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HEADER HYDROLASE 11-APR-19 6OJD
TITLE A HIGH-RESOLUTION CRYSTAL STRUCTURE OF COVALENT COMPLEX OF NOCB
TITLE 2 THIOESTERASE DOMAIN WITH FLUOROPHOSPHONATE NOCARDICIN G ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NOCB;
COMPND 3 CHAIN: A, B, C, D;
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 6OJD 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. 1.99 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) : 1.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.460
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 57905
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.460
REMARK 3 FREE R VALUE TEST SET COUNT : 2001
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 41.5623 - 4.7940 0.95 4139 141 0.2236 0.2537
REMARK 3 2 4.7940 - 3.8060 0.96 4022 138 0.1568 0.1856
REMARK 3 3 3.8060 - 3.3251 0.96 3971 149 0.1616 0.1861
REMARK 3 4 3.3251 - 3.0212 0.97 3970 140 0.1734 0.2192
REMARK 3 5 3.0212 - 2.8047 0.98 4003 136 0.1699 0.2296
REMARK 3 6 2.8047 - 2.6394 0.98 3981 140 0.1777 0.2318
REMARK 3 7 2.6394 - 2.5072 0.98 3997 149 0.1666 0.2095
REMARK 3 8 2.5072 - 2.3981 0.98 3979 146 0.1695 0.2216
REMARK 3 9 2.3981 - 2.3058 0.99 3997 139 0.1825 0.2030
REMARK 3 10 2.3058 - 2.2262 0.98 3959 153 0.2090 0.2703
REMARK 3 11 2.2262 - 2.1566 0.99 4004 132 0.2088 0.2227
REMARK 3 12 2.1566 - 2.0949 0.99 3978 153 0.2260 0.2642
REMARK 3 13 2.0949 - 2.0398 0.98 3944 139 0.2564 0.2782
REMARK 3 14 2.0398 - 1.9900 0.98 3960 146 0.2939 0.3624
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) : 23.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.68
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 : 0.009 6917
REMARK 3 ANGLE : 0.914 9479
REMARK 3 CHIRALITY : 0.056 1076
REMARK 3 PLANARITY : 0.011 1256
REMARK 3 DIHEDRAL : 17.192 4000
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): 19.4478 28.7118 22.3427
REMARK 3 T TENSOR
REMARK 3 T11: 0.1791 T22: 0.1647
REMARK 3 T33: 0.1801 T12: -0.0084
REMARK 3 T13: 0.0252 T23: 0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.1136 L22: 0.2918
REMARK 3 L33: 0.3765 L12: -0.0675
REMARK 3 L13: 0.0258 L23: 0.0282
REMARK 3 S TENSOR
REMARK 3 S11: 0.0045 S12: 0.0201 S13: -0.0052
REMARK 3 S21: -0.0068 S22: -0.0047 S23: -0.0113
REMARK 3 S31: -0.0163 S32: 0.0019 S33: -0.0016
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 6OJD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-19.
REMARK 100 THE DEPOSITION ID IS D_1000240791.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-18
REMARK 200 TEMPERATURE (KELVIN) : 113.15
REMARK 200 PH : 8.5-9.0
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) : 1.03323
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 : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58017
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990
REMARK 200 RESOLUTION RANGE LOW (A) : 43.370
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.62600
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: 6OJC
REMARK 200
REMARK 200 REMARK: THIN PLATE-LIKE CRYSTALS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM CHES PH 9.0, 250MM CACL2, 30% PEG
REMARK 280 4K, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 36.84000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.44500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.28000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.44500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.84000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.28000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 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 SER A 1695
REMARK 465 GLY A 1923
REMARK 465 GLU A 1924
REMARK 465 ARG A 1925
REMARK 465 MET B 1669
REMARK 465 GLY B 1670
REMARK 465 SER B 1671
REMARK 465 SER B 1672
REMARK 465 HIS B 1673
REMARK 465 HIS B 1674
REMARK 465 HIS B 1675
REMARK 465 HIS B 1676
REMARK 465 HIS B 1677
REMARK 465 HIS B 1678
REMARK 465 SER B 1679
REMARK 465 SER B 1680
REMARK 465 GLY B 1681
REMARK 465 LEU B 1682
REMARK 465 VAL B 1683
REMARK 465 PRO B 1684
REMARK 465 ARG B 1685
REMARK 465 GLY B 1686
REMARK 465 SER B 1687
REMARK 465 HIS B 1688
REMARK 465 MET B 1689
REMARK 465 VAL B 1690
REMARK 465 GLU B 1691
REMARK 465 GLY B 1692
REMARK 465 SER B 1693
REMARK 465 GLY B 1694
REMARK 465 SER B 1695
REMARK 465 ALA B 1696
REMARK 465 GLY B 1707
REMARK 465 GLU B 1924
REMARK 465 ARG B 1925
REMARK 465 MET C 1669
REMARK 465 GLY C 1670
REMARK 465 SER C 1671
REMARK 465 SER C 1672
REMARK 465 HIS C 1673
REMARK 465 HIS C 1674
REMARK 465 HIS C 1675
REMARK 465 HIS C 1676
REMARK 465 HIS C 1677
REMARK 465 HIS C 1678
REMARK 465 SER C 1679
REMARK 465 SER C 1680
REMARK 465 GLY C 1681
REMARK 465 LEU C 1682
REMARK 465 VAL C 1683
REMARK 465 PRO C 1684
REMARK 465 ARG C 1685
REMARK 465 GLY C 1686
REMARK 465 SER C 1687
REMARK 465 HIS C 1688
REMARK 465 MET C 1689
REMARK 465 VAL C 1690
REMARK 465 GLU C 1691
REMARK 465 GLY C 1692
REMARK 465 SER C 1693
REMARK 465 GLY C 1694
REMARK 465 SER C 1695
REMARK 465 ALA C 1696
REMARK 465 ASP C 1873
REMARK 465 GLY C 1874
REMARK 465 ASP C 1875
REMARK 465 GLU C 1924
REMARK 465 ARG C 1925
REMARK 465 MET D 1669
REMARK 465 GLY D 1670
REMARK 465 SER D 1671
REMARK 465 SER D 1672
REMARK 465 HIS D 1673
REMARK 465 HIS D 1674
REMARK 465 HIS D 1675
REMARK 465 HIS D 1676
REMARK 465 HIS D 1677
REMARK 465 HIS D 1678
REMARK 465 SER D 1679
REMARK 465 SER D 1680
REMARK 465 GLY D 1681
REMARK 465 LEU D 1682
REMARK 465 VAL D 1683
REMARK 465 PRO D 1684
REMARK 465 ARG D 1685
REMARK 465 GLY D 1686
REMARK 465 SER D 1687
REMARK 465 HIS D 1688
REMARK 465 MET D 1689
REMARK 465 VAL D 1690
REMARK 465 GLU D 1691
REMARK 465 GLY D 1692
REMARK 465 SER D 1693
REMARK 465 GLY D 1694
REMARK 465 SER D 1695
REMARK 465 ALA D 1696
REMARK 465 PRO D 1814
REMARK 465 ARG D 1815
REMARK 465 THR D 1816
REMARK 465 GLY D 1817
REMARK 465 ASP D 1818
REMARK 465 GLU D 1924
REMARK 465 ARG D 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 GLU A1704 CG CD OE1 OE2
REMARK 470 GLU A1768 CG CD OE1 OE2
REMARK 470 GLU A1770 CG CD OE1 OE2
REMARK 470 ARG A1815 CG CD NE CZ NH1 NH2
REMARK 470 THR A1816 OG1 CG2
REMARK 470 GLU A1821 CG CD OE1 OE2
REMARK 470 GLN A1825 CG CD OE1 NE2
REMARK 470 GLU A1838 CG CD OE1 OE2
REMARK 470 ARG A1862 CG CD NE CZ NH1 NH2
REMARK 470 ASP A1875 CG OD1 OD2
REMARK 470 GLU A1907 CG CD OE1 OE2
REMARK 470 ASP A1912 CG OD1 OD2
REMARK 470 TYR B1697 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B1704 CG CD OE1 OE2
REMARK 470 GLN B1745 CG CD OE1 NE2
REMARK 470 GLU B1770 CG CD OE1 OE2
REMARK 470 GLU B1798 CG CD OE1 OE2
REMARK 470 THR B1816 OG1 CG2
REMARK 470 GLN B1825 CG CD OE1 NE2
REMARK 470 GLU B1838 CG CD OE1 OE2
REMARK 470 GLU B1844 CG CD OE1 OE2
REMARK 470 ARG B1862 CG CD NE CZ NH1 NH2
REMARK 470 ARG B1864 CG CD NE CZ NH1 NH2
REMARK 470 ASP B1873 CG OD1 OD2
REMARK 470 ASP B1875 CG OD1 OD2
REMARK 470 GLU B1895 CG CD OE1 OE2
REMARK 470 GLU B1908 CG CD OE1 OE2
REMARK 470 TYR C1697 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU C1704 CG CD OE1 OE2
REMARK 470 GLN C1745 CG CD OE1 NE2
REMARK 470 SER C1746 OG
REMARK 470 GLU C1770 CG CD OE1 OE2
REMARK 470 GLU C1798 CG CD OE1 OE2
REMARK 470 ARG C1815 CG CD NE CZ NH1 NH2
REMARK 470 THR C1816 OG1 CG2
REMARK 470 GLU C1821 CG CD OE1 OE2
REMARK 470 GLN C1825 CG CD OE1 NE2
REMARK 470 GLU C1838 CG CD OE1 OE2
REMARK 470 GLU C1844 CG CD OE1 OE2
REMARK 470 ARG C1862 CG CD NE CZ NH1 NH2
REMARK 470 ARG C1876 CG CD NE CZ NH1 NH2
REMARK 470 ASP C1877 CG OD1 OD2
REMARK 470 ARG C1880 CG CD NE CZ NH1 NH2
REMARK 470 ASP C1885 CG OD1 OD2
REMARK 470 GLU C1902 CG CD OE1 OE2
REMARK 470 GLU C1907 CG CD OE1 OE2
REMARK 470 GLU C1908 CG CD OE1 OE2
REMARK 470 TYR D1697 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL D1698 CG1 CG2
REMARK 470 GLU D1704 CG CD OE1 OE2
REMARK 470 LEU D1721 CG CD1 CD2
REMARK 470 ASP D1747 CG OD1 OD2
REMARK 470 GLU D1755 CG CD OE1 OE2
REMARK 470 THR D1766 OG1 CG2
REMARK 470 GLU D1770 CG CD OE1 OE2
REMARK 470 GLU D1798 CG CD OE1 OE2
REMARK 470 GLU D1821 CG CD OE1 OE2
REMARK 470 GLN D1825 CG CD OE1 NE2
REMARK 470 ARG D1826 CG CD NE CZ NH1 NH2
REMARK 470 GLU D1838 CG CD OE1 OE2
REMARK 470 ARG D1864 CG CD NE CZ NH1 NH2
REMARK 470 ASP D1873 CG OD1 OD2
REMARK 470 ASP D1875 CG OD1 OD2
REMARK 470 ARG D1876 CG CD NE CZ NH1 NH2
REMARK 470 ARG D1880 CG CD NE CZ NH1 NH2
REMARK 470 GLU D1902 CG CD OE1 OE2
REMARK 470 ARG D1903 CG CD NE CZ NH1 NH2
REMARK 470 GLU D1907 CG CD OE1 OE2
REMARK 470 GLU D1908 CG CD OE1 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 GLY B 1708 HH21 ARG B 1774 1.58
REMARK 500 HE2 HIS C 1808 O HOH C 2204 1.59
REMARK 500 ND2 ASN A 1748 O HOH A 2201 1.91
REMARK 500 OD1 ASP D 1915 NH2 ARG D 1918 1.95
REMARK 500 O HOH A 2300 O HOH A 2309 2.01
REMARK 500 O HOH A 2287 O HOH A 2289 2.10
REMARK 500 O HOH C 2201 O HOH C 2289 2.13
REMARK 500 NH1 ARG C 1864 O HOH C 2201 2.14
REMARK 500 O HOH B 2232 O HOH C 2212 2.15
REMARK 500 O HOH D 2103 O HOH D 2129 2.16
REMARK 500 NH1 ARG D 1820 O HOH D 2101 2.17
REMARK 500 O HOH A 2211 O HOH B 2213 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 OD1 ASP B 1912 O HOH A 2201 4555 1.84
REMARK 500 O HOH C 2252 O HOH D 2128 2565 2.14
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 A1715 -168.97 -75.71
REMARK 500 SER A1779 -122.79 57.80
REMARK 500 THR A1816 -89.27 -84.71
REMARK 500 ASP A1891 64.27 -104.28
REMARK 500 ALA B1705 6.81 -68.19
REMARK 500 ALA B1709 78.99 51.81
REMARK 500 PRO B1715 -168.41 -75.58
REMARK 500 SER B1779 -122.99 56.57
REMARK 500 THR B1816 -70.25 -84.65
REMARK 500 PRO B1871 45.09 -76.84
REMARK 500 THR B1872 50.80 -115.03
REMARK 500 ASP B1891 55.73 -102.26
REMARK 500 PRO C1715 -169.35 -75.53
REMARK 500 SER C1779 -122.40 56.46
REMARK 500 THR C1816 -67.22 -99.87
REMARK 500 ASP C1891 58.68 -101.71
REMARK 500 THR D1706 -162.36 -72.51
REMARK 500 PRO D1715 -166.00 -77.04
REMARK 500 SER D1779 -123.30 57.19
REMARK 500 ASP D1875 156.33 172.32
REMARK 500 ASP D1891 58.68 -101.32
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 A2312 DISTANCE = 6.19 ANGSTROMS
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 CA A2104 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A1818 OD1
REMARK 620 2 ASP A1818 OD2 45.5
REMARK 620 3 HOH A2309 O 131.3 125.4
REMARK 620 4 HOH A2300 O 113.8 85.3 42.4
REMARK 620 5 ALA B1705 O 22.9 68.2 125.5 127.3
REMARK 620 6 ASP B1732 OD1 27.0 72.4 121.9 127.3 4.5
REMARK 620 7 ASP B1732 OD2 28.2 73.6 123.2 129.8 5.3 2.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B2103 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B1818 OD1
REMARK 620 2 ASP B1818 OD2 51.6
REMARK 620 3 ASP C1732 OD1 80.5 79.2
REMARK 620 4 ASP C1732 OD2 130.4 113.7 50.2
REMARK 620 5 GOL B2105 O1 119.3 77.7 124.4 96.6
REMARK 620 6 GOL B2105 O3 77.9 92.4 157.4 149.5 73.0
REMARK 620 7 GOL B2105 O2 145.7 141.6 127.6 78.7 64.5 71.0
REMARK 620 8 HOH C2217 O 84.7 135.4 86.1 86.3 142.0 85.4 79.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C2103 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C1818 OD1
REMARK 620 2 ASP C1818 OD2 50.6
REMARK 620 3 HOH C2263 O 85.4 134.3
REMARK 620 4 GOL C2104 O1 114.6 77.9 141.3
REMARK 620 5 GOL C2104 O2 141.1 141.8 79.0 64.6
REMARK 620 6 GOL C2104 O3 72.3 89.3 87.6 69.5 71.7
REMARK 620 7 ASP D1732 OD1 127.5 77.9 139.1 53.0 84.9 122.5
REMARK 620 8 ASP D1732 OD2 126.5 77.1 139.3 53.7 86.0 123.1 1.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A2103 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A2295 O
REMARK 620 2 HOH A2207 O 99.7
REMARK 620 3 HOH A2302 O 79.2 88.0
REMARK 620 4 HOH A2312 O 73.9 161.4 73.7
REMARK 620 5 HOH A2224 O 85.2 66.8 147.6 128.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 2101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MUY A 2102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 2103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 2104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 2105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 2106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 2107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 2101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 2103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 2104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 2105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 2106
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 2101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 2103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 2104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 2105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MUY B 2102 and SER B
REMARK 800 1779
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MUY C 2102 and SER C
REMARK 800 1779
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide MUY D 2001 and SER D
REMARK 800 1779
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6OJC RELATED DB: PDB
REMARK 900 UNLIGANDED NOCTE
DBREF 6OJD A 1690 1925 UNP Q5J1Q6 Q5J1Q6_9NOCA 1690 1925
DBREF 6OJD B 1690 1925 UNP Q5J1Q6 Q5J1Q6_9NOCA 1690 1925
DBREF 6OJD C 1690 1925 UNP Q5J1Q6 Q5J1Q6_9NOCA 1690 1925
DBREF 6OJD D 1690 1925 UNP Q5J1Q6 Q5J1Q6_9NOCA 1690 1925
SEQADV 6OJD MET A 1669 UNP Q5J1Q6 INITIATING METHIONINE
SEQADV 6OJD GLY A 1670 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER A 1671 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER A 1672 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS A 1673 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS A 1674 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS A 1675 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS A 1676 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS A 1677 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS A 1678 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER A 1679 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER A 1680 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD GLY A 1681 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD LEU A 1682 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD VAL A 1683 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD PRO A 1684 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD ARG A 1685 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD GLY A 1686 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER A 1687 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS A 1688 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD MET A 1689 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD MET B 1669 UNP Q5J1Q6 INITIATING METHIONINE
SEQADV 6OJD GLY B 1670 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER B 1671 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER B 1672 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS B 1673 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS B 1674 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS B 1675 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS B 1676 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS B 1677 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS B 1678 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER B 1679 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER B 1680 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD GLY B 1681 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD LEU B 1682 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD VAL B 1683 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD PRO B 1684 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD ARG B 1685 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD GLY B 1686 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER B 1687 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS B 1688 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD MET B 1689 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD MET C 1669 UNP Q5J1Q6 INITIATING METHIONINE
SEQADV 6OJD GLY C 1670 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER C 1671 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER C 1672 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS C 1673 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS C 1674 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS C 1675 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS C 1676 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS C 1677 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS C 1678 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER C 1679 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER C 1680 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD GLY C 1681 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD LEU C 1682 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD VAL C 1683 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD PRO C 1684 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD ARG C 1685 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD GLY C 1686 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER C 1687 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS C 1688 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD MET C 1689 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD MET D 1669 UNP Q5J1Q6 INITIATING METHIONINE
SEQADV 6OJD GLY D 1670 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER D 1671 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER D 1672 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS D 1673 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS D 1674 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS D 1675 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS D 1676 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS D 1677 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS D 1678 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER D 1679 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER D 1680 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD GLY D 1681 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD LEU D 1682 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD VAL D 1683 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD PRO D 1684 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD ARG D 1685 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD GLY D 1686 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD SER D 1687 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD HIS D 1688 UNP Q5J1Q6 EXPRESSION TAG
SEQADV 6OJD MET D 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
SEQRES 1 B 257 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 257 LEU VAL PRO ARG GLY SER HIS MET VAL GLU GLY SER GLY
SEQRES 3 B 257 SER ALA TYR VAL HIS THR LEU ASN PRO GLU ALA THR GLY
SEQRES 4 B 257 GLY ALA LEU VAL LEU VAL HIS PRO GLY GLU GLY LEU ALA
SEQRES 5 B 257 LEU PRO TYR HIS GLY LEU ALA PRO LEU LEU PRO ASP VAL
SEQRES 6 B 257 ARG LEU HIS VAL LEU SER ASP PRO ARG PHE GLY GLN SER
SEQRES 7 B 257 ASP ASN ARG PHE ALA THR LEU ALA GLU MET ALA THR ARG
SEQRES 8 B 257 TYR VAL GLU TRP VAL ARG THR THR GLU PRO GLU GLY PRO
SEQRES 9 B 257 TYR ARG LEU GLY GLY TRP SER PHE GLY GLY VAL VAL ALA
SEQRES 10 B 257 LEU GLU MET ALA SER GLN MET THR ALA HIS GLY ASP GLU
SEQRES 11 B 257 VAL SER ASP LEU LEU LEU VAL ASP SER HIS ASN LEU ASN
SEQRES 12 B 257 ALA ALA PRO ARG THR GLY ASP PRO ARG GLU GLY VAL ARG
SEQRES 13 B 257 GLN ARG LEU VAL GLU LEU GLY VAL ASP PRO ASP SER PRO
SEQRES 14 B 257 GLU GLY VAL ASP VAL VAL GLU GLU LEU LEU HIS ASN GLY
SEQRES 15 B 257 ALA LEU ALA ALA GLN TYR ALA PRO PRO ALA TYR ARG GLY
SEQRES 16 B 257 ARG VAL SER LEU LEU VAL THR PRO THR ASP GLY ASP ARG
SEQRES 17 B 257 ASP ALA VAL ARG ALA ARG GLY TRP ASP ARG ALA LEU LEU
SEQRES 18 B 257 PRO ASP LEU VAL VAL GLU PRO VAL PRO GLY ALA HIS GLU
SEQRES 19 B 257 ARG LEU PHE ASP GLU GLU HIS LEU SER ASP THR ALA ASP
SEQRES 20 B 257 ALA ILE ARG ARG ALA LEU GLY GLY GLU ARG
SEQRES 1 C 257 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 257 LEU VAL PRO ARG GLY SER HIS MET VAL GLU GLY SER GLY
SEQRES 3 C 257 SER ALA TYR VAL HIS THR LEU ASN PRO GLU ALA THR GLY
SEQRES 4 C 257 GLY ALA LEU VAL LEU VAL HIS PRO GLY GLU GLY LEU ALA
SEQRES 5 C 257 LEU PRO TYR HIS GLY LEU ALA PRO LEU LEU PRO ASP VAL
SEQRES 6 C 257 ARG LEU HIS VAL LEU SER ASP PRO ARG PHE GLY GLN SER
SEQRES 7 C 257 ASP ASN ARG PHE ALA THR LEU ALA GLU MET ALA THR ARG
SEQRES 8 C 257 TYR VAL GLU TRP VAL ARG THR THR GLU PRO GLU GLY PRO
SEQRES 9 C 257 TYR ARG LEU GLY GLY TRP SER PHE GLY GLY VAL VAL ALA
SEQRES 10 C 257 LEU GLU MET ALA SER GLN MET THR ALA HIS GLY ASP GLU
SEQRES 11 C 257 VAL SER ASP LEU LEU LEU VAL ASP SER HIS ASN LEU ASN
SEQRES 12 C 257 ALA ALA PRO ARG THR GLY ASP PRO ARG GLU GLY VAL ARG
SEQRES 13 C 257 GLN ARG LEU VAL GLU LEU GLY VAL ASP PRO ASP SER PRO
SEQRES 14 C 257 GLU GLY VAL ASP VAL VAL GLU GLU LEU LEU HIS ASN GLY
SEQRES 15 C 257 ALA LEU ALA ALA GLN TYR ALA PRO PRO ALA TYR ARG GLY
SEQRES 16 C 257 ARG VAL SER LEU LEU VAL THR PRO THR ASP GLY ASP ARG
SEQRES 17 C 257 ASP ALA VAL ARG ALA ARG GLY TRP ASP ARG ALA LEU LEU
SEQRES 18 C 257 PRO ASP LEU VAL VAL GLU PRO VAL PRO GLY ALA HIS GLU
SEQRES 19 C 257 ARG LEU PHE ASP GLU GLU HIS LEU SER ASP THR ALA ASP
SEQRES 20 C 257 ALA ILE ARG ARG ALA LEU GLY GLY GLU ARG
SEQRES 1 D 257 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 257 LEU VAL PRO ARG GLY SER HIS MET VAL GLU GLY SER GLY
SEQRES 3 D 257 SER ALA TYR VAL HIS THR LEU ASN PRO GLU ALA THR GLY
SEQRES 4 D 257 GLY ALA LEU VAL LEU VAL HIS PRO GLY GLU GLY LEU ALA
SEQRES 5 D 257 LEU PRO TYR HIS GLY LEU ALA PRO LEU LEU PRO ASP VAL
SEQRES 6 D 257 ARG LEU HIS VAL LEU SER ASP PRO ARG PHE GLY GLN SER
SEQRES 7 D 257 ASP ASN ARG PHE ALA THR LEU ALA GLU MET ALA THR ARG
SEQRES 8 D 257 TYR VAL GLU TRP VAL ARG THR THR GLU PRO GLU GLY PRO
SEQRES 9 D 257 TYR ARG LEU GLY GLY TRP SER PHE GLY GLY VAL VAL ALA
SEQRES 10 D 257 LEU GLU MET ALA SER GLN MET THR ALA HIS GLY ASP GLU
SEQRES 11 D 257 VAL SER ASP LEU LEU LEU VAL ASP SER HIS ASN LEU ASN
SEQRES 12 D 257 ALA ALA PRO ARG THR GLY ASP PRO ARG GLU GLY VAL ARG
SEQRES 13 D 257 GLN ARG LEU VAL GLU LEU GLY VAL ASP PRO ASP SER PRO
SEQRES 14 D 257 GLU GLY VAL ASP VAL VAL GLU GLU LEU LEU HIS ASN GLY
SEQRES 15 D 257 ALA LEU ALA ALA GLN TYR ALA PRO PRO ALA TYR ARG GLY
SEQRES 16 D 257 ARG VAL SER LEU LEU VAL THR PRO THR ASP GLY ASP ARG
SEQRES 17 D 257 ASP ALA VAL ARG ALA ARG GLY TRP ASP ARG ALA LEU LEU
SEQRES 18 D 257 PRO ASP LEU VAL VAL GLU PRO VAL PRO GLY ALA HIS GLU
SEQRES 19 D 257 ARG LEU PHE ASP GLU GLU HIS LEU SER ASP THR ALA ASP
SEQRES 20 D 257 ALA ILE ARG ARG ALA LEU GLY GLY GLU ARG
HET GOL A2101 13
HET MUY A2102 47
HET CA A2103 1
HET CA A2104 1
HET GOL A2105 14
HET GOL A2106 14
HET GOL A2107 14
HET GOL B2101 14
HET MUY B2102 47
HET CA B2103 1
HET GOL B2104 14
HET GOL B2105 11
HET GOL B2106 14
HET GOL C2101 14
HET MUY C2102 47
HET CA C2103 1
HET GOL C2104 12
HET GOL C2105 14
HET MUY D2001 47
HET GOL D2002 14
HETNAM GOL GLYCEROL
HETNAM MUY (R)-[(S)-[(3S)-3-{[(2R)-2-AMINO-2-(4-HYDROXYPHENYL)
HETNAM 2 MUY ACETYL]AMINO}-2-OXOAZETIDIN-1-YL](4-HYDROXYPHENYL)
HETNAM 3 MUY METHYL]METHYLPHOSPHINIC ACID
HETNAM CA CALCIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 12(C3 H8 O3)
FORMUL 6 MUY 4(C19 H22 N3 O6 P)
FORMUL 7 CA 4(CA 2+)
FORMUL 25 HOH *390(H2 O)
HELIX 1 AA1 ALA A 1720 ALA A 1727 5 8
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 ASN A 1809 ALA A 1813 5 5
HELIX 5 AA5 ASP A 1818 LEU A 1830 1 13
HELIX 6 AA6 SER A 1836 TYR A 1856 1 21
HELIX 7 AA7 ASP A 1877 ARG A 1882 1 6
HELIX 8 AA8 ALA A 1900 LEU A 1904 5 5
HELIX 9 AA9 ASP A 1906 GLY A 1922 1 17
HELIX 10 AB1 ALA B 1720 LEU B 1730 5 11
HELIX 11 AB2 THR B 1752 GLU B 1768 1 17
HELIX 12 AB3 SER B 1779 HIS B 1795 1 17
HELIX 13 AB4 ASN B 1809 ALA B 1813 5 5
HELIX 14 AB5 ASP B 1818 LEU B 1830 1 13
HELIX 15 AB6 SER B 1836 TYR B 1856 1 21
HELIX 16 AB7 ASP B 1877 ARG B 1882 1 6
HELIX 17 AB8 ALA B 1900 LEU B 1904 5 5
HELIX 18 AB9 HIS B 1909 LEU B 1921 1 13
HELIX 19 AC1 ALA C 1720 LEU C 1730 5 11
HELIX 20 AC2 THR C 1752 GLU C 1768 1 17
HELIX 21 AC3 SER C 1779 HIS C 1795 1 17
HELIX 22 AC4 ASP C 1818 LEU C 1830 1 13
HELIX 23 AC5 SER C 1836 TYR C 1856 1 21
HELIX 24 AC6 VAL C 1879 GLY C 1883 5 5
HELIX 25 AC7 ALA C 1900 LEU C 1904 5 5
HELIX 26 AC8 HIS C 1909 GLY C 1922 1 14
HELIX 27 AC9 ALA D 1720 LEU D 1730 5 11
HELIX 28 AD1 THR D 1752 GLU D 1768 1 17
HELIX 29 AD2 SER D 1779 HIS D 1795 1 17
HELIX 30 AD3 ARG D 1820 LEU D 1830 1 11
HELIX 31 AD4 SER D 1836 TYR D 1856 1 21
HELIX 32 AD5 ASP D 1877 ARG D 1882 1 6
HELIX 33 AD6 ALA D 1900 LEU D 1904 5 5
HELIX 34 AD7 HIS D 1909 GLY D 1922 1 14
SHEET 1 AA1 7 VAL A1698 LEU A1701 0
SHEET 2 AA1 7 ARG A1734 LEU A1738 -1 O VAL A1737 N HIS A1699
SHEET 3 AA1 7 ALA A1709 VAL A1713 1 N LEU A1712 O HIS A1736
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 LEU A1803 N LEU A1775
SHEET 6 AA1 7 VAL A1865 VAL A1869 1 O SER A1866 N LEU A1804
SHEET 7 AA1 7 LEU A1892 PRO A1896 1 O GLU A1895 N LEU A1867
SHEET 1 AA2 7 VAL B1698 LEU B1701 0
SHEET 2 AA2 7 LEU B1735 LEU B1738 -1 O VAL B1737 N HIS B1699
SHEET 3 AA2 7 LEU B1710 VAL B1713 1 N LEU B1712 O HIS B1736
SHEET 4 AA2 7 TYR B1773 TRP B1778 1 O GLY B1776 N VAL B1713
SHEET 5 AA2 7 VAL B1799 VAL B1805 1 O LEU B1803 N LEU B1775
SHEET 6 AA2 7 VAL B1865 VAL B1869 1 O SER B1866 N LEU B1804
SHEET 7 AA2 7 LEU B1892 PRO B1896 1 O VAL B1893 N VAL B1865
SHEET 1 AA3 7 VAL C1698 LEU C1701 0
SHEET 2 AA3 7 LEU C1735 LEU C1738 -1 O VAL C1737 N HIS C1699
SHEET 3 AA3 7 LEU C1710 VAL C1713 1 N LEU C1712 O HIS C1736
SHEET 4 AA3 7 TYR C1773 TRP C1778 1 O ARG C1774 N VAL C1711
SHEET 5 AA3 7 VAL C1799 VAL C1805 1 O LEU C1803 N LEU C1775
SHEET 6 AA3 7 VAL C1865 VAL C1869 1 O SER C1866 N LEU C1804
SHEET 7 AA3 7 LEU C1892 PRO C1896 1 O VAL C1893 N VAL C1865
SHEET 1 AA4 7 VAL D1698 LEU D1701 0
SHEET 2 AA4 7 LEU D1735 LEU D1738 -1 O VAL D1737 N HIS D1699
SHEET 3 AA4 7 LEU D1710 VAL D1713 1 N LEU D1712 O HIS D1736
SHEET 4 AA4 7 TYR D1773 TRP D1778 1 O ARG D1774 N VAL D1711
SHEET 5 AA4 7 VAL D1799 VAL D1805 1 O LEU D1803 N LEU D1775
SHEET 6 AA4 7 VAL D1865 VAL D1869 1 O SER D1866 N LEU D1804
SHEET 7 AA4 7 LEU D1892 PRO D1896 1 O VAL D1893 N VAL D1865
LINK OG SER A1779 P03 MUY A2102 1555 1555 1.59
LINK OD1 ASP A1818 CA CA A2104 1555 1555 2.64
LINK OD2 ASP A1818 CA CA A2104 1555 1555 2.95
LINK OG SER B1779 P03 MUY B2102 1555 1555 1.60
LINK OD1 ASP B1818 CA CA B2103 1555 1555 2.31
LINK OD2 ASP B1818 CA CA B2103 1555 1555 2.68
LINK OD1 ASP C1732 CA CA B2103 1555 1555 2.64
LINK OD2 ASP C1732 CA CA B2103 1555 1555 2.43
LINK OG SER C1779 P03 MUY C2102 1555 1555 1.59
LINK OD1 ASP C1818 CA CA C2103 1555 1555 2.47
LINK OD2 ASP C1818 CA CA C2103 1555 1555 2.68
LINK OG SER D1779 P03 MUY D2001 1555 1555 1.60
LINK CA CA A2103 O HOH A2295 1555 1555 2.62
LINK CA CA A2103 O HOH A2207 1555 1555 2.54
LINK CA CA A2103 O HOH A2302 1555 1555 2.26
LINK CA CA A2103 O HOH A2312 1555 1555 2.48
LINK CA CA A2103 O HOH A2224 1555 1555 2.87
LINK CA CA A2104 O HOH A2309 1555 1555 2.74
LINK CA CA A2104 O HOH A2300 1555 1555 2.81
LINK CA CA B2103 O1 GOL B2105 1555 1555 2.42
LINK CA CA B2103 O3 GOL B2105 1555 1555 2.50
LINK CA CA B2103 O2 GOL B2105 1555 1555 2.36
LINK CA CA B2103 O HOH C2217 1555 1555 2.41
LINK CA CA C2103 O HOH C2263 1555 1555 2.33
LINK CA CA C2103 O1 GOL C2104 1555 1555 2.62
LINK CA CA C2103 O2 GOL C2104 1555 1555 2.37
LINK CA CA C2103 O3 GOL C2104 1555 1555 2.41
LINK O ALA B1705 CA CA A2104 1555 4555 3.13
LINK OD1 ASP B1732 CA CA A2104 1555 4555 2.62
LINK OD2 ASP B1732 CA CA A2104 1555 4555 2.50
LINK OD1 ASP D1732 CA CA C2103 1555 2564 2.64
LINK OD2 ASP D1732 CA CA C2103 1555 2564 2.42
CISPEP 1 GLY A 1771 PRO A 1772 0 -3.37
CISPEP 2 GLY B 1771 PRO B 1772 0 -1.92
CISPEP 3 GLY C 1771 PRO C 1772 0 -3.37
CISPEP 4 GLY D 1771 PRO D 1772 0 -3.68
SITE 1 AC1 6 SER A1790 THR A1793 ALA A1860 ARG A1862
SITE 2 AC1 6 PRO D1859 ALA D1860
SITE 1 AC2 11 GLY A1716 SER A1779 PHE A1780 LEU A1810
SITE 2 AC2 11 LEU A1846 GLY A1850 ALA A1851 HIS A1901
SITE 3 AC2 11 GOL A2106 HOH A2246 HOH A2252
SITE 1 AC3 6 HOH A2207 HOH A2224 HOH A2295 HOH A2302
SITE 2 AC3 6 HOH A2312 ASN D1748
SITE 1 AC4 6 ASP A1818 HOH A2300 HOH A2309 ALA B1705
SITE 2 AC4 6 ASP B1732 GOL B2106
SITE 1 AC5 7 GLU A1787 SER A1790 GLN A1791 PRO A1859
SITE 2 AC5 7 HOH A2244 ALA D1860 ARG D1862
SITE 1 AC6 9 PRO A1715 GLY A1716 GLU A1717 TRP A1778
SITE 2 AC6 9 ARG A1826 GLU A1902 MUY A2102 HOH A2271
SITE 3 AC6 9 HOH A2282
SITE 1 AC7 9 ARG A1880 GLY A1883 TRP A1884 ASP A1885
SITE 2 AC7 9 HOH A2206 HOH A2241 ALA B1812 GLY B1883
SITE 3 AC7 9 HOH B2251
SITE 1 AC8 7 PRO B1715 GLY B1716 GLU B1717 TRP B1778
SITE 2 AC8 7 ARG B1826 GLU B1902 MUY B2102
SITE 1 AC9 4 ASP B1818 GOL B2105 ASP C1732 HOH C2217
SITE 1 AD1 1 MUY B2102
SITE 1 AD2 9 ASP B1818 ARG B1820 GLU B1821 CA B2103
SITE 2 AD2 9 THR C1706 ASP C1732 GOL C2105 HOH C2202
SITE 3 AD2 9 HOH C2217
SITE 1 AD3 6 CA A2104 HOH A2309 GLY B1708 ASP B1732
SITE 2 AD3 6 ARG B1774 ASP D1833
SITE 1 AD4 9 PRO C1715 GLY C1716 GLU C1717 TRP C1778
SITE 2 AD4 9 ARG C1826 GLU C1902 MUY C2102 HOH C2249
SITE 3 AD4 9 HOH C2288
SITE 1 AD5 4 ASP C1818 GOL C2104 HOH C2263 ASP D1732
SITE 1 AD6 8 HOH B2206 ASP C1818 ARG C1820 CA C2103
SITE 2 AD6 8 HOH C2248 HOH C2263 THR D1706 ASP D1732
SITE 1 AD7 5 GOL B2105 GLY C1708 ASP C1732 ARG C1774
SITE 2 AD7 5 ASP C1833
SITE 1 AD8 6 PRO D1715 GLU D1717 PRO D1722 TRP D1778
SITE 2 AD8 6 HOH D2106 HOH D2117
SITE 1 AD9 20 GLY B1716 TRP B1778 PHE B1780 GLY B1781
SITE 2 AD9 20 GLY B1782 VAL B1783 VAL B1805 SER B1807
SITE 3 AD9 20 LEU B1810 ARG B1826 LEU B1846 LEU B1847
SITE 4 AD9 20 GLY B1850 ALA B1851 HIS B1901 GOL B2101
SITE 5 AD9 20 GOL B2104 HOH B2229 HOH B2238 HOH B2242
SITE 1 AE1 18 GLY C1716 TRP C1778 PHE C1780 GLY C1781
SITE 2 AE1 18 GLY C1782 VAL C1783 VAL C1805 SER C1807
SITE 3 AE1 18 LEU C1810 LEU C1846 LEU C1847 GLY C1850
SITE 4 AE1 18 ALA C1851 HIS C1901 GOL C2101 HOH C2233
SITE 5 AE1 18 HOH C2266 HOH D2125
SITE 1 AE2 15 PRO D1715 GLY D1716 TRP D1778 PHE D1780
SITE 2 AE2 15 GLY D1781 GLY D1782 VAL D1783 VAL D1805
SITE 3 AE2 15 SER D1807 HIS D1808 LEU D1810 LEU D1846
SITE 4 AE2 15 GLY D1850 ALA D1851 HIS D1901
CRYST1 73.680 78.560 146.890 90.00 90.00 90.00 P 21 21 21 16
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 0.013572 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012729 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006808 0.00000
TER 3304 GLY A1922
TER 6565 GLY B1923
TER 9748 GLY C1923
TER 12863 GLY D1923
MASTER 679 0 20 34 28 0 50 6 7158 4 374 80
END |