HEADER TRANSFERASE 02-AUG-99 1C9K
TITLE THE THREE DIMENSIONAL STRUCTURE OF ADENOSYLCOBINAMIDE KINASE/
TITLE 2 ADENOSYLCOBINAMIDE PHOSPHATE GUALYLYLTRANSFERASE (COBU) COMPLEXED
TITLE 3 WITH GMP: EVIDENCE FOR A SUBSTRATE INDUCED TRANSFERASE ACTIVE SITE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSYLCOBINAMIDE KINASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: COBU;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA STRUCTURE ROSSMANN FOLD P-LOOP, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.B.THOMPSON,M.G.THOMAS,J.C.ESCLANTE-SEMERENA,I.RAYMENT
REVDAT 7 07-FEB-24 1C9K 1 REMARK LINK
REVDAT 6 31-JAN-18 1C9K 1 REMARK
REVDAT 5 24-FEB-09 1C9K 1 VERSN
REVDAT 4 01-APR-03 1C9K 1 JRNL
REVDAT 3 27-DEC-00 1C9K 1 REMARK
REVDAT 2 19-JAN-00 1C9K 1 JRNL
REVDAT 1 18-AUG-99 1C9K 0
JRNL AUTH T.B.THOMPSON,M.G.THOMAS,J.C.ESCALANTE-SEMERENA,I.RAYMENT
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF ADENOSYLCOBINAMIDE
JRNL TITL 2 KINASE/ADENOSYLCOBINAMIDE PHOSPHATE GUANYLYLTRANSFERASE
JRNL TITL 3 (COBU) COMPLEXED WITH GMP: EVIDENCE FOR A SUBSTRATE-INDUCED
JRNL TITL 4 TRANSFERASE ACTIVE SITE.
JRNL REF BIOCHEMISTRY V. 38 12995 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10529169
JRNL DOI 10.1021/BI990910X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF ADENOSYLCOBINAMIDE
REMARK 1 TITL 2 KINASE/ADENOSYLCOBINAMIDE PHOSPHATE GUANYLYLTRANSFERASE FROM
REMARK 1 TITL 3 SALMONELLA TYPHIMURIUM DETERMINED TO 2.3 A RESOLUTION
REMARK 1 REF BIOCHEMISTRY V. 37 7686 1998
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TNT
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.500
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 26435
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3
REMARK 3 USING ALL DATA, NO SIGMA CUTOFF.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 27168
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3829
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 336
REMARK 3
REMARK 3 WILSON B VALUE (FROM FCALC, A**2) : 41.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.011 ; NULL ; NULL
REMARK 3 BOND ANGLES (DEGREES) : 2.320 ; NULL ; NULL
REMARK 3 TORSION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES (A) : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS (A) : NULL ; NULL ; NULL
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 RESTRAINT LIBRARIES.
REMARK 3 STEREOCHEMISTRY : TNT REFINEMENT SOFTWARE
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: USED WEIGHTED FULL MATRIX LEAST SQUARES
REMARK 3 PROCEDURE FROM TNT
REMARK 4
REMARK 4 1C9K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000009461.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-98
REMARK 200 TEMPERATURE (KELVIN) : 133
REMARK 200 PH : 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 : 14-BM-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26435
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.05300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.22700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 4000 100 MM CACL2 50 MM CHES,
REMARK 280 PH 9.0, BATCH, TEMPERATURE 277.0K
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 29.19000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.82000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.88500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.82000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.19000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.88500
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 35
REMARK 465 ASP A 36
REMARK 465 ASP A 37
REMARK 465 GLU A 38
REMARK 465 MET A 39
REMARK 465 ALA A 40
REMARK 465 GLY A 94
REMARK 465 GLY A 95
REMARK 465 GLU A 96
REMARK 465 ASN A 97
REMARK 465 ASP C 36
REMARK 465 ASP C 37
REMARK 465 GLU C 38
REMARK 465 MET C 39
REMARK 465 ALA C 40
REMARK 465 ALA C 41
REMARK 465 ARG C 42
REMARK 465 ILE C 43
REMARK 465 GLN C 44
REMARK 465 GLU C 58
REMARK 465 CYS C 59
REMARK 465 TRP C 60
REMARK 465 GLY C 95
REMARK 465 GLU C 96
REMARK 465 ASN C 97
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 GLN A 25 CG CD OE1 NE2
REMARK 470 GLN A 44 CG CD OE1 NE2
REMARK 470 HIS A 45 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 46 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 55 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 143 CG CD OE1 OE2
REMARK 470 ARG B 14 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 25 CG CD OE1 NE2
REMARK 470 LEU B 35 CG CD1 CD2
REMARK 470 ASP B 36 CG OD1 OD2
REMARK 470 ASP B 37 CG OD1 OD2
REMARK 470 GLU B 38 CG CD OE1 OE2
REMARK 470 GLN B 44 CG CD OE1 NE2
REMARK 470 HIS B 45 CG ND1 CD2 CE1 NE2
REMARK 470 HIS B 46 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 55 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 74 CG OD1 OD2
REMARK 470 GLU B 96 CG CD OE1 OE2
REMARK 470 GLU B 100 CG CD OE1 OE2
REMARK 470 GLU B 143 CG CD OE1 OE2
REMARK 470 ARG C 14 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 25 CG CD OE1 NE2
REMARK 470 LEU C 35 CG CD1 CD2
REMARK 470 HIS C 45 CG ND1 CD2 CE1 NE2
REMARK 470 HIS C 46 CG ND1 CD2 CE1 NE2
REMARK 470 ARG C 55 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 61 CG CD NE CZ NH1 NH2
REMARK 470 HIS C 62 CG ND1 CD2 CE1 NE2
REMARK 470 ASP C 74 CG OD1 OD2
REMARK 470 GLU C 100 CG CD OE1 OE2
REMARK 470 GLU C 143 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 58 N GLU B 58 CA -0.171
REMARK 500 ALA C 23 CA ALA C 23 C -0.165
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 A 9 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 9 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP A 48 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 61 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ASP A 64 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 PRO A 73 C - N - CD ANGL. DEV. = -15.0 DEGREES
REMARK 500 ASP A 98 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 98 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP A 112 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 124 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP A 152 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 152 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP B 22 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 22 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 PRO B 51 C - N - CD ANGL. DEV. = -13.4 DEGREES
REMARK 500 ALA B 57 CA - C - N ANGL. DEV. = -18.0 DEGREES
REMARK 500 ALA B 57 O - C - N ANGL. DEV. = 16.9 DEGREES
REMARK 500 GLU B 58 C - N - CA ANGL. DEV. = 16.5 DEGREES
REMARK 500 ASP B 112 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP B 113 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP B 152 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ASP C 22 N - CA - CB ANGL. DEV. = -13.6 DEGREES
REMARK 500 ASP C 22 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ALA C 23 O - C - N ANGL. DEV. = 13.8 DEGREES
REMARK 500 ARG C 61 CA - C - N ANGL. DEV. = -19.8 DEGREES
REMARK 500 ARG C 61 O - C - N ANGL. DEV. = 12.3 DEGREES
REMARK 500 HIS C 62 C - N - CA ANGL. DEV. = 17.4 DEGREES
REMARK 500 HIS C 62 CA - C - N ANGL. DEV. = -13.5 DEGREES
REMARK 500 ASP C 70 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP C 70 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ASP C 75 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP C 113 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP C 113 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 HIS C 149 CA - CB - CG ANGL. DEV. = -12.4 DEGREES
REMARK 500 ASP C 152 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG C 156 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ASP C 166 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP C 166 CB - CG - OD2 ANGL. DEV. = -5.5 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 ASP A 22 35.03 -88.50
REMARK 500 PRO A 51 164.64 -48.21
REMARK 500 PRO A 99 -12.89 -25.55
REMARK 500 GLN A 101 34.33 -83.46
REMARK 500 LEU B 35 32.58 -97.34
REMARK 500 TRP B 60 8.81 -156.07
REMARK 500 GLU B 96 35.01 -77.72
REMARK 500 GLN B 101 23.37 -74.79
REMARK 500 ASP B 103 73.44 -109.31
REMARK 500 ASP C 22 -80.74 -59.88
REMARK 500 ALA C 23 97.15 68.86
REMARK 500 PRO C 24 -67.44 -29.96
REMARK 500 ASP C 70 30.86 -95.54
REMARK 500 PRO C 99 8.12 -65.44
REMARK 500 ASP C 103 77.47 -101.07
REMARK 500 ALA C 165 161.50 -49.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 GLU B 58 -10.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 5GP C 606
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 MG C 607 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER C 13 OG
REMARK 620 2 GLU C 80 OE1 69.1
REMARK 620 3 POP C 608 O1 55.7 113.2
REMARK 620 4 POP C 608 O4 101.5 168.4 63.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GP A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GP B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP C 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5GP C 606
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CBU RELATED DB: PDB
REMARK 900 THE APO STRUCTURE OF COBU
DBREF 1C9K A 1 180 UNP Q05599 COBU_SALTY 2 181
DBREF 1C9K B 1 180 UNP Q05599 COBU_SALTY 2 181
DBREF 1C9K C 1 180 UNP Q05599 COBU_SALTY 2 181
SEQRES 1 A 180 MET ILE LEU VAL THR GLY GLY ALA ARG SER GLY LYS SER
SEQRES 2 A 180 ARG HIS ALA GLU ALA LEU ILE GLY ASP ALA PRO GLN VAL
SEQRES 3 A 180 LEU TYR ILE ALA THR SER GLN ILE LEU ASP ASP GLU MET
SEQRES 4 A 180 ALA ALA ARG ILE GLN HIS HIS LYS ASP GLY ARG PRO ALA
SEQRES 5 A 180 HIS TRP ARG THR ALA GLU CYS TRP ARG HIS LEU ASP THR
SEQRES 6 A 180 LEU ILE THR ALA ASP LEU ALA PRO ASP ASP ALA ILE LEU
SEQRES 7 A 180 LEU GLU CYS ILE THR THR MET VAL THR ASN LEU LEU PHE
SEQRES 8 A 180 ALA LEU GLY GLY GLU ASN ASP PRO GLU GLN TRP ASP TYR
SEQRES 9 A 180 ALA ALA MET GLU ARG ALA ILE ASP ASP GLU ILE GLN ILE
SEQRES 10 A 180 LEU ILE ALA ALA CYS GLN ARG CYS PRO ALA LYS VAL VAL
SEQRES 11 A 180 LEU VAL THR ASN GLU VAL GLY MET GLY ILE VAL PRO GLU
SEQRES 12 A 180 ASN ARG LEU ALA ARG HIS PHE ARG ASP ILE ALA GLY ARG
SEQRES 13 A 180 VAL ASN GLN ARG LEU ALA ALA ALA ALA ASP GLU VAL TRP
SEQRES 14 A 180 LEU VAL VAL SER GLY ILE GLY VAL LYS ILE LYS
SEQRES 1 B 180 MET ILE LEU VAL THR GLY GLY ALA ARG SER GLY LYS SER
SEQRES 2 B 180 ARG HIS ALA GLU ALA LEU ILE GLY ASP ALA PRO GLN VAL
SEQRES 3 B 180 LEU TYR ILE ALA THR SER GLN ILE LEU ASP ASP GLU MET
SEQRES 4 B 180 ALA ALA ARG ILE GLN HIS HIS LYS ASP GLY ARG PRO ALA
SEQRES 5 B 180 HIS TRP ARG THR ALA GLU CYS TRP ARG HIS LEU ASP THR
SEQRES 6 B 180 LEU ILE THR ALA ASP LEU ALA PRO ASP ASP ALA ILE LEU
SEQRES 7 B 180 LEU GLU CYS ILE THR THR MET VAL THR ASN LEU LEU PHE
SEQRES 8 B 180 ALA LEU GLY GLY GLU ASN ASP PRO GLU GLN TRP ASP TYR
SEQRES 9 B 180 ALA ALA MET GLU ARG ALA ILE ASP ASP GLU ILE GLN ILE
SEQRES 10 B 180 LEU ILE ALA ALA CYS GLN ARG CYS PRO ALA LYS VAL VAL
SEQRES 11 B 180 LEU VAL THR ASN GLU VAL GLY MET GLY ILE VAL PRO GLU
SEQRES 12 B 180 ASN ARG LEU ALA ARG HIS PHE ARG ASP ILE ALA GLY ARG
SEQRES 13 B 180 VAL ASN GLN ARG LEU ALA ALA ALA ALA ASP GLU VAL TRP
SEQRES 14 B 180 LEU VAL VAL SER GLY ILE GLY VAL LYS ILE LYS
SEQRES 1 C 180 MET ILE LEU VAL THR GLY GLY ALA ARG SER GLY LYS SER
SEQRES 2 C 180 ARG HIS ALA GLU ALA LEU ILE GLY ASP ALA PRO GLN VAL
SEQRES 3 C 180 LEU TYR ILE ALA THR SER GLN ILE LEU ASP ASP GLU MET
SEQRES 4 C 180 ALA ALA ARG ILE GLN HIS HIS LYS ASP GLY ARG PRO ALA
SEQRES 5 C 180 HIS TRP ARG THR ALA GLU CYS TRP ARG HIS LEU ASP THR
SEQRES 6 C 180 LEU ILE THR ALA ASP LEU ALA PRO ASP ASP ALA ILE LEU
SEQRES 7 C 180 LEU GLU CYS ILE THR THR MET VAL THR ASN LEU LEU PHE
SEQRES 8 C 180 ALA LEU GLY GLY GLU ASN ASP PRO GLU GLN TRP ASP TYR
SEQRES 9 C 180 ALA ALA MET GLU ARG ALA ILE ASP ASP GLU ILE GLN ILE
SEQRES 10 C 180 LEU ILE ALA ALA CYS GLN ARG CYS PRO ALA LYS VAL VAL
SEQRES 11 C 180 LEU VAL THR ASN GLU VAL GLY MET GLY ILE VAL PRO GLU
SEQRES 12 C 180 ASN ARG LEU ALA ARG HIS PHE ARG ASP ILE ALA GLY ARG
SEQRES 13 C 180 VAL ASN GLN ARG LEU ALA ALA ALA ALA ASP GLU VAL TRP
SEQRES 14 C 180 LEU VAL VAL SER GLY ILE GLY VAL LYS ILE LYS
HET PO4 A 600 5
HET 5GP A 604 24
HET PO4 B 601 5
HET 5GP B 605 24
HET MG C 607 1
HET POP C 608 9
HET 5GP C 606 20
HETNAM PO4 PHOSPHATE ION
HETNAM 5GP GUANOSINE-5'-MONOPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM POP PYROPHOSPHATE 2-
FORMUL 4 PO4 2(O4 P 3-)
FORMUL 5 5GP 3(C10 H14 N5 O8 P)
FORMUL 8 MG MG 2+
FORMUL 9 POP H2 O7 P2 2-
FORMUL 11 HOH *336(H2 O)
HELIX 1 1 GLY A 11 GLY A 21 1 11
HELIX 2 2 ALA A 41 GLY A 49 1 9
HELIX 3 3 HIS A 62 LEU A 66 5 5
HELIX 4 4 CYS A 81 LEU A 93 1 13
HELIX 5 5 ASP A 103 CYS A 125 1 23
HELIX 6 6 ASN A 144 ALA A 165 1 22
HELIX 7 7 GLY B 11 GLY B 21 1 11
HELIX 8 8 ASP B 36 ARG B 50 1 15
HELIX 9 9 HIS B 62 LEU B 66 5 5
HELIX 10 10 CYS B 81 GLY B 95 1 15
HELIX 11 11 ASP B 98 TRP B 102 5 5
HELIX 12 12 ASP B 103 CYS B 125 1 23
HELIX 13 13 ASN B 144 ALA B 165 1 22
HELIX 14 14 GLY C 11 GLY C 21 1 11
HELIX 15 15 HIS C 45 ARG C 50 1 6
HELIX 16 16 HIS C 62 LEU C 66 5 5
HELIX 17 17 CYS C 81 GLY C 94 1 14
HELIX 18 18 ASP C 103 CYS C 125 1 23
HELIX 19 19 ASN C 144 ALA C 165 1 22
SHEET 1 A 7 TRP A 54 ALA A 57 0
SHEET 2 A 7 VAL A 26 ALA A 30 1 O VAL A 26 N ARG A 55
SHEET 3 A 7 ALA A 76 GLU A 80 1 O ALA A 76 N LEU A 27
SHEET 4 A 7 LYS A 128 VAL A 132 1 O LYS A 128 N ILE A 77
SHEET 5 A 7 ILE A 2 GLY A 6 1 O ILE A 2 N LEU A 131
SHEET 6 A 7 GLU A 167 VAL A 172 1 O GLU A 167 N LEU A 3
SHEET 7 A 7 ILE A 175 LYS A 178 -1 O ILE A 175 N VAL A 172
SHEET 1 B 7 TRP B 54 ALA B 57 0
SHEET 2 B 7 VAL B 26 ALA B 30 1 O VAL B 26 N ARG B 55
SHEET 3 B 7 ALA B 76 GLU B 80 1 O ALA B 76 N LEU B 27
SHEET 4 B 7 LYS B 128 ASN B 134 1 O LYS B 128 N ILE B 77
SHEET 5 B 7 ILE B 2 GLY B 6 1 O ILE B 2 N LEU B 131
SHEET 6 B 7 GLU B 167 VAL B 172 1 O GLU B 167 N LEU B 3
SHEET 7 B 7 ILE B 175 LYS B 178 -1 O ILE B 175 N VAL B 172
SHEET 1 C 7 ARG C 55 ALA C 57 0
SHEET 2 C 7 VAL C 26 ALA C 30 1 O VAL C 26 N ARG C 55
SHEET 3 C 7 ALA C 76 GLU C 80 1 O ALA C 76 N LEU C 27
SHEET 4 C 7 LYS C 128 VAL C 132 1 O LYS C 128 N ILE C 77
SHEET 5 C 7 ILE C 2 GLY C 6 1 O ILE C 2 N LEU C 131
SHEET 6 C 7 GLU C 167 VAL C 172 1 O GLU C 167 N LEU C 3
SHEET 7 C 7 ILE C 175 LYS C 178 -1 N ILE C 175 O VAL C 172
LINK OG SER C 13 MG MG C 607 1555 1555 1.99
LINK OE1 GLU C 80 MG MG C 607 1555 1555 3.13
LINK MG MG C 607 O1 POP C 608 1555 1555 2.89
LINK MG MG C 607 O4 POP C 608 1555 1555 2.32
CISPEP 1 GLU A 80 CYS A 81 0 0.21
CISPEP 2 GLU B 80 CYS B 81 0 -0.39
CISPEP 3 GLU C 80 CYS C 81 0 -0.20
SITE 1 AC1 7 GLY A 7 ARG A 9 SER A 10 GLY A 11
SITE 2 AC1 7 LYS A 12 SER A 13 HOH A 851
SITE 1 AC2 8 GLY B 7 ARG B 9 SER B 10 GLY B 11
SITE 2 AC2 8 LYS B 12 SER B 13 HOH B 725 HOH B 749
SITE 1 AC3 3 SER C 13 GLU C 80 POP C 608
SITE 1 AC4 12 TYR A 28 ALA A 30 THR A 31 SER A 32
SITE 2 AC4 12 ILE A 34 ILE A 43 HIS A 46 LYS A 47
SITE 3 AC4 12 ARG A 50 GLU A 58 GLU A 80 CYS A 81
SITE 1 AC5 12 SER B 13 TYR B 28 ALA B 30 THR B 31
SITE 2 AC5 12 SER B 32 ILE B 43 HIS B 46 LYS B 47
SITE 3 AC5 12 ARG B 50 GLU B 58 GLU B 80 CYS B 81
SITE 1 AC6 10 GLY C 7 ALA C 8 ARG C 9 SER C 10
SITE 2 AC6 10 GLY C 11 LYS C 12 SER C 13 MG C 607
SITE 3 AC6 10 HOH C 739 HOH C 898
SITE 1 AC7 10 TYR C 28 ALA C 30 THR C 31 SER C 32
SITE 2 AC7 10 ILE C 34 LYS C 47 ARG C 50 GLU C 80
SITE 3 AC7 10 CYS C 81 THR C 84
CRYST1 58.380 87.770 101.640 90.00 90.00 90.00 P 21 21 21 12
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 0.017129 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011393 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009839 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
