Header list of 1g5w.pdb file
Complete list - b 23 2 Bytes
HEADER LIPID BINDING PROTEIN 02-NOV-00 1G5W
TITLE SOLUTION STRUCTURE OF HUMAN HEART-TYPE FATTY ACID BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: HEART;
SOURCE 6 TISSUE: MUSCLE;
SOURCE 7 GENE: FABP3;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET3D
KEYWDS NMR SPECTROSCOPY, PROTEIN-LIGAND INTERACTIONS, SELECTED-FIT BINDING,
KEYWDS 2 LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.LUECKE,M.RADEMACHER,A.ZIMMERMAN,H.T.B.VAN MOERKERK,J.H.VEERKAMP,
AUTHOR 2 H.RUETERJANS
REVDAT 4 23-FEB-22 1G5W 1 REMARK
REVDAT 3 24-FEB-09 1G5W 1 VERSN
REVDAT 2 01-APR-03 1G5W 1 JRNL
REVDAT 1 07-MAR-01 1G5W 0
JRNL AUTH C.LUCKE,M.RADEMACHER,A.W.ZIMMERMAN,H.T.VAN MOERKERK,
JRNL AUTH 2 J.H.VEERKAMP,H.RUTERJANS
JRNL TITL SPIN-SYSTEM HETEROGENEITIES INDICATE A SELECTED-FIT
JRNL TITL 2 MECHANISM IN FATTY ACID BINDING TO HEART-TYPE FATTY
JRNL TITL 3 ACID-BINDING PROTEIN (H-FABP).
JRNL REF BIOCHEM.J. V. 354 259 2001
JRNL REFN ISSN 0264-6021
JRNL PMID 11171102
JRNL DOI 10.1042/0264-6021:3540259
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.ZANOTTI,G.SCAPIN,P.SPANDON,J.H.VEERKAMP,J.C.SACCHETTINI
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF RECOMBINANT HUMAN MUSCLE
REMARK 1 TITL 2 FATTY ACID-BINDING PROTEIN
REMARK 1 REF J.BIOL.CHEM. V. 267 18541 1992
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.C.M.YOUNG,G.SCAPIN,A.KROMMINGA,S.B.PATEL,J.H.VEERKAMP,
REMARK 1 AUTH 2 J.C.SACCHETTINI
REMARK 1 TITL STRUCTURAL STUDIES ON HUMAN MUSCLE FATTY ACID-BINDING
REMARK 1 TITL 2 PROTEIN AT 1.4 A RESOLUTION: BINDING INTERACTIONS WITH THREE
REMARK 1 TITL 3 C18 FATTY ACIDS
REMARK 1 REF STRUCTURE V. 2 523 1994
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 3
REMARK 1 AUTH D.LASSEN,C.LUECKE,M.KVEDER,A.MESGARZADEH,J.M.SCHMIDT,
REMARK 1 AUTH 2 B.SPECHT,A.LEZIUS,F.SPENER,H.RUETERJANS
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF BOVINE HEART
REMARK 1 TITL 2 FATTY-ACID-BINDING PROTEIN WITH BOUND PALMITIC ACID,
REMARK 1 TITL 3 DETERMINED BY MULTIDIMENSIONAL NMR SPECTROSCOPY
REMARK 1 REF EUR.J.BIOCHEM. V. 230 266 1995
REMARK 1 REFN ISSN 0014-2956
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.3, DISCOVER 97
REMARK 3 AUTHORS : BRUKER (XWINNMR), MSI (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS DETERMINED BASED ON
REMARK 3 2589 NOE-DERIVED DISTANCE CONSTRAINTS AND 40 H-BOND CONSTRAINTS.
REMARK 4
REMARK 4 1G5W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012272.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 20
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1-3 MM H-FABP (NON-LABELLED OR
REMARK 210 15N-LABELLED); 20 MM PHOSPHATE
REMARK 210 BUFFER (PH 5.5); 0.05% NAN3; 1-3
REMARK 210 MM H-FABP (U-15N); 20 MM
REMARK 210 PHOSPHATE BUFFER (PH 5.5); 0.05%
REMARK 210 NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_NOESY; 3D_15N-SEPARATED_NOESY
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 : AURELIA 2.5.9, DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING AND ENERGY
REMARK 210 -MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH LOWEST
REMARK 210 VIOLATIONS OF EXPERIMENTAL
REMARK 210 CONSTRAINTS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING NON-DELIPIDATED
REMARK 210 RECOMBINANT HUMAN H-FABP SAMPLES.
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 43 CD GLU A 43 OE2 0.118
REMARK 500 1 GLU A 61 CD GLU A 61 OE2 0.116
REMARK 500 1 GLU A 69 CD GLU A 69 OE2 0.117
REMARK 500 1 GLU A 72 CD GLU A 72 OE2 0.119
REMARK 500 1 HIS A 93 CG HIS A 93 CD2 0.056
REMARK 500 1 GLU A 101 CD GLU A 101 OE2 0.119
REMARK 500 1 GLU A 107 CD GLU A 107 OE2 0.118
REMARK 500 1 GLU A 129 CD GLU A 129 OE2 0.118
REMARK 500 1 GLU A 131 CD GLU A 131 OE2 0.115
REMARK 500 1 ALA A 132 C ALA A 132 OXT -0.122
REMARK 500 2 GLU A 43 CD GLU A 43 OE2 0.117
REMARK 500 2 GLU A 61 CD GLU A 61 OE2 0.114
REMARK 500 2 GLU A 69 CD GLU A 69 OE2 0.117
REMARK 500 2 GLU A 72 CD GLU A 72 OE2 0.117
REMARK 500 2 HIS A 93 CG HIS A 93 CD2 0.058
REMARK 500 2 GLU A 101 CD GLU A 101 OE2 0.118
REMARK 500 2 GLU A 107 CD GLU A 107 OE2 0.117
REMARK 500 2 GLU A 129 CD GLU A 129 OE2 0.117
REMARK 500 2 GLU A 131 CD GLU A 131 OE2 0.117
REMARK 500 2 ALA A 132 C ALA A 132 OXT -0.123
REMARK 500 3 GLU A 43 CD GLU A 43 OE2 0.117
REMARK 500 3 GLU A 61 CD GLU A 61 OE2 0.117
REMARK 500 3 GLU A 69 CD GLU A 69 OE2 0.119
REMARK 500 3 GLU A 72 CD GLU A 72 OE2 0.116
REMARK 500 3 HIS A 93 CG HIS A 93 CD2 0.058
REMARK 500 3 GLU A 101 CD GLU A 101 OE2 0.118
REMARK 500 3 GLU A 107 CD GLU A 107 OE2 0.117
REMARK 500 3 GLU A 129 CD GLU A 129 OE2 0.116
REMARK 500 3 GLU A 131 CD GLU A 131 OE2 0.116
REMARK 500 3 ALA A 132 C ALA A 132 OXT -0.123
REMARK 500 4 GLU A 43 CD GLU A 43 OE2 0.117
REMARK 500 4 GLU A 61 CD GLU A 61 OE2 0.118
REMARK 500 4 GLU A 69 CD GLU A 69 OE2 0.118
REMARK 500 4 GLU A 72 CD GLU A 72 OE2 0.118
REMARK 500 4 HIS A 93 CG HIS A 93 CD2 0.055
REMARK 500 4 GLU A 101 CD GLU A 101 OE2 0.118
REMARK 500 4 GLU A 107 CD GLU A 107 OE2 0.118
REMARK 500 4 GLU A 129 CD GLU A 129 OE2 0.117
REMARK 500 4 GLU A 131 CD GLU A 131 OE2 0.118
REMARK 500 4 ALA A 132 C ALA A 132 OXT -0.124
REMARK 500 5 GLU A 43 CD GLU A 43 OE2 0.117
REMARK 500 5 GLU A 61 CD GLU A 61 OE2 0.114
REMARK 500 5 GLU A 69 CD GLU A 69 OE2 0.118
REMARK 500 5 GLU A 72 CD GLU A 72 OE2 0.117
REMARK 500 5 HIS A 93 CG HIS A 93 CD2 0.055
REMARK 500 5 GLU A 101 CD GLU A 101 OE2 0.117
REMARK 500 5 GLU A 107 CD GLU A 107 OE2 0.118
REMARK 500 5 GLU A 129 CD GLU A 129 OE2 0.117
REMARK 500 5 GLU A 131 CD GLU A 131 OE2 0.116
REMARK 500 5 ALA A 132 C ALA A 132 OXT -0.124
REMARK 500
REMARK 500 THIS ENTRY HAS 201 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 ASP A 2 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 ASP A 12 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 1 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 ASP A 47 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 1 HIS A 54 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 ASP A 71 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 ASP A 76 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 1 ASP A 77 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 1 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ASP A 87 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 HIS A 93 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 1 ASP A 98 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 1 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 ASP A 110 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 1 HIS A 119 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 DEGREES
REMARK 500 1 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 ASP A 2 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 ASP A 12 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 ASP A 17 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 ASP A 18 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 2 ASP A 18 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 HIS A 54 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 2 ASP A 71 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 ASP A 76 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 ASP A 77 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 2 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ASP A 87 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 HIS A 93 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 ASP A 98 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ASP A 110 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 HIS A 119 ND1 - CE1 - NE2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 2 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ASP A 2 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 3 ASP A 12 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 3 ASP A 17 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 3 ASP A 17 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 3 ASP A 18 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 3 ASP A 18 CB - CG - OD2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 3 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 3 ASP A 47 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 3 HIS A 54 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 3 ASP A 71 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 3 ASP A 76 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 3 ASP A 77 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 3 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 3 ASP A 87 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 3 HIS A 93 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 3 ASP A 98 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 386 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 45 -78.51 -134.55
REMARK 500 1 ASP A 47 -12.05 66.62
REMARK 500 1 PHE A 57 -81.46 -157.04
REMARK 500 1 LEU A 66 90.21 60.78
REMARK 500 1 LEU A 104 76.18 -111.73
REMARK 500 1 HIS A 119 -102.90 -129.48
REMARK 500 1 ALA A 122 95.68 -163.66
REMARK 500 1 GLU A 131 50.94 -119.04
REMARK 500 2 ALA A 28 -50.07 78.25
REMARK 500 2 LEU A 66 82.73 52.81
REMARK 500 2 ASP A 77 80.17 63.01
REMARK 500 2 HIS A 119 -101.51 -126.42
REMARK 500 3 ALA A 28 -58.13 79.13
REMARK 500 3 LYS A 58 123.29 61.41
REMARK 500 3 ASP A 77 75.22 62.58
REMARK 500 3 LEU A 104 79.68 -111.16
REMARK 500 3 ALA A 122 99.09 -164.06
REMARK 500 3 GLU A 131 55.76 -118.27
REMARK 500 4 LYS A 14 -75.45 -83.99
REMARK 500 4 ASN A 15 44.20 -106.44
REMARK 500 4 ASP A 17 -53.47 -168.20
REMARK 500 4 PHE A 27 -54.88 -146.37
REMARK 500 4 LYS A 58 90.51 62.55
REMARK 500 4 LEU A 66 93.07 63.21
REMARK 500 4 ASP A 76 51.32 -111.18
REMARK 500 4 ASP A 77 73.67 51.84
REMARK 500 4 ALA A 122 86.62 -158.11
REMARK 500 5 LYS A 14 -88.16 -81.92
REMARK 500 5 ASN A 15 43.03 -98.10
REMARK 500 5 PHE A 57 75.08 -101.42
REMARK 500 5 LYS A 58 132.62 64.44
REMARK 500 5 LEU A 66 93.57 65.60
REMARK 500 5 ASP A 77 69.74 66.78
REMARK 500 5 ASP A 87 79.22 -109.40
REMARK 500 5 ASP A 98 -101.36 67.15
REMARK 500 5 HIS A 119 -105.49 -132.59
REMARK 500 5 ALA A 122 84.22 -161.68
REMARK 500 5 GLU A 131 47.95 -99.06
REMARK 500 6 ALA A 28 -52.05 78.76
REMARK 500 6 THR A 56 -43.46 89.40
REMARK 500 6 PHE A 57 -70.97 -62.10
REMARK 500 6 LEU A 66 88.70 60.65
REMARK 500 6 ASP A 77 68.81 64.01
REMARK 500 6 THR A 121 -44.32 66.58
REMARK 500 6 GLU A 131 50.97 -111.52
REMARK 500 7 ASP A 47 -23.96 70.99
REMARK 500 7 THR A 56 46.61 -94.87
REMARK 500 7 PHE A 57 -79.01 -164.41
REMARK 500 7 ASP A 77 72.51 58.33
REMARK 500 7 ASP A 98 -101.50 66.84
REMARK 500
REMARK 500 THIS ENTRY HAS 161 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 LEU A 108 ILE A 109 18 143.12
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 10 TYR A 128 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BWY RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF BOVINE HEART-TYPE FABP
REMARK 900 RELATED ID: 2HMB RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN HEART-TYPE FABP
REMARK 900 RELATED ID: 1HMR RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN HEART-TYPE FABP WITH ELAIDIC ACID
REMARK 900 RELATED ID: 1HMS RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN HEART-TYPE FABP WITH OLEIC ACID
REMARK 900 RELATED ID: 1HMT RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN HEART-TYPE FABP WITH STEARIC ACID
DBREF 1G5W A 1 132 UNP P05413 FABPH_HUMAN 1 132
SEQRES 1 A 132 VAL ASP ALA PHE LEU GLY THR TRP LYS LEU VAL ASP SER
SEQRES 2 A 132 LYS ASN PHE ASP ASP TYR MET LYS SER LEU GLY VAL GLY
SEQRES 3 A 132 PHE ALA THR ARG GLN VAL ALA SER MET THR LYS PRO THR
SEQRES 4 A 132 THR ILE ILE GLU LYS ASN GLY ASP ILE LEU THR LEU LYS
SEQRES 5 A 132 THR HIS SER THR PHE LYS ASN THR GLU ILE SER PHE LYS
SEQRES 6 A 132 LEU GLY VAL GLU PHE ASP GLU THR THR ALA ASP ASP ARG
SEQRES 7 A 132 LYS VAL LYS SER ILE VAL THR LEU ASP GLY GLY LYS LEU
SEQRES 8 A 132 VAL HIS LEU GLN LYS TRP ASP GLY GLN GLU THR THR LEU
SEQRES 9 A 132 VAL ARG GLU LEU ILE ASP GLY LYS LEU ILE LEU THR LEU
SEQRES 10 A 132 THR HIS GLY THR ALA VAL CYS THR ARG THR TYR GLU LYS
SEQRES 11 A 132 GLU ALA
HELIX 1 1 VAL A 1 LEU A 5 5 5
HELIX 2 2 ASN A 15 GLY A 24 1 10
HELIX 3 3 GLY A 26 THR A 36 1 11
SHEET 1 A10 THR A 60 PHE A 64 0
SHEET 2 A10 LEU A 49 HIS A 54 -1 N LEU A 49 O PHE A 64
SHEET 3 A10 THR A 39 GLU A 43 -1 O THR A 39 N HIS A 54
SHEET 4 A10 GLY A 6 LYS A 14 -1 O GLY A 6 N ILE A 42
SHEET 5 A10 VAL A 123 LYS A 130 -1 O THR A 125 N LYS A 14
SHEET 6 A10 LYS A 112 THR A 118 -1 N LEU A 113 O TYR A 128
SHEET 7 A10 GLN A 100 LEU A 108 -1 N THR A 103 O THR A 118
SHEET 8 A10 LYS A 90 TRP A 97 -1 O LEU A 91 N ARG A 106
SHEET 9 A10 LYS A 79 LEU A 86 -1 N LYS A 81 O LYS A 96
SHEET 10 A10 VAL A 68 THR A 73 -1 O VAL A 68 N VAL A 84
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 - b 23 2 Bytes