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HEADER HYDROLASE 18-JUN-12 4FMP
TITLE CRYSTAL STRUCTURE OF THERMOSTABLE, ORGANIC-SOLVENT TOLERANT LIPASE
TITLE 2 FROM GEOBACILLUS SP. STRAIN ARM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 35-415;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS STEAROTHERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 1422;
SOURCE 4 STRAIN: ARM;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTRCHIS2
KEYWDS ALPHA/BETA HYDROLASE FOLD, ALPHA/BETA FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.D.NISBAR,R.N.Z.R.A.RAHMAN,M.S.M.ALI,A.T.C.LEOW
REVDAT 1 31-JUL-13 4FMP 0
JRNL AUTH N.D.NISBAR,R.N.Z.R.A.RAHMAN,M.S.M.ALI,A.T.C.LEOW
JRNL TITL CRYSTALLIZATION OF NOVEL ARM LIPASE AND ELUCIDATION OF ITS
JRNL TITL 2 SPACE-GROWN CRYSTAL STRUCTURE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 40490
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2152
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2894
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 145
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6016
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 361
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.87000
REMARK 3 B22 (A**2) : -1.46000
REMARK 3 B33 (A**2) : -1.99000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.265
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.225
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.164
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.787
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6184 ; 0.020 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8410 ; 1.854 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 760 ; 6.534 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 309 ;34.579 ;23.107
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 933 ;15.814 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;16.764 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 880 ; 0.134 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4882 ; 0.010 ; 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): 3766 ; 1.007 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6024 ; 1.849 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2418 ; 3.021 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2386 ; 4.713 ; 4.500
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4FMP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB073091.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : 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 : DOUBLE-CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42814
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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 : 2.000
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 2DSN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES MONOHYDRATE, 12% V/V PEG
REMARK 280 20000, PH 6.5, EVAPORATION, 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 71.69600
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: 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 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 ALA B 137 O HOH B 618 1.74
REMARK 500 CG2 ILE B 362 O HOH B 675 1.86
REMARK 500 N VAL B 142 O HOH B 618 1.89
REMARK 500 NH2 ARG A 271 O HOH A 522 1.90
REMARK 500 O HOH B 598 O HOH B 622 1.92
REMARK 500 N ASP B 175 O HOH B 523 1.97
REMARK 500 OE1 GLU B 100 O HOH B 673 1.97
REMARK 500 O HOH A 569 O HOH A 604 2.02
REMARK 500 CB GLN B 114 O HOH B 676 2.03
REMARK 500 O HOH A 530 O HOH B 562 2.04
REMARK 500 O HOH B 580 O HOH B 608 2.09
REMARK 500 CD1 LEU A 379 O HOH A 658 2.10
REMARK 500 CZ ARG A 271 O HOH A 522 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 505 O HOH B 528 1455 1.78
REMARK 500 O HOH A 573 O HOH B 530 2555 1.91
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 VAL A 187 CB VAL A 187 CG1 -0.136
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 271 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU A 285 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 ARG A 330 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 VAL A 361 CB - CA - C ANGL. DEV. = -13.5 DEGREES
REMARK 500 ARG B 271 NE - CZ - NH2 ANGL. DEV. = -3.0 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 113 -136.65 54.83
REMARK 500 VAL A 203 -67.17 63.14
REMARK 500 ARG A 271 35.49 -153.34
REMARK 500 ASN A 304 99.32 -161.47
REMARK 500 ASP A 310 -161.86 -121.83
REMARK 500 ILE A 319 -37.64 -145.65
REMARK 500 LYS A 329 -51.31 -127.01
REMARK 500 ASP A 371 79.57 -100.15
REMARK 500 SER B 113 -133.60 56.81
REMARK 500 ASN B 141 72.59 44.09
REMARK 500 VAL B 203 -72.94 68.32
REMARK 500 LYS B 207 42.66 79.12
REMARK 500 LEU B 208 36.24 -99.34
REMARK 500 ARG B 271 49.59 -145.42
REMARK 500 ASN B 304 95.12 -166.85
REMARK 500 ASP B 310 -163.43 -109.77
REMARK 500 ILE B 319 -36.95 -135.33
REMARK 500 LYS B 329 -49.77 -140.64
REMARK 500 ASN B 367 93.56 -163.37
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 PHE B 16 THR B 17 149.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 PHE B 154 22.8 L L OUTSIDE RANGE
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 573 DISTANCE = 8.44 ANGSTROMS
REMARK 525 HOH A 599 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH A 608 DISTANCE = 9.12 ANGSTROMS
REMARK 525 HOH B 528 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH B 569 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B 571 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH B 572 DISTANCE = 7.46 ANGSTROMS
REMARK 525 HOH B 573 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH B 581 DISTANCE = 8.65 ANGSTROMS
REMARK 525 HOH B 583 DISTANCE = 12.38 ANGSTROMS
REMARK 525 HOH B 584 DISTANCE = 16.97 ANGSTROMS
REMARK 525 HOH B 585 DISTANCE = 16.91 ANGSTROMS
REMARK 525 HOH B 600 DISTANCE = 11.56 ANGSTROMS
REMARK 525 HOH B 609 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH B 623 DISTANCE = 7.03 ANGSTROMS
REMARK 525 HOH B 624 DISTANCE = 5.72 ANGSTROMS
REMARK 525 HOH B 686 DISTANCE = 7.81 ANGSTROMS
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 ZN B 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 87 NE2
REMARK 620 2 ASP B 238 OD2 95.9
REMARK 620 3 HIS B 81 NE2 109.8 111.9
REMARK 620 4 ASP B 61 OD1 121.3 124.7 93.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 238 OD2
REMARK 620 2 ASP A 61 OD1 129.4
REMARK 620 3 HIS A 87 NE2 97.2 119.1
REMARK 620 4 HIS A 81 NE2 108.9 99.0 99.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 286 O
REMARK 620 2 GLU B 360 OE2 84.3
REMARK 620 3 PRO B 366 O 171.5 89.8
REMARK 620 4 ASP B 365 OD2 104.8 116.4 83.3
REMARK 620 5 HOH B 580 O 85.0 86.2 88.5 155.7
REMARK 620 6 HOH B 608 O 97.0 125.6 81.4 115.6 40.3
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 GLY A 286 O
REMARK 620 2 GLU A 360 OE2 88.4
REMARK 620 3 PRO A 366 O 165.4 102.4
REMARK 620 4 HOH A 611 O 81.3 125.1 84.5
REMARK 620 5 ASP A 365 OD2 94.7 113.5 90.0 120.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 401
DBREF 4FMP A 5 385 UNP Q93A71 Q93A71_GEOSE 35 415
DBREF 4FMP B 5 385 UNP Q93A71 Q93A71_GEOSE 35 415
SEQRES 1 A 381 ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS GLY PHE THR
SEQRES 2 A 381 GLY TRP GLY ARG GLU GLU MET PHE GLY PHE LYS TYR TRP
SEQRES 3 A 381 GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP LEU ASN ASP
SEQRES 4 A 381 ASN GLY TYR ARG THR TYR THR LEU ALA VAL GLY PRO LEU
SEQRES 5 A 381 SER SER ASN TRP ASP ARG ALA CYS GLU ALA TYR ALA GLN
SEQRES 6 A 381 LEU VAL GLY GLY THR VAL ASP TYR GLY ALA ALA HIS ALA
SEQRES 7 A 381 ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG THR TYR PRO
SEQRES 8 A 381 GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY ARG ILE HIS
SEQRES 9 A 381 ILE ILE ALA HIS SER GLN GLY GLY GLN THR ALA ARG MET
SEQRES 10 A 381 LEU VAL SER LEU LEU GLU ASN GLY SER GLN GLU GLU ARG
SEQRES 11 A 381 GLU TYR ALA LYS ALA HIS ASN VAL SER LEU SER PRO LEU
SEQRES 12 A 381 PHE GLU GLY GLY HIS HIS PHE VAL LEU SER VAL THR THR
SEQRES 13 A 381 ILE ALA THR PRO HIS ASP GLY THR THR LEU VAL ASN MET
SEQRES 14 A 381 VAL ASP PHE THR ASP ARG PHE PHE ASP LEU GLN LYS ALA
SEQRES 15 A 381 VAL LEU LYS ALA ALA ALA VAL ALA SER ASN VAL PRO TYR
SEQRES 16 A 381 THR SER GLN VAL TYR ASP PHE LYS LEU ASP GLN TRP GLY
SEQRES 17 A 381 LEU ARG ARG GLN PRO GLY GLU SER PHE ASP GLN TYR PHE
SEQRES 18 A 381 GLU ARG LEU LYS ARG SER PRO VAL TRP THR SER THR ASP
SEQRES 19 A 381 THR ALA ARG TYR ASP LEU SER VAL PRO GLY ALA GLU LYS
SEQRES 20 A 381 LEU ASN GLN TRP VAL LYS ALA SER PRO ASN THR TYR TYR
SEQRES 21 A 381 LEU SER PHE ALA THR GLU ARG THR TYR ARG GLY ALA LEU
SEQRES 22 A 381 THR GLY ASN TYR TYR PRO GLU LEU GLY MET ASN ALA PHE
SEQRES 23 A 381 SER ALA VAL VAL CYS ALA PRO PHE LEU GLY SER TYR ARG
SEQRES 24 A 381 ASN ALA THR LEU GLY ILE ASP ASP ARG TRP LEU GLU ASN
SEQRES 25 A 381 ASP GLY ILE VAL ASN THR PHE SER MET ASN GLY PRO LYS
SEQRES 26 A 381 ARG GLY SER THR ASP ARG ILE VAL PRO TYR ASP GLY THR
SEQRES 27 A 381 ILE LYS LYS GLY VAL TRP ASN ASP MET GLY THR TYR ASN
SEQRES 28 A 381 VAL ASP HIS LEU GLU VAL ILE GLY VAL ASP PRO ASN PRO
SEQRES 29 A 381 LEU PHE ASP ILE ARG ALA PHE TYR LEU ARG LEU ALA GLU
SEQRES 30 A 381 GLN LEU ALA SER
SEQRES 1 B 381 ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS GLY PHE THR
SEQRES 2 B 381 GLY TRP GLY ARG GLU GLU MET PHE GLY PHE LYS TYR TRP
SEQRES 3 B 381 GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP LEU ASN ASP
SEQRES 4 B 381 ASN GLY TYR ARG THR TYR THR LEU ALA VAL GLY PRO LEU
SEQRES 5 B 381 SER SER ASN TRP ASP ARG ALA CYS GLU ALA TYR ALA GLN
SEQRES 6 B 381 LEU VAL GLY GLY THR VAL ASP TYR GLY ALA ALA HIS ALA
SEQRES 7 B 381 ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG THR TYR PRO
SEQRES 8 B 381 GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY ARG ILE HIS
SEQRES 9 B 381 ILE ILE ALA HIS SER GLN GLY GLY GLN THR ALA ARG MET
SEQRES 10 B 381 LEU VAL SER LEU LEU GLU ASN GLY SER GLN GLU GLU ARG
SEQRES 11 B 381 GLU TYR ALA LYS ALA HIS ASN VAL SER LEU SER PRO LEU
SEQRES 12 B 381 PHE GLU GLY GLY HIS HIS PHE VAL LEU SER VAL THR THR
SEQRES 13 B 381 ILE ALA THR PRO HIS ASP GLY THR THR LEU VAL ASN MET
SEQRES 14 B 381 VAL ASP PHE THR ASP ARG PHE PHE ASP LEU GLN LYS ALA
SEQRES 15 B 381 VAL LEU LYS ALA ALA ALA VAL ALA SER ASN VAL PRO TYR
SEQRES 16 B 381 THR SER GLN VAL TYR ASP PHE LYS LEU ASP GLN TRP GLY
SEQRES 17 B 381 LEU ARG ARG GLN PRO GLY GLU SER PHE ASP GLN TYR PHE
SEQRES 18 B 381 GLU ARG LEU LYS ARG SER PRO VAL TRP THR SER THR ASP
SEQRES 19 B 381 THR ALA ARG TYR ASP LEU SER VAL PRO GLY ALA GLU LYS
SEQRES 20 B 381 LEU ASN GLN TRP VAL LYS ALA SER PRO ASN THR TYR TYR
SEQRES 21 B 381 LEU SER PHE ALA THR GLU ARG THR TYR ARG GLY ALA LEU
SEQRES 22 B 381 THR GLY ASN TYR TYR PRO GLU LEU GLY MET ASN ALA PHE
SEQRES 23 B 381 SER ALA VAL VAL CYS ALA PRO PHE LEU GLY SER TYR ARG
SEQRES 24 B 381 ASN ALA THR LEU GLY ILE ASP ASP ARG TRP LEU GLU ASN
SEQRES 25 B 381 ASP GLY ILE VAL ASN THR PHE SER MET ASN GLY PRO LYS
SEQRES 26 B 381 ARG GLY SER THR ASP ARG ILE VAL PRO TYR ASP GLY THR
SEQRES 27 B 381 ILE LYS LYS GLY VAL TRP ASN ASP MET GLY THR TYR ASN
SEQRES 28 B 381 VAL ASP HIS LEU GLU VAL ILE GLY VAL ASP PRO ASN PRO
SEQRES 29 B 381 LEU PHE ASP ILE ARG ALA PHE TYR LEU ARG LEU ALA GLU
SEQRES 30 B 381 GLN LEU ALA SER
HET ZN A 400 1
HET CA A 401 1
HET ZN B 400 1
HET CA B 401 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 CA 2(CA 2+)
FORMUL 7 HOH *361(H2 O)
HELIX 1 1 GLU A 22 PHE A 27 5 6
HELIX 2 2 GLY A 31 GLY A 35 5 5
HELIX 3 3 ASP A 36 ASN A 44 1 9
HELIX 4 4 SER A 58 GLY A 72 1 15
HELIX 5 5 GLY A 78 GLY A 86 1 9
HELIX 6 6 LEU A 98 GLY A 104 5 7
HELIX 7 7 GLN A 114 GLY A 129 1 16
HELIX 8 8 SER A 130 ASN A 141 1 12
HELIX 9 9 SER A 145 GLU A 149 5 5
HELIX 10 10 THR A 168 MET A 173 5 6
HELIX 11 11 ASP A 175 ALA A 191 1 17
HELIX 12 12 LEU A 208 GLY A 212 5 5
HELIX 13 13 SER A 220 ARG A 230 1 11
HELIX 14 14 SER A 231 SER A 236 1 6
HELIX 15 15 THR A 239 SER A 245 1 7
HELIX 16 16 SER A 245 VAL A 256 1 12
HELIX 17 17 ASN A 288 CYS A 295 1 8
HELIX 18 18 CYS A 295 TYR A 302 1 8
HELIX 19 19 ASN A 304 GLY A 308 5 5
HELIX 20 20 ASP A 310 LEU A 314 5 5
HELIX 21 21 ASN A 321 MET A 325 5 5
HELIX 22 22 ASP A 371 SER A 385 1 15
HELIX 23 23 GLU B 23 PHE B 27 5 5
HELIX 24 24 GLY B 31 GLY B 35 5 5
HELIX 25 25 ASP B 36 ASN B 44 1 9
HELIX 26 26 SER B 58 GLY B 72 1 15
HELIX 27 27 GLY B 78 GLY B 86 1 9
HELIX 28 28 LEU B 98 GLY B 104 5 7
HELIX 29 29 GLN B 114 GLY B 129 1 16
HELIX 30 30 SER B 130 ASN B 141 1 12
HELIX 31 31 SER B 145 GLU B 149 5 5
HELIX 32 32 THR B 168 MET B 173 5 6
HELIX 33 33 ASP B 175 ALA B 191 1 17
HELIX 34 34 LEU B 208 GLY B 212 5 5
HELIX 35 35 SER B 220 ARG B 230 1 11
HELIX 36 36 SER B 231 SER B 236 1 6
HELIX 37 37 THR B 239 SER B 245 1 7
HELIX 38 38 SER B 245 VAL B 256 1 12
HELIX 39 39 ASN B 288 CYS B 295 1 8
HELIX 40 40 CYS B 295 GLY B 300 1 6
HELIX 41 41 ASP B 310 LEU B 314 5 5
HELIX 42 42 ASN B 321 MET B 325 5 5
HELIX 43 43 ASP B 371 SER B 385 1 15
SHEET 1 A 7 THR A 48 LEU A 51 0
SHEET 2 A 7 ILE A 10 LEU A 13 1 N LEU A 12 O LEU A 51
SHEET 3 A 7 ILE A 107 HIS A 112 1 O HIS A 108 N VAL A 11
SHEET 4 A 7 VAL A 155 ILE A 161 1 O LEU A 156 N ILE A 107
SHEET 5 A 7 TYR A 263 THR A 269 1 O TYR A 263 N VAL A 158
SHEET 6 A 7 TRP A 348 TYR A 354 1 O TYR A 354 N ALA A 268
SHEET 7 A 7 ILE A 336 PRO A 338 1 N VAL A 337 O TRP A 348
SHEET 1 B 2 GLY A 73 ASP A 76 0
SHEET 2 B 2 PHE A 90 TYR A 94 -1 O TYR A 94 N GLY A 73
SHEET 1 C 2 THR A 272 ARG A 274 0
SHEET 2 C 2 TYR A 281 PRO A 283 -1 O TYR A 282 N TYR A 273
SHEET 1 D 7 THR B 48 LEU B 51 0
SHEET 2 D 7 ILE B 10 LEU B 13 1 N LEU B 12 O TYR B 49
SHEET 3 D 7 ILE B 107 HIS B 112 1 O ILE B 110 N LEU B 13
SHEET 4 D 7 VAL B 155 ILE B 161 1 O SER B 157 N ILE B 109
SHEET 5 D 7 TYR B 263 THR B 269 1 O PHE B 267 N THR B 160
SHEET 6 D 7 TRP B 348 TYR B 354 1 O ASN B 349 N TYR B 264
SHEET 7 D 7 ILE B 336 PRO B 338 1 N VAL B 337 O TRP B 348
SHEET 1 E 2 GLY B 73 ASP B 76 0
SHEET 2 E 2 PHE B 90 TYR B 94 -1 O TYR B 94 N GLY B 73
SHEET 1 F 2 THR B 272 ARG B 274 0
SHEET 2 F 2 TYR B 281 PRO B 283 -1 O TYR B 282 N TYR B 273
LINK NE2 HIS B 87 ZN ZN B 400 1555 1555 1.95
LINK OD2 ASP A 238 ZN ZN A 400 1555 1555 1.99
LINK OD1 ASP A 61 ZN ZN A 400 1555 1555 2.01
LINK OD2 ASP B 238 ZN ZN B 400 1555 1555 2.02
LINK NE2 HIS B 81 ZN ZN B 400 1555 1555 2.05
LINK NE2 HIS A 87 ZN ZN A 400 1555 1555 2.07
LINK NE2 HIS A 81 ZN ZN A 400 1555 1555 2.10
LINK OD1 ASP B 61 ZN ZN B 400 1555 1555 2.11
LINK O GLY B 286 CA CA B 401 1555 1555 2.30
LINK O GLY A 286 CA CA A 401 1555 1555 2.42
LINK OE2 GLU A 360 CA CA A 401 1555 1555 2.45
LINK O PRO A 366 CA CA A 401 1555 1555 2.49
LINK OE2 GLU B 360 CA CA B 401 1555 1555 2.59
LINK O PRO B 366 CA CA B 401 1555 1555 2.60
LINK CA CA A 401 O HOH A 611 1555 1555 2.66
LINK OD2 ASP B 365 CA CA B 401 1555 1555 2.86
LINK OD2 ASP A 365 CA CA A 401 1555 1555 2.89
LINK CA CA B 401 O HOH B 580 1555 1555 2.89
LINK CA CA B 401 O HOH B 608 1555 1555 3.13
SITE 1 AC1 4 ASP A 61 HIS A 81 HIS A 87 ASP A 238
SITE 1 AC2 5 GLY A 286 GLU A 360 ASP A 365 PRO A 366
SITE 2 AC2 5 HOH A 611
SITE 1 AC3 4 ASP B 61 HIS B 81 HIS B 87 ASP B 238
SITE 1 AC4 5 GLY B 286 GLU B 360 ASP B 365 PRO B 366
SITE 2 AC4 5 HOH B 580
CRYST1 55.786 143.392 63.965 90.00 105.88 90.00 P 1 21 1 4
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 0.017926 0.000000 0.005099 0.00000
SCALE2 0.000000 0.006974 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016254 0.00000
TER 3009 SER A 385
TER 6018 SER B 385
MASTER 475 0 4 43 22 0 6 6 6381 2 25 60
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