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HEADER HYDROLASE 11-APR-19 6OJC
TITLE A HIGH-RESOLUTION CRYSTAL STRUCTURE OF NOCB THIOESTERASE DOMAIN FROM
TITLE 2 NOCARDICIN CLUSTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NOCB;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOCARDIA UNIFORMIS SUBSP. TSUYAMANENSIS;
SOURCE 3 ORGANISM_TAXID: 96045;
SOURCE 4 GENE: NOCB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS NONRIBOSOMAL PEPTIDE SYNTHETASE (NRPS), THIOESTERASE, EPIMERIZATION,
KEYWDS 2 ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.D.PATEL,A.M.GULICK
REVDAT 1 11-SEP-19 6OJC 0
JRNL AUTH K.D.PATEL,F.B.D'ANDREA,N.M.GAUDELLI,A.R.BULLER,C.A.TOWNSEND,
JRNL AUTH 2 A.M.GULICK
JRNL TITL STRUCTURE OF A BOUND PEPTIDE PHOSPHONATE REVEALS THE
JRNL TITL 2 MECHANISM OF NOCARDICIN BIFUNCTIONAL THIOESTERASE
JRNL TITL 3 EPIMERASE-HYDROLASE HALF-REACTIONS.
JRNL REF NAT COMMUN V. 10 3868 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 31455765
JRNL DOI 10.1038/S41467-019-11740-6
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.240
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 26292
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1561
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 29.2443 - 4.3103 0.99 2349 153 0.1903 0.1980
REMARK 3 2 4.3103 - 3.4230 1.00 2265 144 0.1835 0.2103
REMARK 3 3 3.4230 - 2.9908 1.00 2272 142 0.2129 0.2182
REMARK 3 4 2.9908 - 2.7175 1.00 2243 139 0.2228 0.2950
REMARK 3 5 2.7175 - 2.5229 1.00 2244 138 0.2240 0.2633
REMARK 3 6 2.5229 - 2.3742 1.00 2248 140 0.2274 0.2402
REMARK 3 7 2.3742 - 2.2553 1.00 2222 141 0.2277 0.2663
REMARK 3 8 2.2553 - 2.1572 0.99 2216 140 0.2457 0.2826
REMARK 3 9 2.1572 - 2.0742 1.00 2239 143 0.2240 0.2730
REMARK 3 10 2.0742 - 2.0026 1.00 2226 143 0.2398 0.2776
REMARK 3 11 2.0026 - 1.9400 1.00 2207 138 0.2956 0.3241
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) : 0.240
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.76
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 : 0.017 1725
REMARK 3 ANGLE : 1.539 2366
REMARK 3 CHIRALITY : 0.083 263
REMARK 3 PLANARITY : 0.011 312
REMARK 3 DIHEDRAL : 14.430 1003
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): -44.7209 14.2554 14.8500
REMARK 3 T TENSOR
REMARK 3 T11: 0.2832 T22: 0.2457
REMARK 3 T33: 0.2781 T12: 0.0355
REMARK 3 T13: 0.0174 T23: -0.0526
REMARK 3 L TENSOR
REMARK 3 L11: 3.0331 L22: 5.1849
REMARK 3 L33: 3.3151 L12: -1.1812
REMARK 3 L13: 0.5937 L23: -1.2396
REMARK 3 S TENSOR
REMARK 3 S11: 0.1546 S12: 0.2319 S13: 0.1055
REMARK 3 S21: -0.3060 S22: -0.1388 S23: 0.1067
REMARK 3 S31: 0.0024 S32: -0.0612 S33: -0.0135
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 6OJC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1000240785.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-18
REMARK 200 TEMPERATURE (KELVIN) : 113.15
REMARK 200 PH : 5.0-6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03321
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26388
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.790
REMARK 200 RESOLUTION RANGE LOW (A) : 99.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.400
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.79
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : 1.54000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: OCTAHEDRAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0M AMMONIUM SULFATE, 0.05M BISTRIS
REMARK 280 PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 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: MONOMERIC
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 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 S SO4 A2001 LIES ON A SPECIAL POSITION.
REMARK 375 O1 SO4 A2001 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2191 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 MET A 1669
REMARK 465 GLY A 1670
REMARK 465 SER A 1671
REMARK 465 SER A 1672
REMARK 465 HIS A 1673
REMARK 465 HIS A 1674
REMARK 465 HIS A 1675
REMARK 465 HIS A 1676
REMARK 465 HIS A 1677
REMARK 465 HIS A 1678
REMARK 465 SER A 1679
REMARK 465 SER A 1680
REMARK 465 GLY A 1681
REMARK 465 LEU A 1682
REMARK 465 VAL A 1683
REMARK 465 PRO A 1684
REMARK 465 ARG A 1685
REMARK 465 GLY A 1686
REMARK 465 SER A 1687
REMARK 465 HIS A 1688
REMARK 465 MET A 1689
REMARK 465 VAL A 1690
REMARK 465 GLU A 1691
REMARK 465 GLY A 1692
REMARK 465 SER A 1693
REMARK 465 GLY A 1694
REMARK 465 ARG A 1815
REMARK 465 THR A 1816
REMARK 465 GLY A 1817
REMARK 465 ASP A 1818
REMARK 465 PRO A 1819
REMARK 465 ARG A 1820
REMARK 465 GLU A 1821
REMARK 465 GLU A 1924
REMARK 465 ARG A 1925
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 VAL A1823 CG1 CG2
REMARK 470 ARG A1826 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1830 CG CD1 CD2
REMARK 470 GLU A1838 CG CD OE1 OE2
REMARK 470 ASP A1873 CG OD1 OD2
REMARK 470 ASP A1875 CG OD1 OD2
REMARK 470 GLU A1895 CG CD OE1 OE2
REMARK 470 ARG A1903 CG CD NE CZ NH1 NH2
REMARK 470 GLU A1907 CG CD OE1 OE2
REMARK 470 GLU A1908 CG CD OE1 OE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASP A 1747 OD1 OD2
REMARK 480 ARG A 1759 NE CZ NH1 NH2
REMARK 480 GLU A 1770 CG CD OE1 OE2
REMARK 480 GLU A 1798 CG OE1
REMARK 480 GLU A 1829 CG CD OE1 OE2
REMARK 480 VAL A 1840 CG1
REMARK 480 GLU A 1844 CG OE2
REMARK 480 HIS A 1848 ND1
REMARK 480 ARG A 1862 NE CZ NH1 NH2
REMARK 480 ARG A 1876 CD NE CZ NH1 NH2
REMARK 480 GLU A 1902 CG OE2
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 2162 O HOH A 2164 2.09
REMARK 500 O LEU A 1846 O HOH A 2101 2.15
REMARK 500 NH1 ARG A 1759 OE1 GLU A 1762 2.16
REMARK 500 O THR A 1870 O HOH A 2102 2.18
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 2174 O HOH A 2174 5555 1.93
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 ARG A1765 NE - CZ - NH1 ANGL. DEV. = -3.2 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 SER A1779 -118.54 49.01
REMARK 500 ALA A1812 -63.79 -97.99
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 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 2006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 2007
DBREF 6OJC A 1690 1925 UNP Q5J1Q6 Q5J1Q6_9NOCA 1690 1925
SEQADV 6OJC MET A 1669 UNP Q5J1Q6 INITIATING METHIONINE
SEQADV 6OJC GLY A 1670 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC SER A 1671 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC SER A 1672 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC HIS A 1673 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC HIS A 1674 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC HIS A 1675 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC HIS A 1676 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC HIS A 1677 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC HIS A 1678 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC SER A 1679 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC SER A 1680 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC GLY A 1681 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC LEU A 1682 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC VAL A 1683 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC PRO A 1684 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC ARG A 1685 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC GLY A 1686 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC SER A 1687 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC HIS A 1688 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJC MET A 1689 UNP Q5J1Q6 EXPRESSION TAG
SEQRES 1 A 257 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 257 LEU VAL PRO ARG GLY SER HIS MET VAL GLU GLY SER GLY
SEQRES 3 A 257 SER ALA TYR VAL HIS THR LEU ASN PRO GLU ALA THR GLY
SEQRES 4 A 257 GLY ALA LEU VAL LEU VAL HIS PRO GLY GLU GLY LEU ALA
SEQRES 5 A 257 LEU PRO TYR HIS GLY LEU ALA PRO LEU LEU PRO ASP VAL
SEQRES 6 A 257 ARG LEU HIS VAL LEU SER ASP PRO ARG PHE GLY GLN SER
SEQRES 7 A 257 ASP ASN ARG PHE ALA THR LEU ALA GLU MET ALA THR ARG
SEQRES 8 A 257 TYR VAL GLU TRP VAL ARG THR THR GLU PRO GLU GLY PRO
SEQRES 9 A 257 TYR ARG LEU GLY GLY TRP SER PHE GLY GLY VAL VAL ALA
SEQRES 10 A 257 LEU GLU MET ALA SER GLN MET THR ALA HIS GLY ASP GLU
SEQRES 11 A 257 VAL SER ASP LEU LEU LEU VAL ASP SER HIS ASN LEU ASN
SEQRES 12 A 257 ALA ALA PRO ARG THR GLY ASP PRO ARG GLU GLY VAL ARG
SEQRES 13 A 257 GLN ARG LEU VAL GLU LEU GLY VAL ASP PRO ASP SER PRO
SEQRES 14 A 257 GLU GLY VAL ASP VAL VAL GLU GLU LEU LEU HIS ASN GLY
SEQRES 15 A 257 ALA LEU ALA ALA GLN TYR ALA PRO PRO ALA TYR ARG GLY
SEQRES 16 A 257 ARG VAL SER LEU LEU VAL THR PRO THR ASP GLY ASP ARG
SEQRES 17 A 257 ASP ALA VAL ARG ALA ARG GLY TRP ASP ARG ALA LEU LEU
SEQRES 18 A 257 PRO ASP LEU VAL VAL GLU PRO VAL PRO GLY ALA HIS GLU
SEQRES 19 A 257 ARG LEU PHE ASP GLU GLU HIS LEU SER ASP THR ALA ASP
SEQRES 20 A 257 ALA ILE ARG ARG ALA LEU GLY GLY GLU ARG
HET SO4 A2001 5
HET SO4 A2002 5
HET SO4 A2003 5
HET SO4 A2004 5
HET SO4 A2005 5
HET SO4 A2006 5
HET GOL A2007 13
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 6(O4 S 2-)
FORMUL 8 GOL C3 H8 O3
FORMUL 9 HOH *91(H2 O)
HELIX 1 AA1 ALA A 1720 LEU A 1730 5 11
HELIX 2 AA2 THR A 1752 GLU A 1768 1 17
HELIX 3 AA3 SER A 1779 HIS A 1795 1 17
HELIX 4 AA4 VAL A 1823 GLY A 1831 1 9
HELIX 5 AA5 SER A 1836 TYR A 1856 1 21
HELIX 6 AA6 THR A 1872 ARG A 1876 5 5
HELIX 7 AA7 VAL A 1879 GLY A 1883 5 5
HELIX 8 AA8 ALA A 1900 LEU A 1904 5 5
HELIX 9 AA9 HIS A 1909 GLY A 1922 1 14
SHEET 1 AA1 7 VAL A1698 LEU A1701 0
SHEET 2 AA1 7 ARG A1734 LEU A1738 -1 O LEU A1735 N LEU A1701
SHEET 3 AA1 7 ALA A1709 VAL A1713 1 N LEU A1712 O LEU A1738
SHEET 4 AA1 7 TYR A1773 TRP A1778 1 O GLY A1776 N VAL A1713
SHEET 5 AA1 7 VAL A1799 VAL A1805 1 O VAL A1805 N GLY A1777
SHEET 6 AA1 7 VAL A1865 VAL A1869 1 O SER A1866 N LEU A1802
SHEET 7 AA1 7 LEU A1892 PRO A1896 1 O GLU A1895 N VAL A1869
CISPEP 1 GLY A 1771 PRO A 1772 0 0.85
SITE 1 AC1 1 ARG A1919
SITE 1 AC2 3 PRO A1741 ARG A1742 ARG A1759
SITE 1 AC3 4 GLY A1899 ALA A1900 HIS A1909 HOH A2111
SITE 1 AC4 5 SER A1800 ASP A1801 ARG A1864 LEU A1921
SITE 2 AC4 5 GLY A1923
SITE 1 AC5 3 HIS A1699 THR A1700 HOH A2104
SITE 1 AC6 3 ARG A1876 ASP A1877 ARG A1880
SITE 1 AC7 7 GLY A1716 SER A1779 PHE A1780 HIS A1808
SITE 2 AC7 7 HIS A1901 HOH A2105 HOH A2163
CRYST1 114.730 114.730 46.601 90.00 90.00 120.00 P 3 2 1 6
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 0.008716 0.005032 0.000000 0.00000
SCALE2 0.000000 0.010065 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021459 0.00000
TER 3204 GLY A1923
MASTER 405 0 7 9 7 0 9 6 1774 1 43 20
END |