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HEADER HYDROLASE 07-JUN-12 4FHZ
TITLE CRYSTAL STRUCTURE OF A CARBOXYL ESTERASE AT 2.0 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE/CARBOXYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES;
SOURCE 3 ORGANISM_TAXID: 1063;
SOURCE 4 STRAIN: CGMCC1.1737;
SOURCE 5 GENE: RSP_2728;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-30A
KEYWDS ESTERASE, ALPHA/BETA HYDROLASE SUPERFAMILY, CENTRAL BETA-STRANDED
KEYWDS 2 SHEET, FLANKED ALPHA HELICES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.WU,J.MA,J.ZHOU,H.YU
REVDAT 1 03-OCT-12 4FHZ 0
JRNL AUTH J.MA,L.WU,F.GUO,J.GU,X.TANG,L.JIANG,J.LIU,J.ZHOU,H.YU
JRNL TITL ENHANCED ENANTIOSELECTIVITY OF A CARBOXYL ESTERASE FROM
JRNL TITL 2 RHODOBACTER SPHAEROIDES BY DIRECTED EVOLUTION.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. 2012
JRNL REFN ESSN 1432-0614
JRNL PMID 22987200
JRNL DOI 10.1007/S00253-012-4396-2
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.34
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 23106
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150
REMARK 3 FREE R VALUE TEST SET COUNT : 1191
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 34.3407 - 4.1779 0.95 2498 116 0.1607 0.1874
REMARK 3 2 4.1779 - 3.3170 1.00 2505 118 0.1503 0.1977
REMARK 3 3 3.3170 - 2.8980 1.00 2447 141 0.1786 0.2610
REMARK 3 4 2.8980 - 2.6331 1.00 2438 138 0.1777 0.2557
REMARK 3 5 2.6331 - 2.4444 1.00 2427 129 0.1552 0.2352
REMARK 3 6 2.4444 - 2.3003 1.00 2427 156 0.1435 0.1994
REMARK 3 7 2.3003 - 2.1852 1.00 2383 139 0.1203 0.2074
REMARK 3 8 2.1852 - 2.0901 1.00 2437 127 0.1410 0.2061
REMARK 3 9 2.0901 - 2.0100 0.98 2353 127 0.1779 0.2578
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 57.31
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.850
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.86440
REMARK 3 B22 (A**2) : -0.86440
REMARK 3 B33 (A**2) : 1.72880
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 1763
REMARK 3 ANGLE : 0.920 2420
REMARK 3 CHIRALITY : 0.067 266
REMARK 3 PLANARITY : 0.005 328
REMARK 3 DIHEDRAL : 12.445 668
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4FHZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB072924.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23109
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 8.400
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : 0.09000
REMARK 200 FOR THE DATA SET : 18.1280
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.00
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: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3M SODIUM CHLORIDE, CITRIC ACID,1%
REMARK 280 PEG3350, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.72200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.86100
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.86100
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 75.72200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 1510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -75.72200
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 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 11
REMARK 465 VAL A 12
REMARK 465 PRO A 13
REMARK 465 ARG A 14
REMARK 465 GLY A 15
REMARK 465 SER A 16
REMARK 465 GLY A 17
REMARK 465 MET A 18
REMARK 465 LYS A 19
REMARK 465 GLU A 20
REMARK 465 THR A 21
REMARK 465 ALA A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 LYS A 25
REMARK 465 PHE A 26
REMARK 465 GLU A 27
REMARK 465 ARG A 28
REMARK 465 GLN A 29
REMARK 465 HIS A 30
REMARK 465 MET A 31
REMARK 465 ASP A 32
REMARK 465 SER A 33
REMARK 465 PRO A 34
REMARK 465 ASP A 35
REMARK 465 LEU A 36
REMARK 465 GLY A 37
REMARK 465 THR A 38
REMARK 465 ASP A 39
REMARK 465 ASP A 40
REMARK 465 ASP A 41
REMARK 465 ASP A 42
REMARK 465 LYS A 43
REMARK 465 ALA A 44
REMARK 465 MET A 45
REMARK 465 ALA A 46
REMARK 465 ASP A 47
REMARK 465 ASP A 268
REMARK 465 ALA A 269
REMARK 465 CYS A 270
REMARK 465 GLY A 271
REMARK 465 ARG A 272
REMARK 465 THR A 273
REMARK 465 ARG A 274
REMARK 465 ALA A 275
REMARK 465 PRO A 276
REMARK 465 PRO A 277
REMARK 465 PRO A 278
REMARK 465 PRO A 279
REMARK 465 PRO A 280
REMARK 465 LEU A 281
REMARK 465 ARG A 282
REMARK 465 SER A 283
REMARK 465 GLY A 284
REMARK 465 CYS A 285
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 MET A 243 CA CB CG SD CE
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 ARG A 58 N ARG A 58 CA -0.126
REMARK 500 ARG A 58 CA ARG A 58 C -0.247
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 58 CA - C - O ANGL. DEV. = -17.9 DEGREES
REMARK 500 ARG A 58 CA - C - N ANGL. DEV. = 19.1 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 77 -159.32 -100.77
REMARK 500 SER A 165 -118.74 56.25
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 ARG A 58 24.0 L L OUTSIDE RANGE
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 NA A 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 108 O
REMARK 620 2 HOH A 458 O 104.4
REMARK 620 3 HOH A 457 O 118.4 112.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 436 O
REMARK 620 2 GLY A 187 O 133.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 102 O
REMARK 620 2 HOH A 431 O 119.4
REMARK 620 3 HOH A 412 O 98.2 54.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 308 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 165 OG
REMARK 620 2 HOH A 401 O 68.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FTW RELATED DB: PDB
DBREF 4FHZ A 49 268 UNP Q3J2V1 Q3J2V1_RHOS4 1 220
SEQADV 4FHZ MET A 1 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ HIS A 2 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ HIS A 3 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ HIS A 4 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ HIS A 5 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ HIS A 6 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ HIS A 7 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ SER A 8 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ SER A 9 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ GLY A 10 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ LEU A 11 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ VAL A 12 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ PRO A 13 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ARG A 14 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ GLY A 15 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ SER A 16 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ GLY A 17 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ MET A 18 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ LYS A 19 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ GLU A 20 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ THR A 21 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ALA A 22 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ALA A 23 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ALA A 24 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ LYS A 25 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ PHE A 26 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ GLU A 27 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ARG A 28 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ GLN A 29 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ HIS A 30 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ MET A 31 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ASP A 32 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ SER A 33 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ PRO A 34 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ASP A 35 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ LEU A 36 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ GLY A 37 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ THR A 38 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ASP A 39 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ASP A 40 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ASP A 41 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ASP A 42 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ LYS A 43 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ALA A 44 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ MET A 45 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ALA A 46 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ASP A 47 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ILE A 48 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ALA A 269 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ CYS A 270 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ GLY A 271 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ARG A 272 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ THR A 273 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ARG A 274 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ALA A 275 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ PRO A 276 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ PRO A 277 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ PRO A 278 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ PRO A 279 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ PRO A 280 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ LEU A 281 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ ARG A 282 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ SER A 283 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ GLY A 284 UNP Q3J2V1 EXPRESSION TAG
SEQADV 4FHZ CYS A 285 UNP Q3J2V1 EXPRESSION TAG
SEQRES 1 A 285 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 A 285 ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE
SEQRES 3 A 285 GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP
SEQRES 4 A 285 ASP ASP ASP LYS ALA MET ALA ASP ILE MET THR ARG LYS
SEQRES 5 A 285 LEU THR PHE GLY ARG ARG GLY ALA ALA PRO GLY GLU ALA
SEQRES 6 A 285 THR SER LEU VAL VAL PHE LEU HIS GLY TYR GLY ALA ASP
SEQRES 7 A 285 GLY ALA ASP LEU LEU GLY LEU ALA GLU PRO LEU ALA PRO
SEQRES 8 A 285 HIS LEU PRO GLY THR ALA PHE VAL ALA PRO ASP ALA PRO
SEQRES 9 A 285 GLU PRO CYS ARG ALA ASN GLY PHE GLY PHE GLN TRP PHE
SEQRES 10 A 285 PRO ILE PRO TRP LEU ASP GLY SER SER GLU THR ALA ALA
SEQRES 11 A 285 ALA GLU GLY MET ALA ALA ALA ALA ARG ASP LEU ASP ALA
SEQRES 12 A 285 PHE LEU ASP GLU ARG LEU ALA GLU GLU GLY LEU PRO PRO
SEQRES 13 A 285 GLU ALA LEU ALA LEU VAL GLY PHE SER GLN GLY THR MET
SEQRES 14 A 285 MET ALA LEU HIS VAL ALA PRO ARG ARG ALA GLU GLU ILE
SEQRES 15 A 285 ALA GLY ILE VAL GLY PHE SER GLY ARG LEU LEU ALA PRO
SEQRES 16 A 285 GLU ARG LEU ALA GLU GLU ALA ARG SER LYS PRO PRO VAL
SEQRES 17 A 285 LEU LEU VAL HIS GLY ASP ALA ASP PRO VAL VAL PRO PHE
SEQRES 18 A 285 ALA ASP MET SER LEU ALA GLY GLU ALA LEU ALA GLU ALA
SEQRES 19 A 285 GLY PHE THR THR TYR GLY HIS VAL MET LYS GLY THR GLY
SEQRES 20 A 285 HIS GLY ILE ALA PRO ASP GLY LEU SER VAL ALA LEU ALA
SEQRES 21 A 285 PHE LEU LYS GLU ARG LEU PRO ASP ALA CYS GLY ARG THR
SEQRES 22 A 285 ARG ALA PRO PRO PRO PRO PRO LEU ARG SER GLY CYS
HET NA A 301 1
HET NA A 302 1
HET NA A 303 1
HET NA A 304 1
HET PEG A 305 7
HET NA A 306 1
HET NA A 307 1
HET NA A 308 1
HETNAM NA SODIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 2 NA 7(NA 1+)
FORMUL 6 PEG C4 H10 O3
FORMUL 10 HOH *90(H2 O)
HELIX 1 1 ASP A 78 GLY A 84 1 7
HELIX 2 2 LEU A 85 ALA A 90 1 6
HELIX 3 3 PRO A 91 LEU A 93 5 3
HELIX 4 4 ILE A 119 GLY A 124 1 6
HELIX 5 5 SER A 126 GLY A 153 1 28
HELIX 6 6 PRO A 155 GLU A 157 5 3
HELIX 7 7 SER A 165 ARG A 178 1 14
HELIX 8 8 ALA A 194 ALA A 202 1 9
HELIX 9 9 PHE A 221 ALA A 234 1 14
HELIX 10 10 ALA A 251 LEU A 266 1 16
SHEET 1 A 7 PHE A 55 GLY A 59 0
SHEET 2 A 7 THR A 96 PRO A 101 -1 O PHE A 98 N ARG A 58
SHEET 3 A 7 SER A 67 LEU A 72 1 N PHE A 71 O VAL A 99
SHEET 4 A 7 LEU A 159 PHE A 164 1 O ALA A 160 N LEU A 68
SHEET 5 A 7 GLY A 184 PHE A 188 1 O VAL A 186 N GLY A 163
SHEET 6 A 7 VAL A 208 GLY A 213 1 O LEU A 209 N ILE A 185
SHEET 7 A 7 THR A 238 MET A 243 1 O TYR A 239 N VAL A 208
SHEET 1 B 2 GLU A 105 PRO A 106 0
SHEET 2 B 2 PHE A 114 GLN A 115 -1 O GLN A 115 N GLU A 105
LINK O ARG A 108 NA NA A 304 1555 1555 2.78
LINK OD1 ASP A 102 NA NA A 302 1555 1555 2.81
LINK NA NA A 303 O HOH A 436 1555 1555 2.85
LINK O GLY A 187 NA NA A 303 1555 1555 2.86
LINK NA NA A 304 O HOH A 458 1555 1555 2.87
LINK NA NA A 304 O HOH A 457 1555 1555 2.87
LINK O ASP A 102 NA NA A 301 1555 1555 2.88
LINK OG SER A 165 NA NA A 308 1555 1555 2.92
LINK NA NA A 301 O HOH A 431 1555 1555 3.09
LINK NA NA A 301 O HOH A 412 1555 1555 3.17
LINK NA NA A 308 O HOH A 401 1555 1555 3.17
SITE 1 AC1 4 LEU A 53 THR A 54 ASP A 102 HOH A 431
SITE 1 AC2 3 GLY A 79 ALA A 80 ASP A 102
SITE 1 AC3 6 THR A 168 GLY A 187 PHE A 188 SER A 189
SITE 2 AC3 6 GLY A 190 HOH A 436
SITE 1 AC4 6 ARG A 108 PRO A 217 GLY A 247 HIS A 248
SITE 2 AC4 6 HOH A 457 HOH A 458
SITE 1 AC5 2 LEU A 122 NA A 308
SITE 1 AC6 5 HIS A 73 GLY A 74 LEU A 82 PHE A 112
SITE 2 AC6 5 HOH A 404
SITE 1 AC7 4 ARG A 191 LEU A 192 ASP A 223 ALA A 227
SITE 1 AC8 4 TYR A 75 SER A 165 GLN A 166 PEG A 305
CRYST1 72.042 72.042 113.583 90.00 90.00 120.00 P 32 2 1 6
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 0.013881 0.008014 0.000000 0.00000
SCALE2 0.000000 0.016028 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008804 0.00000
TER 1707 PRO A 267
MASTER 439 0 8 10 9 0 11 6 1715 1 23 22
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