Header list of 1kgl.pdb file
Complete list - b 23 2 Bytes
HEADER LIPID BINDING PROTEIN 27-NOV-01 1KGL
TITLE SOLUTION STRUCTURE OF CELLULAR RETINOL BINDING PROTEIN TYPE-I IN
TITLE 2 COMPLEX WITH ALL-TRANS-RETINOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELLULAR RETINOL-BINDING PROTEIN TYPE I;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CRBP-I;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: RBP-1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11B
KEYWDS BETA BARREL, RETINOID CARRIER, HOLO FORM, NMR SPECTROSCOPY, 15N
KEYWDS 2 ISOTOPE ENRICHMENT, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.FRANZONI,C.LUECKE,C.PEREZ,D.CAVAZZINI,M.RADEMACHER,C.LUDWIG,
AUTHOR 2 A.SPISNI,G.L.ROSSI,H.RUETERJANS
REVDAT 5 23-FEB-22 1KGL 1 REMARK
REVDAT 4 24-FEB-09 1KGL 1 VERSN
REVDAT 3 01-APR-03 1KGL 1 JRNL
REVDAT 2 03-JUL-02 1KGL 1 TITLE
REVDAT 1 19-JUN-02 1KGL 0
JRNL AUTH L.FRANZONI,C.LUCKE,C.PEREZ,D.CAVAZZINI,M.RADEMACHER,
JRNL AUTH 2 C.LUDWIG,A.SPISNI,G.L.ROSSI,H.RUTERJANS
JRNL TITL STRUCTURE AND BACKBONE DYNAMICS OF APO- AND HOLO-CELLULAR
JRNL TITL 2 RETINOL-BINDING PROTEIN IN SOLUTION.
JRNL REF J.BIOL.CHEM. V. 277 21983 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11934897
JRNL DOI 10.1074/JBC.M201994200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.W.COWAN,M.E.NEWCOMER,T.A.JONES
REMARK 1 TITL CRYSTALLOGRAPHIC STUDIES ON A FAMILY OF CELLULAR LIPOPHILIC
REMARK 1 TITL 2 TRANSPORT PROTEINS
REMARK 1 REF J.MOL.BIOL. V. 230 1225 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1993.1238
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 2826 NOE-DERIVED DISTANCE RESTRAINTS
REMARK 4
REMARK 4 1KGL COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014934.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298.00
REMARK 210 PH : 6.00
REMARK 210 IONIC STRENGTH : 20MM POTASSIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.8MM CRBP-I PHOSPHATE BUFFER;
REMARK 210 0.05% SODIUM AZIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D_TOCSY; 2D_NOESY; 2D_ 15N
REMARK 210 -HSQC; 2D_15N-HTQC; 3D_15N-TOCSY-
REMARK 210 HSQC; 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 FELIX 97, NMR2ST 2.05, 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 : 100
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 HD2 ASP A 73 OD1 ASP A 79 1.58
REMARK 500 HH TYR A 60 OE1 GLU A 72 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 14 CD GLU A 14 OE2 0.114
REMARK 500 1 GLU A 17 CD GLU A 17 OE2 0.112
REMARK 500 1 GLU A 18 CD GLU A 18 OE2 0.118
REMARK 500 1 GLU A 41 CD GLU A 41 OE2 0.113
REMARK 500 1 HIS A 48 CG HIS A 48 CD2 0.056
REMARK 500 1 GLU A 69 CD GLU A 69 OE2 0.110
REMARK 500 1 GLU A 71 CD GLU A 71 OE2 0.113
REMARK 500 1 GLU A 72 CD GLU A 72 OE2 0.106
REMARK 500 1 GLU A 100 CD GLU A 100 OE2 0.113
REMARK 500 1 GLU A 102 CD GLU A 102 OE2 0.109
REMARK 500 1 GLU A 111 CD GLU A 111 OE2 0.115
REMARK 500 1 GLU A 114 CD GLU A 114 OE2 0.113
REMARK 500 1 GLU A 118 CD GLU A 118 OE2 0.110
REMARK 500 1 GLU A 122 CD GLU A 122 OE2 0.109
REMARK 500 2 GLU A 14 CD GLU A 14 OE2 0.111
REMARK 500 2 GLU A 17 CD GLU A 17 OE2 0.112
REMARK 500 2 GLU A 18 CD GLU A 18 OE2 0.113
REMARK 500 2 GLU A 41 CD GLU A 41 OE2 0.110
REMARK 500 2 HIS A 48 CG HIS A 48 CD2 0.055
REMARK 500 2 GLU A 69 CD GLU A 69 OE2 0.112
REMARK 500 2 GLU A 71 CD GLU A 71 OE2 0.109
REMARK 500 2 GLU A 72 CD GLU A 72 OE2 0.115
REMARK 500 2 GLU A 100 CD GLU A 100 OE2 0.110
REMARK 500 2 GLU A 102 CD GLU A 102 OE2 0.110
REMARK 500 2 GLU A 111 CD GLU A 111 OE2 0.109
REMARK 500 2 GLU A 114 CD GLU A 114 OE2 0.114
REMARK 500 2 GLU A 118 CD GLU A 118 OE2 0.111
REMARK 500 2 GLU A 122 CD GLU A 122 OE2 0.113
REMARK 500 3 GLU A 14 CD GLU A 14 OE2 0.111
REMARK 500 3 GLU A 17 CD GLU A 17 OE2 0.111
REMARK 500 3 GLU A 18 CD GLU A 18 OE2 0.114
REMARK 500 3 GLU A 41 CD GLU A 41 OE2 0.110
REMARK 500 3 HIS A 48 CG HIS A 48 CD2 0.060
REMARK 500 3 GLU A 69 CD GLU A 69 OE2 0.110
REMARK 500 3 GLU A 71 CD GLU A 71 OE2 0.114
REMARK 500 3 GLU A 72 CD GLU A 72 OE2 0.107
REMARK 500 3 GLU A 100 CD GLU A 100 OE2 0.113
REMARK 500 3 GLU A 102 CD GLU A 102 OE2 0.111
REMARK 500 3 GLU A 111 CD GLU A 111 OE2 0.114
REMARK 500 3 GLU A 114 CD GLU A 114 OE2 0.110
REMARK 500 3 GLU A 118 CD GLU A 118 OE2 0.114
REMARK 500 3 GLU A 122 CD GLU A 122 OE2 0.110
REMARK 500 4 GLU A 14 CD GLU A 14 OE2 0.114
REMARK 500 4 GLU A 17 CD GLU A 17 OE2 0.110
REMARK 500 4 GLU A 18 CD GLU A 18 OE2 0.118
REMARK 500 4 GLU A 41 CD GLU A 41 OE2 0.110
REMARK 500 4 HIS A 48 CG HIS A 48 CD2 0.055
REMARK 500 4 GLU A 69 CD GLU A 69 OE2 0.115
REMARK 500 4 GLU A 71 CD GLU A 71 OE2 0.110
REMARK 500 4 GLU A 72 CD GLU A 72 OE2 0.109
REMARK 500
REMARK 500 THIS ENTRY HAS 279 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 - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 1 ASP A 3 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 ASP A 24 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 1 ASP A 24 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 1 ASP A 45 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 1 ASP A 45 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 ASP A 47 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 1 HIS A 48 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 1 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 1 ASP A 63 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 1 ASP A 63 CB - CG - OD2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 1 ASP A 73 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 1 ASP A 79 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 1 ASP A 79 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 1 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 ASP A 89 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 ASP A 91 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 1 ARG A 104 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ASP A 113 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 1 ASP A 113 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 1 HIS A 116 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 1 ARG A 120 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 1 HIS A 134 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 ASP A 3 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ASP A 24 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 2 ASP A 24 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 ASP A 39 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 ASP A 45 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 2 ASP A 45 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 2 ASP A 47 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 2 ASP A 47 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 2 HIS A 48 ND1 - CE1 - NE2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 2 ARG A 52 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 2 ASP A 63 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 ASP A 73 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 2 ASP A 73 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 ASP A 78 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 2 ASP A 78 CB - CG - OD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 2 ASP A 79 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 2 ASP A 79 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 2 ARG A 80 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ASP A 89 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 2 ASP A 89 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 2 ASP A 91 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 580 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 5 104.94 -58.25
REMARK 500 1 ASP A 89 62.88 -105.06
REMARK 500 2 PRO A 1 -78.27 -69.48
REMARK 500 2 ASP A 3 86.44 70.31
REMARK 500 2 GLU A 14 -71.38 -96.05
REMARK 500 2 ASP A 78 -1.02 -141.30
REMARK 500 2 ASP A 79 65.26 63.93
REMARK 500 3 ASN A 5 108.57 -57.83
REMARK 500 4 ASP A 24 5.33 174.94
REMARK 500 4 ASP A 45 75.97 -105.48
REMARK 500 4 ILE A 77 -82.01 -116.21
REMARK 500 4 ASP A 89 66.25 -107.69
REMARK 500 5 GLU A 14 -64.80 -93.07
REMARK 500 5 LEU A 74 49.59 -84.93
REMARK 500 5 ASP A 89 61.16 -111.59
REMARK 500 6 ILE A 77 -70.02 -72.11
REMARK 500 6 ASP A 113 41.27 -102.43
REMARK 500 7 PRO A 1 -121.02 -76.18
REMARK 500 7 ASP A 3 83.06 65.44
REMARK 500 7 LEU A 74 49.38 -99.15
REMARK 500 7 ASP A 78 25.35 -149.84
REMARK 500 7 ASP A 89 75.68 -101.06
REMARK 500 8 ASN A 5 106.29 -58.87
REMARK 500 8 GLU A 71 96.49 -69.98
REMARK 500 8 ILE A 77 -88.79 -92.30
REMARK 500 8 ASP A 89 72.03 -103.71
REMARK 500 9 LEU A 74 55.29 -101.30
REMARK 500 9 ILE A 77 -72.34 -78.34
REMARK 500 9 GLU A 100 -46.08 70.11
REMARK 500 10 ASN A 5 108.86 -54.84
REMARK 500 10 ASP A 24 48.71 71.93
REMARK 500 10 LEU A 74 44.18 -105.15
REMARK 500 10 ASP A 78 17.56 -146.76
REMARK 500 10 ASP A 89 73.39 -111.79
REMARK 500 11 ASP A 3 86.28 67.99
REMARK 500 11 ASP A 24 -7.49 177.22
REMARK 500 11 ASP A 45 74.97 -100.19
REMARK 500 11 LEU A 74 52.49 -98.04
REMARK 500 12 ASN A 5 105.68 -57.82
REMARK 500 12 ILE A 77 -75.26 -100.75
REMARK 500 13 ASP A 24 62.78 69.60
REMARK 500 13 ASP A 45 -60.80 -93.70
REMARK 500 13 ASP A 47 -45.16 60.46
REMARK 500 13 ILE A 77 -73.27 -87.13
REMARK 500 14 ILE A 77 -74.33 -93.66
REMARK 500 14 ASP A 89 67.35 -112.18
REMARK 500 15 ASN A 5 108.61 -58.01
REMARK 500 15 ILE A 77 -74.19 -78.66
REMARK 500 16 LEU A 74 45.49 -96.73
REMARK 500 16 ILE A 77 -75.66 -78.03
REMARK 500
REMARK 500 THIS ENTRY HAS 64 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 ASP A 24 VAL A 25 4 -146.96
REMARK 500 ASP A 24 VAL A 25 11 -136.52
REMARK 500 THR A 75 GLY A 76 14 -148.41
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 104 0.08 SIDE CHAIN
REMARK 500 3 PHE A 16 0.08 SIDE CHAIN
REMARK 500 3 TYR A 60 0.07 SIDE CHAIN
REMARK 500 4 ARG A 80 0.10 SIDE CHAIN
REMARK 500 7 TYR A 60 0.07 SIDE CHAIN
REMARK 500 9 ARG A 104 0.07 SIDE CHAIN
REMARK 500 10 TYR A 60 0.08 SIDE CHAIN
REMARK 500 11 TYR A 60 0.07 SIDE CHAIN
REMARK 500 16 TYR A 60 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RTL A 175
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JBH RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CELLULAR RETINOL BINDING PROTEIN TYPE-I IN
REMARK 900 THE LIGAND-FREE STATE
REMARK 900 RELATED ID: 1CRB RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF THE CELLULAR RETINOL BINDING PROTEIN TYPE-I IN
REMARK 900 COMPLEX WITH ALL-TRANS-RETINOL
DBREF 1KGL A 0 134 UNP P02696 RET1_RAT 0 134
SEQRES 1 A 135 MET PRO VAL ASP PHE ASN GLY TYR TRP LYS MET LEU SER
SEQRES 2 A 135 ASN GLU ASN PHE GLU GLU TYR LEU ARG ALA LEU ASP VAL
SEQRES 3 A 135 ASN VAL ALA LEU ARG LYS ILE ALA ASN LEU LEU LYS PRO
SEQRES 4 A 135 ASP LYS GLU ILE VAL GLN ASP GLY ASP HIS MET ILE ILE
SEQRES 5 A 135 ARG THR LEU SER THR PHE ARG ASN TYR ILE MET ASP PHE
SEQRES 6 A 135 GLN VAL GLY LYS GLU PHE GLU GLU ASP LEU THR GLY ILE
SEQRES 7 A 135 ASP ASP ARG LYS CYS MET THR THR VAL SER TRP ASP GLY
SEQRES 8 A 135 ASP LYS LEU GLN CYS VAL GLN LYS GLY GLU LYS GLU GLY
SEQRES 9 A 135 ARG GLY TRP THR GLN TRP ILE GLU GLY ASP GLU LEU HIS
SEQRES 10 A 135 LEU GLU MET ARG ALA GLU GLY VAL THR CYS LYS GLN VAL
SEQRES 11 A 135 PHE LYS LYS VAL HIS
HET RTL A 175 51
HETNAM RTL RETINOL
FORMUL 2 RTL C20 H30 O
HELIX 1 1 PHE A 16 LEU A 23 1 8
HELIX 2 2 VAL A 27 LEU A 35 1 9
SHEET 1 A10 ASN A 59 GLN A 65 0
SHEET 2 A10 HIS A 48 LEU A 54 -1 N MET A 49 O PHE A 64
SHEET 3 A10 ASP A 39 ASP A 45 -1 O ASP A 39 N LEU A 54
SHEET 4 A10 GLY A 6 GLU A 14 -1 O GLY A 6 N ILE A 42
SHEET 5 A10 VAL A 124 LYS A 132 -1 O VAL A 129 N LEU A 11
SHEET 6 A10 GLU A 114 ALA A 121 -1 O LEU A 115 N PHE A 130
SHEET 7 A10 ARG A 104 GLU A 111 -1 N GLY A 105 O ARG A 120
SHEET 8 A10 LYS A 92 LYS A 98 -1 N LEU A 93 O GLN A 108
SHEET 9 A10 ARG A 80 ASP A 89 -1 N MET A 83 O LYS A 98
SHEET 10 A10 LYS A 68 ASP A 73 -1 O PHE A 70 N THR A 84
SITE 1 AC1 12 PHE A 16 LYS A 40 ILE A 51 THR A 53
SITE 2 AC1 12 ARG A 58 TYR A 60 MET A 62 GLY A 76
SITE 3 AC1 12 ILE A 77 TRP A 106 GLN A 108 MET A 119
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