| content |
HEADER HYDROLASE 12-AUG-17 6ANE
TITLE CRYSTAL STRUCTURE OF IDEONELLA SAKAIENSIS PET HYDROLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: RESIDUES 28-290;
COMPND 5 SYNONYM: PETASE;
COMPND 6 EC: 3.1.1.101;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN 201-F6);
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 STRAIN: 201-F6;
SOURCE 5 GENE: ISF6_4831;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24B
KEYWDS PETASE, AB HYDROLASE, CUTINASE, PLASTIC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.GALAZ-DAVISON,M.SOTOMAYOR,L.P.PARRA,C.A.RAMIREZ-SARMIENTO
REVDAT 1 18-APR-18 6ANE 0
JRNL AUTH T.FECKER,P.GALAZ-DAVISON,F.ENGELBERGER,Y.NARUI,M.SOTOMAYOR,
JRNL AUTH 2 L.P.PARRA,C.A.RAMIREZ-SARMIENTO
JRNL TITL ACTIVE SITE FLEXIBILITY AS A HALLMARK FOR EFFICIENT PET
JRNL TITL 2 DEGRADATION BY I. SAKAIENSIS PETASE.
JRNL REF BIOPHYS. J. V. 114 1302 2018
JRNL REFN ESSN 1542-0086
JRNL PMID 29590588
JRNL DOI 10.1016/J.BPJ.2018.02.005
REMARK 2
REMARK 2 RESOLUTION. 2.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 116.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 61680
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3205
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) : 2.02
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4259
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE SET COUNT : 232
REMARK 3 BIN FREE R VALUE : 0.2930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5786
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 474
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.00000
REMARK 3 B22 (A**2) : -1.79000
REMARK 3 B33 (A**2) : -0.21000
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): 0.153
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.102
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.865
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5955 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5230 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8123 ; 1.508 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12171 ; 1.006 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 788 ; 6.568 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 234 ;33.910 ;23.504
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 866 ;11.597 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 39 ;13.062 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 892 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6819 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1236 ; 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): 3149 ; 1.275 ; 2.079
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3148 ; 1.272 ; 2.079
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3932 ; 1.918 ; 3.108
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3933 ; 1.918 ; 3.109
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2806 ; 1.565 ; 2.229
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2806 ; 1.564 ; 2.229
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4190 ; 2.382 ; 3.291
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6871 ; 3.631 ;25.281
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6779 ; 3.564 ;25.080
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 6ANE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1000229494.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-17
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-003
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.541870
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 200K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67721
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 116.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.10400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.8300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.65300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
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: 4CG1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5 1.6 M MGSO4 20%
REMARK 280 GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.53800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.53800
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 1.000000 0.000000 0.000000 26.43400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 116.92600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.43400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 116.92600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 82.53800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.43400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 116.92600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 82.53800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.43400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 116.92600
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
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: 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: 3
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: 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 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 0
REMARK 465 GLN A 1
REMARK 465 LEU A 264
REMARK 465 GLU A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 HIS A 271
REMARK 465 MET B 0
REMARK 465 GLN B 1
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 465 HIS B 271
REMARK 465 MET C 0
REMARK 465 GLN C 1
REMARK 465 SER C 263
REMARK 465 LEU C 264
REMARK 465 GLU C 265
REMARK 465 HIS C 266
REMARK 465 HIS C 267
REMARK 465 HIS C 268
REMARK 465 HIS C 269
REMARK 465 HIS C 270
REMARK 465 HIS C 271
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 ARG A 32 70.49 -119.09
REMARK 500 THR A 61 -0.87 67.47
REMARK 500 SER A 133 -125.20 67.01
REMARK 500 ALA A 156 51.94 39.29
REMARK 500 SER A 187 -83.87 -137.18
REMARK 500 ASN B 46 71.28 46.96
REMARK 500 SER B 133 -121.25 67.67
REMARK 500 ALA B 153 66.15 -150.30
REMARK 500 SER B 187 -78.65 -128.94
REMARK 500 THR C 61 -9.85 72.32
REMARK 500 SER C 133 -116.57 65.49
REMARK 500 SER C 187 -84.37 -134.96
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 MG C 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 541 O
REMARK 620 2 HOH C 464 O 162.8
REMARK 620 3 HOH C 425 O 95.8 100.8
REMARK 620 4 HOH C 425 O 87.2 75.7 168.3
REMARK 620 5 HOH C 464 O 87.8 89.2 86.0 82.8
REMARK 620 6 HOH C 541 O 84.4 94.2 108.5 83.1 164.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 301
DBREF1 6ANE A 1 263 UNP PETH_IDESA
DBREF2 6ANE A A0A0K8P6T7 28 290
DBREF1 6ANE B 1 263 UNP PETH_IDESA
DBREF2 6ANE B A0A0K8P6T7 28 290
DBREF1 6ANE C 1 263 UNP PETH_IDESA
DBREF2 6ANE C A0A0K8P6T7 28 290
SEQADV 6ANE MET A 0 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 6ANE LEU A 264 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE GLU A 265 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS A 266 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS A 267 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS A 268 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS A 269 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS A 270 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS A 271 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE MET B 0 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 6ANE LEU B 264 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE GLU B 265 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS B 266 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS B 267 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS B 268 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS B 269 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS B 270 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS B 271 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE MET C 0 UNP A0A0K8P6T INITIATING METHIONINE
SEQADV 6ANE LEU C 264 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE GLU C 265 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS C 266 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS C 267 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS C 268 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS C 269 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS C 270 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6ANE HIS C 271 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 272 MET GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 A 272 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 A 272 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 4 A 272 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 5 A 272 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 6 A 272 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 A 272 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 A 272 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 A 272 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 A 272 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 11 A 272 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 A 272 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 13 A 272 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 A 272 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 15 A 272 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 16 A 272 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 17 A 272 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 18 A 272 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 A 272 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 20 A 272 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 21 A 272 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 272 MET GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 B 272 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 B 272 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 4 B 272 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 5 B 272 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 6 B 272 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 B 272 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 B 272 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 B 272 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 B 272 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 11 B 272 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 B 272 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 13 B 272 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 B 272 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 15 B 272 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 16 B 272 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 17 B 272 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 18 B 272 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 B 272 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 20 B 272 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 21 B 272 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 272 MET GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 C 272 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 C 272 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 4 C 272 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 5 C 272 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 6 C 272 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 C 272 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 C 272 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 C 272 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 C 272 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 11 C 272 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 C 272 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 13 C 272 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 C 272 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 15 C 272 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 16 C 272 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 17 C 272 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 18 C 272 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 C 272 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 20 C 272 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 21 C 272 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
HET MG C 301 1
HETNAM MG MAGNESIUM ION
FORMUL 4 MG MG 2+
FORMUL 5 HOH *474(H2 O)
HELIX 1 AA1 THR A 12 ALA A 18 1 7
HELIX 2 AA2 ARG A 63 LYS A 68 1 6
HELIX 3 AA3 TRP A 69 PHE A 79 1 11
HELIX 4 AA4 GLN A 92 GLY A 112 1 21
HELIX 5 AA5 SER A 133 ASN A 146 1 14
HELIX 6 AA6 PRO A 183 SER A 186 5 4
HELIX 7 AA7 SER A 187 MET A 195 1 9
HELIX 8 AA8 ASN A 219 ASP A 236 1 18
HELIX 9 AA9 ASP A 238 ARG A 240 5 3
HELIX 10 AB1 TYR A 241 GLU A 247 1 7
HELIX 11 AB2 THR B 12 ALA B 18 1 7
HELIX 12 AB3 ARG B 63 LYS B 68 5 6
HELIX 13 AB4 TRP B 69 SER B 76 1 8
HELIX 14 AB5 GLN B 92 GLY B 112 1 21
HELIX 15 AB6 SER B 133 ASN B 146 1 14
HELIX 16 AB7 SER B 187 MET B 195 1 9
HELIX 17 AB8 ASN B 219 ASP B 236 1 18
HELIX 18 AB9 ASP B 238 ARG B 240 5 3
HELIX 19 AC1 TYR B 241 GLU B 247 1 7
HELIX 20 AC2 THR C 12 ALA C 18 1 7
HELIX 21 AC3 ARG C 63 LYS C 68 5 6
HELIX 22 AC4 TRP C 69 PHE C 79 1 11
HELIX 23 AC5 GLN C 92 GLY C 112 1 21
HELIX 24 AC6 SER C 133 ASN C 146 1 14
HELIX 25 AC7 PRO C 183 SER C 186 5 4
HELIX 26 AC8 SER C 187 MET C 195 1 9
HELIX 27 AC9 ASN C 219 ASP C 236 1 18
HELIX 28 AD1 ASP C 238 ARG C 240 5 3
HELIX 29 AD2 TYR C 241 GLU C 247 1 7
SHEET 1 AA1 6 VAL A 25 THR A 29 0
SHEET 2 AA1 6 ALA A 38 PRO A 44 -1 O VAL A 41 N PHE A 28
SHEET 3 AA1 6 VAL A 80 ASP A 85 -1 O VAL A 81 N TYR A 42
SHEET 4 AA1 6 VAL A 51 VAL A 57 1 N ILE A 56 O ILE A 82
SHEET 5 AA1 6 VAL A 122 GLY A 131 1 O ASP A 123 N VAL A 51
SHEET 6 AA1 6 ALA A 151 ALA A 152 1 O ALA A 151 N VAL A 129
SHEET 1 AA2 3 THR A 171 CYS A 176 0
SHEET 2 AA2 3 LYS A 200 ILE A 205 1 O GLN A 201 N ILE A 173
SHEET 3 AA2 3 VAL A 254 ALA A 260 -1 O ASP A 256 N GLU A 204
SHEET 1 AA3 6 VAL B 25 THR B 29 0
SHEET 2 AA3 6 ALA B 38 PRO B 44 -1 O VAL B 41 N PHE B 28
SHEET 3 AA3 6 VAL B 80 ASP B 85 -1 O VAL B 81 N TYR B 42
SHEET 4 AA3 6 VAL B 51 VAL B 57 1 N ILE B 54 O ILE B 82
SHEET 5 AA3 6 VAL B 122 TRP B 132 1 O ASP B 123 N VAL B 51
SHEET 6 AA3 6 ALA B 151 GLN B 155 1 O GLN B 155 N GLY B 131
SHEET 1 AA4 3 THR B 171 CYS B 176 0
SHEET 2 AA4 3 LYS B 200 ILE B 205 1 O GLN B 201 N ILE B 173
SHEET 3 AA4 3 VAL B 254 ALA B 260 -1 O ARG B 258 N PHE B 202
SHEET 1 AA5 6 VAL C 25 THR C 29 0
SHEET 2 AA5 6 ALA C 38 PRO C 44 -1 O VAL C 41 N PHE C 28
SHEET 3 AA5 6 VAL C 80 ASP C 85 -1 O VAL C 81 N TYR C 42
SHEET 4 AA5 6 VAL C 51 VAL C 57 1 N ILE C 56 O ILE C 82
SHEET 5 AA5 6 VAL C 122 TRP C 132 1 O GLY C 128 N ALA C 53
SHEET 6 AA5 6 ALA C 151 GLN C 155 1 O GLN C 155 N GLY C 131
SHEET 1 AA6 3 THR C 171 CYS C 176 0
SHEET 2 AA6 3 LYS C 200 ILE C 205 1 O GLN C 201 N ILE C 173
SHEET 3 AA6 3 VAL C 254 ALA C 260 -1 O ASP C 256 N GLU C 204
SSBOND 1 CYS A 176 CYS A 212 1555 1555 2.04
SSBOND 2 CYS A 246 CYS A 262 1555 1555 2.05
SSBOND 3 CYS B 176 CYS B 212 1555 1555 2.07
SSBOND 4 CYS B 246 CYS B 262 1555 1555 2.05
SSBOND 5 CYS C 176 CYS C 212 1555 1555 2.03
SSBOND 6 CYS C 246 CYS C 262 1555 1555 2.08
LINK MG MG C 301 O HOH C 541 1555 1555 2.00
LINK MG MG C 301 O HOH C 464 1555 1555 2.03
LINK MG MG C 301 O HOH C 425 1555 1555 1.93
LINK MG MG C 301 O HOH C 425 1555 3554 2.46
LINK MG MG C 301 O HOH C 464 1555 3554 2.14
LINK MG MG C 301 O HOH C 541 1555 3554 1.89
SITE 1 AC1 3 HOH C 425 HOH C 464 HOH C 541
CRYST1 52.868 233.852 165.076 90.00 90.00 90.00 C 2 2 21 24
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 0.018915 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004276 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006058 0.00000
TER 1926 SER A 263
TER 3880 GLU B 265
TER 5811 CYS C 262
MASTER 355 0 1 29 27 0 1 6 6261 3 16 63
END |