Header list of 1jtb.pdb file
Complete list - r 25 2 Bytes
HEADER LIPID TRANSPORT 03-DEC-96 1JTB
TITLE LIPID TRANSFER PROTEIN COMPLEXED WITH PALMITOYL COENZYME A, NMR, 16
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPID TRANSFER PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LTP
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HORDEUM VULGARE;
SOURCE 3 ORGANISM_TAXID: 4513;
SOURCE 4 ORGAN: SEEDS
KEYWDS LIPID TRANSPORT, LIPID TRANSFER PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 16
AUTHOR M.H.LERCHE,B.B.KRAGELUND,L.M.BECH,F.M.POULSEN
REVDAT 4 05-OCT-11 1JTB 1 LINK
REVDAT 3 17-AUG-11 1JTB 1 HETATM VERSN
REVDAT 2 24-FEB-09 1JTB 1 VERSN
REVDAT 1 07-JUL-97 1JTB 0
JRNL AUTH M.H.LERCHE,B.B.KRAGELUND,L.M.BECH,F.M.POULSEN
JRNL TITL BARLEY LIPID-TRANSFER PROTEIN COMPLEXED WITH PALMITOYL COA:
JRNL TITL 2 THE STRUCTURE REVEALS A HYDROPHOBIC BINDING SITE THAT CAN
JRNL TITL 3 EXPAND TO FIT BOTH LARGE AND SMALL LIPID-LIKE LIGANDS.
JRNL REF STRUCTURE V. 5 291 1997
JRNL REFN ISSN 0969-2126
JRNL PMID 9032083
JRNL DOI 10.1016/S0969-2126(97)00186-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH B.HEINEMANN,K.V.ANDERSEN,P.R.NIELSEN,L.M.BECH,F.M.POULSEN
REMARK 1 TITL STRUCTURE IN SOLUTION OF A FOUR-HELIX LIPID BINDING PROTEIN
REMARK 1 REF PROTEIN SCI. V. 5 13 1996
REMARK 1 REFN ISSN 0961-8368
REMARK 1 REFERENCE 2
REMARK 1 AUTH D.H.SHIN,J.Y.LEE,K.Y.HWANG,K.K.KIM,S.W.SUH
REMARK 1 TITL HIGH-RESOLUTION CRYSTAL STRUCTURE OF THE NON-SPECIFIC
REMARK 1 TITL 2 LIPID-TRANSFER PROTEIN FROM MAIZE SEEDLINGS
REMARK 1 REF STRUCTURE V. 3 189 1995
REMARK 1 REFN ISSN 0969-2126
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JTB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 13 ARG A 56 CZ ARG A 56 NH2 -0.081
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 CYS A 3 CA - CB - SG ANGL. DEV. = 9.2 DEGREES
REMARK 500 1 ASP A 33 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 ARG A 44 NE - CZ - NH1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 CYS A 50 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 1 TYR A 79 CB - CG - CD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 1 ASP A 86 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 1 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 2 ASP A 33 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 2 ASP A 43 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 2 ARG A 44 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 2 TYR A 79 CB - CG - CD1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 2 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 3 ASP A 33 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 3 ASP A 43 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 3 ARG A 44 NH1 - CZ - NH2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 3 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 3 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 3 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 4 CYS A 3 N - CA - CB ANGL. DEV. = -13.5 DEGREES
REMARK 500 4 ARG A 32 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 4 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 4 ASP A 86 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 4 ASP A 86 CB - CG - OD2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 5 CYS A 3 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 5 ASP A 33 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 5 ALA A 38 N - CA - C ANGL. DEV. = -20.7 DEGREES
REMARK 500 5 ARG A 44 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 5 LYS A 72 N - CA - CB ANGL. DEV. = -11.0 DEGREES
REMARK 500 5 TYR A 79 CB - CG - CD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 5 ASP A 86 CB - CG - OD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 5 ARG A 89 NE - CZ - NH1 ANGL. DEV. = -5.2 DEGREES
REMARK 500 6 TYR A 16 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 6 CYS A 27 CA - CB - SG ANGL. DEV. = 8.8 DEGREES
REMARK 500 6 ARG A 32 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 6 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 6 ARG A 56 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 6 TYR A 79 CB - CG - CD2 ANGL. DEV. = -5.0 DEGREES
REMARK 500 6 TYR A 79 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 6 ASP A 86 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 7 ARG A 32 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 7 ASP A 33 CB - CG - OD2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 7 ARG A 44 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 7 ILE A 58 N - CA - C ANGL. DEV. = 17.8 DEGREES
REMARK 500 7 ASP A 86 CB - CG - OD2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 7 ARG A 89 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 8 ARG A 32 NH1 - CZ - NH2 ANGL. DEV. = 10.0 DEGREES
REMARK 500 8 ARG A 32 NE - CZ - NH2 ANGL. DEV. = -10.3 DEGREES
REMARK 500 8 ASP A 33 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 8 CYS A 50 CA - CB - SG ANGL. DEV. = 8.5 DEGREES
REMARK 500 8 ARG A 56 NH1 - CZ - NH2 ANGL. DEV. = 8.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 93 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 ASN A 2 -49.80 -174.37
REMARK 500 1 CYS A 3 48.64 -101.28
REMARK 500 1 VAL A 6 -60.67 -19.40
REMARK 500 1 PRO A 21 49.62 -67.10
REMARK 500 1 SER A 24 -87.50 32.09
REMARK 500 1 ASP A 33 -82.79 -55.99
REMARK 500 1 LEU A 34 -52.90 -28.65
REMARK 500 1 ALA A 38 35.29 -83.89
REMARK 500 1 SER A 40 -64.51 -97.64
REMARK 500 1 ASP A 43 -59.84 -14.95
REMARK 500 1 ARG A 56 -50.11 -19.71
REMARK 500 1 ILE A 58 -164.29 24.05
REMARK 500 1 HIS A 59 -84.90 -104.76
REMARK 500 1 LEU A 61 103.84 -48.58
REMARK 500 1 ASN A 74 54.46 19.92
REMARK 500 1 ASN A 76 55.94 -3.84
REMARK 500 1 TYR A 79 35.76 7.31
REMARK 500 1 THR A 80 -63.65 66.15
REMARK 500 1 ILE A 85 124.04 -16.54
REMARK 500 2 PRO A 12 -30.91 -36.70
REMARK 500 2 PRO A 21 173.82 -47.03
REMARK 500 2 SER A 24 37.99 11.17
REMARK 500 2 SER A 41 -55.32 -14.90
REMARK 500 2 ARG A 56 -50.62 -18.87
REMARK 500 2 ILE A 58 -67.20 10.07
REMARK 500 2 HIS A 59 -50.41 163.32
REMARK 500 2 ASN A 60 171.88 166.20
REMARK 500 2 LEU A 63 -58.04 -20.87
REMARK 500 2 ASN A 64 -32.50 -35.18
REMARK 500 2 ALA A 67 -39.91 -33.64
REMARK 500 2 ASN A 74 60.19 35.10
REMARK 500 2 ASN A 76 69.40 -34.27
REMARK 500 2 TYR A 79 74.93 -13.79
REMARK 500 2 THR A 80 -47.32 21.72
REMARK 500 2 ILE A 81 64.63 19.15
REMARK 500 2 ASP A 84 57.34 -113.62
REMARK 500 2 ILE A 85 106.33 -18.28
REMARK 500 3 CYS A 3 -72.01 -102.82
REMARK 500 3 VAL A 6 -70.71 -47.09
REMARK 500 3 ALA A 38 46.65 -78.41
REMARK 500 3 SER A 41 65.61 -13.24
REMARK 500 3 ASP A 43 -168.94 -70.14
REMARK 500 3 GLN A 45 -15.24 -43.40
REMARK 500 3 ARG A 56 -53.87 -18.76
REMARK 500 3 ILE A 58 -61.94 -16.37
REMARK 500 3 HIS A 59 -65.76 124.33
REMARK 500 3 ASN A 60 -41.60 -130.02
REMARK 500 3 LEU A 61 108.55 46.84
REMARK 500 3 LEU A 63 -57.57 -2.32
REMARK 500 3 ASN A 76 -71.57 46.70
REMARK 500
REMARK 500 THIS ENTRY HAS 289 RAMACHANDRAN OUTLIERS.
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 GLY A 20 PRO A 21 3 124.24
REMARK 500 VAL A 77 PRO A 78 6 134.63
REMARK 500 VAL A 77 PRO A 78 8 126.69
REMARK 500 SER A 82 PRO A 83 8 147.26
REMARK 500 VAL A 77 PRO A 78 9 -141.80
REMARK 500 VAL A 77 PRO A 78 10 129.95
REMARK 500 GLY A 20 PRO A 21 11 -127.27
REMARK 500 VAL A 77 PRO A 78 11 124.58
REMARK 500 VAL A 77 PRO A 78 13 120.96
REMARK 500 GLY A 20 PRO A 21 14 121.12
REMARK 500 VAL A 77 PRO A 78 16 149.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 32 0.19 SIDE CHAIN
REMARK 500 1 ARG A 44 0.31 SIDE CHAIN
REMARK 500 1 ARG A 56 0.28 SIDE CHAIN
REMARK 500 1 ARG A 89 0.15 SIDE CHAIN
REMARK 500 2 ARG A 32 0.26 SIDE CHAIN
REMARK 500 2 ARG A 44 0.23 SIDE CHAIN
REMARK 500 2 ARG A 56 0.20 SIDE CHAIN
REMARK 500 2 ARG A 89 0.22 SIDE CHAIN
REMARK 500 3 ARG A 32 0.32 SIDE CHAIN
REMARK 500 3 ARG A 44 0.29 SIDE CHAIN
REMARK 500 3 ARG A 56 0.30 SIDE CHAIN
REMARK 500 3 ARG A 89 0.21 SIDE CHAIN
REMARK 500 4 ARG A 32 0.20 SIDE CHAIN
REMARK 500 4 ARG A 44 0.23 SIDE CHAIN
REMARK 500 4 ARG A 56 0.21 SIDE CHAIN
REMARK 500 4 ARG A 89 0.29 SIDE CHAIN
REMARK 500 5 ARG A 32 0.30 SIDE CHAIN
REMARK 500 5 ARG A 44 0.28 SIDE CHAIN
REMARK 500 5 ARG A 56 0.19 SIDE CHAIN
REMARK 500 5 ARG A 89 0.29 SIDE CHAIN
REMARK 500 6 ARG A 44 0.27 SIDE CHAIN
REMARK 500 6 ARG A 56 0.29 SIDE CHAIN
REMARK 500 6 ARG A 89 0.28 SIDE CHAIN
REMARK 500 7 ARG A 32 0.20 SIDE CHAIN
REMARK 500 7 ARG A 44 0.13 SIDE CHAIN
REMARK 500 7 ARG A 56 0.29 SIDE CHAIN
REMARK 500 7 ARG A 89 0.32 SIDE CHAIN
REMARK 500 8 ARG A 32 0.23 SIDE CHAIN
REMARK 500 8 ARG A 44 0.16 SIDE CHAIN
REMARK 500 8 ARG A 56 0.16 SIDE CHAIN
REMARK 500 8 ARG A 89 0.16 SIDE CHAIN
REMARK 500 9 ARG A 32 0.24 SIDE CHAIN
REMARK 500 9 ARG A 44 0.14 SIDE CHAIN
REMARK 500 9 ARG A 56 0.32 SIDE CHAIN
REMARK 500 9 ARG A 89 0.27 SIDE CHAIN
REMARK 500 10 ARG A 32 0.26 SIDE CHAIN
REMARK 500 10 ARG A 44 0.25 SIDE CHAIN
REMARK 500 10 ARG A 56 0.28 SIDE CHAIN
REMARK 500 10 ARG A 89 0.25 SIDE CHAIN
REMARK 500 11 ARG A 32 0.25 SIDE CHAIN
REMARK 500 11 ARG A 44 0.28 SIDE CHAIN
REMARK 500 11 ARG A 56 0.30 SIDE CHAIN
REMARK 500 11 ARG A 89 0.19 SIDE CHAIN
REMARK 500 12 ARG A 32 0.32 SIDE CHAIN
REMARK 500 12 ARG A 44 0.30 SIDE CHAIN
REMARK 500 12 ARG A 56 0.31 SIDE CHAIN
REMARK 500 12 ARG A 89 0.30 SIDE CHAIN
REMARK 500 13 ARG A 32 0.10 SIDE CHAIN
REMARK 500 13 ARG A 44 0.21 SIDE CHAIN
REMARK 500 13 ARG A 56 0.28 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 63 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 5 ALA A 38 50.3 L L OUTSIDE RANGE
REMARK 500 7 ILE A 58 24.0 L L OUTSIDE RANGE
REMARK 500 8 ILE A 58 23.6 L L OUTSIDE RANGE
REMARK 500 9 CYS A 48 45.1 L L OUTSIDE RANGE
REMARK 500 10 ILE A 58 24.0 L L OUTSIDE RANGE
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 2 PLM A 96
REMARK 610 3 PLM A 96
REMARK 610 4 PLM A 96
REMARK 610 5 PLM A 96
REMARK 610 6 PLM A 96
REMARK 610 7 PLM A 96
REMARK 610 8 PLM A 96
REMARK 610 9 PLM A 96
REMARK 610 10 PLM A 96
REMARK 610 11 PLM A 96
REMARK 610 12 PLM A 96
REMARK 610 13 PLM A 96
REMARK 610 15 PLM A 96
REMARK 610 16 PLM A 96
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 92
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLM A 96
DBREF 1JTB A 1 91 UNP P07597 NLT1_HORVU 27 117
SEQRES 1 A 91 LEU ASN CYS GLY GLN VAL ASP SER LYS MET LYS PRO CYS
SEQRES 2 A 91 LEU THR TYR VAL GLN GLY GLY PRO GLY PRO SER GLY GLU
SEQRES 3 A 91 CYS CYS ASN GLY VAL ARG ASP LEU HIS ASN GLN ALA GLN
SEQRES 4 A 91 SER SER GLY ASP ARG GLN THR VAL CYS ASN CYS LEU LYS
SEQRES 5 A 91 GLY ILE ALA ARG GLY ILE HIS ASN LEU ASN LEU ASN ASN
SEQRES 6 A 91 ALA ALA SER ILE PRO SER LYS CYS ASN VAL ASN VAL PRO
SEQRES 7 A 91 TYR THR ILE SER PRO ASP ILE ASP CYS SER ARG ILE TYR
HET COA A 92 79
HET PLM A 96 48
HETNAM COA COENZYME A
HETNAM PLM PALMITIC ACID
FORMUL 2 COA C21 H36 N7 O16 P3 S
FORMUL 3 PLM C16 H32 O2
HELIX 1 H1 CYS A 3 GLY A 19 1IRREGULAR DUE TO PRO 12 17
HELIX 2 H2 GLY A 25 GLN A 37 1 13
HELIX 3 H3 ARG A 44 ARG A 56 1 13
HELIX 4 H4 LEU A 63 ASN A 74 1IRREGULAR DUE TO PRO 70 12
SSBOND 1 CYS A 3 CYS A 50 1555 1555 2.02
SSBOND 2 CYS A 13 CYS A 27 1555 1555 2.02
SSBOND 3 CYS A 28 CYS A 73 1555 1555 2.02
SSBOND 4 CYS A 48 CYS A 87 1555 1555 2.02
LINK S1P COA A 92 C1 PLM A 96 1555 1555 1.81
CISPEP 1 GLY A 22 PRO A 23 1 -6.41
CISPEP 2 GLY A 22 PRO A 23 2 -12.34
CISPEP 3 GLY A 22 PRO A 23 3 4.67
CISPEP 4 GLY A 22 PRO A 23 4 -15.31
CISPEP 5 GLY A 22 PRO A 23 5 20.21
CISPEP 6 GLY A 22 PRO A 23 6 10.75
CISPEP 7 GLY A 22 PRO A 23 7 -21.68
CISPEP 8 GLY A 22 PRO A 23 8 -3.64
CISPEP 9 GLY A 22 PRO A 23 9 -25.67
CISPEP 10 GLY A 22 PRO A 23 10 -15.42
CISPEP 11 GLY A 22 PRO A 23 11 15.41
CISPEP 12 GLY A 22 PRO A 23 12 16.18
CISPEP 13 GLY A 22 PRO A 23 13 18.51
CISPEP 14 GLY A 22 PRO A 23 14 10.00
CISPEP 15 GLY A 22 PRO A 23 15 11.48
CISPEP 16 GLY A 22 PRO A 23 16 -1.11
SITE 1 AC1 11 LEU A 1 ASN A 2 CYS A 3 GLY A 4
SITE 2 AC1 11 VAL A 6 ASP A 7 MET A 10 LEU A 14
SITE 3 AC1 11 LEU A 51 ILE A 54 PLM A 96
SITE 1 AC2 13 VAL A 6 MET A 10 VAL A 31 LEU A 34
SITE 2 AC2 13 HIS A 35 VAL A 47 LEU A 51 ILE A 69
SITE 3 AC2 13 PRO A 70 VAL A 77 TYR A 79 ILE A 81
SITE 4 AC2 13 COA A 92
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 - r 25 2 Bytes