Header list of 1peh.pdb file
Complete list - 3 20 Bytes
HEADER NUCLEOTIDYLTRANSFERASE 10-JUN-96 1PEH
TITLE NMR STRUCTURE OF THE MEMBRANE-BINDING DOMAIN OF CTP PHOSPHOCHOLINE
TITLE 2 CYTIDYLYLTRANSFERASE, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPNH1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 236 - 268;
COMPND 5 SYNONYM: CYTIDYLYLTRANSFERASE MEMBRANE BINDING DOMAIN PEPTIDE;
COMPND 6 EC: 2.7.7.15;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 4 ORGANISM_COMMON: NORWAY RAT;
SOURCE 5 ORGANISM_TAXID: 10116
KEYWDS TRANSFERASE, NUCLEOTIDYLTRANSFERASE, PHOSPHOLIPID BIOSYNTHESIS,
KEYWDS 2 MEMBRANE, PHOSPHORYLATION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR S.J.DUNNE,R.B.CORNELL,J.E.JOHNSON,N.R.GLOVER,A.S.TRACEY
REVDAT 5 03-NOV-21 1PEH 1 REMARK SEQADV LINK
REVDAT 4 14-MAR-18 1PEH 1 COMPND SOURCE JRNL REMARK
REVDAT 3 24-FEB-09 1PEH 1 VERSN
REVDAT 2 01-APR-03 1PEH 1 JRNL
REVDAT 1 07-DEC-96 1PEH 0
JRNL AUTH S.J.DUNNE,R.B.CORNELL,J.E.JOHNSON,N.R.GLOVER,A.S.TRACEY
JRNL TITL STRUCTURE OF THE MEMBRANE BINDING DOMAIN OF
JRNL TITL 2 CTP:PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE.
JRNL REF BIOCHEMISTRY V. 35 11975 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8810902
JRNL DOI 10.1021/BI960821+
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.E.JOHNSON,R.B.CORNELL
REMARK 1 TITL MEMBRANE-BINDING AMPHIPATHIC ALPHA-HELICAL PEPTIDE DERIVED
REMARK 1 TITL 2 FROM CTP:PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE
REMARK 1 REF BIOCHEMISTRY V. 33 4327 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 8155650
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII
REMARK 3 AUTHORS : BIOSYM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PEH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175627.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.20
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : BIOSYM MOLECULAR
REMARK 210 SIMULATIONS/FELIX SIMULATIONS/
REMARK 210 FELIX
REMARK 210 METHOD USED : RESTRAINED DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 10
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
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: CLOSE CONTACTS
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 HD12 LEU A 242 HG22 VAL A 246 1.32
REMARK 500
REMARK 500 REMARK: NULL
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 237 CD GLU A 237 OE1 0.111
REMARK 500 1 GLU A 244 CD GLU A 244 OE1 0.110
REMARK 500 1 GLU A 257 CD GLU A 257 OE2 0.111
REMARK 500 1 GLU A 258 CD GLU A 258 OE2 0.110
REMARK 500 1 GLU A 262 CD GLU A 262 OE1 0.109
REMARK 500 1 GLU A 268 CD GLU A 268 OE1 0.116
REMARK 500 2 GLU A 237 CD GLU A 237 OE2 0.110
REMARK 500 2 GLU A 244 CD GLU A 244 OE1 0.110
REMARK 500 2 GLU A 257 CD GLU A 257 OE1 0.110
REMARK 500 2 GLU A 258 CD GLU A 258 OE2 0.110
REMARK 500 2 GLU A 262 CD GLU A 262 OE2 0.110
REMARK 500 2 GLU A 268 CD GLU A 268 OE2 0.115
REMARK 500 3 GLU A 237 CD GLU A 237 OE1 0.111
REMARK 500 3 GLU A 244 CD GLU A 244 OE2 0.111
REMARK 500 3 GLU A 257 CD GLU A 257 OE1 0.111
REMARK 500 3 GLU A 258 CD GLU A 258 OE2 0.110
REMARK 500 3 GLU A 262 CD GLU A 262 OE2 0.110
REMARK 500 3 GLU A 268 CD GLU A 268 OE2 0.117
REMARK 500 4 GLU A 237 CD GLU A 237 OE1 0.110
REMARK 500 4 GLU A 244 CD GLU A 244 OE1 0.110
REMARK 500 4 GLU A 257 CD GLU A 257 OE1 0.109
REMARK 500 4 GLU A 258 CD GLU A 258 OE2 0.112
REMARK 500 4 GLU A 262 CD GLU A 262 OE1 0.109
REMARK 500 4 GLU A 268 CD GLU A 268 OE2 0.115
REMARK 500 5 GLU A 237 CD GLU A 237 OE1 0.111
REMARK 500 5 GLU A 244 CD GLU A 244 OE2 0.110
REMARK 500 5 GLU A 257 CD GLU A 257 OE1 0.109
REMARK 500 5 GLU A 258 CD GLU A 258 OE1 0.110
REMARK 500 5 GLU A 262 CD GLU A 262 OE2 0.110
REMARK 500 5 GLU A 268 CD GLU A 268 OE1 0.113
REMARK 500 6 GLU A 237 CD GLU A 237 OE2 0.111
REMARK 500 6 GLU A 244 CD GLU A 244 OE2 0.110
REMARK 500 6 GLU A 257 CD GLU A 257 OE1 0.110
REMARK 500 6 GLU A 258 CD GLU A 258 OE2 0.109
REMARK 500 6 GLU A 262 CD GLU A 262 OE2 0.110
REMARK 500 6 GLU A 268 CD GLU A 268 OE2 0.112
REMARK 500 7 GLU A 237 CD GLU A 237 OE2 0.111
REMARK 500 7 GLU A 244 CD GLU A 244 OE1 0.109
REMARK 500 7 GLU A 257 CD GLU A 257 OE2 0.110
REMARK 500 7 GLU A 258 CD GLU A 258 OE2 0.109
REMARK 500 7 GLU A 262 CD GLU A 262 OE2 0.110
REMARK 500 7 GLU A 268 CD GLU A 268 OE2 0.115
REMARK 500 8 GLU A 237 CD GLU A 237 OE2 0.112
REMARK 500 8 GLU A 244 CD GLU A 244 OE1 0.110
REMARK 500 8 GLU A 257 CD GLU A 257 OE2 0.110
REMARK 500 8 GLU A 258 CD GLU A 258 OE2 0.110
REMARK 500 8 GLU A 262 CD GLU A 262 OE1 0.109
REMARK 500 8 GLU A 268 CD GLU A 268 OE2 0.115
REMARK 500 9 GLU A 237 CD GLU A 237 OE1 0.111
REMARK 500 9 GLU A 244 CD GLU A 244 OE2 0.110
REMARK 500
REMARK 500 THIS ENTRY HAS 60 BOND DEVIATIONS.
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 ARG A 245 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ARG A 245 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 245 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 ARG A 245 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 ARG A 245 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 5 ASP A 247 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 6 HIS A 241 CB - CG - CD2 ANGL. DEV. = -9.7 DEGREES
REMARK 500 6 ARG A 245 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 7 ARG A 245 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 8 ARG A 245 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 9 HIS A 241 CB - CG - CD2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 9 ARG A 245 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 10 HIS A 241 CB - CG - CD2 ANGL. DEV. = -10.1 DEGREES
REMARK 500 10 ARG A 245 NE - CZ - NH1 ANGL. DEV. = 4.0 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 1 TYR A 240 -86.40 -86.14
REMARK 500 1 HIS A 241 47.89 29.59
REMARK 500 1 LEU A 242 50.16 -104.64
REMARK 500 1 ARG A 245 -43.54 -150.78
REMARK 500 2 TYR A 240 -88.47 -84.21
REMARK 500 2 HIS A 241 45.06 30.51
REMARK 500 2 GLU A 244 37.22 -95.26
REMARK 500 2 ARG A 245 -40.47 -152.41
REMARK 500 3 LYS A 239 -77.17 -62.65
REMARK 500 3 TYR A 240 -80.57 -52.77
REMARK 500 3 HIS A 241 42.32 23.04
REMARK 500 3 ARG A 245 -46.91 -133.14
REMARK 500 4 TYR A 240 -89.29 -85.14
REMARK 500 4 HIS A 241 49.00 28.52
REMARK 500 4 ARG A 245 -46.21 -144.37
REMARK 500 5 LYS A 238 -34.56 -38.77
REMARK 500 5 TYR A 240 -90.27 -86.45
REMARK 500 5 HIS A 241 46.11 28.76
REMARK 500 5 ARG A 245 -44.92 -155.34
REMARK 500 6 TYR A 240 -86.86 -78.69
REMARK 500 6 HIS A 241 46.61 20.25
REMARK 500 6 ARG A 245 -45.27 -145.51
REMARK 500 7 LYS A 238 -73.15 -82.21
REMARK 500 7 TYR A 240 -89.50 -80.58
REMARK 500 7 HIS A 241 48.25 29.59
REMARK 500 7 ARG A 245 -42.94 -154.54
REMARK 500 8 TYR A 240 -87.23 -86.38
REMARK 500 8 HIS A 241 48.60 31.61
REMARK 500 8 ARG A 245 -41.72 -151.43
REMARK 500 9 TYR A 240 -84.30 -76.12
REMARK 500 9 HIS A 241 42.09 29.19
REMARK 500 9 GLU A 244 33.59 -99.77
REMARK 500 9 ARG A 245 -43.53 -148.15
REMARK 500 10 TYR A 240 -85.88 -68.60
REMARK 500 10 HIS A 241 52.28 21.04
REMARK 500 10 ARG A 245 -44.98 -147.92
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 ACE A 235
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 269
DBREF 1PEH A 236 268 UNP P19836 PCY1A_RAT 236 268
SEQADV 1PEH TRP A 263 UNP P19836 PHE 263 ENGINEERED MUTATION
SEQRES 1 A 35 ACE ASN GLU LYS LYS TYR HIS LEU GLN GLU ARG VAL ASP
SEQRES 2 A 35 LYS VAL LYS LYS LYS VAL LYS ASP VAL GLU GLU LYS SER
SEQRES 3 A 35 LYS GLU TRP VAL GLN LYS VAL GLU NH2
HET ACE A 235 6
HET NH2 A 269 3
HETNAM ACE ACETYL GROUP
HETNAM NH2 AMINO GROUP
FORMUL 1 ACE C2 H4 O
FORMUL 1 NH2 H2 N
HELIX 1 1 LYS A 248 LYS A 252 5 5
HELIX 2 2 LYS A 261 VAL A 267 1 7
LINK C ACE A 235 N ASN A 236 1555 1555 1.30
LINK C GLU A 268 N NH2 A 269 1555 1555 1.32
SITE 1 AC1 1 GLU A 237
SITE 1 AC2 1 GLU A 268
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 - 3 20 Bytes