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HEADER BIOSYNTHETIC PROTEIN 01-SEP-16 5T6O
TITLE STRUCTURE OF THE CATALYTIC DOMAIN OF THE CLASS I POLYHYDROXYBUTYRATE
TITLE 2 SYNTHASE FROM CUPRIAVIDUS NECATOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY-BETA-HYDROXYBUTERATE POLYMERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 201-589;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CUPRIAVIDUS NECATOR;
SOURCE 3 ORGANISM_COMMON: ALCALIGENES EUTROPHUS;
SOURCE 4 ORGANISM_TAXID: 106590;
SOURCE 5 GENE: PHAC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS POLYHYDROXYBUTYRATE SYNTHASE, PHAC, ALPHA/BETA HYDROLASE FOLD,
KEYWDS 2 NONTEMPLATE-DEPENDENT POLYMERIZATION, TRANSFERASE, BIOSYNTHETIC
KEYWDS 3 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.C.WITTENBORN,M.JOST,C.L.DRENNAN
REVDAT 3 07-DEC-16 5T6O 1 JRNL
REVDAT 2 02-NOV-16 5T6O 1 JRNL
REVDAT 1 26-OCT-16 5T6O 0
JRNL AUTH E.C.WITTENBORN,M.JOST,Y.WEI,J.STUBBE,C.L.DRENNAN
JRNL TITL STRUCTURE OF THE CATALYTIC DOMAIN OF THE CLASS I
JRNL TITL 2 POLYHYDROXYBUTYRATE SYNTHASE FROM CUPRIAVIDUS NECATOR.
JRNL REF J.BIOL.CHEM. V. 291 25264 2016
JRNL REFN ESSN 1083-351X
JRNL PMID 27742839
JRNL DOI 10.1074/JBC.M116.756833
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.4-1496
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 40645
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2032
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 74.0121 - 4.4389 1.00 2732 143 0.1530 0.1676
REMARK 3 2 4.4389 - 3.5233 1.00 2623 138 0.1401 0.1429
REMARK 3 3 3.5233 - 3.0779 1.00 2601 137 0.1741 0.2095
REMARK 3 4 3.0779 - 2.7965 1.00 2595 137 0.1864 0.2126
REMARK 3 5 2.7965 - 2.5960 1.00 2562 135 0.1859 0.2092
REMARK 3 6 2.5960 - 2.4430 1.00 2583 136 0.1733 0.2310
REMARK 3 7 2.4430 - 2.3206 1.00 2546 134 0.1734 0.1985
REMARK 3 8 2.3206 - 2.2196 1.00 2552 134 0.1864 0.2645
REMARK 3 9 2.2196 - 2.1341 1.00 2559 135 0.1790 0.2299
REMARK 3 10 2.1341 - 2.0605 1.00 2553 134 0.1747 0.2184
REMARK 3 11 2.0605 - 1.9961 1.00 2538 134 0.1918 0.2517
REMARK 3 12 1.9961 - 1.9390 1.00 2527 133 0.1918 0.2231
REMARK 3 13 1.9390 - 1.8879 1.00 2568 135 0.2502 0.3122
REMARK 3 14 1.8879 - 1.8419 1.00 2535 134 0.2409 0.2825
REMARK 3 15 1.8419 - 1.8000 1.00 2539 133 0.2511 0.2872
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.560
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) : 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 : 0.006 3051
REMARK 3 ANGLE : 0.821 4197
REMARK 3 CHIRALITY : 0.054 465
REMARK 3 PLANARITY : 0.006 538
REMARK 3 DIHEDRAL : 13.184 1748
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND RESID 201 THROUGH 589)
REMARK 3 ORIGIN FOR THE GROUP (A): 86.6891 28.4958 18.1841
REMARK 3 T TENSOR
REMARK 3 T11: 0.1813 T22: 0.1893
REMARK 3 T33: 0.1864 T12: -0.0151
REMARK 3 T13: 0.0010 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.6131 L22: 1.0266
REMARK 3 L33: 1.0579 L12: -0.1179
REMARK 3 L13: 0.1081 L23: 0.1514
REMARK 3 S TENSOR
REMARK 3 S11: 0.0024 S12: 0.0106 S13: -0.0203
REMARK 3 S21: 0.0038 S22: 0.0700 S23: -0.1317
REMARK 3 S31: -0.0236 S32: 0.0942 S33: -0.0698
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 5T6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000223776.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-AUG-15
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 : APS
REMARK 200 BEAMLINE : 24-ID-C
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20141103
REMARK 200 DATA SCALING SOFTWARE : XSCALE 20141103
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40649
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04600
REMARK 200 FOR THE DATA SET : 25.7600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.240
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXDE 97-2.20090721
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.9 M AMMONIUM SULFATE, 0.1 M HEPES PH
REMARK 280 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 36.04000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.91000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 68.55000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.04000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.91000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.55000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.04000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.91000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.55000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.04000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 43.91000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 68.55000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 48360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.0 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 144.16000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 87.82000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 144.16000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 87.82000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 884 LIES ON A SPECIAL POSITION.
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 LEU A 369
REMARK 465 ARG A 370
REMARK 465 GLU A 371
REMARK 465 ALA A 372
REMARK 465 THR A 373
REMARK 465 LEU A 374
REMARK 465 GLY A 375
REMARK 465 GLY A 376
REMARK 465 GLY A 377
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 SER A 201 OG
REMARK 470 ARG A 207 CZ NH1 NH2
REMARK 470 LYS A 229 NZ
REMARK 470 LYS A 234 NZ
REMARK 470 GLU A 258 CD OE1 OE2
REMARK 470 GLU A 267 OE1 OE2
REMARK 470 LEU A 358 CD1 CD2
REMARK 470 ALA A 378 N CA CB
REMARK 470 LYS A 451 NZ
REMARK 470 LYS A 455 NZ
REMARK 470 LYS A 498 CD CE NZ
REMARK 470 LYS A 518 CG CD CE NZ
REMARK 470 ASN A 519 CG OD1 ND2
REMARK 470 LYS A 520 CE NZ
REMARK 470 GLU A 531 CG CD OE1 OE2
REMARK 470 ALA A 561 CB
REMARK 470 ARG A 573 CD NE CZ NH1 NH2
REMARK 470 LYS A 588 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 715 O HOH A 935 2765 1.80
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 ASN A 248 -174.68 56.85
REMARK 500 ASP A 254 55.76 -141.56
REMARK 500 LEU A 255 -86.95 -71.76
REMARK 500 ASP A 281 -168.01 -107.85
REMARK 500 ALA A 296 -59.47 -126.53
REMARK 500 ALA A 319 -132.51 59.31
REMARK 500 THR A 444 -77.80 -113.10
REMARK 500 ASN A 497 -167.61 75.88
REMARK 500 SER A 506 -164.04 83.54
REMARK 500 ARG A 521 -153.02 65.15
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 SO4 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604
DBREF 5T6O A 201 589 UNP D3UAK8 D3UAK8_CUPNE 201 589
SEQADV 5T6O ALA A 319 UNP D3UAK8 CYS 319 ENGINEERED MUTATION
SEQRES 1 A 389 SER ALA PHE GLU VAL GLY ARG ASN VAL ALA VAL THR GLU
SEQRES 2 A 389 GLY ALA VAL VAL PHE GLU ASN GLU TYR PHE GLN LEU LEU
SEQRES 3 A 389 GLN TYR LYS PRO LEU THR ASP LYS VAL HIS ALA ARG PRO
SEQRES 4 A 389 LEU LEU MET VAL PRO PRO CYS ILE ASN LYS TYR TYR ILE
SEQRES 5 A 389 LEU ASP LEU GLN PRO GLU SER SER LEU VAL ARG HIS VAL
SEQRES 6 A 389 VAL GLU GLN GLY HIS THR VAL PHE LEU VAL SER TRP ARG
SEQRES 7 A 389 ASN PRO ASP ALA SER MET ALA GLY SER THR TRP ASP ASP
SEQRES 8 A 389 TYR ILE GLU HIS ALA ALA ILE ARG ALA ILE GLU VAL ALA
SEQRES 9 A 389 ARG ASP ILE SER GLY GLN ASP LYS ILE ASN VAL LEU GLY
SEQRES 10 A 389 PHE ALA VAL GLY GLY THR ILE VAL SER THR ALA LEU ALA
SEQRES 11 A 389 VAL LEU ALA ALA ARG GLY GLU HIS PRO ALA ALA SER VAL
SEQRES 12 A 389 THR LEU LEU THR THR LEU LEU ASP PHE ALA ASP THR GLY
SEQRES 13 A 389 ILE LEU ASP VAL PHE VAL ASP GLU GLY HIS VAL GLN LEU
SEQRES 14 A 389 ARG GLU ALA THR LEU GLY GLY GLY ALA GLY ALA PRO CYS
SEQRES 15 A 389 ALA LEU LEU ARG GLY LEU GLU LEU ALA ASN THR PHE SER
SEQRES 16 A 389 PHE LEU ARG PRO ASN ASP LEU VAL TRP ASN TYR VAL VAL
SEQRES 17 A 389 ASP ASN TYR LEU LYS GLY ASN THR PRO VAL PRO PHE ASP
SEQRES 18 A 389 LEU LEU PHE TRP ASN GLY ASP ALA THR ASN LEU PRO GLY
SEQRES 19 A 389 PRO TRP TYR CYS TRP TYR LEU ARG HIS THR TYR LEU GLN
SEQRES 20 A 389 ASN GLU LEU LYS VAL PRO GLY LYS LEU THR VAL CYS GLY
SEQRES 21 A 389 VAL PRO VAL ASP LEU ALA SER ILE ASP VAL PRO THR TYR
SEQRES 22 A 389 ILE TYR GLY SER ARG GLU ASP HIS ILE VAL PRO TRP THR
SEQRES 23 A 389 ALA ALA TYR ALA SER THR ALA LEU LEU ALA ASN LYS LEU
SEQRES 24 A 389 ARG PHE VAL LEU GLY ALA SER GLY HIS ILE ALA GLY VAL
SEQRES 25 A 389 ILE ASN PRO PRO ALA LYS ASN LYS ARG SER HIS TRP THR
SEQRES 26 A 389 ASN ASP ALA LEU PRO GLU SER PRO GLN GLN TRP LEU ALA
SEQRES 27 A 389 GLY ALA ILE GLU HIS HIS GLY SER TRP TRP PRO ASP TRP
SEQRES 28 A 389 THR ALA TRP LEU ALA GLY GLN ALA GLY ALA LYS ARG ALA
SEQRES 29 A 389 ALA PRO ALA ASN TYR GLY ASN ALA ARG TYR ARG ALA ILE
SEQRES 30 A 389 GLU PRO ALA PRO GLY ARG TYR VAL LYS ALA LYS ALA
HET SO4 A 601 5
HET SO4 A 602 5
HET SO4 A 603 5
HET SO4 A 604 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 6 HOH *283(H2 O)
HELIX 1 AA1 LYS A 249 LEU A 255 5 7
HELIX 2 AA2 GLN A 256 SER A 259 5 4
HELIX 3 AA3 SER A 260 GLN A 268 1 9
HELIX 4 AA4 ASP A 281 ALA A 285 5 5
HELIX 5 AA5 THR A 288 ALA A 296 1 9
HELIX 6 AA6 ALA A 296 GLY A 309 1 14
HELIX 7 AA7 ALA A 319 ARG A 335 1 17
HELIX 8 AA8 LEU A 358 VAL A 362 5 5
HELIX 9 AA9 PRO A 381 LEU A 385 5 5
HELIX 10 AB1 ASP A 401 THR A 416 1 16
HELIX 11 AB2 PRO A 419 ASP A 428 1 10
HELIX 12 AB3 GLY A 434 THR A 444 1 11
HELIX 13 AB4 ASP A 464 ILE A 468 5 5
HELIX 14 AB5 PRO A 484 ALA A 490 1 7
HELIX 15 AB6 SER A 491 LEU A 494 5 4
HELIX 16 AB7 GLY A 507 ILE A 513 1 7
HELIX 17 AB8 PRO A 515 ASN A 519 5 5
HELIX 18 AB9 SER A 532 ALA A 540 1 9
HELIX 19 AC1 TRP A 547 ALA A 559 1 13
HELIX 20 AC2 ARG A 583 ALA A 587 5 5
SHEET 1 AA111 ILE A 541 HIS A 544 0
SHEET 2 AA111 SER A 522 THR A 525 -1 N HIS A 523 O HIS A 543
SHEET 3 AA111 LEU A 499 GLY A 504 -1 N LEU A 503 O TRP A 524
SHEET 4 AA111 THR A 472 SER A 477 1 N ILE A 474 O ARG A 500
SHEET 5 AA111 ALA A 340 LEU A 346 1 N LEU A 345 O TYR A 473
SHEET 6 AA111 ILE A 313 PHE A 318 1 N GLY A 317 O LEU A 346
SHEET 7 AA111 LEU A 240 VAL A 243 1 N VAL A 243 O LEU A 316
SHEET 8 AA111 VAL A 272 TRP A 277 1 O PHE A 273 N MET A 242
SHEET 9 AA111 PHE A 223 TYR A 228 -1 N LEU A 226 O LEU A 274
SHEET 10 AA111 GLY A 214 GLU A 219 -1 N PHE A 218 O LEU A 225
SHEET 11 AA111 GLU A 578 PRO A 579 -1 O GLU A 578 N VAL A 216
SHEET 1 AA2 2 LYS A 234 HIS A 236 0
SHEET 2 AA2 2 LYS A 562 ALA A 564 -1 O ARG A 563 N VAL A 235
SHEET 1 AA3 2 LEU A 388 ALA A 391 0
SHEET 2 AA3 2 THR A 430 PRO A 433 -1 O LEU A 432 N GLU A 389
SHEET 1 AA4 2 THR A 457 VAL A 458 0
SHEET 2 AA4 2 VAL A 461 PRO A 462 -1 O VAL A 461 N VAL A 458
SSBOND 1 CYS A 382 CYS A 438 1555 1555 2.05
CISPEP 1 ALA A 580 PRO A 581 0 9.40
SITE 1 AC1 3 ARG A 478 TRP A 485 HOH A 765
SITE 1 AC2 8 SER A 201 ALA A 202 PHE A 218 ASN A 220
SITE 2 AC2 8 ARG A 299 HOH A 760 HOH A 806 HOH A 925
SITE 1 AC3 8 PRO A 381 CYS A 382 TRP A 439 ARG A 442
SITE 2 AC3 8 HIS A 443 SO4 A 604 HOH A 738 HOH A 817
SITE 1 AC4 6 GLY A 379 ARG A 442 HIS A 443 GLN A 447
SITE 2 AC4 6 SO4 A 603 HOH A 715
CRYST1 72.080 87.820 137.100 90.00 90.00 90.00 I 2 2 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 0.013873 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011387 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007294 0.00000
TER 2943 ALA A 589
MASTER 356 0 4 20 17 0 7 6 3218 1 22 30
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