Header list of 1kzw.pdb file
Complete list - b 23 2 Bytes
HEADER LIPID BINDING PROTEIN 08-FEB-02 1KZW TITLE SOLUTION STRUCTURE OF HUMAN INTESTINAL FATTY ACID BINDING PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTESTINAL FATTY ACID-BINDING PROTEIN (A54); COMPND 3 CHAIN: A; COMPND 4 SYNONYM: I-FABP, FABPI; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: FABP2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-3D KEYWDS NMR SPECTROSCOPY, 15N ISOTOPE LABELLING, FATTY ACID BINDING, TYPE 2 KEYWDS 2 DIABETES, SINGLE BASE POLYMORPHISM, HOLO-FORM, LIPID BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR F.ZHANG,C.LUECKE,L.J.BAIER,J.C.SACCHETTINI,J.A.HAMILTON REVDAT 4 23-FEB-22 1KZW 1 REMARK REVDAT 3 24-FEB-09 1KZW 1 VERSN REVDAT 2 08-JUL-03 1KZW 1 TITLE REVDAT 1 01-JUL-03 1KZW 0 JRNL AUTH F.ZHANG,C.LUECKE,L.J.BAIER,J.C.SACCHETTINI,J.A.HAMILTON JRNL TITL SOLUTION STRUCTURE OF HUMAN INTESTINAL FATTY ACID BINDING JRNL TITL 2 PROTEIN WITH A NATURALLY-OCCURRING SINGLE AMINO ACID JRNL TITL 3 SUBSTITUTION (A54T) THAT IS ASSOCIATED WITH ALTERED LIPID JRNL TITL 4 METABOLISM JRNL REF BIOCHEMISTRY V. 42 7339 2003 JRNL REFN ISSN 0006-2960 JRNL PMID 12809489 JRNL DOI 10.1021/BI0273617 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH F.ZHANG,C.LUECKE,L.J.BAIER,J.C.SACCHETTINI,J.A.HAMILTON REMARK 1 TITL SOLUTION STRUCTURE OF HUMAN INTESTINAL FATTY ACID BINDING REMARK 1 TITL 2 PROTEIN: IMPLICATIONS FOR LIGAND ENTRY AND EXIT REMARK 1 REF J.BIOMOL.NMR V. 9 213 1997 REMARK 1 REFN ISSN 0925-2738 REMARK 1 DOI 10.1023/A:1018666522787 REMARK 1 REFERENCE 2 REMARK 1 AUTH L.J.BAIER,C.BOGARDUS,J.C.SACCHETTINI REMARK 1 TITL A POLYMORPHISM IN THE HUMAN INTESTINAL FATTY ACID BINDING REMARK 1 TITL 2 PROTEIN ALTERS FATTY ACID TRANSPORT ACROSS CACO-2 CELLS REMARK 1 REF J.BIOL.CHEM. V. 271 10892 1996 REMARK 1 REFN ISSN 0021-9258 REMARK 1 DOI 10.1074/JBC.271.20.11689 REMARK 1 REFERENCE 3 REMARK 1 AUTH L.J.BAIER,J.C.SACCHETTINI,W.C.KNOWLER,J.EADS,G.PAOLISSO, REMARK 1 AUTH 2 P.A.TATARANNI,H.MOCHIZUKI,H.P.BENNET,C.BOGARDUS,M.PROCHAZKA REMARK 1 TITL AN AMINO ACID SUBSTITUTION IN THE HUMAN INTESTINAL FATTY REMARK 1 TITL 2 ACID BINDING PROTEIN IS ASSOCIATED WITH INCREASED FATTY ACID REMARK 1 TITL 3 BINDING, INCREASED FAT OXIDATION, AND INSULIN RESISTANCE REMARK 1 REF J.CLIN.INVEST. V. 95 1281 1995 REMARK 1 REFN ISSN 0021-9738 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 STRUCTURES ARE BASED ON A TOTAL REMARK 3 NUMBER OF 2538 DISTANCE RESTRAINTS REMARK 4 REMARK 4 1KZW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-02. REMARK 100 THE DEPOSITION ID IS D_1000015518. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 20MM PHOSPHATE BUFFER REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 3-4MM I-FABP, 20MM PHOSPHATE REMARK 210 BUFFER, 0.05% SODIUM AZIDE; 3- REMARK 210 4MM I-FABP U-15N, 20MM PHOSPHATE REMARK 210 BUFFER, 0.05% SODIUM AZIDE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-1H_TOCSY, 1H-1H_NOESY; 1H REMARK 210 -15N_HSQC, 1H-15N_HTQC, 3D_1H- REMARK 210 15N_TOCSY-HMQC, 3D_1H-15N_NOESY- REMARK 210 HMQC REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMR2ST 2.05, DYANA 1.5 REMARK 210 METHOD USED : SIMULATED ANNEALING COMBINED REMARK 210 WITH TORSION ANGLE DYNAMICS AND REMARK 210 FOLLOWED BY ENERGY MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 300 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 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: 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 HG SER A 52 OD1 ASN A 57 1.51 REMARK 500 O ASP A 3 HG SER A 4 1.57 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 12 CD GLU A 12 OE1 0.117 REMARK 500 1 GLU A 19 CD GLU A 19 OE1 0.118 REMARK 500 1 GLU A 43 CD GLU A 43 OE2 0.114 REMARK 500 1 GLU A 51 CD GLU A 51 OE2 0.113 REMARK 500 1 GLU A 59 CD GLU A 59 OE1 0.110 REMARK 500 1 GLU A 63 CD GLU A 63 OE1 0.110 REMARK 500 1 GLU A 77 CD GLU A 77 OE2 0.110 REMARK 500 1 GLU A 85 CD GLU A 85 OE2 0.114 REMARK 500 1 GLU A 101 CD GLU A 101 OE1 0.111 REMARK 500 1 GLU A 107 CD GLU A 107 OE2 0.113 REMARK 500 1 GLU A 112 CD GLU A 112 OE1 0.110 REMARK 500 1 GLU A 120 CD GLU A 120 OE2 0.114 REMARK 500 1 GLU A 123 CD GLU A 123 OE1 0.111 REMARK 500 2 GLU A 12 CD GLU A 12 OE2 0.113 REMARK 500 2 GLU A 19 CD GLU A 19 OE1 0.115 REMARK 500 2 GLU A 43 CD GLU A 43 OE1 0.111 REMARK 500 2 GLU A 51 CD GLU A 51 OE1 0.111 REMARK 500 2 GLU A 59 CD GLU A 59 OE2 0.111 REMARK 500 2 GLU A 63 CD GLU A 63 OE1 0.110 REMARK 500 2 GLU A 77 CD GLU A 77 OE2 0.108 REMARK 500 2 GLU A 85 CD GLU A 85 OE1 0.114 REMARK 500 2 GLU A 101 CD GLU A 101 OE1 0.115 REMARK 500 2 GLU A 107 CD GLU A 107 OE1 0.113 REMARK 500 2 GLU A 112 CD GLU A 112 OE1 0.109 REMARK 500 2 GLU A 120 CD GLU A 120 OE2 0.115 REMARK 500 2 GLU A 123 CD GLU A 123 OE1 0.110 REMARK 500 3 GLU A 12 CD GLU A 12 OE2 0.115 REMARK 500 3 GLU A 19 CD GLU A 19 OE1 0.113 REMARK 500 3 GLU A 43 CD GLU A 43 OE1 0.111 REMARK 500 3 GLU A 51 CD GLU A 51 OE1 0.112 REMARK 500 3 GLU A 59 CD GLU A 59 OE1 0.114 REMARK 500 3 GLU A 63 CD GLU A 63 OE1 0.110 REMARK 500 3 GLU A 77 CD GLU A 77 OE1 0.113 REMARK 500 3 GLU A 85 CD GLU A 85 OE1 0.117 REMARK 500 3 GLU A 101 CD GLU A 101 OE1 0.115 REMARK 500 3 GLU A 107 CD GLU A 107 OE1 0.110 REMARK 500 3 GLU A 112 CD GLU A 112 OE2 0.111 REMARK 500 3 GLU A 120 CD GLU A 120 OE2 0.110 REMARK 500 3 GLU A 123 CD GLU A 123 OE1 0.111 REMARK 500 4 GLU A 12 CD GLU A 12 OE1 0.113 REMARK 500 4 GLU A 19 CD GLU A 19 OE2 0.110 REMARK 500 4 GLU A 43 CD GLU A 43 OE2 0.109 REMARK 500 4 GLU A 51 CD GLU A 51 OE2 0.113 REMARK 500 4 GLU A 59 CD GLU A 59 OE1 0.109 REMARK 500 4 GLU A 63 CD GLU A 63 OE2 0.115 REMARK 500 4 GLU A 77 CD GLU A 77 OE1 0.113 REMARK 500 4 GLU A 85 CD GLU A 85 OE1 0.113 REMARK 500 4 GLU A 101 CD GLU A 101 OE2 0.108 REMARK 500 4 GLU A 107 CD GLU A 107 OE1 0.114 REMARK 500 4 GLU A 112 CD GLU A 112 OE2 0.117 REMARK 500 REMARK 500 THIS ENTRY HAS 261 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 3 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES REMARK 500 1 ASP A 9 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES REMARK 500 1 ASP A 9 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES REMARK 500 1 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 1 ASP A 15 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 1 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 1 HIS A 33 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES REMARK 500 1 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 1 ASP A 74 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES REMARK 500 1 ASP A 74 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES REMARK 500 1 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 1 TRP A 82 CD1 - NE1 - CE2 ANGL. DEV. = -5.6 DEGREES REMARK 500 1 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES REMARK 500 1 ARG A 95 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 1 ASP A 97 CB - CG - OD1 ANGL. DEV. = -5.9 DEGREES REMARK 500 1 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 1 ARG A 106 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 1 ASP A 111 CB - CG - OD1 ANGL. DEV. = -6.1 DEGREES REMARK 500 1 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 1 ASP A 131 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES REMARK 500 1 ASP A 131 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 2 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 2 ASP A 15 CB - CG - OD1 ANGL. DEV. = -6.3 DEGREES REMARK 500 2 ASP A 15 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 2 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 2 HIS A 33 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES REMARK 500 2 ASP A 34 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES REMARK 500 2 ASP A 74 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES REMARK 500 2 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 2 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 2 TRP A 82 CD1 - NE1 - CE2 ANGL. DEV. = -5.4 DEGREES REMARK 500 2 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 2 ASP A 97 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES REMARK 500 2 ASP A 97 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 2 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 2 ARG A 106 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 2 ASP A 111 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES REMARK 500 2 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 2 ASP A 131 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 3 ASP A 3 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES REMARK 500 3 ASP A 3 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES REMARK 500 3 ASP A 9 CB - CG - OD1 ANGL. DEV. = -6.2 DEGREES REMARK 500 3 ARG A 10 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 3 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 3 HIS A 33 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES REMARK 500 3 ASP A 34 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES REMARK 500 3 ASP A 34 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES REMARK 500 3 ARG A 56 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 3 ASP A 74 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 3 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 395 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 PHE A 2 -54.97 73.82 REMARK 500 1 ASN A 45 -55.96 66.73 REMARK 500 1 LEU A 72 -132.04 -81.72 REMARK 500 1 ASP A 74 -76.38 -99.26 REMARK 500 1 ASN A 87 -55.55 72.91 REMARK 500 1 ASN A 98 -46.11 -130.23 REMARK 500 1 GLU A 120 -79.33 66.12 REMARK 500 2 PHE A 2 -52.63 72.46 REMARK 500 2 ASN A 13 59.70 -141.92 REMARK 500 2 ASP A 15 -55.79 -154.78 REMARK 500 2 HIS A 33 56.26 -90.24 REMARK 500 2 ASN A 35 64.11 71.02 REMARK 500 2 PHE A 55 -57.29 -175.92 REMARK 500 2 ALA A 73 46.90 -71.35 REMARK 500 2 ASP A 74 -80.56 -138.90 REMARK 500 2 GLU A 85 -79.05 -107.45 REMARK 500 2 THR A 96 -73.59 -70.97 REMARK 500 2 GLU A 120 68.53 66.19 REMARK 500 3 PHE A 2 -49.80 74.99 REMARK 500 3 GLU A 12 -81.46 -82.40 REMARK 500 3 ASN A 13 55.97 -108.32 REMARK 500 3 ASP A 15 -66.35 -158.05 REMARK 500 3 HIS A 33 52.96 -90.49 REMARK 500 3 ALA A 73 -64.31 58.07 REMARK 500 3 ASP A 74 -83.71 -82.98 REMARK 500 3 ASN A 98 -41.44 -133.92 REMARK 500 4 HIS A 33 53.53 -91.62 REMARK 500 4 ASN A 45 -15.04 66.82 REMARK 500 4 PHE A 55 -60.89 -168.78 REMARK 500 4 ALA A 73 -70.99 -154.36 REMARK 500 4 ASP A 97 -62.28 -177.70 REMARK 500 4 GLU A 120 -78.68 65.03 REMARK 500 5 PHE A 2 65.03 64.91 REMARK 500 5 GLU A 12 -95.79 -83.36 REMARK 500 5 ASN A 35 84.68 -68.80 REMARK 500 5 GLU A 43 77.18 -118.02 REMARK 500 5 ALA A 73 -51.44 63.57 REMARK 500 5 ASP A 74 -81.52 -74.22 REMARK 500 5 ASP A 97 42.68 -98.37 REMARK 500 5 ASN A 98 -50.99 -156.62 REMARK 500 5 ILE A 109 -76.54 -98.15 REMARK 500 5 ASP A 111 47.11 -92.91 REMARK 500 5 GLU A 120 -41.42 62.01 REMARK 500 6 PHE A 2 -21.58 67.31 REMARK 500 6 GLU A 12 -73.02 -79.22 REMARK 500 6 ASP A 15 -57.43 -146.05 REMARK 500 6 HIS A 33 32.98 -98.69 REMARK 500 6 ASN A 35 63.47 65.50 REMARK 500 6 ASN A 45 -23.49 69.89 REMARK 500 6 PHE A 55 -53.84 -145.27 REMARK 500 REMARK 500 THIS ENTRY HAS 154 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 THR A 81 TRP A 82 6 146.88 REMARK 500 THR A 96 ASP A 97 11 -148.98 REMARK 500 ARG A 126 ILE A 127 14 -146.71 REMARK 500 THR A 81 TRP A 82 19 143.66 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 95 0.09 SIDE CHAIN REMARK 500 2 TYR A 117 0.07 SIDE CHAIN REMARK 500 4 TYR A 14 0.08 SIDE CHAIN REMARK 500 4 TYR A 117 0.07 SIDE CHAIN REMARK 500 6 TYR A 117 0.07 SIDE CHAIN REMARK 500 10 PHE A 68 0.09 SIDE CHAIN REMARK 500 10 TYR A 119 0.09 SIDE CHAIN REMARK 500 11 TYR A 119 0.08 SIDE CHAIN REMARK 500 12 TYR A 117 0.09 SIDE CHAIN REMARK 500 13 ARG A 95 0.09 SIDE CHAIN REMARK 500 13 TYR A 119 0.07 SIDE CHAIN REMARK 500 14 PHE A 17 0.07 SIDE CHAIN REMARK 500 14 ARG A 95 0.08 SIDE CHAIN REMARK 500 14 TYR A 119 0.09 SIDE CHAIN REMARK 500 15 ARG A 28 0.10 SIDE CHAIN REMARK 500 15 TYR A 117 0.07 SIDE CHAIN REMARK 500 19 TYR A 117 0.07 SIDE CHAIN REMARK 500 20 TYR A 119 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1KZX RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE THR54 MUTANT OF HUMAN INTESTINAL FATTY REMARK 900 ACID BINDING PROTEIN (I-FABP) REMARK 900 RELATED ID: 3IFB RELATED DB: PDB REMARK 900 NMR STUDY OF HUMAN INTESTINAL FATTY ACID BINDING PROTEIN DBREF 1KZW A 1 131 UNP P12104 FABPI_HUMAN 1 131 SEQRES 1 A 131 ALA PHE ASP SER THR TRP LYS VAL ASP ARG SER GLU ASN SEQRES 2 A 131 TYR ASP LYS PHE MET GLU LYS MET GLY VAL ASN ILE VAL SEQRES 3 A 131 LYS ARG LYS LEU ALA ALA HIS ASP ASN LEU LYS LEU THR SEQRES 4 A 131 ILE THR GLN GLU GLY ASN LYS PHE THR VAL LYS GLU SER SEQRES 5 A 131 SER ALA PHE ARG ASN ILE GLU VAL VAL PHE GLU LEU GLY SEQRES 6 A 131 VAL THR PHE ASN TYR ASN LEU ALA ASP GLY THR GLU LEU SEQRES 7 A 131 ARG GLY THR TRP SER LEU GLU GLY ASN LYS LEU ILE GLY SEQRES 8 A 131 LYS PHE LYS ARG THR ASP ASN GLY ASN GLU LEU ASN THR SEQRES 9 A 131 VAL ARG GLU ILE ILE GLY ASP GLU LEU VAL GLN THR TYR SEQRES 10 A 131 VAL TYR GLU GLY VAL GLU ALA LYS ARG ILE PHE LYS LYS SEQRES 11 A 131 ASP HELIX 1 1 TYR A 14 GLY A 22 1 9 HELIX 2 2 ILE A 25 HIS A 33 1 9 SHEET 1 A10 ASN A 57 PHE A 62 0 SHEET 2 A10 PHE A 47 SER A 52 -1 N PHE A 47 O PHE A 62 SHEET 3 A10 LEU A 36 GLN A 42 -1 N LYS A 37 O SER A 52 SHEET 4 A10 PHE A 2 GLU A 12 -1 O TRP A 6 N LEU A 38 SHEET 5 A10 GLU A 123 LYS A 130 -1 N LYS A 125 O GLU A 12 SHEET 6 A10 LEU A 113 VAL A 118 -1 N LEU A 113 O PHE A 128 SHEET 7 A10 ASN A 100 ILE A 108 -1 N ASN A 103 O VAL A 118 SHEET 8 A10 LEU A 89 ARG A 95 -1 O LEU A 89 N ARG A 106 SHEET 9 A10 THR A 76 LEU A 84 -1 N ARG A 79 O LYS A 94 SHEET 10 A10 THR A 67 LEU A 72 -1 N PHE A 68 O GLY A 80 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