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HEADER HYDROLASE 02-SEP-14 3WYN
TITLE STRUCTURE OF CALCIUM BOUND CUTINASE EST119 FROM THERMOBIFIDA ALBA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA ALBA;
SOURCE 3 ORGANISM_TAXID: 53522;
SOURCE 4 STRAIN: AHK119;
SOURCE 5 GENE: EST2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE80L-EST119
KEYWDS ALPHA/BETA-HYDROLASE FOLD, ESTERASE, POLYETHYLENE TEREPHTHALATE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KITADOKORO,U.THUMARAT,F.KAWAI
REVDAT 1 24-SEP-14 3WYN 0
JRNL AUTH K.KITADOKORO,U.THUMARAT,F.KAWAI
JRNL TITL STRUCTURE OF CALCIUM BOUND CUTINASE EST119 FROM THERMOBIFIDA
JRNL TITL 2 ALBA.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 48769
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2609
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) : 1.68
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.73
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3080
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.3750
REMARK 3 BIN FREE R VALUE SET COUNT : 155
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4012
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 425
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.82000
REMARK 3 B22 (A**2) : -0.65000
REMARK 3 B33 (A**2) : 2.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.36000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.128
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.112
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.327
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4138 ; 0.023 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5629 ; 2.416 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 518 ; 7.266 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 183 ;32.702 ;22.787
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 624 ;13.082 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;16.185 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 612 ; 0.165 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3202 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 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): 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 : 2
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 38 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2598 -26.5843 23.7553
REMARK 3 T TENSOR
REMARK 3 T11: 0.0315 T22: 0.0636
REMARK 3 T33: 0.0552 T12: -0.0013
REMARK 3 T13: 0.0397 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.2779 L22: 0.3604
REMARK 3 L33: 0.2837 L12: 0.0645
REMARK 3 L13: 0.2664 L23: -0.0354
REMARK 3 S TENSOR
REMARK 3 S11: -0.0233 S12: 0.0049 S13: 0.0009
REMARK 3 S21: -0.0316 S22: 0.0144 S23: -0.0099
REMARK 3 S31: -0.0101 S32: 0.0052 S33: 0.0089
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 40 B 300
REMARK 3 ORIGIN FOR THE GROUP (A): 21.9594 -0.3960 3.0262
REMARK 3 T TENSOR
REMARK 3 T11: 0.0217 T22: 0.0428
REMARK 3 T33: 0.0354 T12: -0.0043
REMARK 3 T13: 0.0245 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.3214 L22: 0.3423
REMARK 3 L33: 0.8175 L12: -0.0112
REMARK 3 L13: 0.4622 L23: -0.1475
REMARK 3 S TENSOR
REMARK 3 S11: -0.0304 S12: 0.0038 S13: 0.0102
REMARK 3 S21: 0.0139 S22: 0.0098 S23: 0.0028
REMARK 3 S31: -0.0451 S32: 0.0402 S33: 0.0206
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: NULL
REMARK 4
REMARK 4 3WYN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-SEP-14.
REMARK 100 THE RCSB ID CODE IS RCSB096957.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48769
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.05700
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) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.24300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 15.000
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 3VIS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% (W/V) PEG 3000, 0.2M SODIUM
REMARK 280 CHLORIDE, 0.1M SODIUM POTASSIUM PHOSPHATE , PH 6.2, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 50.73650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.87000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 50.73650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 43.87000
REMARK 290 SMTRY3 4 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 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 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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 VAL A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 PRO A 6
REMARK 465 ARG A 7
REMARK 465 ARG A 8
REMARK 465 GLU A 9
REMARK 465 THR A 10
REMARK 465 SER A 11
REMARK 465 LEU A 12
REMARK 465 LEU A 13
REMARK 465 SER A 14
REMARK 465 ARG A 15
REMARK 465 ALA A 16
REMARK 465 LEU A 17
REMARK 465 ARG A 18
REMARK 465 ALA A 19
REMARK 465 THR A 20
REMARK 465 ALA A 21
REMARK 465 ALA A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 THR A 25
REMARK 465 ALA A 26
REMARK 465 VAL A 27
REMARK 465 VAL A 28
REMARK 465 ALA A 29
REMARK 465 THR A 30
REMARK 465 VAL A 31
REMARK 465 ALA A 32
REMARK 465 LEU A 33
REMARK 465 ALA A 34
REMARK 465 ALA A 35
REMARK 465 PRO A 36
REMARK 465 ALA A 37
REMARK 465 GLY A 286
REMARK 465 LEU A 287
REMARK 465 LEU A 288
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 VAL B 3
REMARK 465 THR B 4
REMARK 465 THR B 5
REMARK 465 PRO B 6
REMARK 465 ARG B 7
REMARK 465 ARG B 8
REMARK 465 GLU B 9
REMARK 465 THR B 10
REMARK 465 SER B 11
REMARK 465 LEU B 12
REMARK 465 LEU B 13
REMARK 465 SER B 14
REMARK 465 ARG B 15
REMARK 465 ALA B 16
REMARK 465 LEU B 17
REMARK 465 ARG B 18
REMARK 465 ALA B 19
REMARK 465 THR B 20
REMARK 465 ALA B 21
REMARK 465 ALA B 22
REMARK 465 ALA B 23
REMARK 465 ALA B 24
REMARK 465 THR B 25
REMARK 465 ALA B 26
REMARK 465 VAL B 27
REMARK 465 VAL B 28
REMARK 465 ALA B 29
REMARK 465 THR B 30
REMARK 465 VAL B 31
REMARK 465 ALA B 32
REMARK 465 LEU B 33
REMARK 465 ALA B 34
REMARK 465 ALA B 35
REMARK 465 PRO B 36
REMARK 465 ALA B 37
REMARK 465 GLN B 38
REMARK 465 ALA B 39
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 O ILE B 252 O HOH B 672 1.76
REMARK 500 O PHE B 300 O HOH B 686 1.92
REMARK 500 O HOH B 658 O HOH B 682 1.94
REMARK 500 CZ2 TRP A 108 O HOH A 675 1.96
REMARK 500 C ILE B 252 O HOH B 672 2.06
REMARK 500 C PHE A 300 O HOH A 659 2.07
REMARK 500 CH2 TRP A 108 O HOH A 675 2.14
REMARK 500 CZ2 TRP B 108 O HOH B 672 2.19
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 GLY A 117 N GLY A 117 CA 0.100
REMARK 500 GLY A 173 C GLY A 173 O 0.102
REMARK 500 THR A 175 C THR A 175 O 0.127
REMARK 500 MET A 259 C MET A 259 O 0.120
REMARK 500 ALA A 263 C ALA A 263 O 0.120
REMARK 500 TRP A 264 CZ3 TRP A 264 CH2 0.101
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 ARG A 45 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 SER A 96 CB - CA - C ANGL. DEV. = -11.7 DEGREES
REMARK 500 ARG A 112 NE - CZ - NH1 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ILE A 210 CG1 - CB - CG2 ANGL. DEV. = -14.9 DEGREES
REMARK 500 LYS A 225 CD - CE - NZ ANGL. DEV. = -14.3 DEGREES
REMARK 500 ARG B 267 NE - CZ - NH2 ANGL. DEV. = -4.4 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 SER A 169 -114.61 56.37
REMARK 500 THR A 192 68.05 38.99
REMARK 500 HIS A 223 -83.51 -122.33
REMARK 500 THR A 253 124.35 -31.38
REMARK 500 THR A 297 43.53 -100.03
REMARK 500 THR B 100 -2.81 67.03
REMARK 500 SER B 169 -114.52 58.30
REMARK 500 HIS B 223 -84.45 -126.38
REMARK 500 THR B 253 118.48 -35.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU B 288 SER B 289 -145.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ILE A 210 -10.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 627 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH A 689 DISTANCE = 5.74 ANGSTROMS
REMARK 525 HOH A 710 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A 711 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH A 712 DISTANCE = 6.61 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 2PE B 401
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 292 OE1
REMARK 620 2 ASP B 243 OD1 78.7
REMARK 620 3 GLU B 213 OE1 77.0 80.7
REMARK 620 4 HOH B 600 O 125.0 70.7 137.4
REMARK 620 5 GLU B 213 OE2 66.7 122.7 48.7 165.5
REMARK 620 6 HOH B 678 O 169.3 106.5 94.4 65.7 102.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 292 OE1
REMARK 620 2 HOH A 504 O 161.5
REMARK 620 3 ASP A 243 OD1 90.5 98.0
REMARK 620 4 GLU A 213 OE2 81.8 79.9 126.9
REMARK 620 5 GLU A 213 OE1 88.3 77.2 79.5 48.0
REMARK 620 6 HOH A 501 O 56.0 139.6 91.1 124.3 143.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 670 O
REMARK 620 2 HOH B 700 O 89.8
REMARK 620 3 THR B 297 O 115.7 129.9
REMARK 620 4 PRO B 299 O 159.3 70.6 83.0
REMARK 620 5 HOH B 647 O 94.7 73.3 139.0 73.9
REMARK 620 6 ASP B 236 OD1 90.8 143.7 81.6 101.1 70.5
REMARK 620 7 HOH B 592 O 84.4 71.1 69.6 95.0 144.3 145.0
REMARK 620 N 1 2 3 4 5 6
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PE B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VIS RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH CALCIUM.
DBREF 3WYN A 1 300 UNP F7IX06 F7IX06_9ACTO 1 300
DBREF 3WYN B 1 300 UNP F7IX06 F7IX06_9ACTO 1 300
SEQADV 3WYN HIS A -5 UNP F7IX06 EXPRESSION TAG
SEQADV 3WYN HIS A -4 UNP F7IX06 EXPRESSION TAG
SEQADV 3WYN HIS A -3 UNP F7IX06 EXPRESSION TAG
SEQADV 3WYN HIS A -2 UNP F7IX06 EXPRESSION TAG
SEQADV 3WYN HIS A -1 UNP F7IX06 EXPRESSION TAG
SEQADV 3WYN HIS A 0 UNP F7IX06 EXPRESSION TAG
SEQADV 3WYN HIS B -5 UNP F7IX06 EXPRESSION TAG
SEQADV 3WYN HIS B -4 UNP F7IX06 EXPRESSION TAG
SEQADV 3WYN HIS B -3 UNP F7IX06 EXPRESSION TAG
SEQADV 3WYN HIS B -2 UNP F7IX06 EXPRESSION TAG
SEQADV 3WYN HIS B -1 UNP F7IX06 EXPRESSION TAG
SEQADV 3WYN HIS B 0 UNP F7IX06 EXPRESSION TAG
SEQRES 1 A 306 HIS HIS HIS HIS HIS HIS MET SER VAL THR THR PRO ARG
SEQRES 2 A 306 ARG GLU THR SER LEU LEU SER ARG ALA LEU ARG ALA THR
SEQRES 3 A 306 ALA ALA ALA ALA THR ALA VAL VAL ALA THR VAL ALA LEU
SEQRES 4 A 306 ALA ALA PRO ALA GLN ALA ALA ASN PRO TYR GLU ARG GLY
SEQRES 5 A 306 PRO ASN PRO THR GLU SER MET LEU GLU ALA ARG SER GLY
SEQRES 6 A 306 PRO PHE SER VAL SER GLU GLU ARG ALA SER ARG PHE GLY
SEQRES 7 A 306 ALA ASP GLY PHE GLY GLY GLY THR ILE TYR TYR PRO ARG
SEQRES 8 A 306 GLU ASN ASN THR TYR GLY ALA ILE ALA ILE SER PRO GLY
SEQRES 9 A 306 TYR THR GLY THR GLN SER SER ILE ALA TRP LEU GLY GLU
SEQRES 10 A 306 ARG ILE ALA SER HIS GLY PHE VAL VAL ILE ALA ILE ASP
SEQRES 11 A 306 THR ASN THR THR LEU ASP GLN PRO ASP SER ARG ALA ARG
SEQRES 12 A 306 GLN LEU ASN ALA ALA LEU ASP TYR MET LEU THR ASP ALA
SEQRES 13 A 306 SER SER ALA VAL ARG ASN ARG ILE ASP ALA SER ARG LEU
SEQRES 14 A 306 ALA VAL MET GLY HIS SER MET GLY GLY GLY GLY THR LEU
SEQRES 15 A 306 ARG LEU ALA SER GLN ARG PRO ASP LEU LYS ALA ALA ILE
SEQRES 16 A 306 PRO LEU THR PRO TRP HIS LEU ASN LYS SER TRP ARG ASP
SEQRES 17 A 306 ILE THR VAL PRO THR LEU ILE ILE GLY ALA GLU TYR ASP
SEQRES 18 A 306 THR ILE ALA SER VAL THR LEU HIS SER LYS PRO PHE TYR
SEQRES 19 A 306 ASN SER ILE PRO SER PRO THR ASP LYS ALA TYR LEU GLU
SEQRES 20 A 306 LEU ASP GLY ALA SER HIS PHE ALA PRO ASN ILE THR ASN
SEQRES 21 A 306 LYS THR ILE GLY MET TYR SER VAL ALA TRP LEU LYS ARG
SEQRES 22 A 306 PHE VAL ASP GLU ASP THR ARG TYR THR GLN PHE LEU CYS
SEQRES 23 A 306 PRO GLY PRO ARG THR GLY LEU LEU SER ASP VAL GLU GLU
SEQRES 24 A 306 TYR ARG SER THR CYS PRO PHE
SEQRES 1 B 306 HIS HIS HIS HIS HIS HIS MET SER VAL THR THR PRO ARG
SEQRES 2 B 306 ARG GLU THR SER LEU LEU SER ARG ALA LEU ARG ALA THR
SEQRES 3 B 306 ALA ALA ALA ALA THR ALA VAL VAL ALA THR VAL ALA LEU
SEQRES 4 B 306 ALA ALA PRO ALA GLN ALA ALA ASN PRO TYR GLU ARG GLY
SEQRES 5 B 306 PRO ASN PRO THR GLU SER MET LEU GLU ALA ARG SER GLY
SEQRES 6 B 306 PRO PHE SER VAL SER GLU GLU ARG ALA SER ARG PHE GLY
SEQRES 7 B 306 ALA ASP GLY PHE GLY GLY GLY THR ILE TYR TYR PRO ARG
SEQRES 8 B 306 GLU ASN ASN THR TYR GLY ALA ILE ALA ILE SER PRO GLY
SEQRES 9 B 306 TYR THR GLY THR GLN SER SER ILE ALA TRP LEU GLY GLU
SEQRES 10 B 306 ARG ILE ALA SER HIS GLY PHE VAL VAL ILE ALA ILE ASP
SEQRES 11 B 306 THR ASN THR THR LEU ASP GLN PRO ASP SER ARG ALA ARG
SEQRES 12 B 306 GLN LEU ASN ALA ALA LEU ASP TYR MET LEU THR ASP ALA
SEQRES 13 B 306 SER SER ALA VAL ARG ASN ARG ILE ASP ALA SER ARG LEU
SEQRES 14 B 306 ALA VAL MET GLY HIS SER MET GLY GLY GLY GLY THR LEU
SEQRES 15 B 306 ARG LEU ALA SER GLN ARG PRO ASP LEU LYS ALA ALA ILE
SEQRES 16 B 306 PRO LEU THR PRO TRP HIS LEU ASN LYS SER TRP ARG ASP
SEQRES 17 B 306 ILE THR VAL PRO THR LEU ILE ILE GLY ALA GLU TYR ASP
SEQRES 18 B 306 THR ILE ALA SER VAL THR LEU HIS SER LYS PRO PHE TYR
SEQRES 19 B 306 ASN SER ILE PRO SER PRO THR ASP LYS ALA TYR LEU GLU
SEQRES 20 B 306 LEU ASP GLY ALA SER HIS PHE ALA PRO ASN ILE THR ASN
SEQRES 21 B 306 LYS THR ILE GLY MET TYR SER VAL ALA TRP LEU LYS ARG
SEQRES 22 B 306 PHE VAL ASP GLU ASP THR ARG TYR THR GLN PHE LEU CYS
SEQRES 23 B 306 PRO GLY PRO ARG THR GLY LEU LEU SER ASP VAL GLU GLU
SEQRES 24 B 306 TYR ARG SER THR CYS PRO PHE
HET CA A 401 1
HET 2PE B 401 24
HET CA B 402 1
HET CA B 403 1
HETNAM CA CALCIUM ION
HETNAM 2PE NONAETHYLENE GLYCOL
FORMUL 3 CA 3(CA 2+)
FORMUL 4 2PE C18 H38 O10
FORMUL 7 HOH *425(H2 O)
HELIX 1 1 THR A 50 ALA A 56 1 7
HELIX 2 2 THR A 102 SER A 115 1 14
HELIX 3 3 GLN A 131 ASP A 149 1 19
HELIX 4 4 SER A 151 ASN A 156 1 6
HELIX 5 5 SER A 169 ARG A 182 1 14
HELIX 6 6 HIS A 223 SER A 230 1 8
HELIX 7 7 PHE A 248 ILE A 252 5 5
HELIX 8 8 ASN A 254 ASP A 270 1 17
HELIX 9 9 ASP A 272 ARG A 274 5 3
HELIX 10 10 TYR A 275 CYS A 280 1 6
HELIX 11 11 THR B 50 ALA B 56 1 7
HELIX 12 12 THR B 102 SER B 105 5 4
HELIX 13 13 ILE B 106 SER B 115 1 10
HELIX 14 14 GLN B 131 ASP B 149 1 19
HELIX 15 15 SER B 151 ASN B 156 1 6
HELIX 16 16 SER B 169 ARG B 182 1 14
HELIX 17 17 HIS B 223 ILE B 231 1 9
HELIX 18 18 PHE B 248 ILE B 252 5 5
HELIX 19 19 ASN B 254 ASP B 270 1 17
HELIX 20 20 ASP B 272 ARG B 274 5 3
HELIX 21 21 TYR B 275 CYS B 280 1 6
SHEET 1 A 6 VAL A 63 ALA A 68 0
SHEET 2 A 6 GLY A 79 PRO A 84 -1 O ILE A 81 N GLU A 66
SHEET 3 A 6 PHE A 118 ILE A 123 -1 O VAL A 120 N TYR A 82
SHEET 4 A 6 TYR A 90 SER A 96 1 N ILE A 93 O ILE A 121
SHEET 5 A 6 ILE A 158 HIS A 168 1 O ASP A 159 N TYR A 90
SHEET 6 A 6 ALA A 187 LEU A 191 1 O LEU A 191 N GLY A 167
SHEET 1 B 3 THR A 207 ALA A 212 0
SHEET 2 B 3 LYS A 237 LEU A 242 1 O LEU A 240 N GLY A 211
SHEET 3 B 3 VAL A 291 SER A 296 -1 O GLU A 293 N GLU A 241
SHEET 1 C 6 VAL B 63 ALA B 68 0
SHEET 2 C 6 GLY B 79 PRO B 84 -1 O ILE B 81 N GLU B 66
SHEET 3 C 6 VAL B 119 ILE B 123 -1 O VAL B 120 N TYR B 82
SHEET 4 C 6 TYR B 90 SER B 96 1 N ILE B 93 O VAL B 119
SHEET 5 C 6 ILE B 158 HIS B 168 1 O ASP B 159 N TYR B 90
SHEET 6 C 6 ALA B 187 LEU B 191 1 O LEU B 191 N GLY B 167
SHEET 1 D 3 THR B 207 ALA B 212 0
SHEET 2 D 3 LYS B 237 LEU B 242 1 O LEU B 242 N GLY B 211
SHEET 3 D 3 VAL B 291 SER B 296 -1 O GLU B 293 N GLU B 241
SSBOND 1 CYS A 280 CYS A 298 1555 1555 2.09
SSBOND 2 CYS B 280 CYS B 298 1555 1555 2.06
LINK OE1 GLU B 292 CA CA B 402 1555 1555 2.21
LINK OE1 GLU A 292 CA CA A 401 1555 1555 2.30
LINK CA CA B 403 O HOH B 670 1555 1555 2.33
LINK CA CA A 401 O HOH A 504 1555 1555 2.40
LINK CA CA B 403 O HOH B 700 1555 1555 2.41
LINK OD1 ASP A 243 CA CA A 401 1555 1555 2.42
LINK O THR B 297 CA CA B 403 1555 1555 2.43
LINK OD1 ASP B 243 CA CA B 402 1555 1555 2.45
LINK OE1 GLU B 213 CA CA B 402 1555 1555 2.45
LINK O PRO B 299 CA CA B 403 1555 1555 2.45
LINK CA CA B 403 O HOH B 647 1555 1555 2.55
LINK OD1 ASP B 236 CA CA B 403 1555 1555 2.58
LINK OE2 GLU A 213 CA CA A 401 1555 1555 2.58
LINK CA CA B 402 O HOH B 600 1555 1555 2.59
LINK CA CA B 403 O HOH B 592 1555 1555 2.59
LINK OE1 GLU A 213 CA CA A 401 1555 1555 2.65
LINK OE2 GLU B 213 CA CA B 402 1555 1555 2.80
LINK CA CA B 402 O HOH B 678 1555 1555 3.00
LINK CA CA A 401 O HOH A 501 1555 1555 3.08
CISPEP 1 SER A 233 PRO A 234 0 1.32
CISPEP 2 CYS A 280 PRO A 281 0 4.08
CISPEP 3 CYS A 298 PRO A 299 0 6.33
CISPEP 4 SER B 233 PRO B 234 0 -5.00
CISPEP 5 CYS B 280 PRO B 281 0 14.03
CISPEP 6 CYS B 298 PRO B 299 0 -5.53
SITE 1 AC1 6 GLU A 213 ASP A 243 GLU A 292 HOH A 501
SITE 2 AC1 6 HOH A 504 HOH A 686
SITE 1 AC2 9 THR A 100 MET A 170 LEU A 222 TYR B 99
SITE 2 AC2 9 GLN B 131 MET B 170 TRP B 194 HOH B 524
SITE 3 AC2 9 HOH B 609
SITE 1 AC3 5 GLU B 213 ASP B 243 GLU B 292 HOH B 600
SITE 2 AC3 5 HOH B 678
SITE 1 AC4 7 ASP B 236 THR B 297 PRO B 299 HOH B 592
SITE 2 AC4 7 HOH B 647 HOH B 670 HOH B 700
CRYST1 101.473 87.740 72.619 90.00 133.35 90.00 C 1 2 1 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 0.009855 0.000000 0.009302 0.00000
SCALE2 0.000000 0.011397 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018936 0.00000
TER 2004 PHE A 300
TER 4014 PHE B 300
MASTER 578 0 4 21 18 0 9 6 4464 2 53 48
END |