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HEADER HYDROLASE 03-SEP-20 7CY3
TITLE CRYSTAL STRUCTURE OF A BIODEGRADABLE PLASTIC-DEGRADING CUTINASE FROM
TITLE 2 PARAPHOMA SP. B47-9.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CUTINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.74
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARAPHOMA SP. B47-9;
SOURCE 3 ORGANISM_TAXID: 1804209
KEYWDS SERINE HYDROLASE, CUTINASE, BIODEGRADABLE PLASTIC-DEGRADING ENZYME,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SUZUKI,M.KOITABASHI
REVDAT 1 30-SEP-20 7CY3 0
JRNL AUTH K.SUZUKI,M.KOITABASHI
JRNL TITL CRYSTAL STRUCTURE OF A BIODEGRADABLE PLASTIC-DEGRADING
JRNL TITL 2 CUTINASE FROM PARAPHOMA SP. B47-9.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 3 NUMBER OF REFLECTIONS : 64992
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) : 0.126
REMARK 3 R VALUE (WORKING SET) : 0.124
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3328
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) : 1.27
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.30
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4557
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.1860
REMARK 3 BIN FREE R VALUE SET COUNT : 268
REMARK 3 BIN FREE R VALUE : 0.2440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2787
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 399
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.13000
REMARK 3 B22 (A**2) : -0.22000
REMARK 3 B33 (A**2) : 0.04000
REMARK 3 B12 (A**2) : 0.08000
REMARK 3 B13 (A**2) : -0.17000
REMARK 3 B23 (A**2) : 0.10000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.049
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.053
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.031
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.639
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2850 ; 0.016 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2642 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3877 ; 1.985 ; 1.642
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6113 ; 1.730 ; 1.582
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 386 ; 6.308 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 133 ;35.773 ;22.030
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 425 ;12.400 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;15.292 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 376 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3302 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 570 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2850 ; 3.672 ; 3.000
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 7CY3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-SEP-20.
REMARK 100 THE DEPOSITION ID IS D_1300018387.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-10
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 : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 0.6.0
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68333
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.270
REMARK 200 RESOLUTION RANGE LOW (A) : 36.720
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.5
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
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: 1CEX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE, 0.1M SODIUM
REMARK 280 CACODYLATE, 1MM CALCIUM CHLORIDE, 30% W/V POLYETHYLENE GLYCOL
REMARK 280 8000, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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
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 TOTAL BURIED SURFACE AREA: 130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 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 PCA A 1
REMARK 465 VAL A 2
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 O2 CAD A 202 O HOH A 301 1.40
REMARK 500 O HOH B 523 O HOH B 597 1.87
REMARK 500 AS CAD A 202 O HOH A 301 1.88
REMARK 500 C2 CAD A 202 O HOH A 303 2.06
REMARK 500 O HOH A 356 O HOH A 434 2.19
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 C1 CAD A 202 O1 CAD B 301 1565 1.67
REMARK 500 O2 CAD A 202 O HOH B 462 1565 2.10
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 184 CD GLU A 184 OE1 -0.077
REMARK 500 ASN B 195 C ASN B 195 O 0.161
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 TYR A 135 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 142 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ASN B 195 CA - C - O ANGL. DEV. = -23.3 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 ASN A 16 52.29 -141.93
REMARK 500 THR A 29 -1.20 70.37
REMARK 500 SER A 106 -127.26 69.39
REMARK 500 ASN A 183 -85.00 -130.23
REMARK 500 ASN B 16 47.03 -142.06
REMARK 500 THR B 29 -5.13 76.19
REMARK 500 SER B 106 -128.14 66.38
REMARK 500 ASN B 183 -86.59 -132.66
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 NA A 203 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 8 OE1
REMARK 620 2 GLU A 8 OE2 49.5
REMARK 620 3 GLU A 46 OE1 89.6 93.9
REMARK 620 4 ALA A 51 O 163.3 140.6 101.3
REMARK 620 5 VAL A 54 O 84.4 129.0 108.0 80.2
REMARK 620 6 HOH A 349 O 112.9 63.9 87.4 80.6 157.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 204 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 176 O
REMARK 620 2 ASP A 179 OD1 71.9
REMARK 620 3 ASP A 179 OD2 123.8 53.0
REMARK 620 4 GLU A 180 OE1 83.5 76.8 74.8
REMARK 620 5 GLU A 180 OE2 125.6 119.7 79.8 53.9
REMARK 620 6 HOH A 351 O 81.5 153.4 152.2 99.6 75.3
REMARK 620 7 HOH A 441 O 79.1 84.1 103.3 157.4 148.6 91.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 8 OE1
REMARK 620 2 GLU B 46 OE2 96.4
REMARK 620 3 ALA B 51 O 164.2 97.0
REMARK 620 4 VAL B 54 O 86.3 104.6 82.3
REMARK 620 5 HOH B 500 O 100.3 83.6 89.4 168.9
REMARK 620 6 HOH B 559 O 87.8 163.3 81.6 91.8 79.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 176 O
REMARK 620 2 ASP B 179 OD1 72.4
REMARK 620 3 ASP B 179 OD2 123.1 50.7
REMARK 620 4 GLU B 180 OE1 89.9 83.4 84.4
REMARK 620 5 GLU B 180 OE2 134.2 114.8 78.7 49.5
REMARK 620 6 HOH B 414 O 84.2 156.3 152.5 100.6 84.1
REMARK 620 7 HOH B 457 O 157.0 114.8 67.7 112.2 64.6 85.5
REMARK 620 8 HOH B 540 O 78.6 75.8 86.7 158.4 146.7 96.4 82.2
REMARK 620 N 1 2 3 4 5 6 7
DBREF1 7CY3 A 1 195 UNP A0A060N399_9PLEO
DBREF2 7CY3 A A0A060N399 33 227
DBREF1 7CY3 B 1 195 UNP A0A060N399_9PLEO
DBREF2 7CY3 B A0A060N399 33 227
SEQRES 1 A 195 PCA VAL GLY SER SER LYS ASN GLU LEU GLU THR GLY SER
SEQRES 2 A 195 ALA SER ASN CYS PRO LYS ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 A 195 GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY ALA
SEQRES 4 A 195 PRO LEU GLY ASP ALA LEU GLU SER ARG TYR GLY ALA SER
SEQRES 5 A 195 ASN VAL TRP VAL GLN GLY VAL GLY GLY PRO TYR ASP ALA
SEQRES 6 A 195 ALA LEU GLY ASP ASN ALA LEU PRO ARG GLY SER SER ALA
SEQRES 7 A 195 ALA ALA ILE ARG GLU GLY VAL ARG LEU LEU ASN LEU ALA
SEQRES 8 A 195 ASN SER LYS CYS PRO ASN SER LYS VAL VAL ALA GLY GLY
SEQRES 9 A 195 TYR SER GLN GLY ALA ALA LEU ALA ALA ALA ALA ILE SER
SEQRES 10 A 195 ASP ALA SER THR THR VAL ARG ASN GLN ILE VAL GLY THR
SEQRES 11 A 195 VAL LEU PHE GLY TYR THR LYS ASN GLN GLN ASN ARG GLY
SEQRES 12 A 195 GLY ILE PRO GLY TYR PRO GLN ASP ARG LEU ARG VAL TYR
SEQRES 13 A 195 CYS ALA VAL GLY ASP LEU VAL CYS GLU GLY THR LEU ILE
SEQRES 14 A 195 VAL LEU ALA PRO HIS LEU SER TYR GLY ASP GLU ALA ARG
SEQRES 15 A 195 ASN GLU ALA PRO ALA PHE LEU ILE SER LYS ILE GLY ASN
SEQRES 1 B 195 PCA VAL GLY SER SER LYS ASN GLU LEU GLU THR GLY SER
SEQRES 2 B 195 ALA SER ASN CYS PRO LYS ALA ILE LEU ILE PHE ALA ARG
SEQRES 3 B 195 GLY SER THR GLU THR GLY ASN LEU GLY THR LEU GLY ALA
SEQRES 4 B 195 PRO LEU GLY ASP ALA LEU GLU SER ARG TYR GLY ALA SER
SEQRES 5 B 195 ASN VAL TRP VAL GLN GLY VAL GLY GLY PRO TYR ASP ALA
SEQRES 6 B 195 ALA LEU GLY ASP ASN ALA LEU PRO ARG GLY SER SER ALA
SEQRES 7 B 195 ALA ALA ILE ARG GLU GLY VAL ARG LEU LEU ASN LEU ALA
SEQRES 8 B 195 ASN SER LYS CYS PRO ASN SER LYS VAL VAL ALA GLY GLY
SEQRES 9 B 195 TYR SER GLN GLY ALA ALA LEU ALA ALA ALA ALA ILE SER
SEQRES 10 B 195 ASP ALA SER THR THR VAL ARG ASN GLN ILE VAL GLY THR
SEQRES 11 B 195 VAL LEU PHE GLY TYR THR LYS ASN GLN GLN ASN ARG GLY
SEQRES 12 B 195 GLY ILE PRO GLY TYR PRO GLN ASP ARG LEU ARG VAL TYR
SEQRES 13 B 195 CYS ALA VAL GLY ASP LEU VAL CYS GLU GLY THR LEU ILE
SEQRES 14 B 195 VAL LEU ALA PRO HIS LEU SER TYR GLY ASP GLU ALA ARG
SEQRES 15 B 195 ASN GLU ALA PRO ALA PHE LEU ILE SER LYS ILE GLY ASN
MODRES 7CY3 PCA B 1 GLN MODIFIED RESIDUE
HET PCA B 1 8
HET CAD A 201 5
HET CAD A 202 5
HET NA A 203 1
HET NA A 204 1
HET CAD B 301 5
HET CAD B 302 5
HET NA B 303 1
HET NA B 304 1
HETNAM PCA PYROGLUTAMIC ACID
HETNAM CAD CACODYLIC ACID
HETNAM NA SODIUM ION
HETSYN CAD HYDROXYDIMETHYLARSINE OXIDE
FORMUL 2 PCA C5 H7 N O3
FORMUL 3 CAD 4(C2 H7 AS O2)
FORMUL 5 NA 4(NA 1+)
FORMUL 11 HOH *399(H2 O)
HELIX 1 AA1 ASN A 7 GLY A 12 1 6
HELIX 2 AA2 LEU A 34 GLY A 50 1 17
HELIX 3 AA3 ALA A 66 LEU A 72 5 7
HELIX 4 AA4 SER A 77 CYS A 95 1 19
HELIX 5 AA5 SER A 106 ALA A 119 1 14
HELIX 6 AA6 SER A 120 GLN A 126 1 7
HELIX 7 AA7 PRO A 149 ASP A 151 5 3
HELIX 8 AA8 ASP A 161 GLY A 166 5 6
HELIX 9 AA9 LEU A 171 SER A 176 5 6
HELIX 10 AB1 TYR A 177 ASN A 183 1 7
HELIX 11 AB2 ASN A 183 GLY A 194 1 12
HELIX 12 AB3 ASN B 7 GLY B 12 1 6
HELIX 13 AB4 LEU B 37 GLY B 50 1 14
HELIX 14 AB5 ALA B 66 SER B 76 5 11
HELIX 15 AB6 SER B 77 CYS B 95 1 19
HELIX 16 AB7 SER B 106 ALA B 119 1 14
HELIX 17 AB8 SER B 120 GLN B 126 1 7
HELIX 18 AB9 PRO B 149 ASP B 151 5 3
HELIX 19 AC1 ASP B 161 GLY B 166 5 6
HELIX 20 AC2 LEU B 171 SER B 176 5 6
HELIX 21 AC3 TYR B 177 ASN B 183 1 7
HELIX 22 AC4 ASN B 183 GLY B 194 1 12
SHEET 1 AA1 5 VAL A 54 GLY A 58 0
SHEET 2 AA1 5 ALA A 20 ALA A 25 1 N LEU A 22 O TRP A 55
SHEET 3 AA1 5 LYS A 99 TYR A 105 1 O VAL A 101 N ILE A 21
SHEET 4 AA1 5 ILE A 127 PHE A 133 1 O PHE A 133 N GLY A 104
SHEET 5 AA1 5 LEU A 153 TYR A 156 1 O TYR A 156 N LEU A 132
SHEET 1 AA2 2 LEU A 168 ILE A 169 0
SHEET 2 AA2 2 ILE B 169 VAL B 170 1 O VAL B 170 N LEU A 168
SHEET 1 AA3 5 VAL B 54 GLY B 58 0
SHEET 2 AA3 5 ALA B 20 ALA B 25 1 N LEU B 22 O TRP B 55
SHEET 3 AA3 5 LYS B 99 TYR B 105 1 O VAL B 101 N ILE B 21
SHEET 4 AA3 5 ILE B 127 PHE B 133 1 O PHE B 133 N GLY B 104
SHEET 5 AA3 5 LEU B 153 TYR B 156 1 O TYR B 156 N LEU B 132
SSBOND 1 CYS A 17 CYS A 95 1555 1555 2.06
SSBOND 2 CYS A 157 CYS A 164 1555 1555 2.04
SSBOND 3 CYS B 17 CYS B 95 1555 1555 2.06
SSBOND 4 CYS B 157 CYS B 164 1555 1555 2.02
LINK C PCA B 1 N VAL B 2 1555 1555 1.34
LINK OE1 GLU A 8 NA NA A 203 1555 1555 2.38
LINK OE2 GLU A 8 NA NA A 203 1555 1555 2.74
LINK OE1 GLU A 46 NA NA A 203 1555 1555 2.36
LINK O ALA A 51 NA NA A 203 1555 1555 2.33
LINK O VAL A 54 NA NA A 203 1555 1555 2.33
LINK O SER A 176 NA NA A 204 1555 1555 2.49
LINK OD1 ASP A 179 NA NA A 204 1555 1555 2.45
LINK OD2 ASP A 179 NA NA A 204 1555 1555 2.60
LINK OE1 GLU A 180 NA NA A 204 1555 1555 2.39
LINK OE2 GLU A 180 NA NA A 204 1555 1555 2.54
LINK NA NA A 203 O HOH A 349 1555 1555 2.42
LINK NA NA A 204 O HOH A 351 1555 1555 2.43
LINK NA NA A 204 O HOH A 441 1555 1555 2.44
LINK OE1 GLU B 8 NA NA B 303 1555 1555 2.46
LINK OE2 GLU B 46 NA NA B 303 1555 1555 2.34
LINK O ALA B 51 NA NA B 303 1555 1555 2.39
LINK O VAL B 54 NA NA B 303 1555 1555 2.32
LINK O SER B 176 NA NA B 304 1555 1555 2.43
LINK OD1 ASP B 179 NA NA B 304 1555 1555 2.36
LINK OD2 ASP B 179 NA NA B 304 1555 1555 2.81
LINK OE1 GLU B 180 NA NA B 304 1555 1555 2.42
LINK OE2 GLU B 180 NA NA B 304 1555 1555 2.75
LINK NA NA B 303 O HOH B 500 1555 1555 2.34
LINK NA NA B 303 O HOH B 559 1555 1555 2.41
LINK NA NA B 304 O HOH B 414 1555 1555 2.38
LINK NA NA B 304 O HOH B 457 1555 1555 2.39
LINK NA NA B 304 O HOH B 540 1555 1555 2.48
CRYST1 34.886 43.517 51.724 103.78 92.42 101.49 P 1 2
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 0.028665 0.005825 0.002765 0.00000
SCALE2 0.000000 0.023449 0.006101 0.00000
SCALE3 0.000000 0.000000 0.019995 0.00000
TER 1387 ASN A 195
TER 2789 ASN B 195
MASTER 400 0 9 22 12 0 0 6 3210 2 72 30
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