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HEADER HYDROLASE 22-APR-13 4KAA
TITLE CRYSTAL STRUCTURE OF THE HALOTAG2 PROTEIN AT THE RESOLUTION 2.3A,
TITLE 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET OR150
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 GENE: DHAA
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KUZIN,S.LEW,T.K.NEKLESA,D.NOBLIN,J.SEETHARAMAN,M.MAGLAQUI,R.XIAO,
AUTHOR 2 E.KOHAN,H.WANG,J.K.EVERETT,T.B.ACTON,G.T.MONTELIONE,J.F.HUNT,
AUTHOR 3 C.CREWS,L.TONG,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 1 05-JUN-13 4KAA 0
JRNL AUTH A.KUZIN,S.LEW,T.K.NEKLESA,D.NOBLIN,J.SEETHARAMAN,M.MAGLAQUI,
JRNL AUTH 2 R.XIAO,E.KOHAN,H.WANG,J.K.EVERETT,T.B.ACTON,G.T.MONTELIONE,
JRNL AUTH 3 J.F.HUNT,C.CREWS,L.TONG
JRNL TITL NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR150
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.28 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: DEV_1269)
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) : 2.28
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 27706
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 1392
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 29.6151 - 4.8978 1.00 2948 148 0.1508 0.1680
REMARK 3 2 4.8978 - 3.8903 0.99 2566 123 0.1353 0.2070
REMARK 3 3 3.8903 - 3.3994 0.71 1842 101 0.1866 0.2532
REMARK 3 4 3.3994 - 3.0889 1.00 2762 158 0.1820 0.2219
REMARK 3 5 3.0889 - 2.8677 1.00 2739 164 0.1786 0.2575
REMARK 3 6 2.8677 - 2.6988 1.00 2736 164 0.1725 0.2527
REMARK 3 7 2.6988 - 2.5637 1.00 2765 127 0.1708 0.2491
REMARK 3 8 2.5637 - 2.4521 1.00 2746 144 0.1672 0.2564
REMARK 3 9 2.4521 - 2.3578 1.00 2736 139 0.1783 0.2757
REMARK 3 10 2.3578 - 2.2764 0.90 2474 124 0.1946 0.3172
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.780
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.15
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.83
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 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 : 0.008 4901
REMARK 3 ANGLE : 1.169 6709
REMARK 3 CHIRALITY : 0.085 707
REMARK 3 PLANARITY : 0.006 888
REMARK 3 DIHEDRAL : 13.840 1806
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: all
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0994 -3.6985 36.4341
REMARK 3 T TENSOR
REMARK 3 T11: 0.1378 T22: 0.1439
REMARK 3 T33: 0.1787 T12: 0.0010
REMARK 3 T13: -0.0155 T23: 0.0108
REMARK 3 L TENSOR
REMARK 3 L11: 0.6651 L22: 0.0928
REMARK 3 L33: 1.2481 L12: -0.1171
REMARK 3 L13: -0.6979 L23: 0.1077
REMARK 3 S TENSOR
REMARK 3 S11: 0.0200 S12: 0.0153 S13: 0.0217
REMARK 3 S21: 0.0079 S22: -0.0177 S23: -0.0057
REMARK 3 S31: -0.0468 S32: -0.0001 S33: -0.0004
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 4KAA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-13.
REMARK 100 THE RCSB ID CODE IS RCSB079088.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
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 : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52782
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.276
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: PDB ENTRY 1BN7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 100MM NACL, 5MM DTT,
REMARK 280 0.02% NAN3, 10MM TRIS-HCL (PH 7.5) . RESERVOIR SOLUTION:CACL2
REMARK 280 0.1M, MES 0.1M, PEG 8000 40%, MICROBATCH UNDER OIL, TEMPERATURE
REMARK 280 277K
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 34.81500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.07850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.63100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.07850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.81500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.63100
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 MSE A 1
REMARK 465 GLY 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 HIS A 8
REMARK 465 SER A 9
REMARK 465 HIS A 10
REMARK 465 MSE A 11
REMARK 465 GLY A 12
REMARK 465 MSE B 1
REMARK 465 GLY B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 SER B 9
REMARK 465 HIS B 10
REMARK 465 MSE B 11
REMARK 465 GLY B 12
REMARK 465 SER B 13
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 PHE A 216 CE1 CE2 CZ
REMARK 470 PHE B 216 CE1 CE2 CZ
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 PHE A 216 CG PHE A 216 CD2 0.140
REMARK 500 PHE A 216 CG PHE A 216 CD1 0.144
REMARK 500 PHE B 216 CG PHE B 216 CD2 0.136
REMARK 500 PHE B 216 CG PHE B 216 CD1 0.135
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 PHE A 216 CB - CG - CD2 ANGL. DEV. = -9.5 DEGREES
REMARK 500 PHE A 216 CD1 - CG - CD2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 PHE A 216 CB - CG - CD1 ANGL. DEV. = -9.3 DEGREES
REMARK 500 PHE B 216 CB - CG - CD2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 PHE B 216 CD1 - CG - CD2 ANGL. DEV. = -9.1 DEGREES
REMARK 500 PHE B 216 CB - CG - CD1 ANGL. DEV. = -9.6 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 PRO A 53 51.52 -96.06
REMARK 500 THR A 54 -161.25 -111.76
REMARK 500 SER A 55 -163.89 -161.00
REMARK 500 GLU A 109 -90.91 -99.27
REMARK 500 ASP A 117 -125.36 50.72
REMARK 500 GLU A 141 57.12 39.40
REMARK 500 ASP A 167 -37.90 45.81
REMARK 500 VAL A 256 -68.65 -133.68
REMARK 500 LEU A 282 -101.01 -122.15
REMARK 500 PRO B 20 58.14 -90.42
REMARK 500 PRO B 53 46.98 -95.64
REMARK 500 THR B 54 -162.41 -104.37
REMARK 500 GLU B 109 -103.39 -98.26
REMARK 500 ASP B 117 -126.59 56.05
REMARK 500 GLU B 141 55.79 37.71
REMARK 500 ASP B 167 -56.80 75.27
REMARK 500 VAL B 256 -69.52 -135.90
REMARK 500 LEU B 282 -100.19 -121.70
REMARK 500 ALA B 305 -156.74 -138.50
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 ASP A 167 24.2 L L OUTSIDE RANGE
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 NA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BN7 RELATED DB: PDB
REMARK 900 HOMOLOGY IS 97.95%
REMARK 900 RELATED ID: NESG-OR150 RELATED DB: TARGETTRACK
DBREF 4KAA A 13 304 UNP P0A3G3 DHAA_RHOSO 2 293
DBREF 4KAA B 13 304 UNP P0A3G3 DHAA_RHOSO 2 293
SEQADV 4KAA MSE A 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA GLY A 2 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS A 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS A 4 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS A 5 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS A 6 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS A 7 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS A 8 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA SER A 9 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS A 10 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA MSE A 11 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA GLY A 12 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA MSE A 186 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 4KAA GLY A 187 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 4KAA PHE A 283 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 4KAA LEU A 284 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 4KAA GLY A 303 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 4KAA ALA A 305 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA GLY A 306 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA MSE B 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA GLY B 2 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS B 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS B 4 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS B 5 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS B 6 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS B 7 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS B 8 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA SER B 9 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA HIS B 10 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA MSE B 11 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA GLY B 12 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA MSE B 186 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 4KAA GLY B 187 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 4KAA PHE B 283 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 4KAA LEU B 284 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 4KAA GLY B 303 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 4KAA ALA B 305 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAA GLY B 306 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 306 MSE GLY HIS HIS HIS HIS HIS HIS SER HIS MSE GLY SER
SEQRES 2 A 306 GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 3 A 306 GLU VAL LEU GLY GLU ARG MSE HIS TYR VAL ASP VAL GLY
SEQRES 4 A 306 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 5 A 306 PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS
SEQRES 6 A 306 VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 7 A 306 GLY MSE GLY LYS SER ASP LYS PRO ASP LEU ASP TYR PHE
SEQRES 8 A 306 PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU
SEQRES 9 A 306 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 10 A 306 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 11 A 306 PRO GLU ARG VAL LYS GLY ILE ALA CYS MSE GLU PHE ILE
SEQRES 12 A 306 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 13 A 306 ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP VAL GLY
SEQRES 14 A 306 ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY
SEQRES 15 A 306 ALA LEU PRO MSE GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 16 A 306 GLU MSE ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL
SEQRES 17 A 306 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 18 A 306 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 19 A 306 ALA TYR MSE ASN TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 20 A 306 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 21 A 306 ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS
SEQRES 22 A 306 LYS THR VAL ASP ILE GLY PRO GLY LEU PHE LEU LEU GLN
SEQRES 23 A 306 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 24 A 306 TRP LEU PRO GLY LEU ALA GLY
SEQRES 1 B 306 MSE GLY HIS HIS HIS HIS HIS HIS SER HIS MSE GLY SER
SEQRES 2 B 306 GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 3 B 306 GLU VAL LEU GLY GLU ARG MSE HIS TYR VAL ASP VAL GLY
SEQRES 4 B 306 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 5 B 306 PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE PRO HIS
SEQRES 6 B 306 VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 7 B 306 GLY MSE GLY LYS SER ASP LYS PRO ASP LEU ASP TYR PHE
SEQRES 8 B 306 PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE ILE GLU
SEQRES 9 B 306 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 10 B 306 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 11 B 306 PRO GLU ARG VAL LYS GLY ILE ALA CYS MSE GLU PHE ILE
SEQRES 12 B 306 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 13 B 306 ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP VAL GLY
SEQRES 14 B 306 ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE GLU GLY
SEQRES 15 B 306 ALA LEU PRO MSE GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 16 B 306 GLU MSE ASP HIS TYR ARG GLU PRO PHE LEU LYS PRO VAL
SEQRES 17 B 306 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 18 B 306 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 19 B 306 ALA TYR MSE ASN TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 20 B 306 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 21 B 306 ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO ASN CYS
SEQRES 22 B 306 LYS THR VAL ASP ILE GLY PRO GLY LEU PHE LEU LEU GLN
SEQRES 23 B 306 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 24 B 306 TRP LEU PRO GLY LEU ALA GLY
MODRES 4KAA MSE A 33 MET SELENOMETHIONINE
MODRES 4KAA MSE A 80 MET SELENOMETHIONINE
MODRES 4KAA MSE A 140 MET SELENOMETHIONINE
MODRES 4KAA MSE A 186 MET SELENOMETHIONINE
MODRES 4KAA MSE A 197 MET SELENOMETHIONINE
MODRES 4KAA MSE A 237 MET SELENOMETHIONINE
MODRES 4KAA MSE B 33 MET SELENOMETHIONINE
MODRES 4KAA MSE B 80 MET SELENOMETHIONINE
MODRES 4KAA MSE B 140 MET SELENOMETHIONINE
MODRES 4KAA MSE B 186 MET SELENOMETHIONINE
MODRES 4KAA MSE B 197 MET SELENOMETHIONINE
MODRES 4KAA MSE B 237 MET SELENOMETHIONINE
HET MSE A 33 8
HET MSE A 80 8
HET MSE A 140 8
HET MSE A 186 8
HET MSE A 197 8
HET MSE A 237 8
HET MSE B 33 8
HET MSE B 80 8
HET MSE B 140 8
HET MSE B 186 16
HET MSE B 197 8
HET MSE B 237 8
HET NA A 401 1
HET PEG B 401 7
HET NA B 402 1
HETNAM MSE SELENOMETHIONINE
HETNAM NA SODIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 3 NA 2(NA 1+)
FORMUL 4 PEG C4 H10 O3
FORMUL 6 HOH *320(H2 O)
HELIX 1 1 SER A 55 ARG A 60 5 6
HELIX 2 2 ILE A 62 ALA A 67 1 6
HELIX 3 3 PHE A 91 LEU A 106 1 16
HELIX 4 4 ASP A 117 ASN A 130 1 14
HELIX 5 5 THR A 148 TRP A 152 5 5
HELIX 6 6 PRO A 153 ARG A 164 1 12
HELIX 7 7 ASP A 167 ILE A 174 1 8
HELIX 8 8 ASN A 177 GLY A 182 1 6
HELIX 9 9 GLY A 182 GLY A 187 1 6
HELIX 10 10 THR A 193 GLU A 202 1 10
HELIX 11 11 PRO A 203 LEU A 205 5 3
HELIX 12 12 LYS A 206 ASP A 209 5 4
HELIX 13 13 ARG A 210 PHE A 216 1 7
HELIX 14 14 PRO A 226 SER A 243 1 18
HELIX 15 15 PRO A 259 LEU A 270 1 12
HELIX 16 16 LEU A 284 ASN A 289 1 6
HELIX 17 17 ASN A 289 LEU A 301 1 13
HELIX 18 18 PRO A 302 GLY A 306 5 5
HELIX 19 19 SER B 55 ARG B 60 5 6
HELIX 20 20 ILE B 62 ALA B 67 1 6
HELIX 21 21 PHE B 91 LEU B 106 1 16
HELIX 22 22 ASP B 117 ASN B 130 1 14
HELIX 23 23 THR B 148 TRP B 152 5 5
HELIX 24 24 PRO B 153 PHE B 155 5 3
HELIX 25 25 ALA B 156 ARG B 164 1 9
HELIX 26 26 ASP B 167 ILE B 174 1 8
HELIX 27 27 ASN B 177 GLY B 182 1 6
HELIX 28 28 GLY B 182 GLY B 187 1 6
HELIX 29 29 THR B 193 GLU B 202 1 10
HELIX 30 30 PRO B 203 LEU B 205 5 3
HELIX 31 31 LYS B 206 ASP B 209 5 4
HELIX 32 32 ARG B 210 LEU B 220 1 11
HELIX 33 33 PRO B 226 SER B 243 1 18
HELIX 34 34 PRO B 259 LEU B 270 1 12
HELIX 35 35 LEU B 284 ASN B 289 1 6
HELIX 36 36 ASN B 289 LEU B 301 1 13
HELIX 37 37 PRO B 302 LEU B 304 5 3
SHEET 1 A 8 HIS A 24 VAL A 28 0
SHEET 2 A 8 GLU A 31 VAL A 38 -1 O GLU A 31 N VAL A 28
SHEET 3 A 8 CYS A 72 PRO A 75 -1 O CYS A 72 N VAL A 38
SHEET 4 A 8 VAL A 46 LEU A 49 1 N PHE A 48 O ILE A 73
SHEET 5 A 8 VAL A 111 HIS A 116 1 O VAL A 112 N LEU A 47
SHEET 6 A 8 VAL A 134 MSE A 140 1 O ALA A 138 N LEU A 113
SHEET 7 A 8 LYS A 247 PRO A 254 1 O LEU A 248 N CYS A 139
SHEET 8 A 8 CYS A 273 GLY A 281 1 O LYS A 274 N LEU A 249
SHEET 1 B 8 HIS B 24 VAL B 28 0
SHEET 2 B 8 GLU B 31 VAL B 38 -1 O GLU B 31 N VAL B 28
SHEET 3 B 8 CYS B 72 PRO B 75 -1 O CYS B 72 N VAL B 38
SHEET 4 B 8 VAL B 46 LEU B 49 1 N PHE B 48 O ILE B 73
SHEET 5 B 8 VAL B 111 HIS B 116 1 O VAL B 112 N LEU B 47
SHEET 6 B 8 VAL B 134 MSE B 140 1 O ALA B 138 N LEU B 113
SHEET 7 B 8 LYS B 247 PRO B 254 1 O LEU B 248 N ILE B 137
SHEET 8 B 8 CYS B 273 GLY B 281 1 O LYS B 274 N LEU B 249
LINK C ARG A 32 N MSE A 33 1555 1555 1.32
LINK C MSE A 33 N HIS A 34 1555 1555 1.33
LINK C GLY A 79 N MSE A 80 1555 1555 1.33
LINK C MSE A 80 N GLY A 81 1555 1555 1.33
LINK C CYS A 139 N MSE A 140 1555 1555 1.33
LINK C MSE A 140 N GLU A 141 1555 1555 1.33
LINK C PRO A 185 N MSE A 186 1555 1555 1.33
LINK C MSE A 186 N GLY A 187 1555 1555 1.33
LINK C GLU A 196 N MSE A 197 1555 1555 1.33
LINK C MSE A 197 N ASP A 198 1555 1555 1.33
LINK C TYR A 236 N MSE A 237 1555 1555 1.33
LINK C MSE A 237 N ASN A 238 1555 1555 1.33
LINK C ARG B 32 N MSE B 33 1555 1555 1.32
LINK C MSE B 33 N HIS B 34 1555 1555 1.33
LINK C GLY B 79 N MSE B 80 1555 1555 1.33
LINK C MSE B 80 N GLY B 81 1555 1555 1.33
LINK C CYS B 139 N MSE B 140 1555 1555 1.32
LINK C MSE B 140 N GLU B 141 1555 1555 1.34
LINK C PRO B 185 N AMSE B 186 1555 1555 1.33
LINK C PRO B 185 N BMSE B 186 1555 1555 1.33
LINK C AMSE B 186 N GLY B 187 1555 1555 1.33
LINK C BMSE B 186 N GLY B 187 1555 1555 1.33
LINK C GLU B 196 N MSE B 197 1555 1555 1.33
LINK C MSE B 197 N ASP B 198 1555 1555 1.33
LINK C TYR B 236 N MSE B 237 1555 1555 1.34
LINK C MSE B 237 N ASN B 238 1555 1555 1.33
LINK OD1 ASN B 52 NA NA B 402 1555 1555 2.26
LINK OD1 ASN A 52 NA NA A 401 1555 1555 2.43
CISPEP 1 ASN A 52 PRO A 53 0 -9.65
CISPEP 2 GLU A 225 PRO A 226 0 -3.40
CISPEP 3 THR A 253 PRO A 254 0 1.93
CISPEP 4 ASN B 52 PRO B 53 0 -11.71
CISPEP 5 GLU B 225 PRO B 226 0 -1.46
CISPEP 6 THR B 253 PRO B 254 0 3.43
SITE 1 AC1 4 ASN A 52 TRP A 118 PRO A 217 LEU A 220
SITE 1 AC2 1 ASP B 89
SITE 1 AC3 5 ASN B 52 TRP B 118 PHE B 216 PRO B 217
SITE 2 AC3 5 LEU B 220
CRYST1 69.630 91.262 98.157 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 0.014362 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010957 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010188 0.00000
TER 2361 GLY A 306
TER 4733 GLY B 306
MASTER 383 0 15 37 16 0 4 6 5009 2 139 48
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