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HEADER HYDROLASE 07-MAR-14 4PSC
TITLE STRUCTURE OF CUTINASE FROM TRICHODERMA REESEI IN ITS NATIVE FORM.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOHYDRATE ESTERASE FAMILY 5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MATURE FORM;
COMPND 5 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 FOLD, 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 4PSC 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. 1.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 79.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 68635
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) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.167
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3556
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) : 1.14
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.17
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4171
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE SET COUNT : 234
REMARK 3 BIN FREE R VALUE : 0.2250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1603
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 289
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -0.01000
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): 0.033
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.033
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.021
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.983
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1690 ; 0.022 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1641 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2324 ; 1.951 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3737 ; 1.121 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 234 ; 5.668 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 64 ;38.773 ;26.250
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 254 ;11.773 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;13.817 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 278 ; 0.136 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1968 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 354 ; 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): 3331 ; 6.616 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 66 ;22.351 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3509 ; 6.971 ; 5.000
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4PSC 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 RCSB085159.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
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 : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 81001
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150
REMARK 200 RESOLUTION RANGE LOW (A) : 79.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1CEX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MIXING 300 NL ENZYME AT 10 MG/ML WITH
REMARK 280 100 NL OF PEG3350 (25%), SODIUM CHLORIDE (0.2 M), BIS-TRIS (0.1
REMARK 280 M), PH 5.5, VAPOR DIFFUSION, SITTING DROP, 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 14.57950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.78950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.00100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.78950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 14.57950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.00100
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 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 ASP A 30
REMARK 465 HIS A 251
REMARK 465 HIS A 252
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 HIS A 250 CG ND1 CD2 CE1 NE2
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 651 O HOH A 652 2.15
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 O HOH A 574 O HOH A 615 3755 2.11
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 115 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 THR A 116 CA - CB - CG2 ANGL. DEV. = -10.6 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 ASN A 76 47.67 -146.74
REMARK 500 VAL A 100 -51.60 -138.46
REMARK 500 SER A 164 -128.80 61.20
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 100 23.5 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 588 DISTANCE = 5.22 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PSD RELATED DB: PDB
REMARK 900 RELATED ID: 4PSE RELATED DB: PDB
DBREF 4PSC A 45 248 UNP G0RH85 G0RH85_HYPJQ 1 204
SEQADV 4PSC MET A 1 UNP G0RH85 INITIATING METHIONINE
SEQADV 4PSC ARG A 2 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC SER A 3 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC LEU A 4 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ALA A 5 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ILE A 6 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC LEU A 7 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC THR A 8 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC THR A 9 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC LEU A 10 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC LEU A 11 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ALA A 12 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC GLY A 13 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC HIS A 14 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ALA A 15 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC PHE A 16 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ALA A 17 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC TYR A 18 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC PRO A 19 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC LYS A 20 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC PRO A 21 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ALA A 22 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC PRO A 23 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC GLN A 24 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC SER A 25 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC VAL A 26 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ASN A 27 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ARG A 28 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ARG A 29 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ASP A 30 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC TRP A 31 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC PRO A 32 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC SER A 33 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ILE A 34 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ASN A 35 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC GLU A 36 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC PHE A 37 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC LEU A 38 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC SER A 39 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC GLU A 40 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC LEU A 41 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC ALA A 42 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC LYS A 43 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC VAL A 44 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC HIS A 249 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC HIS A 250 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC HIS A 251 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC HIS A 252 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC HIS A 253 UNP G0RH85 EXPRESSION TAG
SEQADV 4PSC 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
HET GOL A 301 14
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 HOH *289(H2 O)
HELIX 1 1 SER A 33 MET A 45 1 13
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 ASN A 176 1 13
HELIX 7 7 ASP A 178 LYS A 184 1 7
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 GLU A 234 5 9
HELIX 11 11 ASP A 235 VAL A 247 1 13
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 GLY A 161 N LEU A 85
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 2.03
SSBOND 2 CYS A 79 CYS A 153 1555 1555 2.03
SSBOND 3 CYS A 212 CYS A 219 1555 1555 2.10
SITE 1 AC1 9 ARG A 88 GLY A 94 ASN A 95 TYR A 124
SITE 2 AC1 9 ASP A 235 THR A 238 HOH A 420 HOH A 441
SITE 3 AC1 9 HOH A 687
CRYST1 29.159 48.002 141.579 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 0.034295 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020832 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007063 0.00000
TER 3263 HIS A 250
MASTER 395 0 1 11 5 0 3 6 1898 1 20 20
END |