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HEADER HYDROLASE 20-OCT-20 7DBL
TITLE ACYL-COA HYDROLASE MPAH' MUTANT S139A IN COMPLEX WITH MPA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-COA HYDROLASE MPAH';
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PENICILLIUM BREVICOMPACTUM;
SOURCE 3 ORGANISM_TAXID: 5074;
SOURCE 4 STRAIN: NRRL 864;
SOURCE 5 GENE: MPA';
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PETM-11
KEYWDS PEROXISOMAL ACYL-COA HYDROLASE, MPAH', MPA BIOSYNTHESIS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.Y.LI,C.YOU
REVDAT 1 28-APR-21 7DBL 0
JRNL AUTH C.YOU,F.LI,X.ZHANG,L.MA,Y.Z.ZHANG,W.ZHANG,S.LI
JRNL TITL STRUCTURAL BASIS FOR SUBSTRATE SPECIFICITY OF THE
JRNL TITL 2 PEROXISOMAL ACYL-COA HYDROLASE MPAH' INVOLVED IN
JRNL TITL 3 MYCOPHENOLIC ACID BIOSYNTHESIS.
JRNL REF FEBS J. 2021
JRNL REFN ISSN 1742-464X
JRNL PMID 33843134
JRNL DOI 10.1111/FEBS.15874
REMARK 2
REMARK 2 RESOLUTION. 1.84 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) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 154120
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.205
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8119
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) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.89
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10859
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.2850
REMARK 3 BIN FREE R VALUE SET COUNT : 612
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13404
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 92
REMARK 3 SOLVENT ATOMS : 869
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.02000
REMARK 3 B22 (A**2) : 0.77000
REMARK 3 B33 (A**2) : -1.87000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.59000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.130
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.118
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.088
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.033
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13859 ; 0.010 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 12832 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18868 ; 1.657 ; 1.661
REMARK 3 BOND ANGLES OTHERS (DEGREES): 29743 ; 1.367 ; 1.581
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1673 ; 7.268 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 759 ;32.960 ;21.041
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2292 ;14.258 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 120 ;18.641 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1794 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15420 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2964 ; 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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 3 419 B 3 419 13787 0.080 0.050
REMARK 3 2 A 3 419 C 3 419 13827 0.070 0.050
REMARK 3 3 A 1 422 D 1 422 14020 0.060 0.050
REMARK 3 4 B 3 420 C 3 420 13959 0.050 0.050
REMARK 3 5 B 3 419 D 3 419 13599 0.080 0.050
REMARK 3 6 C 3 419 D 3 419 13629 0.080 0.050
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 7DBL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-20.
REMARK 100 THE DEPOSITION ID IS D_1300019087.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-DEC-19
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 : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : SIEMENS-NICOLET
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 162262
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 48.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.88
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.55100
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: PHASER
REMARK 200 STARTING MODEL: 7DBI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: IMIDAZOLE, CALCIUM ACETATE, PEG 8000,
REMARK 280 PH 7.0, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 46.39250
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 GLY A 423
REMARK 465 ARG A 424
REMARK 465 LYS A 425
REMARK 465 LYS A 426
REMARK 465 ARG A 427
REMARK 465 ASN A 428
REMARK 465 ASP A 429
REMARK 465 LYS A 430
REMARK 465 GLY A 431
REMARK 465 LYS A 432
REMARK 465 LEU A 433
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 PRO B 421
REMARK 465 SER B 422
REMARK 465 GLY B 423
REMARK 465 ARG B 424
REMARK 465 LYS B 425
REMARK 465 LYS B 426
REMARK 465 ARG B 427
REMARK 465 ASN B 428
REMARK 465 ASP B 429
REMARK 465 LYS B 430
REMARK 465 GLY B 431
REMARK 465 LYS B 432
REMARK 465 LEU B 433
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 PRO C 421
REMARK 465 SER C 422
REMARK 465 GLY C 423
REMARK 465 ARG C 424
REMARK 465 LYS C 425
REMARK 465 LYS C 426
REMARK 465 ARG C 427
REMARK 465 ASN C 428
REMARK 465 ASP C 429
REMARK 465 LYS C 430
REMARK 465 GLY C 431
REMARK 465 LYS C 432
REMARK 465 LEU C 433
REMARK 465 GLU D 44
REMARK 465 GLY D 45
REMARK 465 PRO D 46
REMARK 465 ARG D 424
REMARK 465 LYS D 425
REMARK 465 LYS D 426
REMARK 465 ARG D 427
REMARK 465 ASN D 428
REMARK 465 ASP D 429
REMARK 465 LYS D 430
REMARK 465 GLY D 431
REMARK 465 LYS D 432
REMARK 465 LEU D 433
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PRO D 419 CG CD
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 OD1 ASN D 27 O HOH D 601 2.18
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 D 364 C GLY D 364 O 0.182
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 B 391 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 PHE D 363 CB - CA - C ANGL. DEV. = 13.2 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 ILE A 18 110.66 72.74
REMARK 500 ASN A 95 -137.34 61.04
REMARK 500 ALA A 139 -125.52 63.45
REMARK 500 ASN A 271 44.73 -141.46
REMARK 500 ALA A 325 52.63 70.13
REMARK 500 ILE B 18 111.66 75.91
REMARK 500 ASN B 95 -136.79 60.65
REMARK 500 ALA B 139 -125.22 63.48
REMARK 500 HIS B 152 76.68 -150.38
REMARK 500 ASN B 271 37.88 -140.70
REMARK 500 ILE C 18 111.57 75.50
REMARK 500 ASN C 95 -136.24 60.31
REMARK 500 MET C 107 59.82 -90.55
REMARK 500 ALA C 139 -125.19 63.29
REMARK 500 ASN C 271 43.78 -142.99
REMARK 500 ILE D 18 110.58 76.05
REMARK 500 ASN D 95 -138.26 59.95
REMARK 500 ALA D 139 -125.35 63.29
REMARK 500 ASN D 271 42.71 -141.49
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 ALA A 323 GLY A 324 147.87
REMARK 500 GLY A 403 LYS A 404 -139.71
REMARK 500 GLY C 403 LYS C 404 -138.44
REMARK 500 PHE D 363 GLY D 364 142.55
REMARK 500 GLY D 403 LYS D 404 -137.46
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 PHE D 363 11.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MOA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MOA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MOA C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MOA D 501
DBREF 7DBL A 1 433 PDB 7DBL 7DBL 1 433
DBREF 7DBL B 1 433 PDB 7DBL 7DBL 1 433
DBREF 7DBL C 1 433 PDB 7DBL 7DBL 1 433
DBREF 7DBL D 1 433 PDB 7DBL 7DBL 1 433
SEQRES 1 A 433 MET SER THR GLU LYS PHE THR ILE THR GLU HIS LEU VAL
SEQRES 2 A 433 PRO GLY SER HIS ILE ARG GLU TYR PRO GLY SER THR VAL
SEQRES 3 A 433 ASN GLN GLU ASP VAL LEU LYS ILE HIS VAL LYS GLN TYR
SEQRES 4 A 433 THR PRO LYS ARG GLU GLY PRO VAL PRO ASP ASP ALA ILE
SEQRES 5 A 433 THR PHE ILE ALA THR HIS GLY VAL GLY LEU PRO LYS GLU
SEQRES 6 A 433 LEU TYR GLU PRO LEU TRP ASP GLU LEU LEU ASP GLN ALA
SEQRES 7 A 433 SER GLY PHE HIS ILE ARG ALA ILE TRP MET ALA ASP VAL
SEQRES 8 A 433 ALA SER MET ASN GLN SER GLY ILE HIS ASN GLU ASP LYS
SEQRES 9 A 433 LEU SER MET ASP CYS SER TRP MET ASP HIS ALA ARG ASP
SEQRES 10 A 433 LEU LEU LEU MET ILE ASN HIS PHE ARG ASP GLN MET PRO
SEQRES 11 A 433 ARG PRO LEU VAL GLY ILE GLY HIS ALA PHE GLY GLY ASN
SEQRES 12 A 433 ILE ILE THR ASN LEU ALA TYR LEU HIS PRO ARG LEU PHE
SEQRES 13 A 433 THR THR LEU LEU LEU LEU ASP PRO LEU ILE GLN LEU SER
SEQRES 14 A 433 PRO PRO SER LEU GLY PHE GLY THR ASP ALA PRO SER ALA
SEQRES 15 A 433 ILE ASN TYR THR LEU TRP ARG ASP ASP VAL TRP PRO SER
SEQRES 16 A 433 ARG GLU VAL ALA ILE ARG ALA ASN ARG ALA ILE MET GLN
SEQRES 17 A 433 GLY MET ASP PRO ARG CYS LEU ASP ARG MET THR LYS HIS
SEQRES 18 A 433 PHE PHE ARG ASP LEU PRO THR PRO LEU TYR PRO ASP VAL
SEQRES 19 A 433 GLU ALA ILE LYS ALA LEU PHE GLY THR THR ALA ASP SER
SEQRES 20 A 433 THR THR THR PRO VAL THR LEU THR THR PRO LYS TYR HIS
SEQRES 21 A 433 GLU LEU VAL ALA GLN ILE ARG GLN ASN PHE ASN ALA ARG
SEQRES 22 A 433 ASP PRO LYS THR GLY ARG ILE GLU VAL PRO ARG ASP THR
SEQRES 23 A 433 HIS ALA ASP MET ASP PRO LEU VAL ALA TYR ILE PRO LEU
SEQRES 24 A 433 TYR ARG PRO GLU PRO ARG SER THR PHE ARG ARG LEU GLU
SEQRES 25 A 433 THR LEU ARG PRO SER CYS LEU TRP VAL ILE ALA GLY ALA
SEQRES 26 A 433 THR PHE LEU ASN ILE ASP GLU ILE ARG GLU GLY VAL LYS
SEQRES 27 A 433 ILE CYS GLY SER GLY ILE GLY GLY SER GLY GLY VAL PRO
SEQRES 28 A 433 ASP GLY ARG VAL ARG GLU VAL VAL LEU PRO GLY PHE GLY
SEQRES 29 A 433 HIS LEU MET PRO PHE GLN GLU VAL LYS THR VAL ALA GLU
SEQRES 30 A 433 THR CYS ILE VAL TRP LEU GLN GLN GLU MET ASP ARG PHE
SEQRES 31 A 433 ARG GLN THR GLU ARG GLN TRP LYS GLU ASP ARG ASP GLY
SEQRES 32 A 433 LYS SER HIS LEU ALA VAL GLU GLU ASN TRP TYR LYS VAL
SEQRES 33 A 433 LEU LYS PRO ILE PRO SER GLY ARG LYS LYS ARG ASN ASP
SEQRES 34 A 433 LYS GLY LYS LEU
SEQRES 1 B 433 MET SER THR GLU LYS PHE THR ILE THR GLU HIS LEU VAL
SEQRES 2 B 433 PRO GLY SER HIS ILE ARG GLU TYR PRO GLY SER THR VAL
SEQRES 3 B 433 ASN GLN GLU ASP VAL LEU LYS ILE HIS VAL LYS GLN TYR
SEQRES 4 B 433 THR PRO LYS ARG GLU GLY PRO VAL PRO ASP ASP ALA ILE
SEQRES 5 B 433 THR PHE ILE ALA THR HIS GLY VAL GLY LEU PRO LYS GLU
SEQRES 6 B 433 LEU TYR GLU PRO LEU TRP ASP GLU LEU LEU ASP GLN ALA
SEQRES 7 B 433 SER GLY PHE HIS ILE ARG ALA ILE TRP MET ALA ASP VAL
SEQRES 8 B 433 ALA SER MET ASN GLN SER GLY ILE HIS ASN GLU ASP LYS
SEQRES 9 B 433 LEU SER MET ASP CYS SER TRP MET ASP HIS ALA ARG ASP
SEQRES 10 B 433 LEU LEU LEU MET ILE ASN HIS PHE ARG ASP GLN MET PRO
SEQRES 11 B 433 ARG PRO LEU VAL GLY ILE GLY HIS ALA PHE GLY GLY ASN
SEQRES 12 B 433 ILE ILE THR ASN LEU ALA TYR LEU HIS PRO ARG LEU PHE
SEQRES 13 B 433 THR THR LEU LEU LEU LEU ASP PRO LEU ILE GLN LEU SER
SEQRES 14 B 433 PRO PRO SER LEU GLY PHE GLY THR ASP ALA PRO SER ALA
SEQRES 15 B 433 ILE ASN TYR THR LEU TRP ARG ASP ASP VAL TRP PRO SER
SEQRES 16 B 433 ARG GLU VAL ALA ILE ARG ALA ASN ARG ALA ILE MET GLN
SEQRES 17 B 433 GLY MET ASP PRO ARG CYS LEU ASP ARG MET THR LYS HIS
SEQRES 18 B 433 PHE PHE ARG ASP LEU PRO THR PRO LEU TYR PRO ASP VAL
SEQRES 19 B 433 GLU ALA ILE LYS ALA LEU PHE GLY THR THR ALA ASP SER
SEQRES 20 B 433 THR THR THR PRO VAL THR LEU THR THR PRO LYS TYR HIS
SEQRES 21 B 433 GLU LEU VAL ALA GLN ILE ARG GLN ASN PHE ASN ALA ARG
SEQRES 22 B 433 ASP PRO LYS THR GLY ARG ILE GLU VAL PRO ARG ASP THR
SEQRES 23 B 433 HIS ALA ASP MET ASP PRO LEU VAL ALA TYR ILE PRO LEU
SEQRES 24 B 433 TYR ARG PRO GLU PRO ARG SER THR PHE ARG ARG LEU GLU
SEQRES 25 B 433 THR LEU ARG PRO SER CYS LEU TRP VAL ILE ALA GLY ALA
SEQRES 26 B 433 THR PHE LEU ASN ILE ASP GLU ILE ARG GLU GLY VAL LYS
SEQRES 27 B 433 ILE CYS GLY SER GLY ILE GLY GLY SER GLY GLY VAL PRO
SEQRES 28 B 433 ASP GLY ARG VAL ARG GLU VAL VAL LEU PRO GLY PHE GLY
SEQRES 29 B 433 HIS LEU MET PRO PHE GLN GLU VAL LYS THR VAL ALA GLU
SEQRES 30 B 433 THR CYS ILE VAL TRP LEU GLN GLN GLU MET ASP ARG PHE
SEQRES 31 B 433 ARG GLN THR GLU ARG GLN TRP LYS GLU ASP ARG ASP GLY
SEQRES 32 B 433 LYS SER HIS LEU ALA VAL GLU GLU ASN TRP TYR LYS VAL
SEQRES 33 B 433 LEU LYS PRO ILE PRO SER GLY ARG LYS LYS ARG ASN ASP
SEQRES 34 B 433 LYS GLY LYS LEU
SEQRES 1 C 433 MET SER THR GLU LYS PHE THR ILE THR GLU HIS LEU VAL
SEQRES 2 C 433 PRO GLY SER HIS ILE ARG GLU TYR PRO GLY SER THR VAL
SEQRES 3 C 433 ASN GLN GLU ASP VAL LEU LYS ILE HIS VAL LYS GLN TYR
SEQRES 4 C 433 THR PRO LYS ARG GLU GLY PRO VAL PRO ASP ASP ALA ILE
SEQRES 5 C 433 THR PHE ILE ALA THR HIS GLY VAL GLY LEU PRO LYS GLU
SEQRES 6 C 433 LEU TYR GLU PRO LEU TRP ASP GLU LEU LEU ASP GLN ALA
SEQRES 7 C 433 SER GLY PHE HIS ILE ARG ALA ILE TRP MET ALA ASP VAL
SEQRES 8 C 433 ALA SER MET ASN GLN SER GLY ILE HIS ASN GLU ASP LYS
SEQRES 9 C 433 LEU SER MET ASP CYS SER TRP MET ASP HIS ALA ARG ASP
SEQRES 10 C 433 LEU LEU LEU MET ILE ASN HIS PHE ARG ASP GLN MET PRO
SEQRES 11 C 433 ARG PRO LEU VAL GLY ILE GLY HIS ALA PHE GLY GLY ASN
SEQRES 12 C 433 ILE ILE THR ASN LEU ALA TYR LEU HIS PRO ARG LEU PHE
SEQRES 13 C 433 THR THR LEU LEU LEU LEU ASP PRO LEU ILE GLN LEU SER
SEQRES 14 C 433 PRO PRO SER LEU GLY PHE GLY THR ASP ALA PRO SER ALA
SEQRES 15 C 433 ILE ASN TYR THR LEU TRP ARG ASP ASP VAL TRP PRO SER
SEQRES 16 C 433 ARG GLU VAL ALA ILE ARG ALA ASN ARG ALA ILE MET GLN
SEQRES 17 C 433 GLY MET ASP PRO ARG CYS LEU ASP ARG MET THR LYS HIS
SEQRES 18 C 433 PHE PHE ARG ASP LEU PRO THR PRO LEU TYR PRO ASP VAL
SEQRES 19 C 433 GLU ALA ILE LYS ALA LEU PHE GLY THR THR ALA ASP SER
SEQRES 20 C 433 THR THR THR PRO VAL THR LEU THR THR PRO LYS TYR HIS
SEQRES 21 C 433 GLU LEU VAL ALA GLN ILE ARG GLN ASN PHE ASN ALA ARG
SEQRES 22 C 433 ASP PRO LYS THR GLY ARG ILE GLU VAL PRO ARG ASP THR
SEQRES 23 C 433 HIS ALA ASP MET ASP PRO LEU VAL ALA TYR ILE PRO LEU
SEQRES 24 C 433 TYR ARG PRO GLU PRO ARG SER THR PHE ARG ARG LEU GLU
SEQRES 25 C 433 THR LEU ARG PRO SER CYS LEU TRP VAL ILE ALA GLY ALA
SEQRES 26 C 433 THR PHE LEU ASN ILE ASP GLU ILE ARG GLU GLY VAL LYS
SEQRES 27 C 433 ILE CYS GLY SER GLY ILE GLY GLY SER GLY GLY VAL PRO
SEQRES 28 C 433 ASP GLY ARG VAL ARG GLU VAL VAL LEU PRO GLY PHE GLY
SEQRES 29 C 433 HIS LEU MET PRO PHE GLN GLU VAL LYS THR VAL ALA GLU
SEQRES 30 C 433 THR CYS ILE VAL TRP LEU GLN GLN GLU MET ASP ARG PHE
SEQRES 31 C 433 ARG GLN THR GLU ARG GLN TRP LYS GLU ASP ARG ASP GLY
SEQRES 32 C 433 LYS SER HIS LEU ALA VAL GLU GLU ASN TRP TYR LYS VAL
SEQRES 33 C 433 LEU LYS PRO ILE PRO SER GLY ARG LYS LYS ARG ASN ASP
SEQRES 34 C 433 LYS GLY LYS LEU
SEQRES 1 D 433 MET SER THR GLU LYS PHE THR ILE THR GLU HIS LEU VAL
SEQRES 2 D 433 PRO GLY SER HIS ILE ARG GLU TYR PRO GLY SER THR VAL
SEQRES 3 D 433 ASN GLN GLU ASP VAL LEU LYS ILE HIS VAL LYS GLN TYR
SEQRES 4 D 433 THR PRO LYS ARG GLU GLY PRO VAL PRO ASP ASP ALA ILE
SEQRES 5 D 433 THR PHE ILE ALA THR HIS GLY VAL GLY LEU PRO LYS GLU
SEQRES 6 D 433 LEU TYR GLU PRO LEU TRP ASP GLU LEU LEU ASP GLN ALA
SEQRES 7 D 433 SER GLY PHE HIS ILE ARG ALA ILE TRP MET ALA ASP VAL
SEQRES 8 D 433 ALA SER MET ASN GLN SER GLY ILE HIS ASN GLU ASP LYS
SEQRES 9 D 433 LEU SER MET ASP CYS SER TRP MET ASP HIS ALA ARG ASP
SEQRES 10 D 433 LEU LEU LEU MET ILE ASN HIS PHE ARG ASP GLN MET PRO
SEQRES 11 D 433 ARG PRO LEU VAL GLY ILE GLY HIS ALA PHE GLY GLY ASN
SEQRES 12 D 433 ILE ILE THR ASN LEU ALA TYR LEU HIS PRO ARG LEU PHE
SEQRES 13 D 433 THR THR LEU LEU LEU LEU ASP PRO LEU ILE GLN LEU SER
SEQRES 14 D 433 PRO PRO SER LEU GLY PHE GLY THR ASP ALA PRO SER ALA
SEQRES 15 D 433 ILE ASN TYR THR LEU TRP ARG ASP ASP VAL TRP PRO SER
SEQRES 16 D 433 ARG GLU VAL ALA ILE ARG ALA ASN ARG ALA ILE MET GLN
SEQRES 17 D 433 GLY MET ASP PRO ARG CYS LEU ASP ARG MET THR LYS HIS
SEQRES 18 D 433 PHE PHE ARG ASP LEU PRO THR PRO LEU TYR PRO ASP VAL
SEQRES 19 D 433 GLU ALA ILE LYS ALA LEU PHE GLY THR THR ALA ASP SER
SEQRES 20 D 433 THR THR THR PRO VAL THR LEU THR THR PRO LYS TYR HIS
SEQRES 21 D 433 GLU LEU VAL ALA GLN ILE ARG GLN ASN PHE ASN ALA ARG
SEQRES 22 D 433 ASP PRO LYS THR GLY ARG ILE GLU VAL PRO ARG ASP THR
SEQRES 23 D 433 HIS ALA ASP MET ASP PRO LEU VAL ALA TYR ILE PRO LEU
SEQRES 24 D 433 TYR ARG PRO GLU PRO ARG SER THR PHE ARG ARG LEU GLU
SEQRES 25 D 433 THR LEU ARG PRO SER CYS LEU TRP VAL ILE ALA GLY ALA
SEQRES 26 D 433 THR PHE LEU ASN ILE ASP GLU ILE ARG GLU GLY VAL LYS
SEQRES 27 D 433 ILE CYS GLY SER GLY ILE GLY GLY SER GLY GLY VAL PRO
SEQRES 28 D 433 ASP GLY ARG VAL ARG GLU VAL VAL LEU PRO GLY PHE GLY
SEQRES 29 D 433 HIS LEU MET PRO PHE GLN GLU VAL LYS THR VAL ALA GLU
SEQRES 30 D 433 THR CYS ILE VAL TRP LEU GLN GLN GLU MET ASP ARG PHE
SEQRES 31 D 433 ARG GLN THR GLU ARG GLN TRP LYS GLU ASP ARG ASP GLY
SEQRES 32 D 433 LYS SER HIS LEU ALA VAL GLU GLU ASN TRP TYR LYS VAL
SEQRES 33 D 433 LEU LYS PRO ILE PRO SER GLY ARG LYS LYS ARG ASN ASP
SEQRES 34 D 433 LYS GLY LYS LEU
HET MOA A 501 23
HET MOA B 501 23
HET MOA C 501 23
HET MOA D 501 23
HETNAM MOA MYCOPHENOLIC ACID
HETSYN MOA 6-(1,3-DIHYDRO-7-HYDROXY-5-METHOXY-4-METHYL-1-
HETSYN 2 MOA OXOISOBENZOFURAN-6-YL)-4-METHYL-4-HEXANOIC ACID
FORMUL 5 MOA 4(C17 H20 O6)
FORMUL 9 HOH *869(H2 O)
HELIX 1 AA1 TYR A 21 THR A 25 5 5
HELIX 2 AA2 PRO A 63 LEU A 66 5 4
HELIX 3 AA3 TYR A 67 GLN A 77 1 11
HELIX 4 AA4 MET A 94 ASN A 101 1 8
HELIX 5 AA5 SER A 110 PHE A 125 1 16
HELIX 6 AA6 ARG A 126 MET A 129 5 4
HELIX 7 AA7 PHE A 140 HIS A 152 1 13
HELIX 8 AA8 SER A 181 ARG A 189 1 9
HELIX 9 AA9 SER A 195 ASN A 203 1 9
HELIX 10 AB1 ASN A 203 GLN A 208 1 6
HELIX 11 AB2 ASP A 211 PHE A 222 1 12
HELIX 12 AB3 ASP A 233 GLY A 242 1 10
HELIX 13 AB4 PRO A 257 ILE A 266 1 10
HELIX 14 AB5 PRO A 283 ALA A 288 1 6
HELIX 15 AB6 ASP A 291 ALA A 295 5 5
HELIX 16 AB7 ARG A 301 ARG A 310 1 10
HELIX 17 AB8 LEU A 311 LEU A 314 5 4
HELIX 18 AB9 ASN A 329 CYS A 340 1 12
HELIX 19 AC1 GLY A 349 GLY A 353 5 5
HELIX 20 AC2 LEU A 366 GLU A 371 1 6
HELIX 21 AC3 GLU A 371 ASP A 402 1 32
HELIX 22 AC4 GLU A 411 LEU A 417 1 7
HELIX 23 AC5 TYR B 21 THR B 25 5 5
HELIX 24 AC6 PRO B 63 LEU B 66 5 4
HELIX 25 AC7 TYR B 67 GLN B 77 1 11
HELIX 26 AC8 MET B 94 ASN B 101 1 8
HELIX 27 AC9 SER B 110 PHE B 125 1 16
HELIX 28 AD1 ARG B 126 MET B 129 5 4
HELIX 29 AD2 PHE B 140 HIS B 152 1 13
HELIX 30 AD3 SER B 181 ARG B 189 1 9
HELIX 31 AD4 SER B 195 ASN B 203 1 9
HELIX 32 AD5 ASN B 203 GLN B 208 1 6
HELIX 33 AD6 ASP B 211 PHE B 222 1 12
HELIX 34 AD7 ASP B 233 GLY B 242 1 10
HELIX 35 AD8 PRO B 257 ILE B 266 1 10
HELIX 36 AD9 PRO B 283 ALA B 288 1 6
HELIX 37 AE1 ASP B 291 ALA B 295 5 5
HELIX 38 AE2 ARG B 301 ARG B 310 1 10
HELIX 39 AE3 LEU B 311 LEU B 314 5 4
HELIX 40 AE4 ASN B 329 CYS B 340 1 12
HELIX 41 AE5 GLY B 349 GLY B 353 5 5
HELIX 42 AE6 LEU B 366 GLU B 371 1 6
HELIX 43 AE7 GLU B 371 ASP B 402 1 32
HELIX 44 AE8 GLU B 411 LEU B 417 1 7
HELIX 45 AE9 TYR C 21 THR C 25 5 5
HELIX 46 AF1 PRO C 63 LEU C 66 5 4
HELIX 47 AF2 TYR C 67 GLN C 77 1 11
HELIX 48 AF3 MET C 94 ASN C 101 1 8
HELIX 49 AF4 SER C 110 PHE C 125 1 16
HELIX 50 AF5 ARG C 126 MET C 129 5 4
HELIX 51 AF6 PHE C 140 HIS C 152 1 13
HELIX 52 AF7 SER C 181 ARG C 189 1 9
HELIX 53 AF8 SER C 195 ASN C 203 1 9
HELIX 54 AF9 ASN C 203 GLN C 208 1 6
HELIX 55 AG1 ASP C 211 PHE C 222 1 12
HELIX 56 AG2 ASP C 233 GLY C 242 1 10
HELIX 57 AG3 PRO C 257 ILE C 266 1 10
HELIX 58 AG4 PRO C 283 ALA C 288 1 6
HELIX 59 AG5 ASP C 291 ALA C 295 5 5
HELIX 60 AG6 ARG C 301 ARG C 310 1 10
HELIX 61 AG7 LEU C 311 LEU C 314 5 4
HELIX 62 AG8 ASN C 329 CYS C 340 1 12
HELIX 63 AG9 GLY C 349 GLY C 353 5 5
HELIX 64 AH1 LEU C 366 GLU C 371 1 6
HELIX 65 AH2 GLU C 371 ASP C 402 1 32
HELIX 66 AH3 GLU C 411 LEU C 417 1 7
HELIX 67 AH4 TYR D 21 THR D 25 5 5
HELIX 68 AH5 PRO D 63 LEU D 66 5 4
HELIX 69 AH6 TYR D 67 GLN D 77 1 11
HELIX 70 AH7 MET D 94 ASN D 101 1 8
HELIX 71 AH8 SER D 110 PHE D 125 1 16
HELIX 72 AH9 ARG D 126 MET D 129 5 4
HELIX 73 AI1 PHE D 140 HIS D 152 1 13
HELIX 74 AI2 SER D 181 ARG D 189 1 9
HELIX 75 AI3 SER D 195 ASN D 203 1 9
HELIX 76 AI4 ASN D 203 GLN D 208 1 6
HELIX 77 AI5 ASP D 211 PHE D 222 1 12
HELIX 78 AI6 ASP D 233 GLY D 242 1 10
HELIX 79 AI7 PRO D 257 ILE D 266 1 10
HELIX 80 AI8 PRO D 283 ALA D 288 1 6
HELIX 81 AI9 ASP D 291 ALA D 295 5 5
HELIX 82 AJ1 ARG D 301 ARG D 310 1 10
HELIX 83 AJ2 LEU D 311 LEU D 314 5 4
HELIX 84 AJ3 ASN D 329 CYS D 340 1 12
HELIX 85 AJ4 GLY D 349 GLY D 353 5 5
HELIX 86 AJ5 PHE D 363 HIS D 365 5 3
HELIX 87 AJ6 LEU D 366 GLU D 371 1 6
HELIX 88 AJ7 GLU D 371 ASP D 402 1 32
HELIX 89 AJ8 GLU D 411 LEU D 417 1 7
SHEET 1 AA1 8 PHE A 6 PRO A 14 0
SHEET 2 AA1 8 LYS A 33 PRO A 41 -1 O GLN A 38 N THR A 9
SHEET 3 AA1 8 ILE A 83 ALA A 89 -1 O ILE A 86 N TYR A 39
SHEET 4 AA1 8 ILE A 52 THR A 57 1 N ALA A 56 O TRP A 87
SHEET 5 AA1 8 LEU A 133 HIS A 138 1 O ILE A 136 N ILE A 55
SHEET 6 AA1 8 PHE A 156 LEU A 162 1 O THR A 157 N LEU A 133
SHEET 7 AA1 8 SER A 317 ALA A 323 1 O VAL A 321 N LEU A 161
SHEET 8 AA1 8 VAL A 355 LEU A 360 1 O ARG A 356 N TRP A 320
SHEET 1 AA2 3 VAL A 192 TRP A 193 0
SHEET 2 AA2 3 VAL A 252 LEU A 254 -1 O VAL A 252 N TRP A 193
SHEET 3 AA2 3 PHE A 223 ASP A 225 -1 N ARG A 224 O THR A 253
SHEET 1 AA3 2 ARG A 267 GLN A 268 0
SHEET 2 AA3 2 LEU A 299 TYR A 300 -1 O TYR A 300 N ARG A 267
SHEET 1 AA4 8 PHE B 6 PRO B 14 0
SHEET 2 AA4 8 LYS B 33 PRO B 41 -1 O GLN B 38 N THR B 9
SHEET 3 AA4 8 ILE B 83 ALA B 89 -1 O ILE B 86 N TYR B 39
SHEET 4 AA4 8 ILE B 52 THR B 57 1 N ALA B 56 O TRP B 87
SHEET 5 AA4 8 LEU B 133 HIS B 138 1 O VAL B 134 N THR B 53
SHEET 6 AA4 8 PHE B 156 LEU B 162 1 O THR B 157 N LEU B 133
SHEET 7 AA4 8 SER B 317 ALA B 323 1 O VAL B 321 N LEU B 161
SHEET 8 AA4 8 VAL B 355 LEU B 360 1 O ARG B 356 N TRP B 320
SHEET 1 AA5 3 VAL B 192 TRP B 193 0
SHEET 2 AA5 3 VAL B 252 LEU B 254 -1 O VAL B 252 N TRP B 193
SHEET 3 AA5 3 PHE B 223 ASP B 225 -1 N ARG B 224 O THR B 253
SHEET 1 AA6 2 ARG B 267 GLN B 268 0
SHEET 2 AA6 2 LEU B 299 TYR B 300 -1 O TYR B 300 N ARG B 267
SHEET 1 AA7 8 PHE C 6 PRO C 14 0
SHEET 2 AA7 8 LYS C 33 PRO C 41 -1 O GLN C 38 N THR C 9
SHEET 3 AA7 8 ILE C 83 ALA C 89 -1 O ILE C 86 N TYR C 39
SHEET 4 AA7 8 ILE C 52 THR C 57 1 N ALA C 56 O TRP C 87
SHEET 5 AA7 8 LEU C 133 HIS C 138 1 O ILE C 136 N ILE C 55
SHEET 6 AA7 8 PHE C 156 LEU C 162 1 O THR C 157 N LEU C 133
SHEET 7 AA7 8 SER C 317 ALA C 323 1 O VAL C 321 N LEU C 161
SHEET 8 AA7 8 VAL C 355 LEU C 360 1 O LEU C 360 N ILE C 322
SHEET 1 AA8 3 VAL C 192 TRP C 193 0
SHEET 2 AA8 3 VAL C 252 LEU C 254 -1 O VAL C 252 N TRP C 193
SHEET 3 AA8 3 PHE C 223 ASP C 225 -1 N ARG C 224 O THR C 253
SHEET 1 AA9 2 ARG C 267 GLN C 268 0
SHEET 2 AA9 2 LEU C 299 TYR C 300 -1 O TYR C 300 N ARG C 267
SHEET 1 AB1 8 PHE D 6 PRO D 14 0
SHEET 2 AB1 8 LYS D 33 PRO D 41 -1 O ILE D 34 N VAL D 13
SHEET 3 AB1 8 ILE D 83 ALA D 89 -1 O ILE D 86 N TYR D 39
SHEET 4 AB1 8 ILE D 52 THR D 57 1 N ALA D 56 O TRP D 87
SHEET 5 AB1 8 LEU D 133 HIS D 138 1 O VAL D 134 N THR D 53
SHEET 6 AB1 8 PHE D 156 LEU D 162 1 O THR D 157 N LEU D 133
SHEET 7 AB1 8 SER D 317 ALA D 323 1 O VAL D 321 N LEU D 161
SHEET 8 AB1 8 VAL D 355 LEU D 360 1 O ARG D 356 N TRP D 320
SHEET 1 AB2 3 VAL D 192 TRP D 193 0
SHEET 2 AB2 3 VAL D 252 LEU D 254 -1 O VAL D 252 N TRP D 193
SHEET 3 AB2 3 PHE D 223 ASP D 225 -1 N ARG D 224 O THR D 253
SHEET 1 AB3 2 ARG D 267 GLN D 268 0
SHEET 2 AB3 2 LEU D 299 TYR D 300 -1 O TYR D 300 N ARG D 267
CISPEP 1 ARG A 131 PRO A 132 0 -2.67
CISPEP 2 LEU A 226 PRO A 227 0 -1.23
CISPEP 3 ARG B 131 PRO B 132 0 -3.20
CISPEP 4 LEU B 226 PRO B 227 0 -1.67
CISPEP 5 ARG C 131 PRO C 132 0 -3.47
CISPEP 6 LEU C 226 PRO C 227 0 -1.79
CISPEP 7 ARG D 131 PRO D 132 0 -2.45
CISPEP 8 LEU D 226 PRO D 227 0 -0.31
SITE 1 AC1 13 GLY A 59 VAL A 60 ALA A 139 PHE A 140
SITE 2 AC1 13 GLN A 167 SER A 169 PRO A 171 ILE A 183
SITE 3 AC1 13 GLN A 265 ARG A 301 PRO A 304 PHE A 327
SITE 4 AC1 13 HIS A 365
SITE 1 AC2 15 GLY B 59 VAL B 60 ALA B 139 PHE B 140
SITE 2 AC2 15 LEU B 165 GLN B 167 PRO B 171 ALA B 182
SITE 3 AC2 15 ILE B 183 GLN B 265 ARG B 301 PHE B 327
SITE 4 AC2 15 HIS B 365 HOH B 662 HOH B 775
SITE 1 AC3 16 GLY C 59 VAL C 60 ALA C 139 PHE C 140
SITE 2 AC3 16 LEU C 165 GLN C 167 PRO C 171 ALA C 182
SITE 3 AC3 16 ILE C 183 GLN C 265 ARG C 301 PRO C 304
SITE 4 AC3 16 PHE C 327 HIS C 365 HOH C 649 HOH C 750
SITE 1 AC4 11 GLY D 59 VAL D 60 ALA D 139 PHE D 140
SITE 2 AC4 11 GLN D 167 PRO D 171 GLN D 265 ARG D 301
SITE 3 AC4 11 PRO D 304 PHE D 327 HIS D 365
CRYST1 64.819 92.785 160.756 90.00 95.39 90.00 P 1 21 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 0.015428 0.000000 0.001455 0.00000
SCALE2 0.000000 0.010778 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006248 0.00000
TER 3370 SER A 422
TER 6713 ILE B 420
TER 10056 ILE C 420
TER 13408 GLY D 423
MASTER 451 0 4 89 52 0 15 614365 4 92 136
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