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HEADER HYDROLASE 18-MAR-14 4PW0
TITLE ALPHA/BETA HYDROLASE FOLD PROTEIN FROM CHITINOPHAGA PINENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHITINOPHAGA PINENSIS;
SOURCE 3 ORGANISM_TAXID: 485918;
SOURCE 4 STRAIN: DSM 2588;
SOURCE 5 GENE: CPIN_2213;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG73
KEYWDS STRUCTURAL GENOMICS, APC103277, ALPHA/BETA HYDROLASE FOLD PROTEIN,
KEYWDS 2 PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,C.TESAR,S.CLANCY,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (MCSG)
REVDAT 1 02-APR-14 4PW0 0
JRNL AUTH J.OSIPIUK,C.TESAR,S.CLANCY,A.JOACHIMIAK
JRNL TITL ALPHA/BETA HYDROLASE FOLD PROTEIN FROM CHITINOPHAGA
JRNL TITL 2 PINENSIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 68260
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) : 0.105
REMARK 3 R VALUE (WORKING SET) : 0.103
REMARK 3 FREE R VALUE : 0.133
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3453
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) : 1.48
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.52
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4704
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.1610
REMARK 3 BIN FREE R VALUE SET COUNT : 257
REMARK 3 BIN FREE R VALUE : 0.2030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2170
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 374
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.10000
REMARK 3 B12 (A**2) : -0.02000
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): 0.041
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.041
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.024
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.428
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.986
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.979
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2449 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2294 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3379 ; 1.662 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5312 ; 0.898 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 335 ; 6.139 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 127 ;33.083 ;24.173
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 393 ;12.440 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;20.933 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 373 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2896 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 610 ; 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): 1170 ; 1.802 ; 1.931
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1169 ; 1.801 ; 1.931
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1478 ; 1.845 ; 2.909
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): 4743 ; 3.798 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 91 ;36.297 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4944 ; 9.720 ; 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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4PW0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085288.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-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 : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 133991
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 37.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.62100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.860
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, MLPHARE, DM, SOLVE/RESOLVE, HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3 M NACL, 0.1 M TRIS-HCL, PH 8.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 39.45600
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 19.72800
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 0.00000
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 39.45600
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 19.72800
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: 3380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 165.57000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 95.59188
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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 HIS A 2
REMARK 465 THR A 3
REMARK 465 PRO A 4
REMARK 465 LEU A 5
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 692 O HOH A 694 2.12
REMARK 500 OE1 GLU A 267 O HOH A 744 2.13
REMARK 500 O HOH A 406 O HOH A 652 2.13
REMARK 500 O HOH A 478 O HOH A 677 2.16
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 CE1 TYR A 182 NH1 ARG A 158 2654 2.05
REMARK 500 CD1 TYR A 182 NH1 ARG A 158 2654 2.15
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 188 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 PHE A 262 CB - CG - CD1 ANGL. DEV. = 4.8 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 THR A 43 -6.16 75.50
REMARK 500 SER A 107 -121.64 63.56
REMARK 500 ARG A 125 -73.02 -93.17
REMARK 500 ALA A 132 -159.94 -138.57
REMARK 500 SER A 193 143.69 95.60
REMARK 500 ASP A 235 114.31 70.18
REMARK 500 ALA A 258 -147.24 -137.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC103277 RELATED DB: TARGETTRACK
DBREF 4PW0 A 1 280 UNP C7PEX8 C7PEX8_CHIPD 1 280
SEQADV 4PW0 SER A -2 UNP C7PEX8 EXPRESSION TAG
SEQADV 4PW0 ASN A -1 UNP C7PEX8 EXPRESSION TAG
SEQADV 4PW0 ALA A 0 UNP C7PEX8 EXPRESSION TAG
SEQRES 1 A 283 SER ASN ALA MSE HIS THR PRO LEU ASN ASP HIS ALA THR
SEQRES 2 A 283 ALA PRO THR GLN TYR ILE GLU VAL ASN GLY THR ARG TYR
SEQRES 3 A 283 ALA TYR ARG SER LEU GLY ALA PRO SER ASP ILE PRO LEU
SEQRES 4 A 283 ILE CYS PHE GLN HIS PHE THR GLY THR LEU ASP ASN TRP
SEQRES 5 A 283 ASP PRO LEU ILE THR ASN GLY LEU SER LYS GLY ARG GLN
SEQRES 6 A 283 LEU ILE ILE PHE ASP ASN LYS GLY VAL GLY LEU SER SER
SEQRES 7 A 283 GLY THR THR PRO ASP ASN VAL ALA ALA MSE THR ALA ASP
SEQRES 8 A 283 ALA LEU GLU PHE ILE THR ALA LEU GLY ILE ARG TYR PHE
SEQRES 9 A 283 ASP VAL LEU GLY PHE SER LEU GLY GLY PHE ILE VAL GLN
SEQRES 10 A 283 TYR MSE ALA HIS ILE GLN PRO ASP MSE ILE ARG LYS ILE
SEQRES 11 A 283 ILE ILE VAL GLY ALA ALA PRO GLN GLY VAL LYS VAL LEU
SEQRES 12 A 283 HIS THR PHE PRO ASP LEU ILE ALA ARG ALA MSE GLN LEU
SEQRES 13 A 283 GLU PRO LYS GLU ARG PHE LEU PHE ILE PHE PHE GLU GLN
SEQRES 14 A 283 SER GLU HIS SER ARG SER LYS GLY LEU ALA THR LEU GLY
SEQRES 15 A 283 ARG LEU TYR GLU ARG THR THR ASP ARG ASP GLN ASP ALA
SEQRES 16 A 283 SER ALA GLN ALA ILE GLY ALA GLN LEU THR ALA ILE THR
SEQRES 17 A 283 ASN TRP GLY LYS LYS THR PRO SER PHE GLU ILE THR SER
SEQRES 18 A 283 ILE GLN HIS PRO VAL PHE VAL VAL GLN GLY SER ASN ASP
SEQRES 19 A 283 GLU MSE MSE ASP THR TYR ASN SER TYR GLU LEU PHE LYS
SEQRES 20 A 283 GLN LEU PRO ASP ALA ILE LEU SER LEU TYR PRO ASP ALA
SEQRES 21 A 283 ALA HIS GLY SER PHE TYR GLN TYR PRO GLU LEU PHE VAL
SEQRES 22 A 283 SER GLN THR GLU TYR PHE LEU ASP SER TYR
MODRES 4PW0 MSE A 85 MET SELENOMETHIONINE
MODRES 4PW0 MSE A 116 MET SELENOMETHIONINE
MODRES 4PW0 MSE A 123 MET SELENOMETHIONINE
MODRES 4PW0 MSE A 151 MET SELENOMETHIONINE
MODRES 4PW0 MSE A 233 MET SELENOMETHIONINE
MODRES 4PW0 MSE A 234 MET SELENOMETHIONINE
HET MSE A 85 8
HET MSE A 116 8
HET MSE A 123 8
HET MSE A 151 8
HET MSE A 233 8
HET MSE A 234 8
HET CL A 301 1
HET CL A 302 1
HET CL A 303 1
HET CL A 304 1
HET CL A 305 1
HET CL A 306 1
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 CL 6(CL 1-)
FORMUL 8 HOH *374(H2 O)
HELIX 1 1 THR A 45 TRP A 49 5 5
HELIX 2 2 ASP A 50 LYS A 59 1 10
HELIX 3 3 ASN A 81 LEU A 96 1 16
HELIX 4 4 SER A 107 GLN A 120 1 14
HELIX 5 5 VAL A 137 HIS A 141 5 5
HELIX 6 6 THR A 142 GLN A 152 1 11
HELIX 7 7 GLU A 154 PHE A 164 1 11
HELIX 8 8 SER A 167 TYR A 182 1 16
HELIX 9 9 SER A 193 LYS A 210 1 18
HELIX 10 10 GLU A 215 ILE A 219 5 5
HELIX 11 11 THR A 236 LEU A 246 1 11
HELIX 12 12 GLY A 260 TYR A 265 1 6
HELIX 13 13 TYR A 265 TYR A 280 1 16
SHEET 1 A 8 GLN A 14 VAL A 18 0
SHEET 2 A 8 THR A 21 LEU A 28 -1 O TYR A 25 N GLN A 14
SHEET 3 A 8 LEU A 63 PHE A 66 -1 O LEU A 63 N LEU A 28
SHEET 4 A 8 LEU A 36 PHE A 39 1 N LEU A 36 O ILE A 64
SHEET 5 A 8 PHE A 101 PHE A 106 1 O ASP A 102 N ILE A 37
SHEET 6 A 8 ILE A 124 VAL A 130 1 O ILE A 128 N GLY A 105
SHEET 7 A 8 VAL A 223 GLY A 228 1 O VAL A 226 N ILE A 129
SHEET 8 A 8 ALA A 249 TYR A 254 1 O ILE A 250 N VAL A 225
LINK C ALA A 84 N MSE A 85 1555 1555 1.35
LINK C MSE A 85 N THR A 86 1555 1555 1.33
LINK C TYR A 115 N MSE A 116 1555 1555 1.32
LINK C MSE A 116 N ALA A 117 1555 1555 1.33
LINK C ASP A 122 N MSE A 123 1555 1555 1.34
LINK C MSE A 123 N ILE A 124 1555 1555 1.34
LINK C ALA A 150 N MSE A 151 1555 1555 1.33
LINK C MSE A 151 N GLN A 152 1555 1555 1.34
LINK C GLU A 232 N MSE A 233 1555 1555 1.34
LINK C MSE A 233 N MSE A 234 1555 1555 1.35
LINK C MSE A 234 N ASP A 235 1555 1555 1.34
SITE 1 AC1 4 HIS A 41 PHE A 42 SER A 107 HIS A 259
SITE 1 AC2 4 GLY A 76 THR A 77 HOH A 492 HOH A 746
SITE 1 AC3 1 GLU A 215
SITE 1 AC4 3 GLN A 120 PRO A 121 ASP A 122
SITE 1 AC5 6 TYR A 265 PRO A 266 GLU A 267 LEU A 268
SITE 2 AC5 6 HOH A 445 HOH A 768
SITE 1 AC6 1 LYS A 138
CRYST1 110.380 110.380 59.184 90.00 90.00 120.00 P 62 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 0.009060 0.005231 0.000000 0.00000
SCALE2 0.000000 0.010461 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016896 0.00000
TER 2361 TYR A 280
MASTER 369 0 12 13 8 0 7 6 2550 1 58 22
END |