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HEADER HYDROLASE 24-NOV-08 3FCX
TITLE CRYSTAL STRUCTURE OF HUMAN ESTERASE D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-FORMYLGLUTATHIONE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: G257D;
COMPND 5 SYNONYM: FGH, ESTERASE D;
COMPND 6 EC: 3.1.2.12;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ESD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS RETINOBLASTOMA, GENETIC MARKER, ESTERASE, HYDROLASE,
KEYWDS 2 CYTOPLASM, CYTOPLASMIC VESICLE, POLYMORPHISM, SERINE
KEYWDS 3 ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.WU,Y.LI,G.SONG,D.ZHANG,N.SHAW,Z.J.LIU
REVDAT 1 09-DEC-08 3FCX 0
JRNL AUTH D.WU,Y.LI,S.GAOJIE,D.ZHANG,N.SHAW,Z.J.LIU
JRNL TITL CRYSTAL STRUCTURE OF HUMAN ESTERASE D: A POTENTIAL
JRNL TITL 2 GENETIC MARKER OF RETINOBLASTOMA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0066
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 65767
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 : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3500
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4782
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2280
REMARK 3 BIN FREE R VALUE SET COUNT : 245
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 4900
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.58000
REMARK 3 B22 (A**2) : 0.73000
REMARK 3 B33 (A**2) : -0.32000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.26000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.127
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.050
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.924
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4381 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5939 ; 1.032 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 540 ; 5.489 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 194 ;35.342 ;24.433
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 696 ;11.193 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;12.432 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 621 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3371 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2701 ; 0.655 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4327 ; 1.253 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1680 ; 2.417 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1611 ; 2.930 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4381 ; 2.325 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 620 ; 1.431 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4257 ; 2.360 ; 3.000
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3FCX COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-NOV-08.
REMARK 100 THE RCSB ID CODE IS RCSB050434.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 193
REMARK 200 PH : 5.6
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) : 0.979
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69289
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.32500
REMARK 200 R SYM (I) : 0.32500
REMARK 200 FOR THE DATA SET : 20.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.32500
REMARK 200 R SYM FOR SHELL (I) : 0.32500
REMARK 200 FOR SHELL : 20.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1PV1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 30.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM AMMONIUM ACETATE, 30%
REMARK 280 PEG4000, PH5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 35.36200
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.6 KCAL/MOL
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 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 30.54726
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 61.53081
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 LYS A 91
REMARK 465 GLY A 92
REMARK 465 GLU A 93
REMARK 465 ASP A 94
REMARK 465 GLU A 95
REMARK 465 SER A 96
REMARK 465 TRP A 97
REMARK 465 ASP A 98
REMARK 465 THR A 194
REMARK 465 ASP A 195
REMARK 465 GLN A 196
REMARK 465 GLY A 213
REMARK 465 SER A 214
REMARK 465 GLN A 215
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 41
REMARK 465 THR B 42
REMARK 465 GLY B 43
REMARK 465 LYS B 44
REMARK 465 ALA B 282
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 OG SER A 197 O HOH A 527 1.80
REMARK 500 NZ LYS A 198 O HOH A 540 1.93
REMARK 500 NH2 ARG A 86 O HOH A 383 2.12
REMARK 500 OE2 GLU A 245 O HOH A 426 2.14
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 CD1 PHE A 99 O HOH A 462 2546 2.13
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 GLU A 58 C GLN A 59 N -0.138
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 MET A 1 CA - CB - CG ANGL. DEV. = 13.0 DEGREES
REMARK 500 GLU A 58 O - C - N ANGL. DEV. = -9.9 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 THR A 57 -162.55 -104.90
REMARK 500 GLU A 126 -60.62 -121.78
REMARK 500 SER A 149 -116.75 60.39
REMARK 500 ASP A 259 -158.22 -108.00
REMARK 500 THR B 55 -10.95 77.63
REMARK 500 THR B 57 -163.94 -108.77
REMARK 500 ALA B 103 45.70 -151.30
REMARK 500 PHE B 105 13.45 59.24
REMARK 500 SER B 149 -120.92 60.99
REMARK 500 ASP B 195 91.11 -69.92
REMARK 500 ASP B 259 -156.03 -105.80
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 B 458 DISTANCE = 13.38 ANGSTROMS
REMARK 525 HOH B 472 DISTANCE = 12.17 ANGSTROMS
REMARK 525 HOH A 492 DISTANCE = 5.78 ANGSTROMS
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 CA B 283 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS B 39 NZ
REMARK 620 2 GLY B 75 O 122.3
REMARK 620 3 ASN B 281 OD1 115.2 120.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 284 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 104 O
REMARK 620 2 VAL B 107 O 102.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 284 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 554 O
REMARK 620 2 HOH A 544 O 126.4
REMARK 620 N 1
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 283
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 284
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 283
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 284
DBREF 3FCX A 1 282 UNP P10768 ESTD_HUMAN 1 282
DBREF 3FCX B 1 282 UNP P10768 ESTD_HUMAN 1 282
SEQADV 3FCX ASP A 257 UNP P10768 GLY 257 ENGINEERED
SEQADV 3FCX ASP B 257 UNP P10768 GLY 257 ENGINEERED
SEQRES 1 A 282 MET ALA LEU LYS GLN ILE SER SER ASN LYS CYS PHE GLY
SEQRES 2 A 282 GLY LEU GLN LYS VAL PHE GLU HIS ASP SER VAL GLU LEU
SEQRES 3 A 282 ASN CYS LYS MET LYS PHE ALA VAL TYR LEU PRO PRO LYS
SEQRES 4 A 282 ALA GLU THR GLY LYS CYS PRO ALA LEU TYR TRP LEU SER
SEQRES 5 A 282 GLY LEU THR CYS THR GLU GLN ASN PHE ILE SER LYS SER
SEQRES 6 A 282 GLY TYR HIS GLN SER ALA SER GLU HIS GLY LEU VAL VAL
SEQRES 7 A 282 ILE ALA PRO ASP THR SER PRO ARG GLY CYS ASN ILE LYS
SEQRES 8 A 282 GLY GLU ASP GLU SER TRP ASP PHE GLY THR GLY ALA GLY
SEQRES 9 A 282 PHE TYR VAL ASP ALA THR GLU ASP PRO TRP LYS THR ASN
SEQRES 10 A 282 TYR ARG MET TYR SER TYR VAL THR GLU GLU LEU PRO GLN
SEQRES 11 A 282 LEU ILE ASN ALA ASN PHE PRO VAL ASP PRO GLN ARG MET
SEQRES 12 A 282 SER ILE PHE GLY HIS SER MET GLY GLY HIS GLY ALA LEU
SEQRES 13 A 282 ILE CYS ALA LEU LYS ASN PRO GLY LYS TYR LYS SER VAL
SEQRES 14 A 282 SER ALA PHE ALA PRO ILE CYS ASN PRO VAL LEU CYS PRO
SEQRES 15 A 282 TRP GLY LYS LYS ALA PHE SER GLY TYR LEU GLY THR ASP
SEQRES 16 A 282 GLN SER LYS TRP LYS ALA TYR ASP ALA THR HIS LEU VAL
SEQRES 17 A 282 LYS SER TYR PRO GLY SER GLN LEU ASP ILE LEU ILE ASP
SEQRES 18 A 282 GLN GLY LYS ASP ASP GLN PHE LEU LEU ASP GLY GLN LEU
SEQRES 19 A 282 LEU PRO ASP ASN PHE ILE ALA ALA CYS THR GLU LYS LYS
SEQRES 20 A 282 ILE PRO VAL VAL PHE ARG LEU GLN GLU ASP TYR ASP HIS
SEQRES 21 A 282 SER TYR TYR PHE ILE ALA THR PHE ILE THR ASP HIS ILE
SEQRES 22 A 282 ARG HIS HIS ALA LYS TYR LEU ASN ALA
SEQRES 1 B 282 MET ALA LEU LYS GLN ILE SER SER ASN LYS CYS PHE GLY
SEQRES 2 B 282 GLY LEU GLN LYS VAL PHE GLU HIS ASP SER VAL GLU LEU
SEQRES 3 B 282 ASN CYS LYS MET LYS PHE ALA VAL TYR LEU PRO PRO LYS
SEQRES 4 B 282 ALA GLU THR GLY LYS CYS PRO ALA LEU TYR TRP LEU SER
SEQRES 5 B 282 GLY LEU THR CYS THR GLU GLN ASN PHE ILE SER LYS SER
SEQRES 6 B 282 GLY TYR HIS GLN SER ALA SER GLU HIS GLY LEU VAL VAL
SEQRES 7 B 282 ILE ALA PRO ASP THR SER PRO ARG GLY CYS ASN ILE LYS
SEQRES 8 B 282 GLY GLU ASP GLU SER TRP ASP PHE GLY THR GLY ALA GLY
SEQRES 9 B 282 PHE TYR VAL ASP ALA THR GLU ASP PRO TRP LYS THR ASN
SEQRES 10 B 282 TYR ARG MET TYR SER TYR VAL THR GLU GLU LEU PRO GLN
SEQRES 11 B 282 LEU ILE ASN ALA ASN PHE PRO VAL ASP PRO GLN ARG MET
SEQRES 12 B 282 SER ILE PHE GLY HIS SER MET GLY GLY HIS GLY ALA LEU
SEQRES 13 B 282 ILE CYS ALA LEU LYS ASN PRO GLY LYS TYR LYS SER VAL
SEQRES 14 B 282 SER ALA PHE ALA PRO ILE CYS ASN PRO VAL LEU CYS PRO
SEQRES 15 B 282 TRP GLY LYS LYS ALA PHE SER GLY TYR LEU GLY THR ASP
SEQRES 16 B 282 GLN SER LYS TRP LYS ALA TYR ASP ALA THR HIS LEU VAL
SEQRES 17 B 282 LYS SER TYR PRO GLY SER GLN LEU ASP ILE LEU ILE ASP
SEQRES 18 B 282 GLN GLY LYS ASP ASP GLN PHE LEU LEU ASP GLY GLN LEU
SEQRES 19 B 282 LEU PRO ASP ASN PHE ILE ALA ALA CYS THR GLU LYS LYS
SEQRES 20 B 282 ILE PRO VAL VAL PHE ARG LEU GLN GLU ASP TYR ASP HIS
SEQRES 21 B 282 SER TYR TYR PHE ILE ALA THR PHE ILE THR ASP HIS ILE
SEQRES 22 B 282 ARG HIS HIS ALA LYS TYR LEU ASN ALA
HET MG A 283 1
HET CA A 284 1
HET CA B 283 1
HET CA B 284 1
HETNAM MG MAGNESIUM ION
HETNAM CA CALCIUM ION
FORMUL 3 MG MG 2+
FORMUL 4 CA 3(CA 2+)
FORMUL 7 HOH *603(H2 O)
HELIX 1 1 PRO A 37 THR A 42 5 6
HELIX 2 2 GLU A 58 GLU A 58 1 1
HELIX 3 3 GLN A 59 SER A 65 1 7
HELIX 4 4 TYR A 67 GLY A 75 1 9
HELIX 5 5 PRO A 113 TYR A 118 1 6
HELIX 6 6 ARG A 119 GLU A 126 1 8
HELIX 7 7 GLU A 126 PHE A 136 1 11
HELIX 8 8 SER A 149 LYS A 161 1 13
HELIX 9 9 ASN A 177 LEU A 180 5 4
HELIX 10 10 CYS A 181 GLY A 193 1 13
HELIX 11 11 LYS A 198 TYR A 202 5 5
HELIX 12 12 ASP A 203 LYS A 209 1 7
HELIX 13 13 ASP A 226 ASP A 231 1 6
HELIX 14 14 LEU A 235 LYS A 246 1 12
HELIX 15 15 SER A 261 LEU A 280 1 20
HELIX 16 16 GLN B 59 SER B 65 1 7
HELIX 17 17 TYR B 67 HIS B 74 1 8
HELIX 18 18 ARG B 119 GLU B 126 1 8
HELIX 19 19 GLU B 126 PHE B 136 1 11
HELIX 20 20 SER B 149 LYS B 161 1 13
HELIX 21 21 ASN B 177 LEU B 180 5 4
HELIX 22 22 CYS B 181 GLY B 193 1 13
HELIX 23 23 ASP B 195 ALA B 201 1 7
HELIX 24 24 ASP B 203 TYR B 211 1 9
HELIX 25 25 ASP B 226 ASP B 231 1 6
HELIX 26 26 LEU B 235 LYS B 247 1 13
HELIX 27 27 SER B 261 ASN B 281 1 21
SHEET 1 A 9 LYS A 4 CYS A 11 0
SHEET 2 A 9 GLY A 14 SER A 23 -1 O GLN A 16 N ASN A 9
SHEET 3 A 9 CYS A 28 LEU A 36 -1 O VAL A 34 N LYS A 17
SHEET 4 A 9 VAL A 77 PRO A 81 -1 O ALA A 80 N ALA A 33
SHEET 5 A 9 CYS A 45 LEU A 51 1 N TRP A 50 O ILE A 79
SHEET 6 A 9 VAL A 138 HIS A 148 1 O ASP A 139 N CYS A 45
SHEET 7 A 9 VAL A 169 PHE A 172 1 O PHE A 172 N GLY A 147
SHEET 8 A 9 ILE A 218 GLY A 223 1 O ASP A 221 N ALA A 171
SHEET 9 A 9 VAL A 250 GLN A 255 1 O GLN A 255 N GLN A 222
SHEET 1 B 9 LYS B 4 CYS B 11 0
SHEET 2 B 9 GLY B 14 SER B 23 -1 O VAL B 18 N ILE B 6
SHEET 3 B 9 CYS B 28 LEU B 36 -1 O VAL B 34 N LYS B 17
SHEET 4 B 9 VAL B 77 PRO B 81 -1 O VAL B 78 N TYR B 35
SHEET 5 B 9 ALA B 47 LEU B 51 1 N TRP B 50 O ILE B 79
SHEET 6 B 9 MET B 143 HIS B 148 1 O PHE B 146 N LEU B 51
SHEET 7 B 9 VAL B 169 PHE B 172 1 O PHE B 172 N GLY B 147
SHEET 8 B 9 ILE B 218 GLY B 223 1 O LEU B 219 N ALA B 171
SHEET 9 B 9 VAL B 250 GLN B 255 1 O GLN B 255 N GLN B 222
LINK NZ LYS B 39 CA CA B 283 1555 1555 2.80
LINK O GLY B 75 CA CA B 283 1555 1555 2.85
LINK O GLY B 104 CA CA B 284 1555 1555 2.84
LINK O VAL B 107 CA CA B 284 1555 1555 2.80
LINK OD1 ASN B 281 CA CA B 283 1555 1555 2.77
LINK CA CA A 284 O HOH A 554 1555 1555 2.43
LINK CA CA A 284 O HOH A 544 1555 1555 2.41
CISPEP 1 ASP A 112 PRO A 113 0 1.43
CISPEP 2 ASP B 112 PRO B 113 0 2.94
SITE 1 AC1 4 HIS A 153 ILE A 175 PRO A 178 ALA A 204
SITE 1 AC2 5 GLN A 227 ASP A 259 HIS A 260 HOH A 544
SITE 2 AC2 5 HOH A 554
SITE 1 AC3 5 LYS B 39 PRO B 46 HIS B 74 GLY B 75
SITE 2 AC3 5 ASN B 281
SITE 1 AC4 4 GLY B 104 VAL B 107 TYR B 118 MET B 120
CRYST1 51.542 70.724 65.014 90.00 108.84 90.00 P 1 21 1 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 0.019402 0.000000 0.006618 0.00000
SCALE2 0.000000 0.014139 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016252 0.00000
END |