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HEADER HYDROLASE 19-MAY-16 5K3F
TITLE CRYSTAL STRUCTURE OF THE FLUOROACETATE DEHALOGENASE RPA1163 -
TITLE 2 HIS280ASN/FLUOROACETATE - COCRYSTALLIZED - SINGLE PROTOMER REACTED
TITLE 3 WITH LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROACETATE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: FLUOROACETATE DEHALOGENASE;
COMPND 8 CHAIN: B;
COMPND 9 EC: 3.8.1.3;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS (STRAIN ATCC BAA-98
SOURCE 3 / CGA009);
SOURCE 4 ORGANISM_TAXID: 258594;
SOURCE 5 STRAIN: ATCC BAA-98 / CGA009;
SOURCE 6 GENE: RPA1163;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS (STRAIN ATCC BAA-98
SOURCE 11 / CGA009);
SOURCE 12 ORGANISM_TAXID: 258594;
SOURCE 13 STRAIN: ATCC BAA-98 / CGA009;
SOURCE 14 GENE: RPA1163;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HOMODIMER, HYDROLASE, DEHALOGENASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.MEHRABI,T.H.KIM,S.R.PROSSER,E.F.PAI
REVDAT 1 01-FEB-17 5K3F 0
JRNL AUTH T.H.KIM,P.MEHRABI,Z.REN,A.SLJOKA,C.ING,A.BEZGINOV,L.YE,
JRNL AUTH 2 R.POMES,R.S.PROSSER,E.F.PAI
JRNL TITL THE ROLE OF DIMER ASYMMETRY AND PROTOMER DYNAMICS IN ENZYME
JRNL TITL 2 CATALYSIS.
JRNL REF SCIENCE V. 355 2017
JRNL REFN ESSN 1095-9203
JRNL PMID 28104837
JRNL DOI 10.1126/SCIENCE.AAG2355
REMARK 2
REMARK 2 RESOLUTION. 1.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 74512
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 3749
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 36.8173 - 4.6168 0.99 2899 127 0.1476 0.1607
REMARK 3 2 4.6168 - 3.6656 0.87 2314 124 0.1217 0.1477
REMARK 3 3 3.6656 - 3.2025 0.80 2109 129 0.1509 0.1840
REMARK 3 4 3.2025 - 2.9099 0.98 2793 162 0.1647 0.2126
REMARK 3 5 2.9099 - 2.7014 0.98 2773 143 0.1723 0.2135
REMARK 3 6 2.7014 - 2.5421 0.97 2758 149 0.1720 0.2173
REMARK 3 7 2.5421 - 2.4148 0.97 2764 126 0.1722 0.2244
REMARK 3 8 2.4148 - 2.3097 0.97 2730 147 0.1726 0.2409
REMARK 3 9 2.3097 - 2.2208 0.94 2661 141 0.1976 0.2359
REMARK 3 10 2.2208 - 2.1442 0.95 2677 147 0.1751 0.2157
REMARK 3 11 2.1442 - 2.0772 0.96 2712 152 0.1876 0.2487
REMARK 3 12 2.0772 - 2.0178 0.94 2657 130 0.2043 0.2299
REMARK 3 13 2.0178 - 1.9647 0.95 2692 141 0.1849 0.2406
REMARK 3 14 1.9647 - 1.9168 0.93 2590 136 0.2265 0.2314
REMARK 3 15 1.9168 - 1.8732 0.93 2615 162 0.2250 0.2860
REMARK 3 16 1.8732 - 1.8333 0.94 2606 145 0.1971 0.2419
REMARK 3 17 1.8333 - 1.7966 0.93 2678 126 0.1896 0.2263
REMARK 3 18 1.7966 - 1.7627 0.93 2628 125 0.1914 0.2381
REMARK 3 19 1.7627 - 1.7313 0.92 2617 119 0.1908 0.2576
REMARK 3 20 1.7313 - 1.7019 0.92 2627 143 0.1947 0.2429
REMARK 3 21 1.7019 - 1.6745 0.93 2573 132 0.1983 0.2532
REMARK 3 22 1.6745 - 1.6487 0.90 2573 139 0.2176 0.2389
REMARK 3 23 1.6487 - 1.6245 0.92 2580 152 0.2185 0.2699
REMARK 3 24 1.6245 - 1.6016 0.91 2570 132 0.2301 0.2730
REMARK 3 25 1.6016 - 1.5799 0.89 2531 136 0.2507 0.3174
REMARK 3 26 1.5799 - 1.5594 0.90 2516 139 0.2580 0.3386
REMARK 3 27 1.5594 - 1.5399 0.90 2520 145 0.2707 0.3144
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.70
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 : 0.007 4861
REMARK 3 ANGLE : 1.154 6631
REMARK 3 CHIRALITY : 0.044 678
REMARK 3 PLANARITY : 0.006 874
REMARK 3 DIHEDRAL : 13.108 1744
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 5K3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221626.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN A200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74512
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.540
REMARK 200 RESOLUTION RANGE LOW (A) : 36.807
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.7
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.02500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.21400
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: PHASER
REMARK 200 STARTING MODEL: 3R3U
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350 19-22%, 200MM CALCIUM
REMARK 280 CHLORIDE, 100MM TRIS HCL PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 39.81000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: 2410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 ASP A 3
REMARK 465 ALA A 301
REMARK 465 PRO A 302
REMARK 465 GLY A 303
REMARK 465 SER A 304
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 ILE B 253
REMARK 465 ALA B 254
REMARK 465 GLN B 255
REMARK 465 SER B 256
REMARK 465 ALA B 300
REMARK 465 ALA B 301
REMARK 465 PRO B 302
REMARK 465 GLY B 303
REMARK 465 SER B 304
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 LYS A 152 CG CD CE NZ
REMARK 470 ASP B 3 CG OD1 OD2
REMARK 470 LEU B 4 CG CD1 CD2
REMARK 470 LYS B 53 CG CD CE NZ
REMARK 470 ARG B 57 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 78 CG CD OE1 OE2
REMARK 470 GLU B 292 CG CD OE1 OE2
REMARK 470 ARG B 296 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 404 O HOH A 423 1.98
REMARK 500 O HOH B 502 O HOH B 523 2.11
REMARK 500 O HOH A 494 O HOH A 706 2.16
REMARK 500 OE1 GLU B 235 O HOH B 501 2.18
REMARK 500 O HOH B 607 O HOH B 673 2.19
REMARK 500 O HOH B 765 O HOH B 788 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 462 O HOH B 784 1556 2.12
REMARK 500 O HOH A 569 O HOH A 601 2557 2.17
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 41 66.38 -100.48
REMARK 500 ASB A 110 -126.48 62.12
REMARK 500 ASP A 173 63.08 -151.24
REMARK 500 ASP A 173 63.08 -150.73
REMARK 500 TYR A 224 -97.26 -124.07
REMARK 500 ALA A 257 50.90 -140.94
REMARK 500 PRO B 41 67.20 -102.09
REMARK 500 GLN B 42 -168.34 -124.69
REMARK 500 ASP B 110 -126.65 54.20
REMARK 500 ASN B 146 -167.77 -103.02
REMARK 500 ILE B 153 54.54 -111.22
REMARK 500 ASP B 173 72.61 -151.55
REMARK 500 TYR B 224 -91.59 -122.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 778 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 779 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH A 780 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A 781 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH B 832 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B 833 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 834 DISTANCE = 6.25 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5K3B RELATED DB: PDB
REMARK 900 RELATED ID: 5K3A RELATED DB: PDB
REMARK 900 RELATED ID: 5K3C RELATED DB: PDB
REMARK 900 RELATED ID: 5K3D RELATED DB: PDB
REMARK 900 RELATED ID: 5K3E RELATED DB: PDB
DBREF 5K3F A 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
DBREF 5K3F B 1 302 UNP Q6NAM1 DEHA_RHOPA 1 302
SEQADV 5K3F GLY A -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3F HIS A 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3F ASN A 280 UNP Q6NAM1 HIS 280 ENGINEERED MUTATION
SEQADV 5K3F GLY A 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3F SER A 304 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3F GLY B -1 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3F HIS B 0 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3F ASN B 280 UNP Q6NAM1 HIS 280 ENGINEERED MUTATION
SEQADV 5K3F GLY B 303 UNP Q6NAM1 EXPRESSION TAG
SEQADV 5K3F SER B 304 UNP Q6NAM1 EXPRESSION TAG
SEQRES 1 A 306 GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE
SEQRES 2 A 306 GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE
SEQRES 3 A 306 ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU
SEQRES 4 A 306 HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL
SEQRES 5 A 306 ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA
SEQRES 6 A 306 ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER
SEQRES 7 A 306 ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA
SEQRES 8 A 306 LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL
SEQRES 9 A 306 HIS PHE ALA LEU ALA GLY HIS ASB ARG GLY ALA ARG VAL
SEQRES 10 A 306 SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER
SEQRES 11 A 306 LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR
SEQRES 12 A 306 TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 A 306 HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU
SEQRES 14 A 306 ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA
SEQRES 15 A 306 LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA
SEQRES 16 A 306 PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE
SEQRES 17 A 306 ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR
SEQRES 18 A 306 ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE
SEQRES 19 A 306 ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU
SEQRES 20 A 306 ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 A 306 THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL
SEQRES 22 A 306 GLN GLY ALA PRO ILE GLU SER GLY ASN PHE LEU PRO GLU
SEQRES 23 A 306 GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE
SEQRES 24 A 306 PHE SER ALA ALA PRO GLY SER
SEQRES 1 B 306 GLY HIS MET PRO ASP LEU ALA ASP LEU PHE PRO GLY PHE
SEQRES 2 B 306 GLY SER GLU TRP ILE ASN THR SER SER GLY ARG ILE PHE
SEQRES 3 B 306 ALA ARG VAL GLY GLY ASP GLY PRO PRO LEU LEU LEU LEU
SEQRES 4 B 306 HIS GLY PHE PRO GLN THR HIS VAL MET TRP HIS ARG VAL
SEQRES 5 B 306 ALA PRO LYS LEU ALA GLU ARG PHE LYS VAL ILE VAL ALA
SEQRES 6 B 306 ASP LEU PRO GLY TYR GLY TRP SER ASP MET PRO GLU SER
SEQRES 7 B 306 ASP GLU GLN HIS THR PRO TYR THR LYS ARG ALA MET ALA
SEQRES 8 B 306 LYS GLN LEU ILE GLU ALA MET GLU GLN LEU GLY HIS VAL
SEQRES 9 B 306 HIS PHE ALA LEU ALA GLY HIS ASP ARG GLY ALA ARG VAL
SEQRES 10 B 306 SER TYR ARG LEU ALA LEU ASP SER PRO GLY ARG LEU SER
SEQRES 11 B 306 LYS LEU ALA VAL LEU ASP ILE LEU PRO THR TYR GLU TYR
SEQRES 12 B 306 TRP GLN ARG MET ASN ARG ALA TYR ALA LEU LYS ILE TYR
SEQRES 13 B 306 HIS TRP SER PHE LEU ALA GLN PRO ALA PRO LEU PRO GLU
SEQRES 14 B 306 ASN LEU LEU GLY GLY ASP PRO ASP PHE TYR VAL LYS ALA
SEQRES 15 B 306 LYS LEU ALA SER TRP THR ARG ALA GLY ASP LEU SER ALA
SEQRES 16 B 306 PHE ASP PRO ARG ALA VAL GLU HIS TYR ARG ILE ALA PHE
SEQRES 17 B 306 ALA ASP PRO MET ARG ARG HIS VAL MET CYS GLU ASP TYR
SEQRES 18 B 306 ARG ALA GLY ALA TYR ALA ASP PHE GLU HIS ASP LYS ILE
SEQRES 19 B 306 ASP VAL GLU ALA GLY ASN LYS ILE PRO VAL PRO MET LEU
SEQRES 20 B 306 ALA LEU TRP GLY ALA SER GLY ILE ALA GLN SER ALA ALA
SEQRES 21 B 306 THR PRO LEU ASP VAL TRP ARG LYS TRP ALA SER ASP VAL
SEQRES 22 B 306 GLN GLY ALA PRO ILE GLU SER GLY ASN PHE LEU PRO GLU
SEQRES 23 B 306 GLU ALA PRO ASP GLN THR ALA GLU ALA LEU VAL ARG PHE
SEQRES 24 B 306 PHE SER ALA ALA PRO GLY SER
MODRES 5K3F ASB A 110 ASP MODIFIED RESIDUE
HET ASB A 110 12
HET CL B 401 1
HETNAM ASB ASPARTIC ACID-4-CARBOXYMETHYL ESTER
HETNAM CL CHLORIDE ION
FORMUL 1 ASB C6 H9 N O6
FORMUL 3 CL CL 1-
FORMUL 4 HOH *715(H2 O)
HELIX 1 AA1 THR A 43 HIS A 48 5 6
HELIX 2 AA2 VAL A 50 ALA A 55 1 6
HELIX 3 AA3 HIS A 80 TYR A 83 5 4
HELIX 4 AA4 THR A 84 LEU A 99 1 16
HELIX 5 AA5 ASB A 110 SER A 123 1 14
HELIX 6 AA6 PRO A 137 ARG A 144 1 8
HELIX 7 AA7 ASN A 146 ILE A 153 1 8
HELIX 8 AA8 TYR A 154 LEU A 159 1 6
HELIX 9 AA9 PRO A 164 GLY A 171 1 8
HELIX 10 AB1 ASP A 173 TRP A 185 1 13
HELIX 11 AB2 ASP A 195 ALA A 207 1 13
HELIX 12 AB3 ASP A 208 TYR A 224 1 17
HELIX 13 AB4 TYR A 224 GLY A 237 1 14
HELIX 14 AB5 GLY A 252 SER A 256 5 5
HELIX 15 AB6 THR A 259 ALA A 268 1 10
HELIX 16 AB7 PHE A 281 ALA A 286 1 6
HELIX 17 AB8 ALA A 286 ALA A 300 1 15
HELIX 18 AB9 THR B 43 HIS B 48 5 6
HELIX 19 AC1 VAL B 50 GLU B 56 1 7
HELIX 20 AC2 HIS B 80 TYR B 83 5 4
HELIX 21 AC3 THR B 84 LEU B 99 1 16
HELIX 22 AC4 ASP B 110 SER B 123 1 14
HELIX 23 AC5 PRO B 137 ARG B 144 1 8
HELIX 24 AC6 ASN B 146 ILE B 153 1 8
HELIX 25 AC7 TYR B 154 LEU B 159 1 6
HELIX 26 AC8 PRO B 164 GLY B 171 1 8
HELIX 27 AC9 ASP B 173 TRP B 185 1 13
HELIX 28 AD1 ASP B 195 ASP B 208 1 14
HELIX 29 AD2 ASP B 208 TYR B 224 1 17
HELIX 30 AD3 TYR B 224 GLY B 237 1 14
HELIX 31 AD4 THR B 259 ARG B 265 1 7
HELIX 32 AD5 PHE B 281 ALA B 286 1 6
HELIX 33 AD6 ALA B 286 SER B 299 1 14
SHEET 1 AA1 8 GLY A 12 ILE A 16 0
SHEET 2 AA1 8 ILE A 23 GLY A 29 -1 O VAL A 27 N GLY A 12
SHEET 3 AA1 8 LYS A 59 ALA A 63 -1 O VAL A 62 N ARG A 26
SHEET 4 AA1 8 PRO A 33 LEU A 37 1 N LEU A 36 O ILE A 61
SHEET 5 AA1 8 PHE A 104 HIS A 109 1 O HIS A 109 N LEU A 37
SHEET 6 AA1 8 LEU A 127 LEU A 133 1 O ALA A 131 N LEU A 106
SHEET 7 AA1 8 MET A 244 GLY A 249 1 O LEU A 245 N VAL A 132
SHEET 8 AA1 8 VAL A 271 ILE A 276 1 O GLN A 272 N ALA A 246
SHEET 1 AA2 8 GLY B 12 ILE B 16 0
SHEET 2 AA2 8 ILE B 23 GLY B 29 -1 O VAL B 27 N GLY B 12
SHEET 3 AA2 8 LYS B 59 ALA B 63 -1 O VAL B 60 N GLY B 28
SHEET 4 AA2 8 PRO B 33 LEU B 37 1 N LEU B 34 O LYS B 59
SHEET 5 AA2 8 PHE B 104 HIS B 109 1 O ALA B 105 N LEU B 35
SHEET 6 AA2 8 LEU B 127 LEU B 133 1 O ALA B 131 N LEU B 106
SHEET 7 AA2 8 MET B 244 GLY B 249 1 O LEU B 245 N VAL B 132
SHEET 8 AA2 8 VAL B 271 ILE B 276 1 O GLN B 272 N MET B 244
LINK C HIS A 109 N ASB A 110 1555 1555 1.33
LINK C ASB A 110 N ARG A 111 1555 1555 1.33
CISPEP 1 PHE A 40 PRO A 41 0 -3.25
CISPEP 2 ALA A 163 PRO A 164 0 2.48
CISPEP 3 PHE B 40 PRO B 41 0 -1.79
CISPEP 4 ALA B 163 PRO B 164 0 4.94
SITE 1 AC1 3 ASP B 110 ARG B 111 ARG B 114
CRYST1 41.830 79.620 85.230 90.00 103.09 90.00 P 1 21 1 2
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 0.023906 0.000000 0.005557 0.00000
SCALE2 0.000000 0.012560 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012046 0.00000
TER 2393 ALA A 300
TER 4697 SER B 299
MASTER 350 0 2 33 16 0 1 6 5353 2 14 48
END |