Header list of 1a57.pdb file
Complete list - v 3 2 Bytes
HEADER FATTY ACID-BINDING 20-FEB-98 1A57 TITLE THE THREE-DIMENSIONAL STRUCTURE OF A HELIX-LESS VARIANT OF INTESTINAL TITLE 2 FATTY ACID BINDING PROTEIN, NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTESTINAL FATTY ACID-BINDING PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: DELTA17SG, IFABP, I-FABP; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: HELIX-LESS, COMPLEXED WITH PALMITATE SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 CELL: SMALL INTESTINAL ENTEROCYTE; SOURCE 6 CELLULAR_LOCATION: CYTOPLASM; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI STR. K-12 SUBSTR. MG1655; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511145; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: MG1655; SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMON5840-IFABP(DELTA17SG); SOURCE 12 OTHER_DETAILS: SEE REMARK 1, REFERENCE 3 KEYWDS FATTY ACID-BINDING, LIPID TRANSPORT, BETA-CLAM, LIPOCALINS EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR R.A.STEELE,D.A.EMMERT,J.KAO,M.E.HODSDON,C.FRIEDEN,D.P.CISTOLA REVDAT 3 03-NOV-21 1A57 1 REMARK SEQADV REVDAT 2 24-FEB-09 1A57 1 VERSN REVDAT 1 27-MAY-98 1A57 0 JRNL AUTH R.A.STEELE,D.A.EMMERT,J.KAO,M.E.HODSDON,C.FRIEDEN, JRNL AUTH 2 D.P.CISTOLA JRNL TITL THE THREE-DIMENSIONAL STRUCTURE OF A HELIX-LESS VARIANT OF JRNL TITL 2 INTESTINAL FATTY ACID-BINDING PROTEIN. JRNL REF PROTEIN SCI. V. 7 1332 1998 JRNL REFN ISSN 0961-8368 JRNL PMID 9655337 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.E.HODSDON,D.P.CISTOLA REMARK 1 TITL DISCRETE BACKBONE DISORDER IN THE NUCLEAR MAGNETIC RESONANCE REMARK 1 TITL 2 STRUCTURE OF APO INTESTINAL FATTY ACID-BINDING PROTEIN: REMARK 1 TITL 3 IMPLICATIONS FOR THE MECHANISM OF LIGAND ENTRY REMARK 1 REF BIOCHEMISTRY V. 36 1450 1997 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH D.P.CISTOLA,K.KIM,H.ROGL,C.FRIEDEN REMARK 1 TITL FATTY ACID INTERACTIONS WITH A HELIX-LESS VARIANT OF REMARK 1 TITL 2 INTESTINAL FATTY ACID-BINDING PROTEIN REMARK 1 REF BIOCHEMISTRY V. 35 7559 1996 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 3 REMARK 1 AUTH K.KIM,D.P.CISTOLA,C.FRIEDEN REMARK 1 TITL INTESTINAL FATTY ACID-BINDING PROTEIN: THE STRUCTURE AND REMARK 1 TITL 2 STABILITY OF A HELIX-LESS VARIANT REMARK 1 REF BIOCHEMISTRY V. 35 7553 1996 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 4 REMARK 1 AUTH M.E.HODSDON,J.W.PONDER,D.P.CISTOLA REMARK 1 TITL THE NMR SOLUTION STRUCTURE OF INTESTINAL FATTY ACID-BINDING REMARK 1 TITL 2 PROTEIN COMPLEXED WITH PALMITATE: APPLICATION OF A NOVEL REMARK 1 TITL 3 DISTANCE GEOMETRY ALGORITHM REMARK 1 REF J.MOL.BIOL. V. 264 585 1996 REMARK 1 REFN ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : TINKER REMARK 3 AUTHORS : PONDER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 DISTANCE GEOMETRY WAS PERFORMED USING 5% PAIRWISE METRIZATION AND REMARK 3 A GAUSSIAN TRIAL DISTRIBUTION FOR THE SELECTION OF DISTANCES USING REMARK 3 THE PROGRAM DISTGEOM, A COMPONENT OF THE TINKER MOLECULAR MODELING REMARK 3 PACKAGE. EMBEDDED STRUCTURES WERE REFINED VERSUS A PENALTY REMARK 3 FUNCTION BASED SOLELY ON THE EXPERIMENTAL RESTRAINTS AND LOCAL REMARK 3 COVALENT GEOMETRY (BOND LENGTHS, ANGLES, CHIRALITY); NO ENERGY- REMARK 3 BASED TERMS WERE INCLUDED. DETAILS OF THE CALCULATIONS AND REMARK 3 STRUCTURAL STATISTICS ARE GIVEN IN THE PAPER CITED ON THE JRNL REMARK 3 RECORDS ABOVE. REMARK 3 REMARK 3 THE LOOP FROM RESIDUES 8 - 20 IS ENTIRELY UNRESTRAINED. REMARK 3 THIS REGION CONTAINS THE SITE OF THE DELETED HELICES OF REMARK 3 I-FABP. CARE SHOULD BE TAKEN WHEN ANALYZING STATISTICS ON REMARK 3 THIS MOLECULE AS THIS UNRESTRAINED LOOP WILL ABNORMALLY REMARK 3 SKEW ANY RESULTS. REMARK 4 REMARK 4 1A57 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_1000170406. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 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 : 3-D 13C-RESOLVED NOESY; 3-D 15N REMARK 210 -RESOLVED NOESY; 2-D 1H- REMARK 210 HOMONUCLEAR NOESY; 2-D 13C- REMARK 210 EDITED NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : TINKER REMARK 210 METHOD USED : DISTANCE GEOMETRY WITH SIMULATED REMARK 210 ANNEALING REFINEMENT REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 23 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : FINAL PENALTY FUNCTION VALUES REMARK 210 GREATER THAN 10.0 OR GREATER REMARK 210 THAN TWO STANDARD DEVIATIONS REMARK 210 FROM THE MEAN WERE OMITTED 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 1 PHE A 2 CZ PHE A 2 CE2 -0.143 REMARK 500 1 TYR A 14 CZ TYR A 14 CE2 -0.170 REMARK 500 1 HIS A 18 CE1 HIS A 18 NE2 0.176 REMARK 500 1 PHE A 32 CZ PHE A 32 CE2 -0.162 REMARK 500 1 PHE A 40 CZ PHE A 40 CE2 -0.170 REMARK 500 1 PHE A 47 CZ PHE A 47 CE2 -0.152 REMARK 500 1 PHE A 53 CE1 PHE A 53 CZ -0.149 REMARK 500 1 TYR A 55 CE1 TYR A 55 CZ -0.184 REMARK 500 1 PHE A 78 CE1 PHE A 78 CZ -0.154 REMARK 500 1 TYR A 102 CE1 TYR A 102 CZ -0.181 REMARK 500 1 TYR A 104 CE1 TYR A 104 CZ -0.188 REMARK 500 1 PHE A 113 CZ PHE A 113 CE2 -0.167 REMARK 500 2 PHE A 2 CE1 PHE A 2 CZ -0.159 REMARK 500 2 TYR A 14 CZ TYR A 14 CE2 -0.169 REMARK 500 2 HIS A 18 CE1 HIS A 18 NE2 0.185 REMARK 500 2 PHE A 32 CZ PHE A 32 CE2 -0.169 REMARK 500 2 PHE A 40 CZ PHE A 40 CE2 -0.171 REMARK 500 2 PHE A 47 CE1 PHE A 47 CZ -0.155 REMARK 500 2 PHE A 53 CE1 PHE A 53 CZ -0.168 REMARK 500 2 TYR A 55 CE1 TYR A 55 CZ -0.177 REMARK 500 2 PHE A 78 CE1 PHE A 78 CZ -0.167 REMARK 500 2 TYR A 102 CZ TYR A 102 CE2 -0.170 REMARK 500 2 TYR A 104 CE1 TYR A 104 CZ -0.191 REMARK 500 2 PHE A 113 CE1 PHE A 113 CZ -0.176 REMARK 500 3 PHE A 2 CZ PHE A 2 CE2 -0.147 REMARK 500 3 TYR A 14 CZ TYR A 14 CE2 -0.146 REMARK 500 3 HIS A 18 CE1 HIS A 18 NE2 0.177 REMARK 500 3 PHE A 32 CZ PHE A 32 CE2 -0.165 REMARK 500 3 PHE A 40 CZ PHE A 40 CE2 -0.150 REMARK 500 3 PHE A 47 CE1 PHE A 47 CZ -0.147 REMARK 500 3 PHE A 53 CE1 PHE A 53 CZ -0.149 REMARK 500 3 TYR A 55 CE1 TYR A 55 CZ -0.161 REMARK 500 3 PHE A 78 CZ PHE A 78 CE2 -0.172 REMARK 500 3 TYR A 102 CZ TYR A 102 CE2 -0.180 REMARK 500 3 TYR A 104 CZ TYR A 104 CE2 -0.186 REMARK 500 3 PHE A 113 CZ PHE A 113 CE2 -0.176 REMARK 500 4 PHE A 2 CZ PHE A 2 CE2 -0.140 REMARK 500 4 TYR A 14 CZ TYR A 14 CE2 -0.152 REMARK 500 4 HIS A 18 CE1 HIS A 18 NE2 0.193 REMARK 500 4 PHE A 32 CZ PHE A 32 CE2 -0.154 REMARK 500 4 PHE A 40 CZ PHE A 40 CE2 -0.169 REMARK 500 4 PHE A 47 CE1 PHE A 47 CZ -0.155 REMARK 500 4 PHE A 53 CE1 PHE A 53 CZ -0.151 REMARK 500 4 TYR A 55 CE1 TYR A 55 CZ -0.175 REMARK 500 4 PHE A 78 CZ PHE A 78 CE2 -0.174 REMARK 500 4 TYR A 102 CZ TYR A 102 CE2 -0.162 REMARK 500 4 TYR A 104 CE1 TYR A 104 CZ -0.187 REMARK 500 4 PHE A 113 CE1 PHE A 113 CZ -0.172 REMARK 500 5 PHE A 2 CZ PHE A 2 CE2 -0.155 REMARK 500 5 TYR A 14 CE1 TYR A 14 CZ -0.158 REMARK 500 REMARK 500 THIS ENTRY HAS 240 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 PHE A 2 CB - CG - CD1 ANGL. DEV. = 5.1 DEGREES REMARK 500 1 TRP A 6 CD1 - NE1 - CE2 ANGL. DEV. = 6.7 DEGREES REMARK 500 1 TRP A 6 O - C - N ANGL. DEV. = 10.6 DEGREES REMARK 500 1 LYS A 7 O - C - N ANGL. DEV. = 13.1 DEGREES REMARK 500 1 ASP A 9 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES REMARK 500 1 TYR A 14 CB - CG - CD2 ANGL. DEV. = 4.4 DEGREES REMARK 500 1 TYR A 14 CZ - CE2 - CD2 ANGL. DEV. = 6.3 DEGREES REMARK 500 1 LEU A 21 O - C - N ANGL. DEV. = 10.4 DEGREES REMARK 500 1 LYS A 22 O - C - N ANGL. DEV. = 10.4 DEGREES REMARK 500 1 LEU A 23 O - C - N ANGL. DEV. = 9.6 DEGREES REMARK 500 1 THR A 26 O - C - N ANGL. DEV. = 10.2 DEGREES REMARK 500 1 GLY A 29 O - C - N ANGL. DEV. = 10.3 DEGREES REMARK 500 1 PHE A 32 CB - CG - CD1 ANGL. DEV. = 4.8 DEGREES REMARK 500 1 PHE A 32 O - C - N ANGL. DEV. = 14.3 DEGREES REMARK 500 1 LYS A 35 CA - C - O ANGL. DEV. = 13.7 DEGREES REMARK 500 1 PHE A 40 O - C - N ANGL. DEV. = 9.7 DEGREES REMARK 500 1 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES REMARK 500 1 VAL A 45 CG1 - CB - CG2 ANGL. DEV. = -10.7 DEGREES REMARK 500 1 PHE A 47 CB - CG - CD2 ANGL. DEV. = 5.5 DEGREES REMARK 500 1 PHE A 47 CB - CG - CD1 ANGL. DEV. = -6.0 DEGREES REMARK 500 1 VAL A 51 CG1 - CB - CG2 ANGL. DEV. = -10.1 DEGREES REMARK 500 1 PHE A 53 CB - CG - CD2 ANGL. DEV. = 4.7 DEGREES REMARK 500 1 TYR A 55 CB - CG - CD1 ANGL. DEV. = 5.6 DEGREES REMARK 500 1 TRP A 67 CD1 - NE1 - CE2 ANGL. DEV. = 7.9 DEGREES REMARK 500 1 TRP A 67 O - C - N ANGL. DEV. = 13.0 DEGREES REMARK 500 1 VAL A 75 CG1 - CB - CG2 ANGL. DEV. = -11.2 DEGREES REMARK 500 1 PHE A 78 CB - CG - CD1 ANGL. DEV. = 8.1 DEGREES REMARK 500 1 LYS A 79 N - CA - CB ANGL. DEV. = -11.8 DEGREES REMARK 500 1 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES REMARK 500 1 ARG A 80 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES REMARK 500 1 GLY A 84 O - C - N ANGL. DEV. = 10.7 DEGREES REMARK 500 1 GLU A 86 O - C - N ANGL. DEV. = 16.9 DEGREES REMARK 500 1 GLY A 95 O - C - N ANGL. DEV. = 9.8 DEGREES REMARK 500 1 GLU A 97 O - C - N ANGL. DEV. = 9.8 DEGREES REMARK 500 1 ILE A 99 O - C - N ANGL. DEV. = 10.5 DEGREES REMARK 500 1 GLN A 100 O - C - N ANGL. DEV. = 9.9 DEGREES REMARK 500 1 TYR A 102 CB - CG - CD2 ANGL. DEV. = 5.2 DEGREES REMARK 500 1 TYR A 102 CB - CG - CD1 ANGL. DEV. = -5.4 DEGREES REMARK 500 1 ALA A 109 CB - CA - C ANGL. DEV. = -10.1 DEGREES REMARK 500 1 ALA A 109 O - C - N ANGL. DEV. = 12.6 DEGREES REMARK 500 2 TRP A 6 CD1 - CG - CD2 ANGL. DEV. = -5.1 DEGREES REMARK 500 2 TRP A 6 CD1 - NE1 - CE2 ANGL. DEV. = 6.0 DEGREES REMARK 500 2 LYS A 7 O - C - N ANGL. DEV. = 11.4 DEGREES REMARK 500 2 VAL A 8 CA - C - O ANGL. DEV. = 15.5 DEGREES REMARK 500 2 TYR A 14 CB - CG - CD2 ANGL. DEV. = 6.1 DEGREES REMARK 500 2 TYR A 14 CZ - CE2 - CD2 ANGL. DEV. = 5.6 DEGREES REMARK 500 2 LYS A 22 O - C - N ANGL. DEV. = 11.8 DEGREES REMARK 500 2 THR A 26 O - C - N ANGL. DEV. = 9.9 DEGREES REMARK 500 2 PHE A 32 CB - CG - CD1 ANGL. DEV. = 5.7 DEGREES REMARK 500 2 PHE A 32 O - C - N ANGL. DEV. = 13.2 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 753 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 LYS A 7 -179.43 61.49 REMARK 500 1 VAL A 8 133.82 29.56 REMARK 500 1 ASP A 9 81.49 -174.56 REMARK 500 1 ASN A 11 -160.68 52.97 REMARK 500 1 ASN A 13 137.23 75.73 REMARK 500 1 TYR A 14 -155.85 -101.89 REMARK 500 1 SER A 15 -158.88 -86.54 REMARK 500 1 ALA A 17 85.50 71.89 REMARK 500 1 ASP A 19 61.42 17.43 REMARK 500 1 LYS A 22 142.19 150.76 REMARK 500 1 THR A 24 110.26 175.95 REMARK 500 1 THR A 26 81.15 -159.20 REMARK 500 1 GLN A 27 151.41 -49.27 REMARK 500 1 GLU A 28 56.09 -151.28 REMARK 500 1 ASN A 30 55.13 34.13 REMARK 500 1 LYS A 31 88.82 -153.46 REMARK 500 1 SER A 38 -142.02 -138.03 REMARK 500 1 ASN A 39 38.53 -96.48 REMARK 500 1 PHE A 40 54.63 -152.42 REMARK 500 1 ARG A 41 -161.78 68.26 REMARK 500 1 ILE A 43 134.89 67.14 REMARK 500 1 PHE A 47 -172.55 170.50 REMARK 500 1 LEU A 49 -115.78 48.73 REMARK 500 1 PHE A 53 159.98 172.33 REMARK 500 1 LEU A 57 -41.85 -141.12 REMARK 500 1 ASP A 59 28.38 42.64 REMARK 500 1 GLU A 62 37.50 -161.77 REMARK 500 1 LEU A 63 99.60 -54.18 REMARK 500 1 GLU A 70 59.71 -119.50 REMARK 500 1 LEU A 74 37.94 -157.97 REMARK 500 1 LYS A 77 122.97 -174.59 REMARK 500 1 ARG A 80 63.02 -113.33 REMARK 500 1 VAL A 81 -44.33 -17.34 REMARK 500 1 ASN A 83 -30.41 168.23 REMARK 500 1 LYS A 85 17.25 50.25 REMARK 500 1 GLU A 86 116.22 161.06 REMARK 500 1 LEU A 87 58.95 -152.76 REMARK 500 1 ILE A 88 -177.49 -67.25 REMARK 500 1 ALA A 89 63.10 -150.21 REMARK 500 1 ILE A 93 96.56 -55.55 REMARK 500 1 GLU A 97 170.73 174.68 REMARK 500 1 ILE A 99 -89.02 -110.01 REMARK 500 1 GLN A 100 90.23 111.10 REMARK 500 1 GLU A 105 30.87 36.06 REMARK 500 1 PHE A 113 -156.19 -137.88 REMARK 500 1 LYS A 114 -138.90 -169.82 REMARK 500 2 ASP A 3 29.29 -169.83 REMARK 500 2 LYS A 7 179.06 51.50 REMARK 500 2 VAL A 8 146.37 22.75 REMARK 500 2 ASP A 9 -126.04 -104.70 REMARK 500 REMARK 500 THIS ENTRY HAS 790 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1A57 A 1 116 UNP P02693 FABPI_RAT 1 131 SEQADV 1A57 A UNP P02693 GLU 15 DELETION SEQADV 1A57 A UNP P02693 LYS 16 DELETION SEQADV 1A57 A UNP P02693 PHE 17 DELETION SEQADV 1A57 A UNP P02693 MET 18 DELETION SEQADV 1A57 A UNP P02693 GLU 19 DELETION SEQADV 1A57 A UNP P02693 LYS 20 DELETION SEQADV 1A57 A UNP P02693 MET 21 DELETION SEQADV 1A57 A UNP P02693 GLY 22 DELETION SEQADV 1A57 A UNP P02693 ILE 23 DELETION SEQADV 1A57 A UNP P02693 ASN 24 DELETION SEQADV 1A57 A UNP P02693 VAL 25 DELETION SEQADV 1A57 A UNP P02693 VAL 26 DELETION SEQADV 1A57 A UNP P02693 LYS 27 DELETION SEQADV 1A57 A UNP P02693 ARG 28 DELETION SEQADV 1A57 A UNP P02693 LYS 29 DELETION SEQADV 1A57 SER A 15 UNP P02693 LEU 30 ENGINEERED MUTATION SEQRES 1 A 116 ALA PHE ASP GLY THR TRP LYS VAL ASP ARG ASN GLU ASN SEQRES 2 A 116 TYR SER GLY ALA HIS ASP ASN LEU LYS LEU THR ILE THR SEQRES 3 A 116 GLN GLU GLY ASN LYS PHE THR VAL LYS GLU SER SER ASN SEQRES 4 A 116 PHE ARG ASN ILE ASP VAL VAL PHE GLU LEU GLY VAL ASP SEQRES 5 A 116 PHE ALA TYR SER LEU ALA ASP GLY THR GLU LEU THR GLY SEQRES 6 A 116 THR TRP THR MET GLU GLY ASN LYS LEU VAL GLY LYS PHE SEQRES 7 A 116 LYS ARG VAL ASP ASN GLY LYS GLU LEU ILE ALA VAL ARG SEQRES 8 A 116 GLU ILE SER GLY ASN GLU LEU ILE GLN THR TYR THR TYR SEQRES 9 A 116 GLU GLY VAL GLU ALA LYS ARG ILE PHE LYS LYS GLU SHEET 1 A 5 GLY A 4 LYS A 7 0 SHEET 2 A 5 LYS A 22 GLU A 28 -1 N LEU A 23 O TRP A 6 SHEET 3 A 5 LYS A 31 SER A 38 -1 N LYS A 35 O THR A 24 SHEET 4 A 5 ARG A 41 GLU A 48 -1 N VAL A 45 O VAL A 34 SHEET 5 A 5 ASP A 52 SER A 56 -1 SHEET 1 B 5 LEU A 63 GLU A 70 0 SHEET 2 B 5 LYS A 73 ARG A 80 -1 N VAL A 75 O THR A 68 SHEET 3 B 5 GLU A 86 SER A 94 -1 N ALA A 89 O GLY A 76 SHEET 4 B 5 GLU A 97 TYR A 104 -1 N THR A 101 O VAL A 90 SHEET 5 B 5 VAL A 107 LYS A 114 -1 N ARG A 111 O GLN A 100 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 - v 3 2 Bytes