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HEADER HYDROLASE 22-APR-13 4KAC
TITLE X-RAY STRUCTURE OF THE COMPLEX HALOTAG2 WITH HALTS. NORTHEAST
TITLE 2 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.KORNHABER,G.T.MONTELIONE,
AUTHOR 3 C.M.CREWS,J.F.HUNT,L.TONG,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 4 (NESG)
REVDAT 1 05-JUN-13 4KAC 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.KORNHABER,
JRNL AUTH 3 G.T.MONTELIONE,C.M.CREWS,J.F.HUNT,L.TONG
JRNL TITL NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR150
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.22 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) : 2.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.890
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 28743
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1456
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 42.7895 - 4.7868 1.00 2784 160 0.1650 0.1987
REMARK 3 2 4.7868 - 3.8002 1.00 2777 137 0.1474 0.2040
REMARK 3 3 3.8002 - 3.3200 1.00 2734 153 0.1746 0.2177
REMARK 3 4 3.3200 - 3.0165 1.00 2775 139 0.1857 0.2766
REMARK 3 5 3.0165 - 2.8004 1.00 2729 143 0.1878 0.2460
REMARK 3 6 2.8004 - 2.6353 0.99 2729 143 0.1881 0.2674
REMARK 3 7 2.6353 - 2.5033 0.99 2706 160 0.1812 0.2725
REMARK 3 8 2.5033 - 2.3944 0.99 2718 138 0.1802 0.3219
REMARK 3 9 2.3944 - 2.3022 0.99 2744 133 0.1822 0.2435
REMARK 3 10 2.3022 - 2.2228 0.95 2591 150 0.1907 0.3189
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.900
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.62
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 4910
REMARK 3 ANGLE : 1.163 6708
REMARK 3 CHIRALITY : 0.081 700
REMARK 3 PLANARITY : 0.007 880
REMARK 3 DIHEDRAL : 14.127 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): 10.0749 11.0063 20.6503
REMARK 3 T TENSOR
REMARK 3 T11: 0.0999 T22: 0.1057
REMARK 3 T33: 0.1286 T12: -0.0090
REMARK 3 T13: -0.0091 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 0.1544 L22: 0.2979
REMARK 3 L33: 0.6525 L12: -0.1125
REMARK 3 L13: -0.2151 L23: 0.3831
REMARK 3 S TENSOR
REMARK 3 S11: -0.0097 S12: 0.0054 S13: 0.0064
REMARK 3 S21: -0.0008 S22: -0.0276 S23: 0.0248
REMARK 3 S31: -0.0067 S32: -0.0343 S33: 0.0424
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 4KAC 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 RCSB079090.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 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) : 0.979
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 : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51681
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.223
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.11800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.3000
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 (%): 42.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
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: AMMONIUM
REMARK 280 NITRATE 0.1M, SODIUM ACETATE 0.1M, MICROBATCH UNDER OIL,
REMARK 280 TEMPERATURE 277K
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 47.49200
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 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 SER A 13
REMARK 465 GLY A 306
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 465 GLY B 306
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 58.29 -103.96
REMARK 500 THR A 54 -155.83 -114.71
REMARK 500 LYS A 85 74.68 -119.36
REMARK 500 GLU A 109 -93.16 -105.85
REMARK 500 ASP A 117 -126.76 53.02
REMARK 500 ARG A 164 42.85 -86.35
REMARK 500 ASP A 167 -71.48 -92.27
REMARK 500 VAL A 256 -63.66 -124.86
REMARK 500 LEU A 282 -96.34 -123.49
REMARK 500 PRO B 53 46.12 -103.17
REMARK 500 THR B 54 -154.80 -107.92
REMARK 500 LEU B 77 155.74 -49.39
REMARK 500 GLU B 109 -93.17 -97.93
REMARK 500 ASP B 117 -130.59 56.64
REMARK 500 GLU B 151 45.32 -69.88
REMARK 500 ARG B 164 38.06 -91.33
REMARK 500 ASP B 167 -66.66 -94.56
REMARK 500 VAL B 256 -66.84 -137.92
REMARK 500 LEU B 282 -91.72 -110.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PE4 B 403
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Q9 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1Q9 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 B 403
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 4KAC A 13 304 UNP P0A3G3 DHAA_RHOSO 2 293
DBREF 4KAC B 13 304 UNP P0A3G3 DHAA_RHOSO 2 293
SEQADV 4KAC MSE A 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC GLY A 2 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS A 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS A 4 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS A 5 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS A 6 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS A 7 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS A 8 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC SER A 9 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS A 10 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC MSE A 11 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC GLY A 12 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC MSE A 186 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 4KAC GLY A 187 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 4KAC PHE A 283 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 4KAC LEU A 284 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 4KAC GLY A 303 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 4KAC ALA A 305 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC GLY A 306 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC MSE B 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC GLY B 2 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS B 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS B 4 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS B 5 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS B 6 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS B 7 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS B 8 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC SER B 9 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC HIS B 10 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC MSE B 11 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC GLY B 12 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC MSE B 186 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 4KAC GLY B 187 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 4KAC PHE B 283 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 4KAC LEU B 284 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 4KAC GLY B 303 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 4KAC ALA B 305 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAC 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 4KAC MSE A 33 MET SELENOMETHIONINE
MODRES 4KAC MSE A 80 MET SELENOMETHIONINE
MODRES 4KAC MSE A 140 MET SELENOMETHIONINE
MODRES 4KAC MSE A 186 MET SELENOMETHIONINE
MODRES 4KAC MSE A 197 MET SELENOMETHIONINE
MODRES 4KAC MSE A 237 MET SELENOMETHIONINE
MODRES 4KAC MSE B 33 MET SELENOMETHIONINE
MODRES 4KAC MSE B 80 MET SELENOMETHIONINE
MODRES 4KAC MSE B 140 MET SELENOMETHIONINE
MODRES 4KAC MSE B 186 MET SELENOMETHIONINE
MODRES 4KAC MSE B 197 MET SELENOMETHIONINE
MODRES 4KAC 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 8
HET MSE B 197 8
HET MSE B 237 8
HET 1Q9 A 401 18
HET NH4 B 401 1
HET 1Q9 B 402 18
HET PE4 B 403 26
HETNAM MSE SELENOMETHIONINE
HETNAM 1Q9 N-(2-ETHOXY-3,5-DIMETHYLBENZYL)-1H-TETRAZOL-5-AMINE
HETNAM NH4 AMMONIUM ION
HETNAM PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM 2 PE4 ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETSYN PE4 POLYETHYLENE GLYCOL PEG4000
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 3 1Q9 2(C12 H17 N5 O)
FORMUL 4 NH4 H4 N 1+
FORMUL 6 PE4 C16 H34 O8
FORMUL 7 HOH *274(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 PHE A 155 5 3
HELIX 7 7 ALA A 156 ARG A 164 1 9
HELIX 8 8 ASP A 167 ILE A 174 1 8
HELIX 9 9 ASN A 177 GLY A 182 1 6
HELIX 10 10 GLY A 182 GLY A 187 1 6
HELIX 11 11 THR A 193 GLU A 202 1 10
HELIX 12 12 PRO A 203 LEU A 205 5 3
HELIX 13 13 LYS A 206 ASP A 209 5 4
HELIX 14 14 ARG A 210 GLU A 219 1 10
HELIX 15 15 PRO A 226 SER A 243 1 18
HELIX 16 16 PRO A 259 LEU A 270 1 12
HELIX 17 17 LEU A 284 ASP A 288 5 5
HELIX 18 18 ASN A 289 LEU A 301 1 13
HELIX 19 19 PRO A 302 LEU A 304 5 3
HELIX 20 20 SER B 55 ARG B 60 5 6
HELIX 21 21 ILE B 62 ALA B 67 1 6
HELIX 22 22 PHE B 91 LEU B 106 1 16
HELIX 23 23 ASP B 117 ASN B 130 1 14
HELIX 24 24 PRO B 153 ARG B 164 1 12
HELIX 25 25 ASP B 167 ILE B 174 1 8
HELIX 26 26 ASN B 177 GLY B 182 1 6
HELIX 27 27 GLY B 182 GLY B 187 1 6
HELIX 28 28 THR B 193 GLU B 202 1 10
HELIX 29 29 PRO B 203 LEU B 205 5 3
HELIX 30 30 LYS B 206 ASP B 209 5 4
HELIX 31 31 ARG B 210 PHE B 216 1 7
HELIX 32 32 PRO B 226 SER B 243 1 18
HELIX 33 33 PRO B 259 LEU B 270 1 12
HELIX 34 34 LEU B 284 ASN B 289 1 6
HELIX 35 35 ASN B 289 LEU B 301 1 13
HELIX 36 36 PRO B 302 ALA B 305 5 4
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 MSE B 33 N VAL B 26
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 CYS B 139
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 1.32
LINK C MSE A 80 N GLY A 81 1555 1555 1.33
LINK C CYS A 139 N MSE A 140 1555 1555 1.32
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 1.33
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 1.33
LINK C MSE B 140 N GLU B 141 1555 1555 1.33
LINK C PRO B 185 N MSE B 186 1555 1555 1.32
LINK C MSE B 186 N GLY B 187 1555 1555 1.32
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 1.33
LINK C MSE B 237 N ASN B 238 1555 1555 1.33
CISPEP 1 ASN A 52 PRO A 53 0 -12.85
CISPEP 2 GLU A 225 PRO A 226 0 -5.35
CISPEP 3 THR A 253 PRO A 254 0 9.70
CISPEP 4 ASN B 52 PRO B 53 0 -5.37
CISPEP 5 GLU B 225 PRO B 226 0 -4.45
CISPEP 6 THR B 253 PRO B 254 0 4.93
SITE 1 AC1 14 ASN A 52 PRO A 53 ASP A 117 TRP A 118
SITE 2 AC1 14 TRP A 152 ALA A 156 PHE A 160 PHE A 179
SITE 3 AC1 14 ALA A 183 GLY A 187 PRO A 217 LEU A 220
SITE 4 AC1 14 VAL A 256 PHE A 283
SITE 1 AC2 4 GLY B 30 ILE B 278 PRO B 280 ASN B 289
SITE 1 AC3 12 ASN B 52 PRO B 53 ASP B 117 TRP B 118
SITE 2 AC3 12 TRP B 152 PHE B 160 PHE B 179 ALA B 183
SITE 3 AC3 12 PRO B 217 VAL B 256 LEU B 257 PHE B 283
SITE 1 AC4 2 LYS B 85 ASP B 87
CRYST1 42.846 94.984 73.587 90.00 93.14 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 0.023339 0.000000 0.001280 0.00000
SCALE2 0.000000 0.010528 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013610 0.00000
TER 2345 ALA A 305
TER 4688 ALA B 305
MASTER 317 0 16 36 16 0 9 6 4996 2 182 48
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