| content |
HEADER HYDROLASE 24-NOV-08 3FCY
TITLE CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE 1 FROM
TITLE 2 THERMOANAEROBACTERIUM SP. JW/SL YS485
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: XYLAN ESTERASE 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 3.1.1.72, 3.1.1.41;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOANAEROBACTERIUM SP. 'JW/SL
SOURCE 3 YS485';
SOURCE 4 ORGANISM_TAXID: 60708;
SOURCE 5 STRAIN: JW/SL YS485;
SOURCE 6 GENE: AXE1;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 STAR (DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET
KEYWDS ALPHA/BETA HYDROLASE, CARBOHYDRATE ESTERASE, CE7,
KEYWDS 2 THERMOANAEROBACTERIUM SP.
EXPDTA X-RAY DIFFRACTION
AUTHOR I.KRASTANOVA,A.CASSETTA,D.LAMBA
REVDAT 1 17-NOV-09 3FCY 0
JRNL AUTH I.KRASTANOVA,A.CASSETTA,J.WIEGEL,D.LAMBA
JRNL TITL CRYSTAL STRUCTURE ANALYSIS OF ACETYL XYLAN ESTERASE
JRNL TITL 2 1 FROM THERMOANAEROBACTERIUM SP. JW/SL YS485
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.SHAO,J.WIEGEL
REMARK 1 TITL PURIFICATION AND CHARACTERIZATION OF TWO
REMARK 1 TITL 2 THERMOSTABLE ACETYL XYLAN ESTERASES FROM
REMARK 1 TITL 3 THERMOANAEROBACTERIUM SP. STRAIN JW/SL-YS485
REMARK 1 REF APPL.ENVIRON.MICROBIOL. V. 61 729 1995
REMARK 1 REFN ISSN 0099-2240
REMARK 1 REFERENCE 2
REMARK 1 AUTH W.W.LORENZ,J.WIEGEL
REMARK 1 TITL ISOLATION, ANALYSIS, AND EXPRESSION OF TWO GENES
REMARK 1 TITL 2 FROM THERMOANAEROBACTERIUM SP. STRAIN JW/SL YS485:
REMARK 1 TITL 3 A BETA-XYLOSIDASE AND A NOVEL ACETYL XYLAN ESTERASE
REMARK 1 TITL 4 WITH CEPHALOSPORIN C DEACETYLASE ACTIVITY
REMARK 1 REF J.BACTERIOL. V. 179 5436 1997
REMARK 1 REFN ISSN 0021-9193
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 66710
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 SET) : 0.184
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6761
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 7572
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 489
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.56
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.70500
REMARK 3 B22 (A**2) : 2.70500
REMARK 3 B33 (A**2) : -5.41000
REMARK 3 B12 (A**2) : 0.70200
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.25
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.124 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.584 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.983 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.894 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 53.97
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3FCY COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-08.
REMARK 100 THE RCSB ID CODE IS RCSB050435.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 0.9786
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66742
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.100
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.60
REMARK 200 R MERGE FOR SHELL (I) : 0.32900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.300
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 3FVR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG 400, 0.1M CALCIUM CHLORIDE,
REMARK 280 0.05M SODIUM HEPES, PH 7.5, MICROBATCH, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 75.27600
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 37.63800
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.63800
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 75.27600
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 37.63800
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CA CA A 321 LIES ON A SPECIAL POSITION.
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 -25
REMARK 465 LYS A -24
REMARK 465 HIS A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 PRO A -17
REMARK 465 MET A -16
REMARK 465 SER A -15
REMARK 465 ASP A -14
REMARK 465 TYR A -13
REMARK 465 ASP A -12
REMARK 465 ILE A -11
REMARK 465 PRO A -10
REMARK 465 THR A -9
REMARK 465 THR A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 ALA A 0
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 LEU A 3
REMARK 465 MET B -25
REMARK 465 LYS B -24
REMARK 465 HIS B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 PRO B -17
REMARK 465 MET B -16
REMARK 465 SER B -15
REMARK 465 ASP B -14
REMARK 465 TYR B -13
REMARK 465 ASP B -12
REMARK 465 ILE B -11
REMARK 465 PRO B -10
REMARK 465 THR B -9
REMARK 465 THR B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 LEU B 3
REMARK 465 MET C -25
REMARK 465 LYS C -24
REMARK 465 HIS C -23
REMARK 465 HIS C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 PRO C -17
REMARK 465 MET C -16
REMARK 465 SER C -15
REMARK 465 ASP C -14
REMARK 465 TYR C -13
REMARK 465 ASP C -12
REMARK 465 ILE C -11
REMARK 465 PRO C -10
REMARK 465 THR C -9
REMARK 465 THR C -8
REMARK 465 GLU C -7
REMARK 465 ASN C -6
REMARK 465 LEU C -5
REMARK 465 TYR C -4
REMARK 465 PHE C -3
REMARK 465 GLN C -2
REMARK 465 GLY C -1
REMARK 465 ALA C 0
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 LEU C 3
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 SER A 92 -3.11 81.54
REMARK 500 SER A 93 -153.26 -92.31
REMARK 500 GLN A 119 -132.34 -102.04
REMARK 500 SER A 182 -118.09 53.81
REMARK 500 TYR A 205 65.61 30.70
REMARK 500 LEU A 208 36.62 74.79
REMARK 500 ASN A 222 -121.95 57.89
REMARK 500 ASP A 235 62.60 -160.88
REMARK 500 SER B 92 -7.07 80.39
REMARK 500 SER B 93 -155.50 -88.14
REMARK 500 GLN B 119 -125.88 -104.44
REMARK 500 SER B 182 -114.03 55.69
REMARK 500 TYR B 205 64.83 31.66
REMARK 500 LEU B 208 33.31 70.01
REMARK 500 ASN B 222 -122.43 59.63
REMARK 500 ASP B 235 59.49 -161.60
REMARK 500 SER C 92 -0.69 79.28
REMARK 500 SER C 93 -156.18 -94.30
REMARK 500 GLN C 119 -129.89 -99.85
REMARK 500 SER C 182 -118.32 54.26
REMARK 500 TYR C 205 67.52 26.77
REMARK 500 LEU C 208 35.91 73.03
REMARK 500 ASN C 222 -122.85 57.66
REMARK 500 ASP C 235 62.94 -161.37
REMARK 500
REMARK 500 REMARK: NULL
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 A 321 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 317 O
REMARK 620 2 TYR A 319 O 81.6
REMARK 620 3 HOH A 395 O 109.8 88.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 321 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 317 O
REMARK 620 2 TYR C 319 O 86.9
REMARK 620 3 HOH C 417 O 80.7 74.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 321
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 321
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ODS RELATED DB: PDB
REMARK 900 CEPHALOSPORIN C DEACETYLASE FROM BACILLUS SUBTILIS
REMARK 900 RELATED ID: 1ODT RELATED DB: PDB
REMARK 900 CEPHALOSPORIN C DEACETYLASE MUTATED, IN COMPLEX WITH ACETATE
REMARK 900 RELATED ID: 1L7A RELATED DB: PDB
REMARK 900 STRUCTURAL GENOMICS, CRYSTAL STRUCTURE OF CEPHALOSPORIN C
REMARK 900 DEACETYLASE
REMARK 900 RELATED ID: 1VLQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE (TM0077) FROM
REMARK 900 THERMOTOGA MARITIMA AT 2.10 A RESOLUTION
DBREF 3FCY A 1 320 UNP O30361 O30361_THESJ 1 320
DBREF 3FCY B 1 320 UNP O30361 O30361_THESJ 1 320
DBREF 3FCY C 1 320 UNP O30361 O30361_THESJ 1 320
SEQADV 3FCY MET A -25 UNP O30361 EXPRESSION TAG
SEQADV 3FCY LYS A -24 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS A -23 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS A -22 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS A -21 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS A -20 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS A -19 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS A -18 UNP O30361 EXPRESSION TAG
SEQADV 3FCY PRO A -17 UNP O30361 EXPRESSION TAG
SEQADV 3FCY MET A -16 UNP O30361 EXPRESSION TAG
SEQADV 3FCY SER A -15 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ASP A -14 UNP O30361 EXPRESSION TAG
SEQADV 3FCY TYR A -13 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ASP A -12 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ILE A -11 UNP O30361 EXPRESSION TAG
SEQADV 3FCY PRO A -10 UNP O30361 EXPRESSION TAG
SEQADV 3FCY THR A -9 UNP O30361 EXPRESSION TAG
SEQADV 3FCY THR A -8 UNP O30361 EXPRESSION TAG
SEQADV 3FCY GLU A -7 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ASN A -6 UNP O30361 EXPRESSION TAG
SEQADV 3FCY LEU A -5 UNP O30361 EXPRESSION TAG
SEQADV 3FCY TYR A -4 UNP O30361 EXPRESSION TAG
SEQADV 3FCY PHE A -3 UNP O30361 EXPRESSION TAG
SEQADV 3FCY GLN A -2 UNP O30361 EXPRESSION TAG
SEQADV 3FCY GLY A -1 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ALA A 0 UNP O30361 EXPRESSION TAG
SEQADV 3FCY MET B -25 UNP O30361 EXPRESSION TAG
SEQADV 3FCY LYS B -24 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS B -23 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS B -22 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS B -21 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS B -20 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS B -19 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS B -18 UNP O30361 EXPRESSION TAG
SEQADV 3FCY PRO B -17 UNP O30361 EXPRESSION TAG
SEQADV 3FCY MET B -16 UNP O30361 EXPRESSION TAG
SEQADV 3FCY SER B -15 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ASP B -14 UNP O30361 EXPRESSION TAG
SEQADV 3FCY TYR B -13 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ASP B -12 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ILE B -11 UNP O30361 EXPRESSION TAG
SEQADV 3FCY PRO B -10 UNP O30361 EXPRESSION TAG
SEQADV 3FCY THR B -9 UNP O30361 EXPRESSION TAG
SEQADV 3FCY THR B -8 UNP O30361 EXPRESSION TAG
SEQADV 3FCY GLU B -7 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ASN B -6 UNP O30361 EXPRESSION TAG
SEQADV 3FCY LEU B -5 UNP O30361 EXPRESSION TAG
SEQADV 3FCY TYR B -4 UNP O30361 EXPRESSION TAG
SEQADV 3FCY PHE B -3 UNP O30361 EXPRESSION TAG
SEQADV 3FCY GLN B -2 UNP O30361 EXPRESSION TAG
SEQADV 3FCY GLY B -1 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ALA B 0 UNP O30361 EXPRESSION TAG
SEQADV 3FCY MET C -25 UNP O30361 EXPRESSION TAG
SEQADV 3FCY LYS C -24 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS C -23 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS C -22 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS C -21 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS C -20 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS C -19 UNP O30361 EXPRESSION TAG
SEQADV 3FCY HIS C -18 UNP O30361 EXPRESSION TAG
SEQADV 3FCY PRO C -17 UNP O30361 EXPRESSION TAG
SEQADV 3FCY MET C -16 UNP O30361 EXPRESSION TAG
SEQADV 3FCY SER C -15 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ASP C -14 UNP O30361 EXPRESSION TAG
SEQADV 3FCY TYR C -13 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ASP C -12 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ILE C -11 UNP O30361 EXPRESSION TAG
SEQADV 3FCY PRO C -10 UNP O30361 EXPRESSION TAG
SEQADV 3FCY THR C -9 UNP O30361 EXPRESSION TAG
SEQADV 3FCY THR C -8 UNP O30361 EXPRESSION TAG
SEQADV 3FCY GLU C -7 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ASN C -6 UNP O30361 EXPRESSION TAG
SEQADV 3FCY LEU C -5 UNP O30361 EXPRESSION TAG
SEQADV 3FCY TYR C -4 UNP O30361 EXPRESSION TAG
SEQADV 3FCY PHE C -3 UNP O30361 EXPRESSION TAG
SEQADV 3FCY GLN C -2 UNP O30361 EXPRESSION TAG
SEQADV 3FCY GLY C -1 UNP O30361 EXPRESSION TAG
SEQADV 3FCY ALA C 0 UNP O30361 EXPRESSION TAG
SEQRES 1 A 346 MET LYS HIS HIS HIS HIS HIS HIS PRO MET SER ASP TYR
SEQRES 2 A 346 ASP ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA
SEQRES 3 A 346 MET GLY LEU PHE ASP MET PRO LEU GLN LYS LEU ARG GLU
SEQRES 4 A 346 TYR THR GLY THR ASN PRO CYS PRO GLU ASP PHE ASP GLU
SEQRES 5 A 346 TYR TRP ASN ARG ALA LEU ASP GLU MET ARG SER VAL ASP
SEQRES 6 A 346 PRO LYS ILE GLU LEU LYS GLU SER SER PHE GLN VAL SER
SEQRES 7 A 346 PHE ALA GLU CYS TYR ASP LEU TYR PHE THR GLY VAL ARG
SEQRES 8 A 346 GLY ALA ARG ILE HIS ALA LYS TYR ILE LYS PRO LYS THR
SEQRES 9 A 346 GLU GLY LYS HIS PRO ALA LEU ILE ARG PHE HIS GLY TYR
SEQRES 10 A 346 SER SER ASN SER GLY ASP TRP ASN ASP LYS LEU ASN TYR
SEQRES 11 A 346 VAL ALA ALA GLY PHE THR VAL VAL ALA MET ASP VAL ARG
SEQRES 12 A 346 GLY GLN GLY GLY GLN SER GLN ASP VAL GLY GLY VAL THR
SEQRES 13 A 346 GLY ASN THR LEU ASN GLY HIS ILE ILE ARG GLY LEU ASP
SEQRES 14 A 346 ASP ASP ALA ASP ASN MET LEU PHE ARG HIS ILE PHE LEU
SEQRES 15 A 346 ASP THR ALA GLN LEU ALA GLY ILE VAL MET ASN MET PRO
SEQRES 16 A 346 GLU VAL ASP GLU ASP ARG VAL GLY VAL MET GLY PRO SER
SEQRES 17 A 346 GLN GLY GLY GLY LEU SER LEU ALA CYS ALA ALA LEU GLU
SEQRES 18 A 346 PRO ARG VAL ARG LYS VAL VAL SER GLU TYR PRO PHE LEU
SEQRES 19 A 346 SER ASP TYR LYS ARG VAL TRP ASP LEU ASP LEU ALA LYS
SEQRES 20 A 346 ASN ALA TYR GLN GLU ILE THR ASP TYR PHE ARG LEU PHE
SEQRES 21 A 346 ASP PRO ARG HIS GLU ARG GLU ASN GLU VAL PHE THR LYS
SEQRES 22 A 346 LEU GLY TYR ILE ASP VAL LYS ASN LEU ALA LYS ARG ILE
SEQRES 23 A 346 LYS GLY ASP VAL LEU MET CYS VAL GLY LEU MET ASP GLN
SEQRES 24 A 346 VAL CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN ASN
SEQRES 25 A 346 ILE GLN SER LYS LYS ASP ILE LYS VAL TYR PRO ASP TYR
SEQRES 26 A 346 GLY HIS GLU PRO MET ARG GLY PHE GLY ASP LEU ALA MET
SEQRES 27 A 346 GLN PHE MET LEU GLU LEU TYR SER
SEQRES 1 B 346 MET LYS HIS HIS HIS HIS HIS HIS PRO MET SER ASP TYR
SEQRES 2 B 346 ASP ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA
SEQRES 3 B 346 MET GLY LEU PHE ASP MET PRO LEU GLN LYS LEU ARG GLU
SEQRES 4 B 346 TYR THR GLY THR ASN PRO CYS PRO GLU ASP PHE ASP GLU
SEQRES 5 B 346 TYR TRP ASN ARG ALA LEU ASP GLU MET ARG SER VAL ASP
SEQRES 6 B 346 PRO LYS ILE GLU LEU LYS GLU SER SER PHE GLN VAL SER
SEQRES 7 B 346 PHE ALA GLU CYS TYR ASP LEU TYR PHE THR GLY VAL ARG
SEQRES 8 B 346 GLY ALA ARG ILE HIS ALA LYS TYR ILE LYS PRO LYS THR
SEQRES 9 B 346 GLU GLY LYS HIS PRO ALA LEU ILE ARG PHE HIS GLY TYR
SEQRES 10 B 346 SER SER ASN SER GLY ASP TRP ASN ASP LYS LEU ASN TYR
SEQRES 11 B 346 VAL ALA ALA GLY PHE THR VAL VAL ALA MET ASP VAL ARG
SEQRES 12 B 346 GLY GLN GLY GLY GLN SER GLN ASP VAL GLY GLY VAL THR
SEQRES 13 B 346 GLY ASN THR LEU ASN GLY HIS ILE ILE ARG GLY LEU ASP
SEQRES 14 B 346 ASP ASP ALA ASP ASN MET LEU PHE ARG HIS ILE PHE LEU
SEQRES 15 B 346 ASP THR ALA GLN LEU ALA GLY ILE VAL MET ASN MET PRO
SEQRES 16 B 346 GLU VAL ASP GLU ASP ARG VAL GLY VAL MET GLY PRO SER
SEQRES 17 B 346 GLN GLY GLY GLY LEU SER LEU ALA CYS ALA ALA LEU GLU
SEQRES 18 B 346 PRO ARG VAL ARG LYS VAL VAL SER GLU TYR PRO PHE LEU
SEQRES 19 B 346 SER ASP TYR LYS ARG VAL TRP ASP LEU ASP LEU ALA LYS
SEQRES 20 B 346 ASN ALA TYR GLN GLU ILE THR ASP TYR PHE ARG LEU PHE
SEQRES 21 B 346 ASP PRO ARG HIS GLU ARG GLU ASN GLU VAL PHE THR LYS
SEQRES 22 B 346 LEU GLY TYR ILE ASP VAL LYS ASN LEU ALA LYS ARG ILE
SEQRES 23 B 346 LYS GLY ASP VAL LEU MET CYS VAL GLY LEU MET ASP GLN
SEQRES 24 B 346 VAL CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN ASN
SEQRES 25 B 346 ILE GLN SER LYS LYS ASP ILE LYS VAL TYR PRO ASP TYR
SEQRES 26 B 346 GLY HIS GLU PRO MET ARG GLY PHE GLY ASP LEU ALA MET
SEQRES 27 B 346 GLN PHE MET LEU GLU LEU TYR SER
SEQRES 1 C 346 MET LYS HIS HIS HIS HIS HIS HIS PRO MET SER ASP TYR
SEQRES 2 C 346 ASP ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA
SEQRES 3 C 346 MET GLY LEU PHE ASP MET PRO LEU GLN LYS LEU ARG GLU
SEQRES 4 C 346 TYR THR GLY THR ASN PRO CYS PRO GLU ASP PHE ASP GLU
SEQRES 5 C 346 TYR TRP ASN ARG ALA LEU ASP GLU MET ARG SER VAL ASP
SEQRES 6 C 346 PRO LYS ILE GLU LEU LYS GLU SER SER PHE GLN VAL SER
SEQRES 7 C 346 PHE ALA GLU CYS TYR ASP LEU TYR PHE THR GLY VAL ARG
SEQRES 8 C 346 GLY ALA ARG ILE HIS ALA LYS TYR ILE LYS PRO LYS THR
SEQRES 9 C 346 GLU GLY LYS HIS PRO ALA LEU ILE ARG PHE HIS GLY TYR
SEQRES 10 C 346 SER SER ASN SER GLY ASP TRP ASN ASP LYS LEU ASN TYR
SEQRES 11 C 346 VAL ALA ALA GLY PHE THR VAL VAL ALA MET ASP VAL ARG
SEQRES 12 C 346 GLY GLN GLY GLY GLN SER GLN ASP VAL GLY GLY VAL THR
SEQRES 13 C 346 GLY ASN THR LEU ASN GLY HIS ILE ILE ARG GLY LEU ASP
SEQRES 14 C 346 ASP ASP ALA ASP ASN MET LEU PHE ARG HIS ILE PHE LEU
SEQRES 15 C 346 ASP THR ALA GLN LEU ALA GLY ILE VAL MET ASN MET PRO
SEQRES 16 C 346 GLU VAL ASP GLU ASP ARG VAL GLY VAL MET GLY PRO SER
SEQRES 17 C 346 GLN GLY GLY GLY LEU SER LEU ALA CYS ALA ALA LEU GLU
SEQRES 18 C 346 PRO ARG VAL ARG LYS VAL VAL SER GLU TYR PRO PHE LEU
SEQRES 19 C 346 SER ASP TYR LYS ARG VAL TRP ASP LEU ASP LEU ALA LYS
SEQRES 20 C 346 ASN ALA TYR GLN GLU ILE THR ASP TYR PHE ARG LEU PHE
SEQRES 21 C 346 ASP PRO ARG HIS GLU ARG GLU ASN GLU VAL PHE THR LYS
SEQRES 22 C 346 LEU GLY TYR ILE ASP VAL LYS ASN LEU ALA LYS ARG ILE
SEQRES 23 C 346 LYS GLY ASP VAL LEU MET CYS VAL GLY LEU MET ASP GLN
SEQRES 24 C 346 VAL CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN ASN
SEQRES 25 C 346 ILE GLN SER LYS LYS ASP ILE LYS VAL TYR PRO ASP TYR
SEQRES 26 C 346 GLY HIS GLU PRO MET ARG GLY PHE GLY ASP LEU ALA MET
SEQRES 27 C 346 GLN PHE MET LEU GLU LEU TYR SER
HET CA A 321 1
HET CA C 321 1
HETNAM CA CALCIUM ION
FORMUL 4 CA 2(CA 2+)
FORMUL 6 HOH *489(H2 O)
HELIX 1 1 PRO A 7 ARG A 12 1 6
HELIX 2 2 ASP A 23 SER A 37 1 15
HELIX 3 3 VAL A 64 GLY A 66 5 3
HELIX 4 4 TRP A 98 ASP A 100 5 3
HELIX 5 5 LYS A 101 ALA A 106 1 6
HELIX 6 6 ASP A 145 ASN A 148 5 4
HELIX 7 7 MET A 149 ASN A 167 1 19
HELIX 8 8 SER A 182 GLU A 195 1 14
HELIX 9 9 ASP A 210 LEU A 217 1 8
HELIX 10 10 LYS A 221 ALA A 223 5 3
HELIX 11 11 TYR A 224 ASP A 235 1 12
HELIX 12 12 ARG A 240 GLY A 249 1 10
HELIX 13 13 ASP A 252 ALA A 257 1 6
HELIX 14 14 LYS A 258 ILE A 260 5 3
HELIX 15 15 PRO A 276 ASN A 285 1 10
HELIX 16 16 GLY A 306 GLU A 317 1 12
HELIX 17 17 PRO B 7 ARG B 12 1 6
HELIX 18 18 ASP B 23 SER B 37 1 15
HELIX 19 19 VAL B 64 GLY B 66 5 3
HELIX 20 20 TRP B 98 ASP B 100 5 3
HELIX 21 21 LYS B 101 ALA B 106 1 6
HELIX 22 22 ASP B 145 ASN B 148 5 4
HELIX 23 23 MET B 149 MET B 166 1 18
HELIX 24 24 SER B 182 GLU B 195 1 14
HELIX 25 25 ASP B 210 LEU B 217 1 8
HELIX 26 26 LYS B 221 ALA B 223 5 3
HELIX 27 27 TYR B 224 ASP B 235 1 12
HELIX 28 28 ARG B 240 GLY B 249 1 10
HELIX 29 29 ASP B 252 ALA B 257 1 6
HELIX 30 30 LYS B 258 ILE B 260 5 3
HELIX 31 31 PRO B 276 ASN B 286 1 11
HELIX 32 32 GLY B 306 LEU B 316 1 11
HELIX 33 33 GLU B 317 TYR B 319 5 3
HELIX 34 34 PRO C 7 ARG C 12 1 6
HELIX 35 35 ASP C 23 SER C 37 1 15
HELIX 36 36 VAL C 64 GLY C 66 5 3
HELIX 37 37 TRP C 98 ASP C 100 5 3
HELIX 38 38 LYS C 101 ALA C 107 1 7
HELIX 39 39 ASP C 145 ASN C 148 5 4
HELIX 40 40 MET C 149 ASN C 167 1 19
HELIX 41 41 SER C 182 GLU C 195 1 14
HELIX 42 42 ASP C 210 LEU C 217 1 8
HELIX 43 43 LYS C 221 ALA C 223 5 3
HELIX 44 44 TYR C 224 ASP C 235 1 12
HELIX 45 45 ARG C 240 GLY C 249 1 10
HELIX 46 46 ASP C 252 ALA C 257 1 6
HELIX 47 47 LYS C 258 ILE C 260 5 3
HELIX 48 48 PRO C 276 ASN C 285 1 10
HELIX 49 49 GLY C 306 LEU C 316 1 11
HELIX 50 50 GLU C 317 TYR C 319 5 3
SHEET 1 A 9 GLU A 43 GLU A 46 0
SHEET 2 A 9 ALA A 54 THR A 62 -1 O ASP A 58 N LYS A 45
SHEET 3 A 9 ARG A 68 PRO A 76 -1 O ILE A 69 N PHE A 61
SHEET 4 A 9 THR A 110 MET A 114 -1 O VAL A 111 N ILE A 74
SHEET 5 A 9 HIS A 82 PHE A 88 1 N ARG A 87 O VAL A 112
SHEET 6 A 9 VAL A 171 PRO A 181 1 O GLY A 177 N ALA A 84
SHEET 7 A 9 LYS A 200 GLU A 204 1 O VAL A 202 N VAL A 178
SHEET 8 A 9 ASP A 263 GLY A 269 1 O LEU A 265 N VAL A 201
SHEET 9 A 9 LYS A 291 TYR A 296 1 O LYS A 294 N MET A 266
SHEET 1 B 9 GLU B 43 GLU B 46 0
SHEET 2 B 9 ALA B 54 THR B 62 -1 O ASP B 58 N LYS B 45
SHEET 3 B 9 ARG B 68 PRO B 76 -1 O ILE B 69 N PHE B 61
SHEET 4 B 9 THR B 110 MET B 114 -1 O VAL B 111 N ILE B 74
SHEET 5 B 9 HIS B 82 PHE B 88 1 N ARG B 87 O VAL B 112
SHEET 6 B 9 VAL B 171 PRO B 181 1 O GLY B 177 N ALA B 84
SHEET 7 B 9 LYS B 200 GLU B 204 1 O GLU B 204 N GLY B 180
SHEET 8 B 9 ASP B 263 GLY B 269 1 O LEU B 265 N VAL B 201
SHEET 9 B 9 LYS B 291 TYR B 296 1 O LYS B 294 N MET B 266
SHEET 1 C 9 GLU C 43 GLU C 46 0
SHEET 2 C 9 ALA C 54 THR C 62 -1 O ASP C 58 N LYS C 45
SHEET 3 C 9 ARG C 68 PRO C 76 -1 O ILE C 69 N PHE C 61
SHEET 4 C 9 THR C 110 MET C 114 -1 O VAL C 111 N ILE C 74
SHEET 5 C 9 HIS C 82 PHE C 88 1 N ARG C 87 O VAL C 112
SHEET 6 C 9 VAL C 171 PRO C 181 1 O GLY C 177 N ALA C 84
SHEET 7 C 9 LYS C 200 GLU C 204 1 O VAL C 202 N VAL C 178
SHEET 8 C 9 ASP C 263 GLY C 269 1 O LEU C 265 N VAL C 201
SHEET 9 C 9 LYS C 291 TYR C 296 1 O TYR C 296 N VAL C 268
LINK O GLU A 317 CA CA A 321 1555 1555 2.62
LINK O TYR A 319 CA CA A 321 1555 1555 2.52
LINK O GLU C 317 CA CA C 321 1555 1555 2.46
LINK O TYR C 319 CA CA C 321 1555 1555 2.49
LINK CA CA A 321 O HOH A 395 1555 1555 2.74
LINK CA CA C 321 O HOH C 417 1555 1555 2.89
SITE 1 AC1 3 GLU A 317 TYR A 319 HOH A 395
SITE 1 AC2 7 GLU B 317 TYR B 319 HOH B 321 HOH B 348
SITE 2 AC2 7 GLU C 317 TYR C 319 HOH C 417
CRYST1 132.263 132.263 112.914 90.00 90.00 120.00 P 32 2 1 18
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 0.007561 0.004365 0.000000 0.00000
SCALE2 0.000000 0.008730 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008856 0.00000
TER 2525 SER A 320
TER 5050 SER B 320
TER 7575 SER C 320
MASTER 431 0 2 50 27 0 3 6 8063 3 8 81
END |