Header list of 1jjx.pdb file
Complete list - b 23 2 Bytes
HEADER LIPID BINDING PROTEIN 10-JUL-01 1JJX TITLE SOLUTION STRUCTURE OF RECOMBINANT HUMAN BRAIN-TYPE FATTY ACID BINDING TITLE 2 PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: BRAIN-TYPE FATTY ACID BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: B-FABP; 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D KEYWDS BETA BARREL, LIPID BINDING PROTEIN, FATTY ACID CARRIER, 15N ISOTOPE KEYWDS 2 ENRICHMENT, NMR SPECTROSCOPY EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.RADEMACHER,A.W.ZIMMERMAN,H.RUETERJANS,J.H.VEERKAMP,C.LUECKE REVDAT 3 23-FEB-22 1JJX 1 REMARK REVDAT 2 24-FEB-09 1JJX 1 VERSN REVDAT 1 30-OCT-02 1JJX 0 JRNL AUTH M.RADEMACHER,A.W.ZIMMERMAN,H.RUTERJANS,J.H.VEERKAMP,C.LUCKE JRNL TITL SOLUTION STRUCTURE OF FATTY ACID-BINDING PROTEIN FROM HUMAN JRNL TITL 2 BRAIN. JRNL REF MOL.CELL.BIOCHEM. V. 239 61 2002 JRNL REFN ISSN 0300-8177 JRNL PMID 12479569 JRNL DOI 10.1023/A:1020566909213 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH G.K.BALENDIRAN,F.SCHNUETGEN,G.SCAPIN,T.BOERCHERS,N.XHONG, REMARK 1 AUTH 2 K.LIM,R.GODBOUT,F.SPENER,J.C.SACCHETTINI REMARK 1 TITL CRYSTAL STRUCTURE AND THERMODYNAMIC ANALYSIS OF HUMAN BRAIN REMARK 1 TITL 2 FATTY ACID-BINDING PROTEIN REMARK 1 REF J.BIOL.CHEM. V. 275 27045 2000 REMARK 1 REFN ISSN 0021-9258 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER 97 REMARK 3 AUTHORS : MSI REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 2490 NOE-DERIVED DISTANCE RESTRAINTS REMARK 4 REMARK 4 1JJX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-01. REMARK 100 THE DEPOSITION ID IS D_1000013860. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298.00 REMARK 210 PH : 7.00 REMARK 210 IONIC STRENGTH : 20MM POTASSIUM PHOSPHATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2-3.5MM B-FABP PHOSPHATE BUFFER; REMARK 210 0.05% SODIUM AZIDE REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_TOCSY; 2D_NOESY; 2D_15N-HSQC; REMARK 210 2D_15N-HTQC; 3D_15N-TOCSY-HSQC; REMARK 210 3D_15N-NOESY-HSQC 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 : XWINNMR 1.3, AURELIA 2.5.9, REMARK 210 DYANA 1.5 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS COMBINED REMARK 210 WITH SIMULATED ANNEALING 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 HE2 GLU A 72 OE1 GLN A 95 1.56 REMARK 500 HG1 THR A 29 O ALA A 75 1.58 REMARK 500 HG1 THR A 36 OG SER A 55 1.58 REMARK 500 O LYS A 37 HG SER A 55 1.59 REMARK 500 O GLY A 24 HD2 ASP A 76 1.59 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 2 CD GLU A 2 OE2 0.115 REMARK 500 1 GLU A 18 CD GLU A 18 OE2 0.109 REMARK 500 1 GLU A 45 CD GLU A 45 OE2 0.115 REMARK 500 1 GLU A 61 CD GLU A 61 OE2 0.113 REMARK 500 1 GLU A 68 CD GLU A 68 OE2 0.114 REMARK 500 1 GLU A 69 CD GLU A 69 OE2 0.110 REMARK 500 1 GLU A 72 CD GLU A 72 OE2 0.108 REMARK 500 1 HIS A 93 CG HIS A 93 CD2 0.055 REMARK 500 1 GLU A 101 CD GLU A 101 OE2 0.110 REMARK 500 1 GLU A 107 CD GLU A 107 OE2 0.110 REMARK 500 1 GLU A 129 CD GLU A 129 OE2 0.117 REMARK 500 2 GLU A 2 CD GLU A 2 OE2 0.114 REMARK 500 2 GLU A 18 CD GLU A 18 OE2 0.111 REMARK 500 2 GLU A 45 CD GLU A 45 OE2 0.110 REMARK 500 2 GLU A 61 CD GLU A 61 OE2 0.110 REMARK 500 2 GLU A 68 CD GLU A 68 OE2 0.111 REMARK 500 2 GLU A 69 CD GLU A 69 OE2 0.110 REMARK 500 2 GLU A 72 CD GLU A 72 OE2 0.110 REMARK 500 2 GLU A 101 CD GLU A 101 OE2 0.114 REMARK 500 2 GLU A 107 CD GLU A 107 OE2 0.116 REMARK 500 2 GLU A 129 CD GLU A 129 OE2 0.108 REMARK 500 3 GLU A 2 CD GLU A 2 OE2 0.110 REMARK 500 3 GLU A 18 CD GLU A 18 OE2 0.108 REMARK 500 3 GLU A 45 CD GLU A 45 OE2 0.112 REMARK 500 3 GLU A 61 CD GLU A 61 OE2 0.110 REMARK 500 3 GLU A 68 CD GLU A 68 OE2 0.111 REMARK 500 3 GLU A 69 CD GLU A 69 OE2 0.110 REMARK 500 3 GLU A 72 CD GLU A 72 OE2 0.118 REMARK 500 3 GLU A 101 CD GLU A 101 OE2 0.114 REMARK 500 3 GLU A 107 CD GLU A 107 OE2 0.110 REMARK 500 3 GLU A 129 CD GLU A 129 OE2 0.114 REMARK 500 4 GLU A 2 CD GLU A 2 OE2 0.110 REMARK 500 4 GLU A 18 CD GLU A 18 OE2 0.111 REMARK 500 4 GLU A 45 CD GLU A 45 OE2 0.109 REMARK 500 4 GLU A 61 CD GLU A 61 OE2 0.109 REMARK 500 4 GLU A 68 CD GLU A 68 OE2 0.115 REMARK 500 4 GLU A 69 CD GLU A 69 OE2 0.109 REMARK 500 4 GLU A 72 CD GLU A 72 OE2 0.113 REMARK 500 4 HIS A 93 CG HIS A 93 CD2 0.055 REMARK 500 4 GLU A 101 CD GLU A 101 OE2 0.113 REMARK 500 4 GLU A 107 CD GLU A 107 OE2 0.117 REMARK 500 4 GLU A 129 CD GLU A 129 OE2 0.115 REMARK 500 5 GLU A 2 CD GLU A 2 OE2 0.117 REMARK 500 5 GLU A 18 CD GLU A 18 OE2 0.109 REMARK 500 5 GLU A 45 CD GLU A 45 OE2 0.109 REMARK 500 5 GLU A 61 CD GLU A 61 OE2 0.113 REMARK 500 5 GLU A 68 CD GLU A 68 OE2 0.115 REMARK 500 5 GLU A 69 CD GLU A 69 OE2 0.110 REMARK 500 5 GLU A 72 CD GLU A 72 OE2 0.110 REMARK 500 5 HIS A 93 CG HIS A 93 CD2 0.055 REMARK 500 REMARK 500 THIS ENTRY HAS 204 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 17 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES REMARK 500 1 ASP A 17 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES REMARK 500 1 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 1 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 1 ASP A 76 CB - CG - OD2 ANGL. DEV. = -5.9 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. = 3.7 DEGREES REMARK 500 1 ASP A 87 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES REMARK 500 1 ASP A 87 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES REMARK 500 1 ASP A 89 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES REMARK 500 1 HIS A 93 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES REMARK 500 1 ASP A 98 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES REMARK 500 1 PHE A 104 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES REMARK 500 1 PHE A 104 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES REMARK 500 1 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 1 ASP A 110 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 1 ASP A 110 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES REMARK 500 1 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 1 HIS A 127 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES REMARK 500 2 ASP A 17 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 2 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 2 ASP A 47 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 2 ASP A 47 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 2 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 2 ASP A 71 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES REMARK 500 2 ASP A 76 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES REMARK 500 2 ASP A 77 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES REMARK 500 2 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 2 ASP A 87 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES REMARK 500 2 ASP A 89 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES REMARK 500 2 HIS A 93 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES REMARK 500 2 ASP A 98 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 2 ASP A 98 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES REMARK 500 2 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 2 ASP A 110 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 2 ASP A 110 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES REMARK 500 2 ASP A 121 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES REMARK 500 2 ASP A 121 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 2 HIS A 127 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES REMARK 500 3 ASP A 17 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES REMARK 500 3 ASP A 17 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES REMARK 500 3 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 3 ASP A 47 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 3 ASP A 47 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES REMARK 500 3 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 3 ASP A 71 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES REMARK 500 3 ASP A 77 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 3 ASP A 77 CB - CG - OD2 ANGL. DEV. = -6.8 DEGREES REMARK 500 3 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 3 ASP A 87 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 408 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 15 70.43 54.58 REMARK 500 1 PHE A 16 61.83 -110.60 REMARK 500 1 ASP A 17 -64.92 -155.51 REMARK 500 1 ASP A 47 -53.24 -132.77 REMARK 500 1 THR A 56 24.24 -70.38 REMARK 500 1 PHE A 57 -58.14 -150.23 REMARK 500 1 ASP A 77 63.21 78.13 REMARK 500 1 LYS A 81 99.12 -65.60 REMARK 500 1 PHE A 119 75.71 -100.59 REMARK 500 2 ASP A 47 -59.87 -139.41 REMARK 500 2 SER A 55 26.90 -78.24 REMARK 500 2 THR A 56 -53.87 65.17 REMARK 500 2 ASP A 77 70.13 70.02 REMARK 500 2 ASP A 87 75.72 -101.30 REMARK 500 3 SER A 13 78.03 -101.18 REMARK 500 3 ASP A 47 -57.27 70.94 REMARK 500 3 PHE A 57 -65.80 -161.37 REMARK 500 3 LEU A 66 120.01 69.75 REMARK 500 3 ASP A 77 65.87 82.10 REMARK 500 3 LYS A 109 -77.02 -90.16 REMARK 500 3 PHE A 119 77.66 -106.54 REMARK 500 4 SER A 55 34.09 -89.26 REMARK 500 4 THR A 56 -58.45 67.78 REMARK 500 4 PHE A 57 -61.27 -91.66 REMARK 500 4 LEU A 66 112.73 67.62 REMARK 500 4 ASP A 77 -1.22 65.91 REMARK 500 5 GLU A 2 -57.95 77.07 REMARK 500 5 ASP A 17 -68.22 -165.07 REMARK 500 5 VAL A 35 47.89 -89.16 REMARK 500 5 THR A 56 -60.72 63.61 REMARK 500 5 ASP A 77 12.22 80.50 REMARK 500 5 ASP A 89 -31.74 92.08 REMARK 500 6 ALA A 28 -55.24 -165.57 REMARK 500 6 GLU A 45 79.97 -114.55 REMARK 500 6 THR A 56 -62.10 63.23 REMARK 500 6 LEU A 66 109.12 -6.07 REMARK 500 6 LYS A 109 -91.05 -93.12 REMARK 500 6 ASP A 110 70.43 -104.70 REMARK 500 7 PHE A 27 -58.33 63.35 REMARK 500 7 THR A 56 15.19 -57.36 REMARK 500 7 PHE A 57 -69.09 -146.32 REMARK 500 7 LEU A 66 105.54 64.85 REMARK 500 8 ALA A 28 -73.09 -142.30 REMARK 500 8 THR A 56 -53.22 68.87 REMARK 500 8 ALA A 75 -8.51 -59.23 REMARK 500 8 ASP A 89 -35.60 91.14 REMARK 500 8 LYS A 109 -107.89 -101.50 REMARK 500 8 PHE A 119 79.68 -116.18 REMARK 500 9 GLU A 2 -42.03 -135.01 REMARK 500 9 ASP A 47 -44.01 -131.69 REMARK 500 REMARK 500 THIS ENTRY HAS 114 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 VAL A 25 GLY A 26 1 149.52 REMARK 500 PHE A 64 GLN A 65 1 149.53 REMARK 500 THR A 56 PHE A 57 9 -149.92 REMARK 500 GLY A 26 PHE A 27 11 148.58 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 PHE A 16 0.08 SIDE CHAIN REMARK 500 2 TYR A 19 0.07 SIDE CHAIN REMARK 500 2 ARG A 126 0.09 SIDE CHAIN REMARK 500 4 TYR A 19 0.06 SIDE CHAIN REMARK 500 4 ARG A 78 0.09 SIDE CHAIN REMARK 500 5 TYR A 19 0.07 SIDE CHAIN REMARK 500 9 TYR A 19 0.07 SIDE CHAIN REMARK 500 16 ARG A 78 0.13 SIDE CHAIN REMARK 500 17 ARG A 126 0.08 SIDE CHAIN REMARK 500 18 ARG A 126 0.10 SIDE CHAIN REMARK 500 19 TYR A 19 0.09 SIDE CHAIN REMARK 500 20 ARG A 126 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1FDQ RELATED DB: PDB REMARK 900 X-RAY STRUCTURE DBREF 1JJX A 1 131 UNP O15540 FABPB_HUMAN 1 131 SEQRES 1 A 131 VAL GLU ALA PHE CYS ALA THR TRP LYS LEU THR ASN SER SEQRES 2 A 131 GLN ASN PHE ASP GLU TYR MET LYS ALA LEU GLY VAL GLY SEQRES 3 A 131 PHE ALA THR ARG GLN VAL GLY ASN VAL THR LYS PRO THR SEQRES 4 A 131 VAL ILE ILE SER GLN GLU GLY ASP LYS VAL VAL ILE ARG SEQRES 5 A 131 THR LEU SER THR PHE LYS ASN THR GLU ILE SER PHE GLN SEQRES 6 A 131 LEU GLY GLU GLU PHE ASP GLU THR THR ALA ASP ASP ARG SEQRES 7 A 131 ASN CYS LYS SER VAL VAL SER LEU ASP GLY ASP LYS LEU SEQRES 8 A 131 VAL HIS ILE GLN LYS TRP ASP GLY LYS GLU THR ASN PHE SEQRES 9 A 131 VAL ARG GLU ILE LYS ASP GLY LYS MET VAL MET THR LEU SEQRES 10 A 131 THR PHE GLY ASP VAL VAL ALA VAL ARG HIS TYR GLU LYS SEQRES 11 A 131 ALA HELIX 1 1 VAL A 1 PHE A 4 5 4 HELIX 2 2 PHE A 16 LEU A 23 1 8 HELIX 3 3 PHE A 27 VAL A 35 1 9 SHEET 1 A10 ASN A 59 PHE A 64 0 SHEET 2 A10 VAL A 49 LEU A 54 -1 N ILE A 51 O ILE A 62 SHEET 3 A10 THR A 39 GLN A 44 -1 N SER A 43 O VAL A 50 SHEET 4 A10 ALA A 6 GLN A 14 -1 N TRP A 8 O VAL A 40 SHEET 5 A10 VAL A 123 LYS A 130 -1 O VAL A 125 N GLN A 14 SHEET 6 A10 MET A 113 THR A 118 -1 N LEU A 117 O ALA A 124 SHEET 7 A10 GLU A 101 ILE A 108 -1 N GLU A 107 O VAL A 114 SHEET 8 A10 LEU A 91 LYS A 96 -1 N GLN A 95 O THR A 102 SHEET 9 A10 ARG A 78 LEU A 86 -1 N SER A 85 O VAL A 92 SHEET 10 A10 GLU A 69 THR A 74 -1 N PHE A 70 O SER A 82 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