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HEADER HYDROLASE 02-MAR-16 5FXM
TITLE STRUCTURE OF FAE SOLVED BY SAD FROM DATA COLLECTED BY DIRECT DATA
TITLE 2 COLLECTION (DDC) USING THE ESRF ROBODIFF GONIOMETER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE Y;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 792-1077;
COMPND 5 SYNONYM: XYLANASE Y, 1,4-BETA-D-XYLAN XYLANOHYDROLASE Y, XYLY,
COMPND 6 FERULIC ACID ESTERASE;
COMPND 7 EC: 3.1.1.73;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RUMINICLOSTRIDIUM THERMOCELLUM;
SOURCE 3 ORGANISM_TAXID: 1515;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.W.BOWLER,D.NURIZZO
REVDAT 3 23-AUG-17 5FXM 1 REMARK
REVDAT 2 17-AUG-16 5FXM 1 JRNL
REVDAT 1 16-MAR-16 5FXM 0
JRNL AUTH D.NURIZZO,M.W.BOWLER,H.CASEROTTO,F.DOBIAS,T.GIRAUD,J.SURR,
JRNL AUTH 2 N.GUICHARD,G.PAPP,M.GUIJARRO,C.MUELLER-DIECKMANN,D.FLOT,
JRNL AUTH 3 S.MCSWEENEY,F.CIPRIANI,P.THEVENEAU,G.A.LEONARD
JRNL TITL ROBODIFF: COMBINING A SAMPLE CHANGER AND GONIOMETER FOR
JRNL TITL 2 HIGHLY AUTOMATED MACROMOLECULAR CRYSTALLOGRAPHY EXPERIMENTS.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 72 966 2016
JRNL REFN ISSN 0907-4449
JRNL PMID 27487827
JRNL DOI 10.1107/S205979831601158X
REMARK 2
REMARK 2 RESOLUTION. 1.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 79.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 27216
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1531
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) : 1807
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.05
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 106
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2290
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 50
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.01
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.05000
REMARK 3 B22 (A**2) : 1.05000
REMARK 3 B33 (A**2) : -2.10000
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): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.862
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2401 ; 0.015 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2127 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3264 ; 1.723 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4897 ; 1.661 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 282 ; 5.894 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 128 ;37.131 ;23.906
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 334 ;14.008 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;18.375 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 322 ; 0.174 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2781 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 634 ; 0.002 ; 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): 1131 ; 1.454 ; 2.513
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1130 ; 1.452 ; 2.512
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1412 ; 2.203 ; 3.761
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1270 ; 1.903 ; 2.759
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 : 1
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 803 A 3090
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0821 24.0285 17.6578
REMARK 3 T TENSOR
REMARK 3 T11: 0.0490 T22: 0.0304
REMARK 3 T33: 0.0375 T12: -0.0054
REMARK 3 T13: -0.0340 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 1.5025 L22: 1.3456
REMARK 3 L33: 2.4613 L12: -0.5212
REMARK 3 L13: 0.1432 L23: -0.4440
REMARK 3 S TENSOR
REMARK 3 S11: 0.0513 S12: 0.0023 S13: 0.0411
REMARK 3 S21: -0.0152 S22: -0.0781 S23: -0.0230
REMARK 3 S31: 0.1155 S32: 0.1121 S33: 0.0268
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
REMARK 3 ION PROBE RADIUS : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 5FXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1290066322.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-16
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 : ESRF
REMARK 200 BEAMLINE : MASSIF-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.966
REMARK 200 MONOCHROMATOR : C110
REMARK 200 OPTICS : BE CRL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32088
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
REMARK 200 RESOLUTION RANGE LOW (A) : 49.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 24.50
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.8
REMARK 200 DATA REDUNDANCY IN SHELL : 22.40
REMARK 200 R MERGE FOR SHELL (I) : 0.64000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXDE
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 33.01550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 55.98700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 55.98700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 16.50775
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 55.98700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 55.98700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 49.52325
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 55.98700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.98700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 16.50775
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 55.98700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.98700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 49.52325
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 33.01550
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.4 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 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 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 MSE A 789
REMARK 465 ALA A 790
REMARK 465 SER A 791
REMARK 465 ASP A 792
REMARK 465 LYS A 793
REMARK 465 PHE A 794
REMARK 465 PRO A 795
REMARK 465 VAL A 796
REMARK 465 ALA A 797
REMARK 465 GLU A 798
REMARK 465 ASN A 799
REMARK 465 PRO A 800
REMARK 465 SER A 801
REMARK 465 SER A 802
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 O HOH A 2032 O HOH A 2032 7556 1.96
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 VAL A 965 CG1 - CB - CG2 ANGL. DEV. = 10.4 DEGREES
REMARK 500 ASP A 980 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ILE A1019 CG1 - CB - CG2 ANGL. DEV. = 16.1 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 TYR A 851 120.81 -34.58
REMARK 500 VAL A 878 -50.28 -128.48
REMARK 500 SEP A 954 -113.04 57.51
REMARK 500 ASN A1047 17.57 -149.90
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 CD A3086 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A1017 OE1
REMARK 620 2 GLU A1017 OE2 52.1
REMARK 620 3 HOH A2027 O 121.7 70.0
REMARK 620 4 CYS A 823 SG 108.3 155.0 129.2
REMARK 620 5 HIS A 886 ND1 86.8 95.4 92.6 99.0
REMARK 620 6 MSE A 889 SE 100.5 89.5 84.1 78.3 172.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A3087 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A1085 NE2
REMARK 620 2 GLU A 894 OE2 91.1
REMARK 620 3 GLU A1079 OE1 136.3 131.9
REMARK 620 4 HIS A1083 ND1 95.1 84.6 83.5
REMARK 620 5 GLU A 894 OE1 140.4 49.5 83.3 86.6
REMARK 620 6 GLU A1079 OE2 83.6 166.0 52.8 82.9 135.7
REMARK 620 7 HIS A1076 ND1 86.3 91.7 98.0 176.1 89.9 100.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A3088 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A1007 OE1
REMARK 620 2 HIS A1084 NE2 95.1
REMARK 620 3 HOH A2050 O 94.2 94.6
REMARK 620 4 HOH A2049 O 89.2 148.8 54.2
REMARK 620 5 GLU A1007 OE2 54.3 115.7 136.1 91.8
REMARK 620 6 HIS A1082 NE2 140.0 108.8 114.6 86.4 86.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A3089 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2038 O
REMARK 620 2 HOH A2036 O 72.6
REMARK 620 3 HOH A2035 O 135.3 63.1
REMARK 620 4 HIS A 947 NE2 87.8 108.8 100.5
REMARK 620 5 HIS A1080 NE2 100.4 157.4 122.8 92.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 3086
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 3087
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 3088
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 3089
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 3090
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FXL RELATED DB: PDB
REMARK 900 STRUCTURE OF TRYPSIN SOLVED BY MR FROM DATA COLLECTED BY DIRECT
REMARK 900 DATA COLLECTION (DDC) USING THE ESRF ROBODIFF GONIOMETER
REMARK 900 RELATED ID: 5FXN RELATED DB: PDB
REMARK 900 STRUCTURE OF THERMOLYSIN SOLVED BY SAD FROM DATA COLLECTED BY
REMARK 900 DIRECT DATA COLLECTION (DDC) USING THE ESRF ROBODIFF GONIOMETER
DBREF 5FXM A 792 1077 UNP P51584 XYNY_CLOTM 792 1077
SEQADV 5FXM MSE A 789 UNP P51584 EXPRESSION TAG
SEQADV 5FXM ALA A 790 UNP P51584 EXPRESSION TAG
SEQADV 5FXM SER A 791 UNP P51584 EXPRESSION TAG
SEQADV 5FXM LEU A 1078 UNP P51584 EXPRESSION TAG
SEQADV 5FXM GLU A 1079 UNP P51584 EXPRESSION TAG
SEQADV 5FXM HIS A 1080 UNP P51584 EXPRESSION TAG
SEQADV 5FXM HIS A 1081 UNP P51584 EXPRESSION TAG
SEQADV 5FXM HIS A 1082 UNP P51584 EXPRESSION TAG
SEQADV 5FXM HIS A 1083 UNP P51584 EXPRESSION TAG
SEQADV 5FXM HIS A 1084 UNP P51584 EXPRESSION TAG
SEQADV 5FXM HIS A 1085 UNP P51584 EXPRESSION TAG
SEQADV 5FXM GLU A 1017 UNP P51584 ASP 1017 CONFLICT
SEQADV 5FXM ASP A 1018 UNP P51584 HIS 1018 CONFLICT
SEQRES 1 A 297 MSE ALA SER ASP LYS PHE PRO VAL ALA GLU ASN PRO SER
SEQRES 2 A 297 SER SER PHE LYS TYR GLU SER ALA VAL GLN TYR ARG PRO
SEQRES 3 A 297 ALA PRO ASP SER TYR LEU ASN PRO CYS PRO GLN ALA GLY
SEQRES 4 A 297 ARG ILE VAL LYS GLU THR TYR THR GLY ILE ASN GLY THR
SEQRES 5 A 297 LYS SER LEU ASN VAL TYR LEU PRO TYR GLY TYR ASP PRO
SEQRES 6 A 297 ASN LYS LYS TYR ASN ILE PHE TYR LEU MSE HIS GLY GLY
SEQRES 7 A 297 GLY GLU ASN GLU ASN THR ILE PHE SER ASN ASP VAL LYS
SEQRES 8 A 297 LEU GLN ASN ILE LEU ASP HIS ALA ILE MSE ASN GLY GLU
SEQRES 9 A 297 LEU GLU PRO LEU ILE VAL VAL THR PRO THR PHE ASN GLY
SEQRES 10 A 297 GLY ASN CYS THR ALA GLN ASN PHE TYR GLN GLU PHE ARG
SEQRES 11 A 297 GLN ASN VAL ILE PRO PHE VAL GLU SER LYS TYR SER THR
SEQRES 12 A 297 TYR ALA GLU SER THR THR PRO GLN GLY ILE ALA ALA SER
SEQRES 13 A 297 ARG MSE HIS ARG GLY PHE GLY GLY PHE SEP MSE GLY GLY
SEQRES 14 A 297 LEU THR THR TRP TYR VAL MSE VAL ASN CYS LEU ASP TYR
SEQRES 15 A 297 VAL ALA TYR PHE MSE PRO LEU SER GLY ASP TYR TRP TYR
SEQRES 16 A 297 GLY ASN SER PRO GLN ASP LYS ALA ASN SER ILE ALA GLU
SEQRES 17 A 297 ALA ILE ASN ARG SER GLY LEU SER LYS ARG GLU TYR PHE
SEQRES 18 A 297 VAL PHE ALA ALA THR GLY SER GLU ASP ILE ALA TYR ALA
SEQRES 19 A 297 ASN MSE ASN PRO GLN ILE GLU ALA MSE LYS ALA LEU PRO
SEQRES 20 A 297 HIS PHE ASP TYR THR SER ASP PHE SER LYS GLY ASN PHE
SEQRES 21 A 297 TYR PHE LEU VAL ALA PRO GLY ALA THR HIS TRP TRP GLY
SEQRES 22 A 297 TYR VAL ARG HIS TYR ILE TYR ASP ALA LEU PRO TYR PHE
SEQRES 23 A 297 PHE HIS GLU LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 5FXM MSE A 863 MET SELENOMETHIONINE
MODRES 5FXM MSE A 889 MET SELENOMETHIONINE
MODRES 5FXM MSE A 946 MET SELENOMETHIONINE
MODRES 5FXM SEP A 954 SER PHOSPHOSERINE
MODRES 5FXM MSE A 955 MET SELENOMETHIONINE
MODRES 5FXM MSE A 964 MET SELENOMETHIONINE
MODRES 5FXM MSE A 975 MET SELENOMETHIONINE
MODRES 5FXM MSE A 1024 MET SELENOMETHIONINE
MODRES 5FXM MSE A 1031 MET SELENOMETHIONINE
HET MSE A 863 8
HET MSE A 889 8
HET MSE A 946 8
HET SEP A 954 10
HET MSE A 955 11
HET MSE A 964 8
HET MSE A 975 8
HET MSE A1024 8
HET MSE A1031 8
HET CD A3086 1
HET CD A3087 1
HET CD A3088 1
HET CD A3089 1
HET CD A3090 1
HETNAM MSE SELENOMETHIONINE
HETNAM SEP PHOSPHOSERINE
HETNAM CD CADMIUM ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 CD 5(CD 2+)
FORMUL 7 HOH *50(H2 O)
HELIX 1 1 PRO A 816 ASN A 821 5 6
HELIX 2 2 LYS A 879 ASN A 890 1 12
HELIX 3 3 ASN A 912 ASN A 920 1 9
HELIX 4 4 ASN A 920 TYR A 929 1 10
HELIX 5 5 THR A 937 SER A 944 1 8
HELIX 6 6 SEP A 954 LEU A 968 1 15
HELIX 7 7 SER A 986 GLY A 1002 1 17
HELIX 8 8 ALA A 1020 LEU A 1034 1 15
HELIX 9 9 TRP A 1059 LEU A 1071 1 13
HELIX 10 10 PRO A 1072 PHE A 1074 5 3
SHEET 1 AA 8 ARG A 828 GLY A 836 0
SHEET 2 AA 8 GLY A 839 LEU A 847 -1 O GLY A 839 N GLY A 836
SHEET 3 AA 8 ILE A 897 THR A 900 -1 O VAL A 898 N TYR A 846
SHEET 4 AA 8 ILE A 859 MSE A 863 1 O PHE A 860 N VAL A 899
SHEET 5 AA 8 ARG A 948 PHE A 953 1 O GLY A 949 N TYR A 861
SHEET 6 AA 8 TYR A 973 LEU A 977 1 O TYR A 973 N PHE A 950
SHEET 7 AA 8 PHE A1009 GLY A1015 1 O PHE A1009 N PHE A 974
SHEET 8 AA 8 PHE A1048 ALA A1053 1 O TYR A1049 N ALA A1012
LINK C LEU A 862 N MSE A 863 1555 1555 1.34
LINK C MSE A 863 N HIS A 864 1555 1555 1.35
LINK C ILE A 888 N MSE A 889 1555 1555 1.31
LINK C MSE A 889 N ASN A 890 1555 1555 1.33
LINK C ARG A 945 N MSE A 946 1555 1555 1.35
LINK C MSE A 946 N HIS A 947 1555 1555 1.33
LINK C PHE A 953 N SEP A 954 1555 1555 1.32
LINK C SEP A 954 N MSE A 955 1555 1555 1.33
LINK C MSE A 955 N GLY A 956 1555 1555 1.33
LINK C VAL A 963 N MSE A 964 1555 1555 1.32
LINK C MSE A 964 N VAL A 965 1555 1555 1.32
LINK C PHE A 974 N MSE A 975 1555 1555 1.33
LINK C MSE A 975 N PRO A 976 1555 1555 1.33
LINK C ASN A1023 N MSE A1024 1555 1555 1.34
LINK C MSE A1024 N ASN A1025 1555 1555 1.33
LINK C ALA A1030 N MSE A1031 1555 1555 1.34
LINK C MSE A1031 N LYS A1032 1555 1555 1.33
LINK CD CD A3086 OE1 GLU A1017 1555 4454 2.48
LINK CD CD A3086 OE2 GLU A1017 1555 4454 2.50
LINK CD CD A3086 O HOH A2027 1555 1555 2.40
LINK CD CD A3086 SG CYS A 823 1555 1555 2.59
LINK CD CD A3086 ND1 HIS A 886 1555 1555 2.40
LINK CD CD A3086 SE MSE A 889 1555 1555 2.79
LINK CD CD A3087 NE2 HIS A1085 1555 1555 2.37
LINK CD CD A3087 OE2 GLU A 894 1555 1555 2.25
LINK CD CD A3087 OE1 GLU A1079 1555 1555 2.19
LINK CD CD A3087 ND1 HIS A1083 1555 1555 2.46
LINK CD CD A3087 OE1 GLU A 894 1555 1555 2.90
LINK CD CD A3087 OE2 GLU A1079 1555 1555 2.60
LINK CD CD A3087 ND1 HIS A1076 1555 1555 2.51
LINK CD CD A3088 OE1 GLU A1007 1555 1555 2.55
LINK CD CD A3088 NE2 HIS A1084 1555 7555 2.25
LINK CD CD A3088 O HOH A2050 1555 7555 2.45
LINK CD CD A3088 O HOH A2049 1555 7555 2.73
LINK CD CD A3088 OE2 GLU A1007 1555 1555 2.23
LINK CD CD A3088 NE2 HIS A1082 1555 7555 2.43
LINK CD CD A3089 O HOH A2038 1555 1555 1.78
LINK CD CD A3089 O HOH A2036 1555 1555 2.16
LINK CD CD A3089 O HOH A2035 1555 1555 2.74
LINK CD CD A3089 NE2 HIS A 947 1555 1555 2.38
LINK CD CD A3089 NE2 HIS A1080 1555 1555 2.28
LINK CD CD A3090 ND1 HIS A1081 1555 1555 1.84
SITE 1 AC1 5 CYS A 823 HIS A 886 MSE A 889 GLU A1017
SITE 2 AC1 5 HOH A2027
SITE 1 AC2 5 GLU A 894 HIS A1076 GLU A1079 HIS A1083
SITE 2 AC2 5 HIS A1085
SITE 1 AC3 5 GLU A1007 HIS A1082 HIS A1084 HOH A2049
SITE 2 AC3 5 HOH A2050
SITE 1 AC4 5 HIS A 947 HIS A1080 HOH A2035 HOH A2036
SITE 2 AC4 5 HOH A2038
SITE 1 AC5 1 HIS A1081
CRYST1 111.974 111.974 66.031 90.00 90.00 90.00 P 41 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 0.008931 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008931 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015144 0.00000
TER 2323 HIS A1085
MASTER 433 0 14 10 8 0 9 6 2345 1 118 23
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