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HEADER HYDROLASE 22-APR-13 4KAJ
TITLE X-RAY STRUCTURE OF THE COMPLEX OF HALOALKANE DEHALOGENASE HALOTAG7
TITLE 2 WITH HALTS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET
TITLE 3 OR151
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PENTAETHYLENE GLYCOL;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES
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 4KAJ 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 OR151
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.430
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 46088
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2319
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 29.4206 - 5.0020 0.99 2544 144 0.1733 0.1762
REMARK 3 2 5.0020 - 3.9733 1.00 2574 137 0.1355 0.1592
REMARK 3 3 3.9733 - 3.4720 1.00 2586 133 0.1498 0.1762
REMARK 3 4 3.4720 - 3.1549 1.00 2586 130 0.1664 0.2235
REMARK 3 5 3.1549 - 2.9290 1.00 2568 136 0.1735 0.2113
REMARK 3 6 2.9290 - 2.7565 1.00 2566 140 0.1672 0.1650
REMARK 3 7 2.7565 - 2.6185 1.00 2571 135 0.1596 0.1947
REMARK 3 8 2.6185 - 2.5046 1.00 2599 130 0.1619 0.2293
REMARK 3 9 2.5046 - 2.4082 1.00 2557 137 0.1602 0.1977
REMARK 3 10 2.4082 - 2.3251 1.00 2578 136 0.1567 0.1941
REMARK 3 11 2.3251 - 2.2525 1.00 2574 138 0.1621 0.2081
REMARK 3 12 2.2525 - 2.1881 1.00 2571 138 0.1676 0.2091
REMARK 3 13 2.1881 - 2.1305 1.00 2603 144 0.1774 0.2412
REMARK 3 14 2.1305 - 2.0785 1.00 2558 133 0.1841 0.2392
REMARK 3 15 2.0785 - 2.0313 1.00 2558 135 0.1986 0.2482
REMARK 3 16 2.0313 - 1.9881 1.00 2584 136 0.2239 0.2425
REMARK 3 17 1.9881 - 1.9483 0.99 2592 137 0.2522 0.3088
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.760
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.48
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 2527
REMARK 3 ANGLE : 1.087 3446
REMARK 3 CHIRALITY : 0.073 360
REMARK 3 PLANARITY : 0.006 450
REMARK 3 DIHEDRAL : 12.700 917
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): -23.4452 1.9718 10.5664
REMARK 3 T TENSOR
REMARK 3 T11: 0.2350 T22: 0.1320
REMARK 3 T33: 0.1592 T12: 0.0073
REMARK 3 T13: -0.0006 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.9135 L22: 0.9090
REMARK 3 L33: 1.6281 L12: 0.1581
REMARK 3 L13: -0.3173 L23: -0.5414
REMARK 3 S TENSOR
REMARK 3 S11: 0.0147 S12: 0.0676 S13: 0.0899
REMARK 3 S21: 0.1997 S22: 0.0496 S23: 0.0496
REMARK 3 S31: -0.3736 S32: -0.1817 S33: -0.0394
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 4KAJ 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 RCSB079097.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46185
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.948
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.9000
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 4E46
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
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:
REMARK 280 MANGANESE CHLORIDE 0.1M, BIS-TRIS PROPANE 0.1M, PEG 4000 20%,
REMARK 280 MICROBATCH UNDER OIL, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.03650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.51300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.51300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 123.05475
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.51300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.51300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 41.01825
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.51300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.51300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 123.05475
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.51300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.51300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 41.01825
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 82.03650
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 300 REMARK: MONOMER,35.49 KD,99.1%
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 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 -10
REMARK 465 GLY A -9
REMARK 465 HIS A -8
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 ALA A 2
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 9 49.86 -86.02
REMARK 500 PRO A 42 48.55 -109.34
REMARK 500 THR A 43 -161.92 -103.69
REMARK 500 GLU A 98 -86.49 -112.03
REMARK 500 ASP A 106 -134.87 56.85
REMARK 500 ARG A 153 45.02 -91.64
REMARK 500 VAL A 245 -70.32 -133.39
REMARK 500 LEU A 271 -99.96 -121.13
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 MN A 302 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 19 O
REMARK 620 2 HOH A 471 O 95.4
REMARK 620 3 HOH A 424 O 92.0 170.3
REMARK 620 4 HOH A 425 O 81.8 168.9 19.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A 303 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 490 O
REMARK 620 2 HOH A 628 O 98.6
REMARK 620 3 HOH A 546 O 106.5 87.4
REMARK 620 4 ASP A 76 OD1 67.9 166.5 97.2
REMARK 620 5 HOH A 585 O 89.3 91.5 164.1 87.6
REMARK 620 N 1 2 3 4
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 GLU A 191 OE2
REMARK 620 2 EDO A 306 O1 110.9
REMARK 620 3 HIS A 188 O 107.9 137.1
REMARK 620 4 HOH A 428 O 99.4 79.2 112.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 305 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 183 OE1
REMARK 620 2 ASP A 187 OD2 94.1
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 1Q9 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN 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 NA A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E46 RELATED DB: PDB
REMARK 900 HOMOLOGY IS 92.49%
REMARK 900 RELATED ID: NESG-OR151 RELATED DB: TARGETTRACK
DBREF 4KAJ A -1 293 UNP P0A3G3 DHAA_RHOSO 2 293
SEQADV 4KAJ MSE A -10 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ GLY A -9 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ HIS A -8 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ HIS A -7 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ HIS A -6 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ HIS A -5 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ HIS A -4 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ HIS A -3 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ HIS A 0 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ MSE A 1 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ ALA A 2 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 4KAJ THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 4KAJ GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 4KAJ PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 4KAJ MSE A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 4KAJ PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 4KAJ THR A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 4KAJ LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 4KAJ VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 4KAJ THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 4KAJ MSE A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 4KAJ GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 4KAJ ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 4KAJ GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 4KAJ ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 4KAJ LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 4KAJ ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 4KAJ ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 4KAJ LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 4KAJ SER A 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 4KAJ THR A 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 4KAJ GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ ILE A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ SER A 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 4KAJ GLY A 297 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 307 MSE GLY HIS HIS HIS HIS HIS HIS SER HIS MSE ALA GLU
SEQRES 2 A 307 ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL GLU
SEQRES 3 A 307 VAL LEU GLY GLU ARG MSE HIS TYR VAL ASP VAL GLY PRO
SEQRES 4 A 307 ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN PRO
SEQRES 5 A 307 THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS VAL
SEQRES 6 A 307 ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE GLY
SEQRES 7 A 307 MSE GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE PHE
SEQRES 8 A 307 ASP ASP HIS VAL ARG PHE MSE ASP ALA PHE ILE GLU ALA
SEQRES 9 A 307 LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP TRP
SEQRES 10 A 307 GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN PRO
SEQRES 11 A 307 GLU ARG VAL LYS GLY ILE ALA PHE MSE GLU PHE ILE ARG
SEQRES 12 A 307 PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA ARG
SEQRES 13 A 307 GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY ARG
SEQRES 14 A 307 LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY THR
SEQRES 15 A 307 LEU PRO MSE GLY VAL VAL ARG PRO LEU THR GLU VAL GLU
SEQRES 16 A 307 MSE ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL ASP
SEQRES 17 A 307 ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO ILE
SEQRES 18 A 307 ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU GLU
SEQRES 19 A 307 TYR MSE ASP TRP LEU HIS GLN SER PRO VAL PRO LYS LEU
SEQRES 20 A 307 LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO ALA
SEQRES 21 A 307 GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS LYS
SEQRES 22 A 307 ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN GLU
SEQRES 23 A 307 ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG TRP
SEQRES 24 A 307 LEU SER THR LEU GLU ILE SER GLY
MODRES 4KAJ MSE A 22 MET SELENOMETHIONINE
MODRES 4KAJ MSE A 69 MET SELENOMETHIONINE
MODRES 4KAJ MSE A 88 MET SELENOMETHIONINE
MODRES 4KAJ MSE A 129 MET SELENOMETHIONINE
MODRES 4KAJ MSE A 175 MET SELENOMETHIONINE
MODRES 4KAJ MSE A 186 MET SELENOMETHIONINE
MODRES 4KAJ MSE A 226 MET SELENOMETHIONINE
HET MSE A 22 8
HET MSE A 69 8
HET MSE A 88 8
HET MSE A 129 8
HET MSE A 175 8
HET MSE A 186 8
HET MSE A 226 8
HET 1Q9 A 301 18
HET MN A 302 1
HET NA A 304 1
HET MN A 303 1
HET NA A 305 1
HET EDO A 306 4
HET EDO A 307 4
HET GOL A 308 6
HETNAM MSE SELENOMETHIONINE
HETNAM 1Q9 N-(2-ETHOXY-3,5-DIMETHYLBENZYL)-1H-TETRAZOL-5-AMINE
HETNAM MN MANGANESE (II) ION
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 7(C5 H11 N O2 SE)
FORMUL 2 1Q9 C12 H17 N5 O
FORMUL 3 MN 2(MN 2+)
FORMUL 4 NA 2(NA 1+)
FORMUL 7 EDO 2(C2 H6 O2)
FORMUL 9 GOL C3 H8 O3
FORMUL 10 HOH *242(H2 O)
HELIX 1 1 SER A 44 ARG A 49 5 6
HELIX 2 2 ILE A 51 ALA A 56 1 6
HELIX 3 3 PHE A 80 LEU A 95 1 16
HELIX 4 4 ASP A 106 ASN A 119 1 14
HELIX 5 5 THR A 137 TRP A 141 5 5
HELIX 6 6 PRO A 142 PHE A 144 5 3
HELIX 7 7 ALA A 145 ARG A 153 1 9
HELIX 8 8 THR A 155 ILE A 163 1 9
HELIX 9 9 ASN A 166 GLY A 171 1 6
HELIX 10 10 LEU A 173 VAL A 177 5 5
HELIX 11 11 THR A 182 GLU A 191 1 10
HELIX 12 12 PRO A 192 LEU A 194 5 3
HELIX 13 13 ASN A 195 ASP A 198 5 4
HELIX 14 14 ARG A 199 LEU A 209 1 11
HELIX 15 15 PRO A 215 SER A 232 1 18
HELIX 16 16 PRO A 248 LEU A 259 1 12
HELIX 17 17 LEU A 273 ASN A 278 1 6
HELIX 18 18 ASN A 278 LEU A 293 1 16
SHEET 1 A 8 HIS A 13 VAL A 17 0
SHEET 2 A 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 A 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 A 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 A 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 A 8 VAL A 123 MSE A 129 1 O ALA A 127 N LEU A 102
SHEET 7 A 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 128
SHEET 8 A 8 CYS A 262 GLY A 270 1 O LYS A 263 N LEU A 238
LINK C ARG A 21 N MSE A 22 1555 1555 1.33
LINK C MSE A 22 N HIS A 23 1555 1555 1.33
LINK C GLY A 68 N MSE A 69 1555 1555 1.33
LINK C MSE A 69 N GLY A 70 1555 1555 1.34
LINK C PHE A 87 N MSE A 88 1555 1555 1.33
LINK C MSE A 88 N ASP A 89 1555 1555 1.34
LINK C PHE A 128 N MSE A 129 1555 1555 1.33
LINK C MSE A 129 N GLU A 130 1555 1555 1.33
LINK C PRO A 174 N MSE A 175 1555 1555 1.33
LINK C MSE A 175 N GLY A 176 1555 1555 1.33
LINK C GLU A 185 N MSE A 186 1555 1555 1.33
LINK C MSE A 186 N ASP A 187 1555 1555 1.33
LINK C TYR A 225 N MSE A 226 1555 1555 1.33
LINK C MSE A 226 N ASP A 227 1555 1555 1.33
LINK O GLY A 19 MN MN A 302 1555 1555 2.04
LINK MN MN A 302 O HOH A 471 1555 1555 2.27
LINK MN MN A 302 O AHOH A 424 1555 1555 2.41
LINK MN MN A 303 O HOH A 490 1555 1555 2.41
LINK MN MN A 303 O HOH A 628 1555 1555 2.44
LINK MN MN A 303 O HOH A 546 1555 1555 2.44
LINK MN MN A 302 O BHOH A 425 1555 1555 2.48
LINK OE2 GLU A 191 NA NA A 304 1555 1555 2.48
LINK OD1 ASP A 76 MN MN A 303 1555 1555 2.52
LINK NA NA A 304 O1 EDO A 306 1555 1555 2.55
LINK MN MN A 303 O HOH A 585 1555 1555 2.60
LINK OE1 GLU A 183 NA NA A 305 1555 1555 2.71
LINK O HIS A 188 NA NA A 304 1555 1555 2.77
LINK OD2 ASP A 187 NA NA A 305 1555 1555 2.85
LINK NA NA A 304 O HOH A 428 1555 1555 2.88
CISPEP 1 ASN A 41 PRO A 42 0 1.05
CISPEP 2 GLU A 214 PRO A 215 0 -4.47
CISPEP 3 THR A 242 PRO A 243 0 1.85
SITE 1 AC1 13 ASN A 41 PRO A 42 ASP A 106 TRP A 107
SITE 2 AC1 13 TRP A 141 ALA A 145 PHE A 149 PHE A 168
SITE 3 AC1 13 THR A 172 GLY A 176 VAL A 245 ASN A 272
SITE 4 AC1 13 LEU A 273
SITE 1 AC2 6 HIS A -5 HIS A -7 GLY A 19 HOH A 424
SITE 2 AC2 6 HOH A 425 HOH A 471
SITE 1 AC3 5 ASP A 76 HOH A 490 HOH A 546 HOH A 585
SITE 2 AC3 5 HOH A 628
SITE 1 AC4 4 HIS A 188 GLU A 191 EDO A 306 HOH A 428
SITE 1 AC5 2 GLU A 183 ASP A 187
SITE 1 AC6 8 PHE A 8 SER A 44 SER A 45 ASP A 65
SITE 2 AC6 8 LYS A 71 NA A 304 HOH A 428 HOH A 465
SITE 1 AC7 4 ASP A 187 GLU A 191 ASN A 195 VAL A 197
SITE 1 AC8 4 GLU A 191 ASN A 195 ASP A 198 HOH A 574
CRYST1 63.026 63.026 164.073 90.00 90.00 90.00 P 43 21 2 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 0.015866 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015866 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006095 0.00000
TER 2415 GLY A 297
MASTER 356 0 15 18 8 0 14 6 2692 1 121 24
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