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HEADER HYDROLASE 22-JAN-09 2ZYH
TITLE MUTANT A. FULGIDUS LIPASE S136A COMPLEXED WITH FATTY ACID
TITLE 2 FRAGMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE, PUTATIVE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS;
SOURCE 3 ORGANISM_TAXID: 2234;
SOURCE 4 GENE: AF_1763;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-23A(+)
KEYWDS LIPASE, ARCHAEOGLOBUS FULGIDUS, FATTY ACID, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.K.CHEN,T.P.KO,R.T.GUO,A.H.WANG
REVDAT 1 16-JUN-09 2ZYH 0
JRNL AUTH C.K.CHEN,G.C.LEE,T.P.KO,R.T.GUO,L.M.HUANG,H.J.LIU,
JRNL AUTH 2 Y.F.HO,J.F.SHAW,A.H.WANG
JRNL TITL STRUCTURE OF THE ALKALOHYPERTHERMOPHILIC
JRNL TITL 2 ARCHAEOGLOBUS FULGIDUS LIPASE CONTAINS A UNIQUE
JRNL TITL 3 C-TERMINAL DOMAIN ESSENTIAL FOR LONG-CHAIN
JRNL TITL 4 SUBSTRATE BINDING.
JRNL REF J.MOL.BIOL. 2009
JRNL REFN ESSN 1089-8638
JRNL PMID 19447113
JRNL DOI 10.1016/J.JMB.2009.05.017
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 98823
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 SET) : 0.187
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4979
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.83
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE : 0.2820
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 465
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7202
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 1226
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.18
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.020
REMARK 3 BOND ANGLES (DEGREES) : 1.80
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZYH COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JAN-09.
REMARK 100 THE RCSB ID CODE IS RCSB028584.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL12B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104198
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 31.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.42900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CACL2, 0.1M SODIUM ACETATE (PH
REMARK 280 4.6), 10% ISOPROPANOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 45.59800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.44800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.93650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.44800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.59800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.93650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 GLY A 3
REMARK 465 LEU A 4
REMARK 465 ALA A 5
REMARK 465 VAL A 6
REMARK 465 LEU A 7
REMARK 465 VAL A 8
REMARK 465 LEU A 9
REMARK 465 LEU A 10
REMARK 465 VAL A 11
REMARK 465 PHE A 12
REMARK 465 ALA A 13
REMARK 465 VAL A 14
REMARK 465 GLN A 15
REMARK 465 VAL A 16
REMARK 465 ALA A 17
REMARK 465 ALA A 18
REMARK 465 ALA A 19
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 GLY B 3
REMARK 465 LEU B 4
REMARK 465 ALA B 5
REMARK 465 VAL B 6
REMARK 465 LEU B 7
REMARK 465 VAL B 8
REMARK 465 LEU B 9
REMARK 465 LEU B 10
REMARK 465 VAL B 11
REMARK 465 PHE B 12
REMARK 465 ALA B 13
REMARK 465 VAL B 14
REMARK 465 GLN B 15
REMARK 465 VAL B 16
REMARK 465 ALA B 17
REMARK 465 ALA B 18
REMARK 465 ALA B 19
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 HOH B 814 O HOH B 815 1.98
REMARK 500 O HOH A 909 O HOH A 910 2.11
REMARK 500 O HOH A 535 O HOH A 954 2.18
REMARK 500 O HOH A 565 O HOH A 1104 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLU B 194 O HOH B 814 4566 2.17
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 LEU A 357 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 LEU B 213 CA - CB - CG ANGL. DEV. = 17.6 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 GLU A 70 42.63 -104.52
REMARK 500 SER A 76 50.78 -146.14
REMARK 500 SER A 80 -149.14 -112.58
REMARK 500 PRO A 92 -24.79 -39.35
REMARK 500 ALA A 136 -121.74 56.64
REMARK 500 ALA A 185 -52.04 -18.67
REMARK 500 LEU A 186 -154.92 -138.82
REMARK 500 PRO A 187 85.63 -59.00
REMARK 500 LEU A 189 -9.23 -55.69
REMARK 500 GLU A 193 -0.86 75.07
REMARK 500 ALA A 255 -48.85 75.79
REMARK 500 LEU A 336 71.15 -119.21
REMARK 500 LYS A 363 110.60 -174.13
REMARK 500 GLU B 70 41.03 -95.86
REMARK 500 ALA B 136 -118.10 54.18
REMARK 500 LEU B 191 -60.02 -99.34
REMARK 500 ALA B 255 -45.37 76.16
REMARK 500 LEU B 336 65.41 -114.31
REMARK 500 LYS B 363 109.20 -179.37
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 B 555 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A 602 DISTANCE = 6.82 ANGSTROMS
REMARK 525 HOH B 611 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH B 616 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH B 629 DISTANCE = 5.50 ANGSTROMS
REMARK 525 HOH B 631 DISTANCE = 6.26 ANGSTROMS
REMARK 525 HOH B 632 DISTANCE = 7.04 ANGSTROMS
REMARK 525 HOH B 644 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH A 654 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH A 698 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH A 707 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH A 781 DISTANCE = 7.70 ANGSTROMS
REMARK 525 HOH A 788 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH A 805 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH B 807 DISTANCE = 6.58 ANGSTROMS
REMARK 525 HOH A 863 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH B 883 DISTANCE = 6.15 ANGSTROMS
REMARK 525 HOH B 893 DISTANCE = 7.08 ANGSTROMS
REMARK 525 HOH B 894 DISTANCE = 8.10 ANGSTROMS
REMARK 525 HOH A 893 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH B 900 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH B 904 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH A 918 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH A 929 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH A 961 DISTANCE = 5.71 ANGSTROMS
REMARK 525 HOH A 962 DISTANCE = 7.32 ANGSTROMS
REMARK 525 HOH A1064 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A1066 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH B1015 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH B1018 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH B1030 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH B1090 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH B1106 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH B1129 DISTANCE = 7.87 ANGSTROMS
REMARK 525 HOH B1198 DISTANCE = 7.06 ANGSTROMS
REMARK 525 HOH B1208 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH B1226 DISTANCE = 8.70 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 CA A 700 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 405 OD1
REMARK 620 2 ARG A 406 O 82.9
REMARK 620 3 ASP A 409 OD2 79.5 86.1
REMARK 620 4 LYS A 411 O 97.5 176.5 90.6
REMARK 620 5 ASP A 431 OD1 88.0 93.4 167.5 90.1
REMARK 620 6 ASP A 431 OD2 137.2 97.3 143.3 84.7 49.2
REMARK 620 7 HOH A 476 O 152.6 82.3 76.6 96.0 115.8 67.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 700 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 405 OD1
REMARK 620 2 ARG B 406 O 85.0
REMARK 620 3 ASP B 409 OD2 77.5 88.1
REMARK 620 4 LYS B 411 O 92.9 177.0 89.3
REMARK 620 5 ASP B 431 OD1 86.3 89.8 163.7 92.2
REMARK 620 6 ASP B 431 OD2 136.3 97.7 146.0 85.3 50.3
REMARK 620 7 HOH B 907 O 154.3 84.9 78.6 96.1 117.3 68.7
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 R16 A 500
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 700
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE R16 B 500
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZYI RELATED DB: PDB
REMARK 900 RELATED ID: 2ZYR RELATED DB: PDB
REMARK 900 RELATED ID: 2ZYS RELATED DB: PDB
DBREF 2ZYH A 1 474 UNP O28511 O28511_ARCFU 1 474
DBREF 2ZYH B 1 474 UNP O28511 O28511_ARCFU 1 474
SEQADV 2ZYH ALA A 136 UNP O28511 SER 136 ENGINEERED
SEQADV 2ZYH VAL A 475 UNP O28511 EXPRESSION TAG
SEQADV 2ZYH ALA B 136 UNP O28511 SER 136 ENGINEERED
SEQADV 2ZYH VAL B 475 UNP O28511 EXPRESSION TAG
SEQRES 1 A 475 MET ARG GLY LEU ALA VAL LEU VAL LEU LEU VAL PHE ALA
SEQRES 2 A 475 VAL GLN VAL ALA ALA ALA GLU ASP PHE ARG PRO VAL VAL
SEQRES 3 A 475 PHE VAL HIS GLY LEU ALA GLY SER ALA GLY GLN PHE GLU
SEQRES 4 A 475 SER GLN GLY MET ARG PHE ALA ALA ASN GLY TYR PRO ALA
SEQRES 5 A 475 GLU TYR VAL LYS THR PHE GLU TYR ASP THR ILE SER TRP
SEQRES 6 A 475 ALA LEU VAL VAL GLU THR ASP MET LEU PHE SER GLY LEU
SEQRES 7 A 475 GLY SER GLU PHE GLY LEU ASN ILE SER GLN ILE ILE ASP
SEQRES 8 A 475 PRO GLU THR LEU ASP LYS ILE LEU SER LYS SER ARG GLU
SEQRES 9 A 475 ARG LEU ILE ASP GLU THR PHE SER ARG LEU ASP ARG VAL
SEQRES 10 A 475 ILE ASP GLU ALA LEU ALA GLU SER GLY ALA ASP LYS VAL
SEQRES 11 A 475 ASP LEU VAL GLY HIS ALA MET GLY THR PHE PHE LEU VAL
SEQRES 12 A 475 ARG TYR VAL ASN SER SER PRO GLU ARG ALA ALA LYS VAL
SEQRES 13 A 475 ALA HIS LEU ILE LEU LEU ASP GLY VAL TRP GLY VAL ASP
SEQRES 14 A 475 ALA PRO GLU GLY ILE PRO THR LEU ALA VAL PHE GLY ASN
SEQRES 15 A 475 PRO LYS ALA LEU PRO ALA LEU GLY LEU PRO GLU GLU LYS
SEQRES 16 A 475 VAL VAL TYR ASN ALA THR ASN VAL TYR PHE ASN ASN MET
SEQRES 17 A 475 THR HIS VAL GLN LEU CYS THR SER PRO GLU THR PHE ALA
SEQRES 18 A 475 VAL MET PHE GLU PHE ILE ASN GLY TYR LYS PRO ALA THR
SEQRES 19 A 475 THR ASP ILE VAL PRO GLN ASP GLY ASP TYR VAL LYS VAL
SEQRES 20 A 475 LYS GLY LYS PHE LEU ALA PHE ALA THR ASN GLY ASP VAL
SEQRES 21 A 475 SER GLY TRP LEU SER ILE TYR PRO ILE ASP GLU ASN GLY
SEQRES 22 A 475 LYS ARG LEU THR ARG LEU PRO VAL LYS PHE MET ARG VAL
SEQRES 23 A 475 LYS GLY ASP PHE GLU VAL ARG LEU ARG LYS GLY GLN LEU
SEQRES 24 A 475 TYR GLU PHE GLN PHE ARG LYS ASP PHE SER PRO ILE ILE
SEQRES 25 A 475 TYR HIS TYR TYR ARG ALA PRO PHE VAL ARG ASP ASP LEU
SEQRES 26 A 475 TRP ALA ARG PHE LEU VAL SER LYS PRO PRO LEU ASP VAL
SEQRES 27 A 475 GLU LEU LEU ILE LEU PRO GLU ARG LEU SER PRO ALA ALA
SEQRES 28 A 475 LYS GLU THR SER GLY LEU LEU LEU ILE ARG TYR LYS GLU
SEQRES 29 A 475 MET ILE GLY GLU TYR ASP GLU GLU ILE GLY GLY VAL ASP
SEQRES 30 A 475 GLU VAL TYR VAL ASN GLY VAL ASN VAL CYS THR GLU ARG
SEQRES 31 A 475 ILE CYS PRO ILE GLU ARG ALA VAL ASN GLY LEU TRP VAL
SEQRES 32 A 475 PHE ASP ARG GLY ALA ASP GLY LYS SER ASP LEU ASP ARG
SEQRES 33 A 475 GLU VAL VAL ARG TYR SER ILE MET PRO PHE MET SER ALA
SEQRES 34 A 475 ALA ASP LEU VAL VAL PRO ALA GLU GLY THR ILE SER ILE
SEQRES 35 A 475 ALA VAL LYS SER ARG THR GLY GLY GLU GLU SER PHE THR
SEQRES 36 A 475 ILE PRO ALA TRP SER ALA ASP ARG HIS SER ILE ILE VAL
SEQRES 37 A 475 GLN PHE SER ASP TYR ILE VAL
SEQRES 1 B 475 MET ARG GLY LEU ALA VAL LEU VAL LEU LEU VAL PHE ALA
SEQRES 2 B 475 VAL GLN VAL ALA ALA ALA GLU ASP PHE ARG PRO VAL VAL
SEQRES 3 B 475 PHE VAL HIS GLY LEU ALA GLY SER ALA GLY GLN PHE GLU
SEQRES 4 B 475 SER GLN GLY MET ARG PHE ALA ALA ASN GLY TYR PRO ALA
SEQRES 5 B 475 GLU TYR VAL LYS THR PHE GLU TYR ASP THR ILE SER TRP
SEQRES 6 B 475 ALA LEU VAL VAL GLU THR ASP MET LEU PHE SER GLY LEU
SEQRES 7 B 475 GLY SER GLU PHE GLY LEU ASN ILE SER GLN ILE ILE ASP
SEQRES 8 B 475 PRO GLU THR LEU ASP LYS ILE LEU SER LYS SER ARG GLU
SEQRES 9 B 475 ARG LEU ILE ASP GLU THR PHE SER ARG LEU ASP ARG VAL
SEQRES 10 B 475 ILE ASP GLU ALA LEU ALA GLU SER GLY ALA ASP LYS VAL
SEQRES 11 B 475 ASP LEU VAL GLY HIS ALA MET GLY THR PHE PHE LEU VAL
SEQRES 12 B 475 ARG TYR VAL ASN SER SER PRO GLU ARG ALA ALA LYS VAL
SEQRES 13 B 475 ALA HIS LEU ILE LEU LEU ASP GLY VAL TRP GLY VAL ASP
SEQRES 14 B 475 ALA PRO GLU GLY ILE PRO THR LEU ALA VAL PHE GLY ASN
SEQRES 15 B 475 PRO LYS ALA LEU PRO ALA LEU GLY LEU PRO GLU GLU LYS
SEQRES 16 B 475 VAL VAL TYR ASN ALA THR ASN VAL TYR PHE ASN ASN MET
SEQRES 17 B 475 THR HIS VAL GLN LEU CYS THR SER PRO GLU THR PHE ALA
SEQRES 18 B 475 VAL MET PHE GLU PHE ILE ASN GLY TYR LYS PRO ALA THR
SEQRES 19 B 475 THR ASP ILE VAL PRO GLN ASP GLY ASP TYR VAL LYS VAL
SEQRES 20 B 475 LYS GLY LYS PHE LEU ALA PHE ALA THR ASN GLY ASP VAL
SEQRES 21 B 475 SER GLY TRP LEU SER ILE TYR PRO ILE ASP GLU ASN GLY
SEQRES 22 B 475 LYS ARG LEU THR ARG LEU PRO VAL LYS PHE MET ARG VAL
SEQRES 23 B 475 LYS GLY ASP PHE GLU VAL ARG LEU ARG LYS GLY GLN LEU
SEQRES 24 B 475 TYR GLU PHE GLN PHE ARG LYS ASP PHE SER PRO ILE ILE
SEQRES 25 B 475 TYR HIS TYR TYR ARG ALA PRO PHE VAL ARG ASP ASP LEU
SEQRES 26 B 475 TRP ALA ARG PHE LEU VAL SER LYS PRO PRO LEU ASP VAL
SEQRES 27 B 475 GLU LEU LEU ILE LEU PRO GLU ARG LEU SER PRO ALA ALA
SEQRES 28 B 475 LYS GLU THR SER GLY LEU LEU LEU ILE ARG TYR LYS GLU
SEQRES 29 B 475 MET ILE GLY GLU TYR ASP GLU GLU ILE GLY GLY VAL ASP
SEQRES 30 B 475 GLU VAL TYR VAL ASN GLY VAL ASN VAL CYS THR GLU ARG
SEQRES 31 B 475 ILE CYS PRO ILE GLU ARG ALA VAL ASN GLY LEU TRP VAL
SEQRES 32 B 475 PHE ASP ARG GLY ALA ASP GLY LYS SER ASP LEU ASP ARG
SEQRES 33 B 475 GLU VAL VAL ARG TYR SER ILE MET PRO PHE MET SER ALA
SEQRES 34 B 475 ALA ASP LEU VAL VAL PRO ALA GLU GLY THR ILE SER ILE
SEQRES 35 B 475 ALA VAL LYS SER ARG THR GLY GLY GLU GLU SER PHE THR
SEQRES 36 B 475 ILE PRO ALA TRP SER ALA ASP ARG HIS SER ILE ILE VAL
SEQRES 37 B 475 GLN PHE SER ASP TYR ILE VAL
HET R16 A 500 16
HET CA A 700 1
HET R16 B 500 16
HET CA B 700 1
HETNAM R16 HEXADECANE
HETNAM CA CALCIUM ION
FORMUL 3 R16 2(C16 H34)
FORMUL 4 CA 2(CA 2+)
FORMUL 7 HOH *1226(H2 O)
HELIX 1 1 SER A 34 GLN A 37 5 4
HELIX 2 2 PHE A 38 ASN A 48 1 11
HELIX 3 3 PRO A 51 GLU A 53 5 3
HELIX 4 4 ASP A 61 VAL A 69 1 9
HELIX 5 5 GLU A 70 PHE A 75 1 6
HELIX 6 6 PHE A 82 ILE A 86 5 5
HELIX 7 7 ASP A 91 SER A 100 1 10
HELIX 8 8 SER A 102 GLY A 126 1 25
HELIX 9 9 ALA A 136 SER A 148 1 13
HELIX 10 10 SER A 149 ALA A 154 1 6
HELIX 11 11 PRO A 183 LEU A 186 5 4
HELIX 12 12 THR A 209 SER A 216 1 8
HELIX 13 13 SER A 216 GLY A 229 1 14
HELIX 14 14 ASP A 337 LEU A 341 5 5
HELIX 15 15 ILE A 342 LEU A 347 1 6
HELIX 16 16 SER A 348 GLU A 353 5 6
HELIX 17 17 PRO A 393 ALA A 397 5 5
HELIX 18 18 ASP A 405 ASP A 409 5 5
HELIX 19 19 VAL A 418 SER A 422 5 5
HELIX 20 20 SER B 34 GLN B 37 5 4
HELIX 21 21 PHE B 38 ASN B 48 1 11
HELIX 22 22 PRO B 51 GLU B 53 5 3
HELIX 23 23 ASP B 61 VAL B 69 1 9
HELIX 24 24 GLU B 70 SER B 76 1 7
HELIX 25 25 SER B 80 LEU B 84 5 5
HELIX 26 26 ASN B 85 ILE B 90 1 6
HELIX 27 27 ASP B 91 SER B 100 1 10
HELIX 28 28 SER B 102 GLY B 126 1 25
HELIX 29 29 ALA B 136 SER B 148 1 13
HELIX 30 30 SER B 149 ALA B 154 1 6
HELIX 31 31 THR B 209 SER B 216 1 8
HELIX 32 32 SER B 216 GLY B 229 1 14
HELIX 33 33 ASP B 337 LEU B 341 5 5
HELIX 34 34 ILE B 342 LEU B 347 1 6
HELIX 35 35 SER B 348 GLU B 353 5 6
HELIX 36 36 PRO B 393 ALA B 397 5 5
HELIX 37 37 ASP B 405 ASP B 409 5 5
HELIX 38 38 VAL B 418 SER B 422 5 5
SHEET 1 A 6 VAL A 55 PHE A 58 0
SHEET 2 A 6 VAL A 25 VAL A 28 1 N VAL A 25 O LYS A 56
SHEET 3 A 6 VAL A 130 HIS A 135 1 O VAL A 133 N VAL A 26
SHEET 4 A 6 VAL A 156 LEU A 162 1 O LEU A 162 N GLY A 134
SHEET 5 A 6 THR A 176 GLY A 181 1 O LEU A 177 N LEU A 161
SHEET 6 A 6 THR A 201 PHE A 205 1 O PHE A 205 N PHE A 180
SHEET 1 B 3 ASP A 289 ARG A 295 0
SHEET 2 B 3 TYR A 244 ALA A 253 -1 N VAL A 247 O VAL A 292
SHEET 3 B 3 ASP A 324 VAL A 331 1 O ASP A 324 N LYS A 248
SHEET 1 C 8 LYS A 282 LYS A 287 0
SHEET 2 C 8 SER A 261 PRO A 268 -1 N GLY A 262 O VAL A 286
SHEET 3 C 8 TYR A 300 LYS A 306 -1 O GLN A 303 N SER A 265
SHEET 4 C 8 ILE A 312 TYR A 316 -1 O TYR A 315 N PHE A 302
SHEET 5 C 8 HIS A 464 GLN A 469 1 O GLN A 469 N TYR A 316
SHEET 6 C 8 LEU A 357 ILE A 360 1 N LEU A 358 O VAL A 468
SHEET 7 C 8 GLY A 400 PHE A 404 -1 O VAL A 403 N LEU A 357
SHEET 8 C 8 MET A 427 ASP A 431 1 O ALA A 430 N TRP A 402
SHEET 1 D 4 VAL A 384 ASN A 385 0
SHEET 2 D 4 GLU A 378 VAL A 381 -1 N VAL A 381 O VAL A 384
SHEET 3 D 4 THR A 439 LYS A 445 -1 O ALA A 443 N TYR A 380
SHEET 4 D 4 GLU A 451 PRO A 457 -1 O GLU A 452 N VAL A 444
SHEET 1 E 6 VAL B 55 PHE B 58 0
SHEET 2 E 6 VAL B 25 VAL B 28 1 N VAL B 25 O LYS B 56
SHEET 3 E 6 VAL B 130 HIS B 135 1 O VAL B 133 N VAL B 28
SHEET 4 E 6 VAL B 156 LEU B 162 1 O ALA B 157 N VAL B 130
SHEET 5 E 6 THR B 176 PHE B 180 1 O LEU B 177 N LEU B 161
SHEET 6 E 6 THR B 201 TYR B 204 1 O THR B 201 N ALA B 178
SHEET 1 F 3 ASP B 289 ARG B 295 0
SHEET 2 F 3 TYR B 244 ALA B 253 -1 N VAL B 245 O LEU B 294
SHEET 3 F 3 ASP B 324 VAL B 331 1 O ASP B 324 N LYS B 246
SHEET 1 G 8 LYS B 282 LYS B 287 0
SHEET 2 G 8 SER B 261 PRO B 268 -1 N LEU B 264 O MET B 284
SHEET 3 G 8 TYR B 300 LYS B 306 -1 O GLN B 303 N SER B 265
SHEET 4 G 8 ILE B 312 ARG B 317 -1 O TYR B 313 N PHE B 304
SHEET 5 G 8 HIS B 464 GLN B 469 1 O ILE B 467 N HIS B 314
SHEET 6 G 8 LEU B 357 ILE B 360 1 N LEU B 358 O VAL B 468
SHEET 7 G 8 GLY B 400 PHE B 404 -1 O VAL B 403 N LEU B 357
SHEET 8 G 8 MET B 427 ASP B 431 1 O ALA B 430 N TRP B 402
SHEET 1 H 4 VAL B 384 ASN B 385 0
SHEET 2 H 4 GLU B 378 VAL B 381 -1 N VAL B 381 O VAL B 384
SHEET 3 H 4 THR B 439 LYS B 445 -1 O ALA B 443 N TYR B 380
SHEET 4 H 4 GLU B 451 PRO B 457 -1 O GLU B 452 N VAL B 444
LINK OD1 ASP A 405 CA CA A 700 1555 1555 2.25
LINK O ARG A 406 CA CA A 700 1555 1555 2.47
LINK OD2 ASP A 409 CA CA A 700 1555 1555 2.52
LINK O LYS A 411 CA CA A 700 1555 1555 2.40
LINK OD1 ASP A 431 CA CA A 700 1555 1555 2.51
LINK OD2 ASP A 431 CA CA A 700 1555 1555 2.74
LINK OD1 ASP B 405 CA CA B 700 1555 1555 2.42
LINK O ARG B 406 CA CA B 700 1555 1555 2.41
LINK OD2 ASP B 409 CA CA B 700 1555 1555 2.53
LINK O LYS B 411 CA CA B 700 1555 1555 2.42
LINK OD1 ASP B 431 CA CA B 700 1555 1555 2.55
LINK OD2 ASP B 431 CA CA B 700 1555 1555 2.64
LINK CA CA A 700 O HOH A 476 1555 1555 2.62
LINK CA CA B 700 O HOH B 907 1555 1555 2.43
CISPEP 1 PRO A 334 PRO A 335 0 0.20
CISPEP 2 PRO B 334 PRO B 335 0 0.53
SITE 1 AC1 5 LEU A 330 GLU A 339 LEU A 358 ASN A 399
SITE 2 AC1 5 HOH A 511
SITE 1 AC2 6 ASP A 405 ARG A 406 ASP A 409 LYS A 411
SITE 2 AC2 6 ASP A 431 HOH A 476
SITE 1 AC3 5 GLN B 37 VAL B 211 LEU B 330 LEU B 358
SITE 2 AC3 5 HOH B 906
SITE 1 AC4 6 ASP B 405 ARG B 406 ASP B 409 LYS B 411
SITE 2 AC4 6 ASP B 431 HOH B 907
CRYST1 91.196 107.873 118.896 90.00 90.00 90.00 P 21 21 21 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 0.010965 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009270 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008411 0.00000
TER 3602 VAL A 475
TER 7204 VAL B 475
MASTER 450 0 4 38 42 0 8 6 8462 2 50 74
END |