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HEADER HYDROLASE 12-APR-19 6JTU
TITLE CRYSTAL STRUCTURE OF MHETASE FROM IDEONELLA SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO(2-HYDROXYETHYL) TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: FERULOYL ESTERASE DOMAIN;
COMPND 5 SYNONYM: MHETASE;
COMPND 6 EC: 3.1.1.102;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 STRAIN: 201-F6;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-Y.SAGONG,H.SEO,K.-J.KIM
REVDAT 1 15-APR-20 6JTU 0
JRNL AUTH H.-Y.SAGONG,H.SEO,K.-J.KIM
JRNL TITL STRUCTURAL INSIGHT INTO MHET HYDROLYSIS BY MHETASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 182668
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9652
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13263
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.51
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE SET COUNT : 655
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12420
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 718
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.82000
REMARK 3 B22 (A**2) : -3.20000
REMARK 3 B33 (A**2) : 3.25000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.33000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.115
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.086
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.393
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
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): 12825 ; 0.014 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 11342 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17447 ; 1.749 ; 1.637
REMARK 3 BOND ANGLES OTHERS (DEGREES): 26252 ; 1.477 ; 1.572
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1680 ; 6.969 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 630 ;30.911 ;21.762
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1779 ;12.334 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 84 ;17.912 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1641 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14934 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2842 ; 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): 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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 6JTU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1300011801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 196929
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.9000
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 (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, HEPES, TACSIMATE PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING 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 107.46550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 86.58150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 107.46550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 86.58150
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, 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 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 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 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 -9
REMARK 465 MET A -8
REMARK 465 ILE A -7
REMARK 465 THR A -6
REMARK 465 LEU A -5
REMARK 465 ARG A -4
REMARK 465 LYS A -3
REMARK 465 LEU A -2
REMARK 465 PRO A -1
REMARK 465 LEU A 0
REMARK 465 ALA A 1
REMARK 465 VAL A 2
REMARK 465 ALA A 3
REMARK 465 VAL A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 GLY A 7
REMARK 465 VAL A 8
REMARK 465 MET A 9
REMARK 465 SER A 10
REMARK 465 ALA A 11
REMARK 465 GLN A 12
REMARK 465 ALA A 13
REMARK 465 MET A 14
REMARK 465 ALA A 15
REMARK 465 MET A 16
REMARK 465 ALA A 17
REMARK 465 CYS A 18
REMARK 465 ALA A 19
REMARK 465 GLY A 20
REMARK 465 GLY A 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 THR A 24
REMARK 465 PRO A 25
REMARK 465 LEU A 26
REMARK 465 PRO A 27
REMARK 465 LEU A 28
REMARK 465 PRO A 29
REMARK 465 GLN A 30
REMARK 465 GLN A 31
REMARK 465 GLN A 32
REMARK 465 PRO A 33
REMARK 465 PRO A 34
REMARK 465 GLN A 35
REMARK 465 GLN A 36
REMARK 465 GLU A 37
REMARK 465 PRO A 38
REMARK 465 PRO A 39
REMARK 465 PRO A 40
REMARK 465 PRO A 41
REMARK 465 PRO A 42
REMARK 465 MET B -9
REMARK 465 MET B -8
REMARK 465 ILE B -7
REMARK 465 THR B -6
REMARK 465 LEU B -5
REMARK 465 ARG B -4
REMARK 465 LYS B -3
REMARK 465 LEU B -2
REMARK 465 PRO B -1
REMARK 465 LEU B 0
REMARK 465 ALA B 1
REMARK 465 VAL B 2
REMARK 465 ALA B 3
REMARK 465 VAL B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 6
REMARK 465 GLY B 7
REMARK 465 VAL B 8
REMARK 465 MET B 9
REMARK 465 SER B 10
REMARK 465 ALA B 11
REMARK 465 GLN B 12
REMARK 465 ALA B 13
REMARK 465 MET B 14
REMARK 465 ALA B 15
REMARK 465 MET B 16
REMARK 465 ALA B 17
REMARK 465 CYS B 18
REMARK 465 ALA B 19
REMARK 465 GLY B 20
REMARK 465 GLY B 21
REMARK 465 GLY B 22
REMARK 465 SER B 23
REMARK 465 THR B 24
REMARK 465 PRO B 25
REMARK 465 LEU B 26
REMARK 465 PRO B 27
REMARK 465 LEU B 28
REMARK 465 PRO B 29
REMARK 465 GLN B 30
REMARK 465 GLN B 31
REMARK 465 GLN B 32
REMARK 465 PRO B 33
REMARK 465 PRO B 34
REMARK 465 GLN B 35
REMARK 465 GLN B 36
REMARK 465 GLU B 37
REMARK 465 PRO B 38
REMARK 465 PRO B 39
REMARK 465 PRO B 40
REMARK 465 PRO B 41
REMARK 465 PRO B 42
REMARK 465 MET C -9
REMARK 465 MET C -8
REMARK 465 ILE C -7
REMARK 465 THR C -6
REMARK 465 LEU C -5
REMARK 465 ARG C -4
REMARK 465 LYS C -3
REMARK 465 LEU C -2
REMARK 465 PRO C -1
REMARK 465 LEU C 0
REMARK 465 ALA C 1
REMARK 465 VAL C 2
REMARK 465 ALA C 3
REMARK 465 VAL C 4
REMARK 465 ALA C 5
REMARK 465 ALA C 6
REMARK 465 GLY C 7
REMARK 465 VAL C 8
REMARK 465 MET C 9
REMARK 465 SER C 10
REMARK 465 ALA C 11
REMARK 465 GLN C 12
REMARK 465 ALA C 13
REMARK 465 MET C 14
REMARK 465 ALA C 15
REMARK 465 MET C 16
REMARK 465 ALA C 17
REMARK 465 CYS C 18
REMARK 465 ALA C 19
REMARK 465 GLY C 20
REMARK 465 GLY C 21
REMARK 465 GLY C 22
REMARK 465 SER C 23
REMARK 465 THR C 24
REMARK 465 PRO C 25
REMARK 465 LEU C 26
REMARK 465 PRO C 27
REMARK 465 LEU C 28
REMARK 465 PRO C 29
REMARK 465 GLN C 30
REMARK 465 GLN C 31
REMARK 465 GLN C 32
REMARK 465 PRO C 33
REMARK 465 PRO C 34
REMARK 465 GLN C 35
REMARK 465 GLN C 36
REMARK 465 GLU C 37
REMARK 465 PRO C 38
REMARK 465 PRO C 39
REMARK 465 PRO C 40
REMARK 465 PRO C 41
REMARK 465 PRO C 42
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 B 359 NE - CZ - NH2 ANGL. DEV. = 3.5 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 ALA A 67 36.86 -93.63
REMARK 500 ASN A 134 -147.31 58.85
REMARK 500 ASN A 171 54.39 -91.54
REMARK 500 TYR A 194 -34.90 -148.45
REMARK 500 SER A 225 -121.05 74.29
REMARK 500 ALA A 249 57.49 34.26
REMARK 500 ASP A 311 10.71 -155.59
REMARK 500 TYR A 373 -101.07 -147.07
REMARK 500 SER A 383 -141.83 -145.34
REMARK 500 VAL A 412 -61.63 -96.28
REMARK 500 SER A 491 32.37 -99.31
REMARK 500 ASN A 527 -154.55 -86.64
REMARK 500 CYS A 529 -35.41 82.51
REMARK 500 ALA B 67 33.16 -88.75
REMARK 500 ASN B 134 -143.95 56.79
REMARK 500 ASN B 171 59.43 -91.19
REMARK 500 TYR B 194 -37.42 -150.00
REMARK 500 SER B 225 -126.31 72.18
REMARK 500 ALA B 249 60.76 30.63
REMARK 500 ASP B 311 11.14 -150.43
REMARK 500 TYR B 373 -98.93 -146.88
REMARK 500 SER B 383 -139.52 -139.58
REMARK 500 VAL B 412 -60.25 -98.33
REMARK 500 ASN B 527 -153.51 -82.82
REMARK 500 CYS B 529 -34.44 77.43
REMARK 500 ASN C 58 -3.55 -56.08
REMARK 500 ASP C 60 40.87 -150.25
REMARK 500 ALA C 67 42.58 -98.57
REMARK 500 ASN C 134 -145.46 55.38
REMARK 500 TYR C 194 -37.42 -152.44
REMARK 500 SER C 225 -127.69 77.88
REMARK 500 ALA C 249 58.92 31.05
REMARK 500 ASP C 311 8.80 -155.00
REMARK 500 TYR C 373 -96.85 -149.42
REMARK 500 SER C 383 -144.40 -141.44
REMARK 500 GLU C 429 74.16 -118.21
REMARK 500 SER C 491 31.74 -99.04
REMARK 500 ASN C 527 -151.55 -88.48
REMARK 500 CYS C 529 -34.31 76.33
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 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 304 O
REMARK 620 2 ASP A 304 OD1 70.8
REMARK 620 3 ASP A 307 OD1 75.7 137.0
REMARK 620 4 ASP A 307 OD2 75.4 137.7 51.5
REMARK 620 5 LEU A 309 O 85.3 79.4 71.6 122.6
REMARK 620 6 ASP A 311 OD1 143.1 72.3 134.6 137.3 86.6
REMARK 620 7 ILE A 313 O 99.4 82.7 129.6 78.4 158.8 77.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 304 O
REMARK 620 2 ASP B 304 OD1 72.7
REMARK 620 3 ASP B 307 OD1 72.7 137.6
REMARK 620 4 ASP B 307 OD2 74.0 136.6 50.8
REMARK 620 5 LEU B 309 O 89.9 83.0 73.1 123.9
REMARK 620 6 ASP B 311 OD1 148.7 76.7 130.6 135.6 80.3
REMARK 620 7 ILE B 313 O 98.4 82.5 126.2 75.6 160.4 83.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 304 O
REMARK 620 2 ASP C 304 OD1 72.7
REMARK 620 3 ASP C 307 OD1 73.0 136.7
REMARK 620 4 ASP C 307 OD2 73.6 138.1 49.7
REMARK 620 5 LEU C 309 O 86.2 81.9 70.3 119.8
REMARK 620 6 ASP C 311 OD1 145.6 73.9 130.2 140.1 80.9
REMARK 620 7 ILE C 313 O 99.8 81.4 130.0 80.5 159.7 83.4
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 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 705
DBREF1 6JTU A 17 603 UNP MHETH_IDESA
DBREF2 6JTU A A0A0K8P8E7 17 603
DBREF1 6JTU B 17 603 UNP MHETH_IDESA
DBREF2 6JTU B A0A0K8P8E7 17 603
DBREF1 6JTU C 17 603 UNP MHETH_IDESA
DBREF2 6JTU C A0A0K8P8E7 17 603
SEQADV 6JTU MET A -9 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6JTU MET A -8 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ILE A -7 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU THR A -6 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU LEU A -5 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ARG A -4 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU LYS A -3 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU LEU A -2 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU PRO A -1 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU LEU A 0 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA A 1 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU VAL A 2 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA A 3 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU VAL A 4 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA A 5 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA A 6 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU GLY A 7 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU VAL A 8 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU MET A 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU SER A 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA A 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU GLN A 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA A 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU MET A 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA A 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU MET A 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU MET B -9 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6JTU MET B -8 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ILE B -7 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU THR B -6 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU LEU B -5 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ARG B -4 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU LYS B -3 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU LEU B -2 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU PRO B -1 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU LEU B 0 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA B 1 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU VAL B 2 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA B 3 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU VAL B 4 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA B 5 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA B 6 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU GLY B 7 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU VAL B 8 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU MET B 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU SER B 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA B 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU GLN B 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA B 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU MET B 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA B 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU MET B 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU MET C -9 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 6JTU MET C -8 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ILE C -7 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU THR C -6 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU LEU C -5 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ARG C -4 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU LYS C -3 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU LEU C -2 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU PRO C -1 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU LEU C 0 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA C 1 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU VAL C 2 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA C 3 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU VAL C 4 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA C 5 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA C 6 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU GLY C 7 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU VAL C 8 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU MET C 9 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU SER C 10 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA C 11 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU GLN C 12 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA C 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU MET C 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU ALA C 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 6JTU MET C 16 UNP A0A0K8P8E EXPRESSION TAG
SEQRES 1 A 613 MET MET ILE THR LEU ARG LYS LEU PRO LEU ALA VAL ALA
SEQRES 2 A 613 VAL ALA ALA GLY VAL MET SER ALA GLN ALA MET ALA MET
SEQRES 3 A 613 ALA CYS ALA GLY GLY GLY SER THR PRO LEU PRO LEU PRO
SEQRES 4 A 613 GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO PRO PRO PRO
SEQRES 5 A 613 VAL PRO LEU ALA SER ARG ALA ALA CYS GLU ALA LEU LYS
SEQRES 6 A 613 ASP GLY ASN GLY ASP MET VAL TRP PRO ASN ALA ALA THR
SEQRES 7 A 613 VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA ALA PRO ALA
SEQRES 8 A 613 THR ALA SER ALA ALA ALA LEU PRO GLU HIS CYS GLU VAL
SEQRES 9 A 613 SER GLY ALA ILE ALA LYS ARG THR GLY ILE ASP GLY TYR
SEQRES 10 A 613 PRO TYR GLU ILE LYS PHE ARG LEU ARG MET PRO ALA GLU
SEQRES 11 A 613 TRP ASN GLY ARG PHE PHE MET GLU GLY GLY SER GLY THR
SEQRES 12 A 613 ASN GLY SER LEU SER ALA ALA THR GLY SER ILE GLY GLY
SEQRES 13 A 613 GLY GLN ILE ALA SER ALA LEU SER ARG ASN PHE ALA THR
SEQRES 14 A 613 ILE ALA THR ASP GLY GLY HIS ASP ASN ALA VAL ASN ASP
SEQRES 15 A 613 ASN PRO ASP ALA LEU GLY THR VAL ALA PHE GLY LEU ASP
SEQRES 16 A 613 PRO GLN ALA ARG LEU ASP MET GLY TYR ASN SER TYR ASP
SEQRES 17 A 613 GLN VAL THR GLN ALA GLY LYS ALA ALA VAL ALA ARG PHE
SEQRES 18 A 613 TYR GLY ARG ALA ALA ASP LYS SER TYR PHE ILE GLY CYS
SEQRES 19 A 613 SER GLU GLY GLY ARG GLU GLY MET MET LEU SER GLN ARG
SEQRES 20 A 613 PHE PRO SER HIS TYR ASP GLY ILE VAL ALA GLY ALA PRO
SEQRES 21 A 613 GLY TYR GLN LEU PRO LYS ALA GLY ILE SER GLY ALA TRP
SEQRES 22 A 613 THR THR GLN SER LEU ALA PRO ALA ALA VAL GLY LEU ASP
SEQRES 23 A 613 ALA GLN GLY VAL PRO LEU ILE ASN LYS SER PHE SER ASP
SEQRES 24 A 613 ALA ASP LEU HIS LEU LEU SER GLN ALA ILE LEU GLY THR
SEQRES 25 A 613 CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY ILE VAL ASP
SEQRES 26 A 613 ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP PRO ALA THR
SEQRES 27 A 613 ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU GLN CYS VAL
SEQRES 28 A 613 GLY ALA LYS THR ALA ASP CYS LEU SER PRO VAL GLN VAL
SEQRES 29 A 613 THR ALA ILE LYS ARG ALA MET ALA GLY PRO VAL ASN SER
SEQRES 30 A 613 ALA GLY THR PRO LEU TYR ASN ARG TRP ALA TRP ASP ALA
SEQRES 31 A 613 GLY MET SER GLY LEU SER GLY THR THR TYR ASN GLN GLY
SEQRES 32 A 613 TRP ARG SER TRP TRP LEU GLY SER PHE ASN SER SER ALA
SEQRES 33 A 613 ASN ASN ALA GLN ARG VAL SER GLY PHE SER ALA ARG SER
SEQRES 34 A 613 TRP LEU VAL ASP PHE ALA THR PRO PRO GLU PRO MET PRO
SEQRES 35 A 613 MET THR GLN VAL ALA ALA ARG MET MET LYS PHE ASP PHE
SEQRES 36 A 613 ASP ILE ASP PRO LEU LYS ILE TRP ALA THR SER GLY GLN
SEQRES 37 A 613 PHE THR GLN SER SER MET ASP TRP HIS GLY ALA THR SER
SEQRES 38 A 613 THR ASP LEU ALA ALA PHE ARG ASP ARG GLY GLY LYS MET
SEQRES 39 A 613 ILE LEU TYR HIS GLY MET SER ASP ALA ALA PHE SER ALA
SEQRES 40 A 613 LEU ASP THR ALA ASP TYR TYR GLU ARG LEU GLY ALA ALA
SEQRES 41 A 613 MET PRO GLY ALA ALA GLY PHE ALA ARG LEU PHE LEU VAL
SEQRES 42 A 613 PRO GLY MET ASN HIS CYS SER GLY GLY PRO GLY THR ASP
SEQRES 43 A 613 ARG PHE ASP MET LEU THR PRO LEU VAL ALA TRP VAL GLU
SEQRES 44 A 613 ARG GLY GLU ALA PRO ASP GLN ILE SER ALA TRP SER GLY
SEQRES 45 A 613 THR PRO GLY TYR PHE GLY VAL ALA ALA ARG THR ARG PRO
SEQRES 46 A 613 LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR LYS GLY SER
SEQRES 47 A 613 GLY ASP ILE ASN THR GLU ALA ASN PHE ALA CYS ALA ALA
SEQRES 48 A 613 PRO PRO
SEQRES 1 B 613 MET MET ILE THR LEU ARG LYS LEU PRO LEU ALA VAL ALA
SEQRES 2 B 613 VAL ALA ALA GLY VAL MET SER ALA GLN ALA MET ALA MET
SEQRES 3 B 613 ALA CYS ALA GLY GLY GLY SER THR PRO LEU PRO LEU PRO
SEQRES 4 B 613 GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO PRO PRO PRO
SEQRES 5 B 613 VAL PRO LEU ALA SER ARG ALA ALA CYS GLU ALA LEU LYS
SEQRES 6 B 613 ASP GLY ASN GLY ASP MET VAL TRP PRO ASN ALA ALA THR
SEQRES 7 B 613 VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA ALA PRO ALA
SEQRES 8 B 613 THR ALA SER ALA ALA ALA LEU PRO GLU HIS CYS GLU VAL
SEQRES 9 B 613 SER GLY ALA ILE ALA LYS ARG THR GLY ILE ASP GLY TYR
SEQRES 10 B 613 PRO TYR GLU ILE LYS PHE ARG LEU ARG MET PRO ALA GLU
SEQRES 11 B 613 TRP ASN GLY ARG PHE PHE MET GLU GLY GLY SER GLY THR
SEQRES 12 B 613 ASN GLY SER LEU SER ALA ALA THR GLY SER ILE GLY GLY
SEQRES 13 B 613 GLY GLN ILE ALA SER ALA LEU SER ARG ASN PHE ALA THR
SEQRES 14 B 613 ILE ALA THR ASP GLY GLY HIS ASP ASN ALA VAL ASN ASP
SEQRES 15 B 613 ASN PRO ASP ALA LEU GLY THR VAL ALA PHE GLY LEU ASP
SEQRES 16 B 613 PRO GLN ALA ARG LEU ASP MET GLY TYR ASN SER TYR ASP
SEQRES 17 B 613 GLN VAL THR GLN ALA GLY LYS ALA ALA VAL ALA ARG PHE
SEQRES 18 B 613 TYR GLY ARG ALA ALA ASP LYS SER TYR PHE ILE GLY CYS
SEQRES 19 B 613 SER GLU GLY GLY ARG GLU GLY MET MET LEU SER GLN ARG
SEQRES 20 B 613 PHE PRO SER HIS TYR ASP GLY ILE VAL ALA GLY ALA PRO
SEQRES 21 B 613 GLY TYR GLN LEU PRO LYS ALA GLY ILE SER GLY ALA TRP
SEQRES 22 B 613 THR THR GLN SER LEU ALA PRO ALA ALA VAL GLY LEU ASP
SEQRES 23 B 613 ALA GLN GLY VAL PRO LEU ILE ASN LYS SER PHE SER ASP
SEQRES 24 B 613 ALA ASP LEU HIS LEU LEU SER GLN ALA ILE LEU GLY THR
SEQRES 25 B 613 CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY ILE VAL ASP
SEQRES 26 B 613 ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP PRO ALA THR
SEQRES 27 B 613 ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU GLN CYS VAL
SEQRES 28 B 613 GLY ALA LYS THR ALA ASP CYS LEU SER PRO VAL GLN VAL
SEQRES 29 B 613 THR ALA ILE LYS ARG ALA MET ALA GLY PRO VAL ASN SER
SEQRES 30 B 613 ALA GLY THR PRO LEU TYR ASN ARG TRP ALA TRP ASP ALA
SEQRES 31 B 613 GLY MET SER GLY LEU SER GLY THR THR TYR ASN GLN GLY
SEQRES 32 B 613 TRP ARG SER TRP TRP LEU GLY SER PHE ASN SER SER ALA
SEQRES 33 B 613 ASN ASN ALA GLN ARG VAL SER GLY PHE SER ALA ARG SER
SEQRES 34 B 613 TRP LEU VAL ASP PHE ALA THR PRO PRO GLU PRO MET PRO
SEQRES 35 B 613 MET THR GLN VAL ALA ALA ARG MET MET LYS PHE ASP PHE
SEQRES 36 B 613 ASP ILE ASP PRO LEU LYS ILE TRP ALA THR SER GLY GLN
SEQRES 37 B 613 PHE THR GLN SER SER MET ASP TRP HIS GLY ALA THR SER
SEQRES 38 B 613 THR ASP LEU ALA ALA PHE ARG ASP ARG GLY GLY LYS MET
SEQRES 39 B 613 ILE LEU TYR HIS GLY MET SER ASP ALA ALA PHE SER ALA
SEQRES 40 B 613 LEU ASP THR ALA ASP TYR TYR GLU ARG LEU GLY ALA ALA
SEQRES 41 B 613 MET PRO GLY ALA ALA GLY PHE ALA ARG LEU PHE LEU VAL
SEQRES 42 B 613 PRO GLY MET ASN HIS CYS SER GLY GLY PRO GLY THR ASP
SEQRES 43 B 613 ARG PHE ASP MET LEU THR PRO LEU VAL ALA TRP VAL GLU
SEQRES 44 B 613 ARG GLY GLU ALA PRO ASP GLN ILE SER ALA TRP SER GLY
SEQRES 45 B 613 THR PRO GLY TYR PHE GLY VAL ALA ALA ARG THR ARG PRO
SEQRES 46 B 613 LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR LYS GLY SER
SEQRES 47 B 613 GLY ASP ILE ASN THR GLU ALA ASN PHE ALA CYS ALA ALA
SEQRES 48 B 613 PRO PRO
SEQRES 1 C 613 MET MET ILE THR LEU ARG LYS LEU PRO LEU ALA VAL ALA
SEQRES 2 C 613 VAL ALA ALA GLY VAL MET SER ALA GLN ALA MET ALA MET
SEQRES 3 C 613 ALA CYS ALA GLY GLY GLY SER THR PRO LEU PRO LEU PRO
SEQRES 4 C 613 GLN GLN GLN PRO PRO GLN GLN GLU PRO PRO PRO PRO PRO
SEQRES 5 C 613 VAL PRO LEU ALA SER ARG ALA ALA CYS GLU ALA LEU LYS
SEQRES 6 C 613 ASP GLY ASN GLY ASP MET VAL TRP PRO ASN ALA ALA THR
SEQRES 7 C 613 VAL VAL GLU VAL ALA ALA TRP ARG ASP ALA ALA PRO ALA
SEQRES 8 C 613 THR ALA SER ALA ALA ALA LEU PRO GLU HIS CYS GLU VAL
SEQRES 9 C 613 SER GLY ALA ILE ALA LYS ARG THR GLY ILE ASP GLY TYR
SEQRES 10 C 613 PRO TYR GLU ILE LYS PHE ARG LEU ARG MET PRO ALA GLU
SEQRES 11 C 613 TRP ASN GLY ARG PHE PHE MET GLU GLY GLY SER GLY THR
SEQRES 12 C 613 ASN GLY SER LEU SER ALA ALA THR GLY SER ILE GLY GLY
SEQRES 13 C 613 GLY GLN ILE ALA SER ALA LEU SER ARG ASN PHE ALA THR
SEQRES 14 C 613 ILE ALA THR ASP GLY GLY HIS ASP ASN ALA VAL ASN ASP
SEQRES 15 C 613 ASN PRO ASP ALA LEU GLY THR VAL ALA PHE GLY LEU ASP
SEQRES 16 C 613 PRO GLN ALA ARG LEU ASP MET GLY TYR ASN SER TYR ASP
SEQRES 17 C 613 GLN VAL THR GLN ALA GLY LYS ALA ALA VAL ALA ARG PHE
SEQRES 18 C 613 TYR GLY ARG ALA ALA ASP LYS SER TYR PHE ILE GLY CYS
SEQRES 19 C 613 SER GLU GLY GLY ARG GLU GLY MET MET LEU SER GLN ARG
SEQRES 20 C 613 PHE PRO SER HIS TYR ASP GLY ILE VAL ALA GLY ALA PRO
SEQRES 21 C 613 GLY TYR GLN LEU PRO LYS ALA GLY ILE SER GLY ALA TRP
SEQRES 22 C 613 THR THR GLN SER LEU ALA PRO ALA ALA VAL GLY LEU ASP
SEQRES 23 C 613 ALA GLN GLY VAL PRO LEU ILE ASN LYS SER PHE SER ASP
SEQRES 24 C 613 ALA ASP LEU HIS LEU LEU SER GLN ALA ILE LEU GLY THR
SEQRES 25 C 613 CYS ASP ALA LEU ASP GLY LEU ALA ASP GLY ILE VAL ASP
SEQRES 26 C 613 ASN TYR ARG ALA CYS GLN ALA ALA PHE ASP PRO ALA THR
SEQRES 27 C 613 ALA ALA ASN PRO ALA ASN GLY GLN ALA LEU GLN CYS VAL
SEQRES 28 C 613 GLY ALA LYS THR ALA ASP CYS LEU SER PRO VAL GLN VAL
SEQRES 29 C 613 THR ALA ILE LYS ARG ALA MET ALA GLY PRO VAL ASN SER
SEQRES 30 C 613 ALA GLY THR PRO LEU TYR ASN ARG TRP ALA TRP ASP ALA
SEQRES 31 C 613 GLY MET SER GLY LEU SER GLY THR THR TYR ASN GLN GLY
SEQRES 32 C 613 TRP ARG SER TRP TRP LEU GLY SER PHE ASN SER SER ALA
SEQRES 33 C 613 ASN ASN ALA GLN ARG VAL SER GLY PHE SER ALA ARG SER
SEQRES 34 C 613 TRP LEU VAL ASP PHE ALA THR PRO PRO GLU PRO MET PRO
SEQRES 35 C 613 MET THR GLN VAL ALA ALA ARG MET MET LYS PHE ASP PHE
SEQRES 36 C 613 ASP ILE ASP PRO LEU LYS ILE TRP ALA THR SER GLY GLN
SEQRES 37 C 613 PHE THR GLN SER SER MET ASP TRP HIS GLY ALA THR SER
SEQRES 38 C 613 THR ASP LEU ALA ALA PHE ARG ASP ARG GLY GLY LYS MET
SEQRES 39 C 613 ILE LEU TYR HIS GLY MET SER ASP ALA ALA PHE SER ALA
SEQRES 40 C 613 LEU ASP THR ALA ASP TYR TYR GLU ARG LEU GLY ALA ALA
SEQRES 41 C 613 MET PRO GLY ALA ALA GLY PHE ALA ARG LEU PHE LEU VAL
SEQRES 42 C 613 PRO GLY MET ASN HIS CYS SER GLY GLY PRO GLY THR ASP
SEQRES 43 C 613 ARG PHE ASP MET LEU THR PRO LEU VAL ALA TRP VAL GLU
SEQRES 44 C 613 ARG GLY GLU ALA PRO ASP GLN ILE SER ALA TRP SER GLY
SEQRES 45 C 613 THR PRO GLY TYR PHE GLY VAL ALA ALA ARG THR ARG PRO
SEQRES 46 C 613 LEU CYS PRO TYR PRO GLN ILE ALA ARG TYR LYS GLY SER
SEQRES 47 C 613 GLY ASP ILE ASN THR GLU ALA ASN PHE ALA CYS ALA ALA
SEQRES 48 C 613 PRO PRO
HET CA A 701 1
HET GOL A 702 6
HET ACT A 703 4
HET FMT A 704 3
HET EDO A 705 4
HET EDO A 706 4
HET CA B 701 1
HET GOL B 702 6
HET GOL B 703 6
HET GOL B 704 6
HET GOL B 705 6
HET GOL B 706 6
HET GOL B 707 6
HET ACT B 708 4
HET CA C 701 1
HET GOL C 702 6
HET GOL C 703 6
HET GOL C 704 6
HET ACT C 705 4
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETNAM ACT ACETATE ION
HETNAM FMT FORMIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 CA 3(CA 2+)
FORMUL 5 GOL 10(C3 H8 O3)
FORMUL 6 ACT 3(C2 H3 O2 1-)
FORMUL 7 FMT C H2 O2
FORMUL 8 EDO 2(C2 H6 O2)
FORMUL 23 HOH *718(H2 O)
HELIX 1 AA1 SER A 47 LEU A 54 1 8
HELIX 2 AA2 ALA A 152 ASN A 156 5 5
HELIX 3 AA3 LEU A 177 LEU A 184 5 8
HELIX 4 AA4 ASP A 185 TYR A 194 1 10
HELIX 5 AA5 TYR A 194 GLY A 213 1 20
HELIX 6 AA6 SER A 225 PHE A 238 1 14
HELIX 7 AA7 GLN A 253 PRO A 255 5 3
HELIX 8 AA8 LYS A 256 ALA A 269 1 14
HELIX 9 AA9 PRO A 270 ALA A 272 5 3
HELIX 10 AB1 LEU A 282 SER A 286 5 5
HELIX 11 AB2 SER A 288 ASP A 304 1 17
HELIX 12 AB3 ALA A 305 GLY A 308 5 4
HELIX 13 AB4 ASN A 316 PHE A 324 1 9
HELIX 14 AB5 SER A 350 GLY A 363 1 14
HELIX 15 AB6 ASP A 379 SER A 383 5 5
HELIX 16 AB7 TRP A 394 LEU A 399 1 6
HELIX 17 AB8 GLY A 414 PHE A 424 1 11
HELIX 18 AB9 PRO A 432 THR A 434 5 3
HELIX 19 AC1 GLN A 435 PHE A 443 1 9
HELIX 20 AC2 ILE A 447 TRP A 453 5 7
HELIX 21 AC3 SER A 462 GLY A 468 1 7
HELIX 22 AC4 LEU A 474 ARG A 480 1 7
HELIX 23 AC5 SER A 496 MET A 511 1 16
HELIX 24 AC6 GLY A 513 GLY A 516 5 4
HELIX 25 AC7 MET A 540 GLY A 551 1 12
HELIX 26 AC8 THR A 563 GLY A 568 5 6
HELIX 27 AC9 THR A 593 ALA A 595 5 3
HELIX 28 AD1 SER B 47 LEU B 54 1 8
HELIX 29 AD2 ALA B 152 ASN B 156 5 5
HELIX 30 AD3 LEU B 177 LEU B 184 5 8
HELIX 31 AD4 ASP B 185 TYR B 194 1 10
HELIX 32 AD5 TYR B 194 GLY B 213 1 20
HELIX 33 AD6 SER B 225 PHE B 238 1 14
HELIX 34 AD7 GLN B 253 PRO B 255 5 3
HELIX 35 AD8 LYS B 256 ALA B 269 1 14
HELIX 36 AD9 PRO B 270 ALA B 272 5 3
HELIX 37 AE1 LEU B 282 SER B 286 5 5
HELIX 38 AE2 SER B 288 ASP B 304 1 17
HELIX 39 AE3 ALA B 305 GLY B 308 5 4
HELIX 40 AE4 ASN B 316 PHE B 324 1 9
HELIX 41 AE5 SER B 350 GLY B 363 1 14
HELIX 42 AE6 ASP B 379 SER B 383 5 5
HELIX 43 AE7 GLY B 414 PHE B 424 1 11
HELIX 44 AE8 PRO B 432 THR B 434 5 3
HELIX 45 AE9 GLN B 435 LYS B 442 1 8
HELIX 46 AF1 ILE B 447 TRP B 453 5 7
HELIX 47 AF2 SER B 462 GLY B 468 1 7
HELIX 48 AF3 LEU B 474 ARG B 480 1 7
HELIX 49 AF4 SER B 496 MET B 511 1 16
HELIX 50 AF5 GLY B 513 GLY B 516 5 4
HELIX 51 AF6 MET B 540 GLY B 551 1 12
HELIX 52 AF7 THR B 563 GLY B 568 5 6
HELIX 53 AF8 THR B 593 ALA B 595 5 3
HELIX 54 AF9 SER C 47 LEU C 54 1 8
HELIX 55 AG1 ALA C 152 ASN C 156 5 5
HELIX 56 AG2 LEU C 177 LEU C 184 5 8
HELIX 57 AG3 ASP C 185 TYR C 194 1 10
HELIX 58 AG4 TYR C 194 GLY C 213 1 20
HELIX 59 AG5 SER C 225 PHE C 238 1 14
HELIX 60 AG6 GLN C 253 PRO C 255 5 3
HELIX 61 AG7 LYS C 256 ALA C 269 1 14
HELIX 62 AG8 PRO C 270 ALA C 272 5 3
HELIX 63 AG9 LEU C 282 PHE C 287 5 6
HELIX 64 AH1 SER C 288 ASP C 304 1 17
HELIX 65 AH2 ALA C 305 GLY C 308 5 4
HELIX 66 AH3 ASN C 316 PHE C 324 1 9
HELIX 67 AH4 SER C 350 GLY C 363 1 14
HELIX 68 AH5 ASP C 379 SER C 383 5 5
HELIX 69 AH6 GLY C 414 PHE C 424 1 11
HELIX 70 AH7 PRO C 432 THR C 434 5 3
HELIX 71 AH8 GLN C 435 LYS C 442 1 8
HELIX 72 AH9 ILE C 447 TRP C 453 5 7
HELIX 73 AI1 SER C 462 HIS C 467 1 6
HELIX 74 AI2 LEU C 474 ARG C 480 1 7
HELIX 75 AI3 SER C 496 MET C 511 1 16
HELIX 76 AI4 GLY C 513 GLY C 516 5 4
HELIX 77 AI5 MET C 540 GLY C 551 1 12
HELIX 78 AI6 THR C 563 GLY C 568 5 6
HELIX 79 AI7 THR C 593 ALA C 595 5 3
SHEET 1 AA1 9 THR A 68 ARG A 76 0
SHEET 2 AA1 9 HIS A 91 THR A 102 -1 O ALA A 97 N VAL A 69
SHEET 3 AA1 9 PRO A 108 PRO A 118 -1 O LEU A 115 N VAL A 94
SHEET 4 AA1 9 ALA A 158 THR A 162 -1 O THR A 159 N ARG A 116
SHEET 5 AA1 9 ARG A 124 GLU A 128 1 N ARG A 124 O ALA A 158
SHEET 6 AA1 9 LYS A 218 CYS A 224 1 O TYR A 220 N PHE A 125
SHEET 7 AA1 9 GLY A 244 GLY A 248 1 O GLY A 248 N GLY A 223
SHEET 8 AA1 9 LYS A 483 GLY A 489 1 O ILE A 485 N ILE A 245
SHEET 9 AA1 9 ALA A 518 VAL A 523 1 O VAL A 523 N HIS A 488
SHEET 1 AA2 2 LEU A 385 SER A 386 0
SHEET 2 AA2 2 THR A 389 TYR A 390 -1 O THR A 389 N SER A 386
SHEET 1 AA3 2 ILE A 557 TRP A 560 0
SHEET 2 AA3 2 THR A 573 LEU A 576 -1 O LEU A 576 N ILE A 557
SHEET 1 AA4 2 ILE A 582 TYR A 585 0
SHEET 2 AA4 2 PHE A 597 ALA A 600 -1 O ALA A 600 N ILE A 582
SHEET 1 AA5 9 THR B 68 ARG B 76 0
SHEET 2 AA5 9 HIS B 91 THR B 102 -1 O ALA B 97 N VAL B 69
SHEET 3 AA5 9 PRO B 108 PRO B 118 -1 O LEU B 115 N VAL B 94
SHEET 4 AA5 9 ALA B 158 THR B 162 -1 O THR B 159 N ARG B 116
SHEET 5 AA5 9 ARG B 124 GLU B 128 1 N ARG B 124 O ALA B 158
SHEET 6 AA5 9 LYS B 218 CYS B 224 1 O TYR B 220 N PHE B 125
SHEET 7 AA5 9 GLY B 244 GLY B 248 1 O GLY B 248 N GLY B 223
SHEET 8 AA5 9 LYS B 483 GLY B 489 1 O ILE B 485 N ILE B 245
SHEET 9 AA5 9 ALA B 518 VAL B 523 1 O ARG B 519 N LEU B 486
SHEET 1 AA6 2 LEU B 385 SER B 386 0
SHEET 2 AA6 2 THR B 389 TYR B 390 -1 O THR B 389 N SER B 386
SHEET 1 AA7 2 ILE B 557 TRP B 560 0
SHEET 2 AA7 2 THR B 573 LEU B 576 -1 O LEU B 576 N ILE B 557
SHEET 1 AA8 2 ILE B 582 TYR B 585 0
SHEET 2 AA8 2 PHE B 597 ALA B 600 -1 O ALA B 600 N ILE B 582
SHEET 1 AA9 9 THR C 68 ARG C 76 0
SHEET 2 AA9 9 HIS C 91 THR C 102 -1 O ALA C 97 N VAL C 69
SHEET 3 AA9 9 PRO C 108 PRO C 118 -1 O LEU C 115 N VAL C 94
SHEET 4 AA9 9 ALA C 158 THR C 162 -1 O THR C 159 N ARG C 116
SHEET 5 AA9 9 ARG C 124 GLU C 128 1 N ARG C 124 O ALA C 158
SHEET 6 AA9 9 LYS C 218 CYS C 224 1 O TYR C 220 N MET C 127
SHEET 7 AA9 9 GLY C 244 GLY C 248 1 O GLY C 248 N GLY C 223
SHEET 8 AA9 9 LYS C 483 GLY C 489 1 O LYS C 483 N ILE C 245
SHEET 9 AA9 9 ALA C 518 VAL C 523 1 O ARG C 519 N LEU C 486
SHEET 1 AB1 2 LEU C 385 SER C 386 0
SHEET 2 AB1 2 THR C 389 TYR C 390 -1 O THR C 389 N SER C 386
SHEET 1 AB2 2 ILE C 557 TRP C 560 0
SHEET 2 AB2 2 THR C 573 LEU C 576 -1 O LEU C 576 N ILE C 557
SHEET 1 AB3 2 ILE C 582 TYR C 585 0
SHEET 2 AB3 2 PHE C 597 ALA C 600 -1 O ALA C 600 N ILE C 582
SSBOND 1 CYS A 51 CYS A 92 1555 1555 2.67
SSBOND 2 CYS A 224 CYS A 529 1555 1555 2.25
SSBOND 3 CYS A 303 CYS A 320 1555 1555 2.24
SSBOND 4 CYS A 340 CYS A 348 1555 1555 2.19
SSBOND 5 CYS A 577 CYS A 599 1555 1555 2.15
SSBOND 6 CYS B 51 CYS B 92 1555 1555 2.25
SSBOND 7 CYS B 224 CYS B 529 1555 1555 2.30
SSBOND 8 CYS B 303 CYS B 320 1555 1555 2.29
SSBOND 9 CYS B 340 CYS B 348 1555 1555 2.20
SSBOND 10 CYS B 577 CYS B 599 1555 1555 2.17
SSBOND 11 CYS C 51 CYS C 92 1555 1555 2.27
SSBOND 12 CYS C 224 CYS C 529 1555 1555 2.28
SSBOND 13 CYS C 303 CYS C 320 1555 1555 2.23
SSBOND 14 CYS C 340 CYS C 348 1555 1555 2.25
SSBOND 15 CYS C 577 CYS C 599 1555 1555 2.16
LINK O ASP A 304 CA CA A 701 1555 1555 2.58
LINK OD1 ASP A 304 CA CA A 701 1555 1555 2.43
LINK OD1 ASP A 307 CA CA A 701 1555 1555 2.61
LINK OD2 ASP A 307 CA CA A 701 1555 1555 2.46
LINK O LEU A 309 CA CA A 701 1555 1555 2.38
LINK OD1 ASP A 311 CA CA A 701 1555 1555 2.51
LINK O ILE A 313 CA CA A 701 1555 1555 2.38
LINK O ASP B 304 CA CA B 701 1555 1555 2.51
LINK OD1 ASP B 304 CA CA B 701 1555 1555 2.35
LINK OD1 ASP B 307 CA CA B 701 1555 1555 2.70
LINK OD2 ASP B 307 CA CA B 701 1555 1555 2.48
LINK O LEU B 309 CA CA B 701 1555 1555 2.36
LINK OD1 ASP B 311 CA CA B 701 1555 1555 2.40
LINK O ILE B 313 CA CA B 701 1555 1555 2.39
LINK O ASP C 304 CA CA C 701 1555 1555 2.49
LINK OD1 ASP C 304 CA CA C 701 1555 1555 2.44
LINK OD1 ASP C 307 CA CA C 701 1555 1555 2.84
LINK OD2 ASP C 307 CA CA C 701 1555 1555 2.51
LINK O LEU C 309 CA CA C 701 1555 1555 2.33
LINK OD1 ASP C 311 CA CA C 701 1555 1555 2.47
LINK O ILE C 313 CA CA C 701 1555 1555 2.30
CISPEP 1 THR A 426 PRO A 427 0 -6.90
CISPEP 2 TYR A 579 PRO A 580 0 1.36
CISPEP 3 THR B 426 PRO B 427 0 -2.79
CISPEP 4 TYR B 579 PRO B 580 0 4.09
CISPEP 5 THR C 426 PRO C 427 0 -5.54
CISPEP 6 TYR C 579 PRO C 580 0 1.74
SITE 1 AC1 5 ASP A 304 ASP A 307 LEU A 309 ASP A 311
SITE 2 AC1 5 ILE A 313
SITE 1 AC2 7 LYS A 205 ALA A 216 ASP A 217 SER A 219
SITE 2 AC2 7 ASP A 243 HOH A 894 HOH A 900
SITE 1 AC3 5 ASP A 465 ASP A 473 LEU A 474 ALA A 475
SITE 2 AC3 5 HOH A 846
SITE 1 AC4 5 LEU A 254 ARG A 411 SER A 416 PHE A 495
SITE 2 AC4 5 HOH A 877
SITE 1 AC5 5 PRO A 186 GLN A 187 ASP A 479 HOH A 820
SITE 2 AC5 5 HOH A 886
SITE 1 AC6 4 ARG A 101 THR A 102 GLN A 187 HOH A 876
SITE 1 AC7 5 ASP B 304 ASP B 307 LEU B 309 ASP B 311
SITE 2 AC7 5 ILE B 313
SITE 1 AC8 6 PRO B 270 ALA B 271 ALA B 272 HOH B 980
SITE 2 AC8 6 TYR C 390 HOH C 893
SITE 1 AC9 6 SER B 143 ILE B 144 GLY B 145 GLN B 148
SITE 2 AC9 6 ALA B 150 HOH B 813
SITE 1 AD1 7 LYS B 205 ALA B 216 ASP B 217 SER B 219
SITE 2 AD1 7 ASP B 243 HOH B 880 HOH B 930
SITE 1 AD2 5 PRO B 64 GOL B 707 HOH B 876 ALA C 206
SITE 2 AD2 5 HOH C 879
SITE 1 AD3 5 CYS B 340 VAL B 341 GLY B 342 ALA B 343
SITE 2 AD3 5 THR B 345
SITE 1 AD4 4 ALA B 206 GOL B 705 HOH B 880 HOH B 943
SITE 1 AD5 5 LEU B 254 ARG B 411 SER B 416 HOH B 877
SITE 2 AD5 5 HOH B 917
SITE 1 AD6 5 ASP C 304 ASP C 307 LEU C 309 ASP C 311
SITE 2 AD6 5 ILE C 313
SITE 1 AD7 6 SER C 143 ILE C 144 GLY C 145 GLN C 148
SITE 2 AD7 6 ALA C 150 HOH C 840
SITE 1 AD8 6 HOH B 876 LYS C 205 ALA C 215 ALA C 216
SITE 2 AD8 6 SER C 219 ASP C 243
SITE 1 AD9 6 TYR C 252 GLN C 253 LYS C 256 TYR C 373
SITE 2 AD9 6 ASP C 499 ARG C 506
SITE 1 AE1 4 LEU C 254 ARG C 411 SER C 416 HOH C 853
CRYST1 214.931 173.163 107.225 90.00 119.86 90.00 C 1 2 1 12
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 0.004653 0.000000 0.002671 0.00000
SCALE2 0.000000 0.005775 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010754 0.00000
TER 4141 PRO A 603
TER 8282 PRO B 603
TER 12423 PRO C 603
MASTER 603 0 19 79 45 0 35 613224 3 140 144
END |