4543 2 9 42
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