Header list of 1ijp.pdb file
Complete list - 27 20 Bytes
HEADER HYDROLASE 27-APR-01 1IJP
TITLE SOLUTION STRUCTURE OF ALA20PRO/PRO64ALA SUBSTITUTED SUBUNIT C OF
TITLE 2 ESCHERICHIA COLI ATP SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SUBUNIT C;
COMPND 5 EC: 3.6.1.34;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: UNCE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JH613;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBR322
KEYWDS TRANSMEMBRANE HELIX, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR O.Y.DMITRIEV,R.H.FILLINGAME
REVDAT 4 27-OCT-21 1IJP 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1IJP 1 VERSN
REVDAT 2 01-APR-03 1IJP 1 JRNL
REVDAT 1 27-MAR-02 1IJP 0
JRNL AUTH O.Y.DMITRIEV,R.H.FILLINGAME
JRNL TITL STRUCTURE OF ALA(20) --> PRO/PRO(64) --> ALA SUBSTITUTED
JRNL TITL 2 SUBUNIT C OF ESCHERICHIA COLI ATP SYNTHASE IN WHICH THE
JRNL TITL 3 ESSENTIAL PROLINE IS SWITCHED BETWEEN TRANSMEMBRANE HELICES.
JRNL REF J.BIOL.CHEM. V. 276 27449 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11331283
JRNL DOI 10.1074/JBC.M100762200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, DISCOVER 3.0
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC. (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IJP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-01.
REMARK 100 THE DEPOSITION ID IS D_1000013341.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 50 MM NACL
REMARK 210 PRESSURE : ATMOSPHERIC ATM
REMARK 210 SAMPLE CONTENTS : 2.2 MM SUBUNIT C, 50 MM NACL, PH
REMARK 210 5.0
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED TOCSY; 2D NOESY; 3D_
REMARK 210 15N-SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 95.0, DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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 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 1 GLU A 2 CD GLU A 2 OE2 0.115
REMARK 500 1 GLU A 37 CD GLU A 37 OE2 0.115
REMARK 500 2 GLU A 2 CD GLU A 2 OE2 0.116
REMARK 500 2 GLU A 37 CD GLU A 37 OE2 0.114
REMARK 500 3 GLU A 2 CD GLU A 2 OE2 0.115
REMARK 500 3 GLU A 37 CD GLU A 37 OE2 0.115
REMARK 500 4 GLU A 2 CD GLU A 2 OE2 0.116
REMARK 500 4 GLU A 37 CD GLU A 37 OE2 0.114
REMARK 500 5 GLU A 2 CD GLU A 2 OE2 0.115
REMARK 500 5 GLU A 37 CD GLU A 37 OE2 0.115
REMARK 500 6 GLU A 2 CD GLU A 2 OE2 0.115
REMARK 500 6 GLU A 37 CD GLU A 37 OE2 0.115
REMARK 500 7 GLU A 2 CD GLU A 2 OE2 0.115
REMARK 500 7 GLU A 37 CD GLU A 37 OE2 0.115
REMARK 500 8 GLU A 2 CD GLU A 2 OE2 0.114
REMARK 500 8 GLU A 37 CD GLU A 37 OE2 0.115
REMARK 500 9 GLU A 2 CD GLU A 2 OE2 0.115
REMARK 500 9 GLU A 37 CD GLU A 37 OE2 0.115
REMARK 500 10 GLU A 2 CD GLU A 2 OE2 0.116
REMARK 500 10 GLU A 37 CD GLU A 37 OE2 0.114
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 1 ASP A 7 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 1 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ASP A 44 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 ARG A 50 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ASP A 61 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 1 ASP A 61 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 2 ASP A 7 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 2 ASP A 7 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 ASP A 44 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 ARG A 50 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 ASP A 61 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 2 ASP A 61 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 3 ASP A 7 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 3 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ASP A 44 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 3 ASP A 44 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 3 ARG A 50 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 3 ASP A 61 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 4 ASP A 7 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 4 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 4 ASP A 44 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 4 ARG A 50 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 ASP A 61 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 5 ASP A 7 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 5 ASP A 7 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 5 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 ASP A 44 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 5 ARG A 50 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 5 ASP A 61 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 6 ASP A 7 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 6 ASP A 7 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 6 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 6 ASP A 44 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 6 ARG A 50 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 ASP A 61 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 6 ASP A 61 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 7 ASP A 7 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 7 TYR A 10 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 7 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 7 ASP A 44 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 7 ARG A 50 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 7 ASP A 61 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 8 ASP A 7 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 8 ASP A 7 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 8 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 8 ASP A 44 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 8 ARG A 50 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 8 ASP A 61 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 8 ASP A 61 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 66 ANGLE DEVIATIONS.
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 1 GLU A 2 -78.94 -97.93
REMARK 500 1 ASP A 44 62.56 -119.39
REMARK 500 2 GLU A 2 80.98 65.91
REMARK 500 2 ILE A 28 -73.58 -44.22
REMARK 500 2 LEU A 59 -2.83 -58.50
REMARK 500 2 ALA A 62 -73.15 -49.90
REMARK 500 3 GLU A 2 -66.31 -108.47
REMARK 500 4 GLU A 2 -76.41 -97.31
REMARK 500 4 ILE A 28 -70.28 -54.65
REMARK 500 4 ASP A 44 60.93 -119.28
REMARK 500 4 LEU A 59 -8.20 -55.76
REMARK 500 4 ALA A 62 -71.20 -48.03
REMARK 500 4 ALA A 77 86.22 71.23
REMARK 500 4 VAL A 78 -62.29 73.72
REMARK 500 5 GLU A 2 -74.38 -128.62
REMARK 500 5 ASN A 3 -49.43 -149.42
REMARK 500 5 LEU A 59 -14.34 -49.52
REMARK 500 6 ILE A 28 -73.76 -47.66
REMARK 500 6 LEU A 59 -17.28 -46.53
REMARK 500 6 ALA A 62 -82.65 -58.16
REMARK 500 7 GLU A 2 -75.28 -98.56
REMARK 500 7 LEU A 59 -2.63 -57.72
REMARK 500 7 ALA A 62 -74.88 -50.19
REMARK 500 8 GLU A 2 -74.57 -116.59
REMARK 500 8 ASN A 3 -65.42 -145.11
REMARK 500 8 ASP A 44 31.62 -97.62
REMARK 500 8 LEU A 59 -4.44 -57.58
REMARK 500 8 ALA A 77 78.82 64.09
REMARK 500 8 VAL A 78 -35.58 73.60
REMARK 500 9 GLU A 2 -76.27 -93.02
REMARK 500 9 LEU A 59 -19.63 -48.86
REMARK 500 9 VAL A 78 74.31 40.57
REMARK 500 10 GLU A 2 70.26 62.69
REMARK 500 10 TYR A 10 -73.72 -37.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 31 GLY A 32 1 147.88
REMARK 500 VAL A 60 ASP A 61 4 148.35
REMARK 500 VAL A 60 ASP A 61 7 148.83
REMARK 500 VAL A 60 ASP A 61 8 148.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A91 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE WILD TYPE SUBUNIT C OF E.COLI ATP
REMARK 900 SYNTHASE AT PH 5.0
REMARK 900 RELATED ID: 1C0V RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE WILD TYPE SUBUNIT C OF E.COLI ATP
REMARK 900 SYNTHASE AT PH 5.0, A MORE RECENT REFINEMENT
REMARK 900 RELATED ID: 1C99 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE WILD TYPE SUBUNIT C OF E.COLI ATP
REMARK 900 SYNTHASE AT PH 8.0
DBREF 1IJP A 1 79 UNP P68699 ATPL_ECOLI 1 79
SEQADV 1IJP PRO A 20 UNP P68699 ALA 20 ENGINEERED MUTATION
SEQADV 1IJP ALA A 64 UNP P68699 PRO 64 ENGINEERED MUTATION
SEQRES 1 A 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 A 79 ALA VAL MET MET GLY LEU PRO ALA ILE GLY ALA ALA ILE
SEQRES 3 A 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 A 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 A 79 PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE ALA MET
SEQRES 6 A 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 A 79 ALA
HELIX 1 1 GLU A 2 LEU A 19 1 18
HELIX 2 2 ILE A 22 GLN A 42 1 21
HELIX 3 3 LEU A 45 VAL A 78 1 34
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - 27 20 Bytes