HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 06-MAY-09 3HCZ
TITLE THE CRYSTAL STRUCTURE OF A DOMAIN OF POSSIBLE THIOL-DISULFIDE
TITLE 2 ISOMERASE FROM CYTOPHAGA HUTCHINSONII ATCC 33406.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POSSIBLE THIOL-DISULFIDE ISOMERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 330-474;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CYTOPHAGA HUTCHINSONII;
SOURCE 3 ORGANISM_TAXID: 269798;
SOURCE 4 STRAIN: ATCC 33406;
SOURCE 5 GENE: CHU_0134, CYTOPHAGA HUTCHINSONII;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: PPK1037;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG19
KEYWDS APC61559.2, THIOL-DISULFIDE ISOMERASE, CYTOPHAGA HUTCHINSONII ATCC,
KEYWDS 2 STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST
KEYWDS 3 CENTER FOR STRUCTURAL GENOMICS, MCSG, ISOMERASE, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,N.MARSHALL,G.COBB,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS (MCSG)
REVDAT 2 13-JUL-11 3HCZ 1 VERSN
REVDAT 1 19-MAY-09 3HCZ 0
JRNL AUTH K.TAN,N.MARSHALL,G.COBB,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF A DOMAIN OF POSSIBLE
JRNL TITL 2 THIOL-DISULFIDE ISOMERASE FROM CYTOPHAGA HUTCHINSONII ATCC
JRNL TITL 3 33406.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0054
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) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.39
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 15660
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 830
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) : 1.88
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.93
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1090
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.64
REMARK 3 BIN R VALUE (WORKING SET) : 0.2160
REMARK 3 BIN FREE R VALUE SET COUNT : 60
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1236
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.22000
REMARK 3 B22 (A**2) : 0.22000
REMARK 3 B33 (A**2) : -0.44000
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): 0.129
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.126
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.498
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
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): 1331 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1810 ; 1.509 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 157 ; 6.416 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 64 ;44.043 ;24.062
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 247 ;16.266 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;16.708 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 190 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 984 ; 0.008 ; 0.020
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): 751 ; 0.881 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1221 ; 1.573 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 580 ; 2.438 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 583 ; 3.906 ; 4.500
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 328 A 473
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7280 -4.8780 15.2150
REMARK 3 T TENSOR
REMARK 3 T11: 0.0549 T22: 0.0337
REMARK 3 T33: 0.1655 T12: 0.0381
REMARK 3 T13: -0.0050 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 2.2029 L22: 2.9573
REMARK 3 L33: 2.2510 L12: 1.4389
REMARK 3 L13: -0.0937 L23: -0.2937
REMARK 3 S TENSOR
REMARK 3 S11: 0.0087 S12: 0.0727 S13: 0.1175
REMARK 3 S21: -0.1291 S22: 0.0074 S23: 0.0617
REMARK 3 S31: -0.0634 S32: 0.0038 S33: -0.0161
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 3HCZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-09.
REMARK 100 THE RCSB ID CODE IS RCSB052982.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.97926
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16600
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
REMARK 200 RESOLUTION RANGE LOW (A) : 33.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 12.000
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 40.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.00
REMARK 200 R MERGE FOR SHELL (I) : 0.87600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD/MLPHARE/DM/ARP/WARP/HKL3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1 M MES,
REMARK 280 30% PEG 5000 MME, 3% 1,6-DIAMINOHEXANE, PH 6.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
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 63.03600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 27.50550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 27.50550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 31.51800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 27.50550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 27.50550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 94.55400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 27.50550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 27.50550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 31.51800
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 27.50550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 27.50550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 94.55400
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 63.03600
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 300 REMARK: EXPERIMENTALLY UNKNOWN. IT IS PREDICTED THAT THE DOMAIN IS
REMARK 300 MONOMERIC.
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -134.0 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 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 63.03600
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 327
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 341 55.85 -106.31
REMARK 500 TYR A 436 -94.28 -110.59
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 SO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 475
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC61559.2 RELATED DB: TARGETDB
DBREF 3HCZ A 330 474 UNP Q11YT9 Q11YT9_CYTH3 330 474
SEQADV 3HCZ SER A 327 UNP Q11YT9 EXPRESSION TAG
SEQADV 3HCZ ASN A 328 UNP Q11YT9 EXPRESSION TAG
SEQADV 3HCZ ALA A 329 UNP Q11YT9 EXPRESSION TAG
SEQRES 1 A 148 SER ASN ALA PRO LEU LEU LEU GLY LYS LYS ALA PRO ASN
SEQRES 2 A 148 LEU TYR MSE THR ASP THR THR GLY THR TYR ARG TYR LEU
SEQRES 3 A 148 TYR ASP VAL GLN ALA LYS TYR THR ILE LEU PHE PHE TRP
SEQRES 4 A 148 ASP SER GLN CYS GLY HIS CYS GLN GLN GLU THR PRO LYS
SEQRES 5 A 148 LEU TYR ASP TRP TRP LEU LYS ASN ARG ALA LYS GLY ILE
SEQRES 6 A 148 GLN VAL TYR ALA ALA ASN ILE GLU ARG LYS ASP GLU GLU
SEQRES 7 A 148 TRP LEU LYS PHE ILE ARG SER LYS LYS ILE GLY GLY TRP
SEQRES 8 A 148 LEU ASN VAL ARG ASP SER LYS ASN HIS THR ASP PHE LYS
SEQRES 9 A 148 ILE THR TYR ASP ILE TYR ALA THR PRO VAL LEU TYR VAL
SEQRES 10 A 148 LEU ASP LYS ASN LYS VAL ILE ILE ALA LYS ARG ILE GLY
SEQRES 11 A 148 TYR GLU ASN LEU ASP ASP PHE LEU VAL GLN TYR GLU LYS
SEQRES 12 A 148 SER LEU LYS THR LYS
MODRES 3HCZ MSE A 342 MET SELENOMETHIONINE
HET MSE A 342 8
HET SO4 A 1 5
HET SO4 A 2 5
HET SO4 A 3 5
HET SO4 A 4 5
HET SO4 A 5 5
HET FMT A 475 3
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM FMT FORMIC ACID
FORMUL 1 MSE C5 H11 N O2 SE
FORMUL 2 SO4 5(O4 S 2-)
FORMUL 7 FMT C H2 O2
FORMUL 8 HOH *124(H2 O)
HELIX 1 1 TYR A 351 VAL A 355 5 5
HELIX 2 2 ASP A 366 GLY A 370 5 5
HELIX 3 3 GLN A 374 ARG A 387 1 14
HELIX 4 4 ASP A 402 LYS A 413 1 12
HELIX 5 5 ASP A 428 ASP A 434 1 7
HELIX 6 6 GLY A 456 GLU A 458 5 3
HELIX 7 7 ASN A 459 LYS A 474 1 16
SHEET 1 A 5 LEU A 418 ARG A 421 0
SHEET 2 A 5 ILE A 391 ASN A 397 1 N ASN A 397 O VAL A 420
SHEET 3 A 5 TYR A 359 TRP A 365 1 N ILE A 361 O GLN A 392
SHEET 4 A 5 VAL A 440 LEU A 444 -1 O VAL A 440 N PHE A 364
SHEET 5 A 5 ILE A 450 LYS A 453 -1 O ILE A 451 N VAL A 443
SSBOND 1 CYS A 372 CYS A 372 1555 7555 2.66
LINK C TYR A 341 N MSE A 342 1555 1555 1.34
LINK C MSE A 342 N THR A 343 1555 1555 1.33
CISPEP 1 THR A 438 PRO A 439 0 2.84
SITE 1 AC1 10 HOH A 11 HOH A 44 HOH A 81 HOH A 92
SITE 2 AC1 10 HOH A 122 PRO A 338 ASN A 339 TYR A 349
SITE 3 AC1 10 TYR A 353 LYS A 424
SITE 1 AC2 3 LYS A 401 ASP A 402 GLU A 403
SITE 1 AC3 5 HOH A 69 HOH A 83 ARG A 350 GLN A 392
SITE 2 AC3 5 ARG A 454
SITE 1 AC4 5 HOH A 117 ALA A 357 LYS A 358 GLY A 390
SITE 2 AC4 5 TYR A 436
SITE 1 AC5 7 HOH A 89 HOH A 108 ARG A 400 THR A 427
SITE 2 AC5 7 ASP A 428 PHE A 429 LYS A 430
SITE 1 AC6 1 HOH A 42
CRYST1 55.011 55.011 126.072 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 0.018178 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018178 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007932 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
