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HEADER HYDROLASE 07-MAR-14 4PSD
TITLE STRUCTURE OF TRICHODERMA REESEI CUTINASE NATIVE FORM.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOHYDRATE ESTERASE FAMILY 5;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TRICHODERMA REESEI;
SOURCE 3 ORGANISM_TAXID: 431241;
SOURCE 4 STRAIN: QM6A;
SOURCE 5 GENE: TRIREDRAFT_60489;
SOURCE 6 EXPRESSION_SYSTEM: TRICHODERMA REESEI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 51453
KEYWDS ALPHA/BETA HYDROLASE, CUTINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ROUSSEL,S.AMARA,A.NYYSSOLA,E.MATEOS-DIAZ,S.BLANGY,H.KONTKANEN,
AUTHOR 2 A.WESTERHOLM-PARVINEN,F.CARRIERE,C.CAMBILLAU
REVDAT 1 17-SEP-14 4PSD 0
JRNL AUTH A.ROUSSEL,S.AMARA,A.NYYSSOLA,E.MATEOS-DIAZ,S.BLANGY,
JRNL AUTH 2 H.KONTKANEN,A.WESTERHOLM-PARVINEN,F.CARRIERE,C.CAMBILLAU
JRNL TITL A CUTINASE FROM TRICHODERMA REESEI WITH A LID-COVERED ACTIVE
JRNL TITL 2 SITE AND KINETIC PROPERTIES OF TRUE LIPASES DEFINES A NEW
JRNL TITL 3 CLASS OF LIPOLYTIC ENZYMES
JRNL REF J.MOL.BIOL. 2014
JRNL REFN ESSN 1089-8638
REMARK 2
REMARK 2 RESOLUTION. 1.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 66100
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 2845
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.52
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.56
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.08
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3746
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2170
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3545
REMARK 3 BIN R VALUE (WORKING SET) : 0.2156
REMARK 3 BIN FREE R VALUE : 0.2429
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.37
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 201
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1633
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 405
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.44430
REMARK 3 B22 (A**2) : -3.44430
REMARK 3 B33 (A**2) : 6.88860
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.174
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.050
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1672 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2287 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 533 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 41 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 247 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1672 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 225 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2363 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 0.97
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.59
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.91
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|31 - A|45}
REMARK 3 ORIGIN FOR THE GROUP (A): 60.4685 70.3204 23.9754
REMARK 3 T TENSOR
REMARK 3 T11: -0.0004 T22: -0.0042
REMARK 3 T33: 0.0056 T12: -0.0052
REMARK 3 T13: -0.0083 T23: -0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.0004 L22: 0.0566
REMARK 3 L33: 0.0000 L12: 0.0253
REMARK 3 L13: 0.0153 L23: 0.0312
REMARK 3 S TENSOR
REMARK 3 S11: 0.0002 S12: 0.0000 S13: 0.0004
REMARK 3 S21: -0.0005 S22: -0.0002 S23: -0.0012
REMARK 3 S31: -0.0009 S32: 0.0006 S33: -0.0001
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|46 - A|60}
REMARK 3 ORIGIN FOR THE GROUP (A): 45.8748 69.8431 15.6370
REMARK 3 T TENSOR
REMARK 3 T11: -0.0118 T22: 0.0292
REMARK 3 T33: -0.0118 T12: 0.0356
REMARK 3 T13: 0.0033 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.1228 L22: -0.0603
REMARK 3 L33: 0.0205 L12: -0.0860
REMARK 3 L13: 0.0053 L23: -0.0973
REMARK 3 S TENSOR
REMARK 3 S11: 0.0020 S12: -0.0004 S13: 0.0005
REMARK 3 S21: -0.0033 S22: -0.0039 S23: -0.0065
REMARK 3 S31: -0.0027 S32: -0.0042 S33: 0.0020
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|61 - A|78}
REMARK 3 ORIGIN FOR THE GROUP (A): 62.5553 62.7334 13.7061
REMARK 3 T TENSOR
REMARK 3 T11: -0.0156 T22: -0.0048
REMARK 3 T33: 0.0222 T12: 0.0102
REMARK 3 T13: 0.0039 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.3265 L22: 0.0273
REMARK 3 L33: 0.0087 L12: 0.0489
REMARK 3 L13: -0.2006 L23: -0.0808
REMARK 3 S TENSOR
REMARK 3 S11: -0.0021 S12: 0.0051 S13: 0.0060
REMARK 3 S21: -0.0003 S22: -0.0016 S23: -0.0014
REMARK 3 S31: -0.0035 S32: 0.0088 S33: 0.0036
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|79 - A|116}
REMARK 3 ORIGIN FOR THE GROUP (A): 61.5655 53.4572 19.5276
REMARK 3 T TENSOR
REMARK 3 T11: -0.0326 T22: 0.0101
REMARK 3 T33: 0.0122 T12: 0.0410
REMARK 3 T13: 0.0006 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.2357 L22: 0.3726
REMARK 3 L33: 0.3682 L12: 0.1757
REMARK 3 L13: -0.5269 L23: -0.1445
REMARK 3 S TENSOR
REMARK 3 S11: 0.0063 S12: -0.0100 S13: -0.0082
REMARK 3 S21: -0.0042 S22: -0.0157 S23: -0.0140
REMARK 3 S31: -0.0149 S32: 0.0178 S33: 0.0094
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|117 - A|143}
REMARK 3 ORIGIN FOR THE GROUP (A): 47.8233 51.6771 11.4385
REMARK 3 T TENSOR
REMARK 3 T11: -0.0250 T22: 0.0366
REMARK 3 T33: -0.0150 T12: 0.0437
REMARK 3 T13: 0.0034 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: -0.0562 L22: 0.2366
REMARK 3 L33: 0.6331 L12: -0.0197
REMARK 3 L13: 0.0515 L23: -0.0625
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: 0.0047 S13: -0.0037
REMARK 3 S21: -0.0043 S22: 0.0057 S23: -0.0049
REMARK 3 S31: 0.0063 S32: -0.0171 S33: -0.0012
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|144 - A|170}
REMARK 3 ORIGIN FOR THE GROUP (A): 55.2732 43.9503 15.5284
REMARK 3 T TENSOR
REMARK 3 T11: 0.0011 T22: 0.0061
REMARK 3 T33: -0.0094 T12: 0.0536
REMARK 3 T13: 0.0165 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.2088 L22: 0.1734
REMARK 3 L33: 0.5154 L12: -0.0229
REMARK 3 L13: 0.3723 L23: -0.1161
REMARK 3 S TENSOR
REMARK 3 S11: -0.0027 S12: 0.0051 S13: 0.0057
REMARK 3 S21: -0.0087 S22: -0.0033 S23: -0.0021
REMARK 3 S31: 0.0242 S32: -0.0114 S33: 0.0060
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {A|171 - A|206}
REMARK 3 ORIGIN FOR THE GROUP (A): 47.9607 43.2077 22.5145
REMARK 3 T TENSOR
REMARK 3 T11: 0.0078 T22: 0.0126
REMARK 3 T33: -0.0157 T12: 0.0276
REMARK 3 T13: 0.0120 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.0295 L22: 0.1667
REMARK 3 L33: 0.0721 L12: -0.0731
REMARK 3 L13: 0.1165 L23: -0.0831
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: 0.0020 S13: -0.0055
REMARK 3 S21: 0.0002 S22: 0.0024 S23: 0.0045
REMARK 3 S31: 0.0250 S32: -0.0182 S33: 0.0021
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {A|207 - A|236}
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0044 59.7292 27.5240
REMARK 3 T TENSOR
REMARK 3 T11: -0.0180 T22: 0.0351
REMARK 3 T33: -0.0180 T12: 0.0552
REMARK 3 T13: 0.0008 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 0.1536 L22: 0.0724
REMARK 3 L33: 0.5968 L12: -0.1076
REMARK 3 L13: -0.2325 L23: 0.0063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0052 S12: 0.0036 S13: -0.0001
REMARK 3 S21: 0.0049 S22: -0.0001 S23: -0.0096
REMARK 3 S31: -0.0017 S32: -0.0155 S33: 0.0054
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {A|237 - A|252}
REMARK 3 ORIGIN FOR THE GROUP (A): 62.5978 42.0946 29.6818
REMARK 3 T TENSOR
REMARK 3 T11: -0.0173 T22: 0.0229
REMARK 3 T33: -0.0028 T12: 0.0321
REMARK 3 T13: -0.0035 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.0342 L22: 0.0129
REMARK 3 L33: 0.0180 L12: -0.0333
REMARK 3 L13: 0.0583 L23: -0.0381
REMARK 3 S TENSOR
REMARK 3 S11: -0.0010 S12: -0.0021 S13: 0.0019
REMARK 3 S21: 0.0007 S22: -0.0004 S23: -0.0012
REMARK 3 S31: 0.0026 S32: -0.0019 S33: 0.0014
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PSD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085160.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.25
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
REMARK 200 MONOCHROMATOR : CHANNEL CUT ESRF MONOCHROMATOR
REMARK 200 AND A NEW TORODIAL FOCUSING
REMARK 200 MIRROR.
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66100
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.520
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4PSC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 300 NL ENZYME AT 10 MG/ML WITH 100 NL
REMARK 280 PEG8000 (30%), SODIUM ACETATE (200 MM), SODIUM CACODYLATE (0.1 M)
REMARK 280 , PH 6.25, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 9.71500
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 19.43000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 14.57250
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 24.28750
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 4.85750
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 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 MET A 1
REMARK 465 ARG A 2
REMARK 465 SER A 3
REMARK 465 LEU A 4
REMARK 465 ALA A 5
REMARK 465 ILE A 6
REMARK 465 LEU A 7
REMARK 465 THR A 8
REMARK 465 THR A 9
REMARK 465 LEU A 10
REMARK 465 LEU A 11
REMARK 465 ALA A 12
REMARK 465 GLY A 13
REMARK 465 HIS A 14
REMARK 465 ALA A 15
REMARK 465 PHE A 16
REMARK 465 ALA A 17
REMARK 465 TYR A 18
REMARK 465 PRO A 19
REMARK 465 LYS A 20
REMARK 465 PRO A 21
REMARK 465 ALA A 22
REMARK 465 PRO A 23
REMARK 465 GLN A 24
REMARK 465 SER A 25
REMARK 465 VAL A 26
REMARK 465 ASN A 27
REMARK 465 ARG A 28
REMARK 465 ARG A 29
REMARK 465 HIS A 253
REMARK 465 HIS A 254
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 ASP A 30 CG OD1 OD2
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 ASP A 30 O HOH A 558 2.08
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 ASN A 76 47.35 -145.80
REMARK 500 VAL A 100 -54.02 -133.36
REMARK 500 SER A 164 -130.69 58.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 136 22.7 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 548 DISTANCE = 5.03 ANGSTROMS
REMARK 525 HOH A 571 DISTANCE = 7.42 ANGSTROMS
REMARK 525 HOH A 633 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH A 659 DISTANCE = 10.36 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PSC RELATED DB: PDB
REMARK 900 RELATED ID: 4PSE RELATED DB: PDB
DBREF 4PSD A 45 248 UNP G0RH85 G0RH85_HYPJQ 1 204
SEQADV 4PSD MET A 1 UNP G0RH85 INITIATING METHIONINE
SEQADV 4PSD ARG A 2 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD SER A 3 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD LEU A 4 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ALA A 5 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ILE A 6 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD LEU A 7 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD THR A 8 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD THR A 9 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD LEU A 10 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD LEU A 11 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ALA A 12 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD GLY A 13 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD HIS A 14 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ALA A 15 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD PHE A 16 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ALA A 17 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD TYR A 18 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD PRO A 19 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD LYS A 20 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD PRO A 21 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ALA A 22 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD PRO A 23 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD GLN A 24 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD SER A 25 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD VAL A 26 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ASN A 27 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ARG A 28 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ARG A 29 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ASP A 30 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD TRP A 31 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD PRO A 32 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD SER A 33 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ILE A 34 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ASN A 35 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD GLU A 36 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD PHE A 37 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD LEU A 38 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD SER A 39 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD GLU A 40 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD LEU A 41 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD ALA A 42 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD LYS A 43 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD VAL A 44 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD HIS A 249 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD HIS A 250 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD HIS A 251 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD HIS A 252 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD HIS A 253 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSD HIS A 254 UNP G0RH85 EXPRESSION TAG
SEQRES 1 A 254 MET ARG SER LEU ALA ILE LEU THR THR LEU LEU ALA GLY
SEQRES 2 A 254 HIS ALA PHE ALA TYR PRO LYS PRO ALA PRO GLN SER VAL
SEQRES 3 A 254 ASN ARG ARG ASP TRP PRO SER ILE ASN GLU PHE LEU SER
SEQRES 4 A 254 GLU LEU ALA LYS VAL MET PRO ILE GLY ASP THR ILE THR
SEQRES 5 A 254 ALA ALA CYS ASP LEU ILE SER ASP GLY GLU ASP ALA ALA
SEQRES 6 A 254 ALA SER LEU PHE GLY ILE SER GLU THR GLU ASN ASP PRO
SEQRES 7 A 254 CYS GLY ASP VAL THR VAL LEU PHE ALA ARG GLY THR CYS
SEQRES 8 A 254 ASP PRO GLY ASN VAL GLY VAL LEU VAL GLY PRO TRP PHE
SEQRES 9 A 254 PHE ASP SER LEU GLN THR ALA LEU GLY SER ARG THR LEU
SEQRES 10 A 254 GLY VAL LYS GLY VAL PRO TYR PRO ALA SER VAL GLN ASP
SEQRES 11 A 254 PHE LEU SER GLY SER VAL GLN ASN GLY ILE ASN MET ALA
SEQRES 12 A 254 ASN GLN ILE LYS SER VAL LEU GLN SER CYS PRO ASN THR
SEQRES 13 A 254 LYS LEU VAL LEU GLY GLY TYR SER GLN GLY SER MET VAL
SEQRES 14 A 254 VAL HIS ASN ALA ALA SER ASN LEU ASP ALA ALA THR MET
SEQRES 15 A 254 SER LYS ILE SER ALA VAL VAL LEU PHE GLY ASP PRO TYR
SEQRES 16 A 254 TYR GLY LYS PRO VAL ALA ASN PHE ASP ALA ALA LYS THR
SEQRES 17 A 254 LEU VAL VAL CYS HIS ASP GLY ASP ASN ILE CYS GLN GLY
SEQRES 18 A 254 GLY ASP ILE ILE LEU LEU PRO HIS LEU THR TYR ALA GLU
SEQRES 19 A 254 ASP ALA ASP THR ALA ALA ALA PHE VAL VAL PRO LEU VAL
SEQRES 20 A 254 SER HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *405(H2 O)
HELIX 1 1 SER A 33 LYS A 43 1 11
HELIX 2 2 THR A 50 GLY A 70 1 21
HELIX 3 3 VAL A 100 GLY A 113 1 14
HELIX 4 4 SER A 127 GLY A 134 1 8
HELIX 5 5 SER A 135 CYS A 153 1 19
HELIX 6 6 SER A 164 LEU A 177 1 14
HELIX 7 7 ASP A 178 SER A 183 1 6
HELIX 8 8 ASP A 204 ALA A 206 5 3
HELIX 9 9 ASP A 216 GLY A 221 5 6
HELIX 10 10 LEU A 226 LEU A 230 5 5
HELIX 11 11 THR A 231 GLU A 234 5 4
HELIX 12 12 ASP A 235 VAL A 244 1 10
HELIX 13 13 PRO A 245 SER A 248 5 4
SHEET 1 A 5 LEU A 117 GLY A 121 0
SHEET 2 A 5 VAL A 82 ALA A 87 1 N VAL A 84 O LYS A 120
SHEET 3 A 5 LYS A 157 TYR A 163 1 O VAL A 159 N THR A 83
SHEET 4 A 5 ILE A 185 PHE A 191 1 O SER A 186 N LEU A 158
SHEET 5 A 5 THR A 208 VAL A 211 1 O VAL A 211 N LEU A 190
SSBOND 1 CYS A 55 CYS A 91 1555 1555 2.05
SSBOND 2 CYS A 79 CYS A 153 1555 1555 2.04
SSBOND 3 CYS A 212 CYS A 219 1555 1555 2.12
CRYST1 148.930 148.930 29.145 90.00 90.00 120.00 P 61 6
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 0.006715 0.003877 0.000000 0.00000
SCALE2 0.000000 0.007753 0.000000 0.00000
SCALE3 0.000000 0.000000 0.034311 0.00000
TER 1634 HIS A 252
MASTER 481 0 0 13 5 0 0 6 2038 1 6 20
END |