Header list of 1la3.pdb file
Complete list - t 27 2 Bytes
HEADER METAL BINDING PROTEIN 27-MAR-02 1LA3
TITLE SOLUTION STRUCTURE OF RECOVERIN MUTANT, E85Q
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECOVERIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 TISSUE: RETINA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTREC2
KEYWDS EF-HAND, CALCIUM, VISION, E85Q, METAL-BINDING PROTEIN, METAL BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR J.B.AMES,N.HAMASAKI,T.MOLCHANOVA
REVDAT 5 27-OCT-21 1LA3 1 KEYWDS REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1LA3 1 VERSN
REVDAT 3 01-APR-03 1LA3 1 JRNL
REVDAT 2 31-JUL-02 1LA3 1 ATOM
REVDAT 1 19-JUN-02 1LA3 0
JRNL AUTH J.B.AMES,N.HAMASAKI,T.MOLCHANOVA
JRNL TITL STRUCTURE AND CALCIUM-BINDING STUDIES OF A RECOVERIN MUTANT
JRNL TITL 2 (E85Q) IN AN ALLOSTERIC INTERMEDIATE STATE.
JRNL REF BIOCHEMISTRY V. 41 5776 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11980481
JRNL DOI 10.1021/BI012153K
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2050 NOE-DERIVED DISTANCE CONSTRAINTS, 230 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS, AND 150 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1LA3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015785.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 50 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM RECOVERIN-E85Q U-15N,13C;
REMARK 210 10 MM IMIDAZOLE, 50MM KCL, 1 MM
REMARK 210 CACL2, 10 MM DITHIOTHREITOL, 1MM
REMARK 210 MGCL2, PH 6.7; 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 14 STRUCTURES WITH
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING STANDARD TRIPLE
REMARK 210 -RESONANCE NMR SPECTROSCOPY
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-14
REMARK 465 RES C SSSEQI
REMARK 465 PRO A 190
REMARK 465 GLN A 191
REMARK 465 LYS A 192
REMARK 465 VAL A 193
REMARK 465 LYS A 194
REMARK 465 GLU A 195
REMARK 465 LYS A 196
REMARK 465 LEU A 197
REMARK 465 LYS A 198
REMARK 465 GLU A 199
REMARK 465 LYS A 200
REMARK 465 LYS A 201
REMARK 465 LEU A 202
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 OD2 ASP A 110 H ASN A 114 1.41
REMARK 500 O ASP A 164 H LYS A 166 1.43
REMARK 500 O ASP A 61 H LYS A 63 1.50
REMARK 500 O PRO A 40 H GLY A 42 1.52
REMARK 500 O HIS A 91 H THR A 93 1.53
REMARK 500 O THR A 127 H LYS A 131 1.53
REMARK 500 O ILE A 88 H MET A 92 1.55
REMARK 500 O LEU A 28 H TYR A 32 1.56
REMARK 500 O ARG A 151 H LYS A 154 1.58
REMARK 500 OD2 ASP A 112 CA CA A 501 1.62
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 TRP A 31 CG TRP A 31 CD2 -0.120
REMARK 500 1 HIS A 68 CG HIS A 68 ND1 -0.119
REMARK 500 1 HIS A 91 CG HIS A 91 ND1 -0.121
REMARK 500 1 TRP A 104 CG TRP A 104 CD2 -0.123
REMARK 500 1 HIS A 140 CG HIS A 140 ND1 -0.120
REMARK 500 1 TRP A 156 CG TRP A 156 CD2 -0.126
REMARK 500 2 TRP A 31 CG TRP A 31 CD2 -0.118
REMARK 500 2 HIS A 68 CG HIS A 68 ND1 -0.122
REMARK 500 2 HIS A 91 CG HIS A 91 ND1 -0.121
REMARK 500 2 TRP A 104 CG TRP A 104 CD2 -0.124
REMARK 500 2 HIS A 140 CG HIS A 140 ND1 -0.119
REMARK 500 2 TRP A 156 CG TRP A 156 CD2 -0.122
REMARK 500 3 TRP A 31 CG TRP A 31 CD2 -0.119
REMARK 500 3 HIS A 68 CG HIS A 68 ND1 -0.122
REMARK 500 3 HIS A 91 CG HIS A 91 ND1 -0.120
REMARK 500 3 TRP A 104 CG TRP A 104 CD2 -0.122
REMARK 500 3 HIS A 140 CG HIS A 140 ND1 -0.119
REMARK 500 3 TRP A 156 CG TRP A 156 CD2 -0.120
REMARK 500 4 TRP A 31 CG TRP A 31 CD2 -0.118
REMARK 500 4 HIS A 68 CG HIS A 68 ND1 -0.121
REMARK 500 4 HIS A 91 CG HIS A 91 ND1 -0.122
REMARK 500 4 TRP A 104 CG TRP A 104 CD2 -0.124
REMARK 500 4 HIS A 140 CG HIS A 140 ND1 -0.119
REMARK 500 4 TRP A 156 CG TRP A 156 CD2 -0.120
REMARK 500 5 TRP A 31 CG TRP A 31 CD2 -0.112
REMARK 500 5 HIS A 68 CG HIS A 68 ND1 -0.120
REMARK 500 5 HIS A 91 CG HIS A 91 ND1 -0.120
REMARK 500 5 TRP A 104 CG TRP A 104 CD2 -0.123
REMARK 500 5 HIS A 140 CG HIS A 140 ND1 -0.121
REMARK 500 5 TRP A 156 CG TRP A 156 CD2 -0.125
REMARK 500 6 TRP A 31 CG TRP A 31 CD2 -0.119
REMARK 500 6 HIS A 68 CG HIS A 68 ND1 -0.121
REMARK 500 6 HIS A 91 CG HIS A 91 ND1 -0.119
REMARK 500 6 TRP A 104 CG TRP A 104 CD2 -0.123
REMARK 500 6 HIS A 140 CG HIS A 140 ND1 -0.120
REMARK 500 6 TRP A 156 CG TRP A 156 CD2 -0.127
REMARK 500 7 TRP A 31 CG TRP A 31 CD2 -0.117
REMARK 500 7 HIS A 68 CG HIS A 68 ND1 -0.121
REMARK 500 7 HIS A 91 CG HIS A 91 ND1 -0.120
REMARK 500 7 TRP A 104 CG TRP A 104 CD2 -0.123
REMARK 500 7 HIS A 140 CG HIS A 140 ND1 -0.119
REMARK 500 7 TRP A 156 CG TRP A 156 CD2 -0.120
REMARK 500 8 TRP A 31 CG TRP A 31 CD2 -0.123
REMARK 500 8 HIS A 68 CG HIS A 68 ND1 -0.121
REMARK 500 8 HIS A 91 CG HIS A 91 ND1 -0.120
REMARK 500 8 TRP A 104 CG TRP A 104 CD2 -0.125
REMARK 500 8 HIS A 140 CG HIS A 140 ND1 -0.121
REMARK 500 8 TRP A 156 CG TRP A 156 CD2 -0.121
REMARK 500 9 TRP A 31 CG TRP A 31 CD2 -0.122
REMARK 500 9 HIS A 68 CG HIS A 68 ND1 -0.122
REMARK 500
REMARK 500 THIS ENTRY HAS 84 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 TRP A 31 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 9.2 DEGREES
REMARK 500 1 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 1 TRP A 104 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 TRP A 104 NE1 - CE2 - CZ2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 1 TRP A 104 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 1 TRP A 156 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 1 TRP A 156 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 TRP A 156 NE1 - CE2 - CZ2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 1 TRP A 156 NE1 - CE2 - CD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 1 TRP A 156 CG - CD2 - CE3 ANGL. DEV. = -5.6 DEGREES
REMARK 500 2 TRP A 31 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 2 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 2 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 2 TRP A 104 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 TRP A 104 NE1 - CE2 - CZ2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 2 TRP A 104 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 2 TRP A 156 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 2 TRP A 156 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 2 TRP A 156 NE1 - CE2 - CZ2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 2 TRP A 156 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 3 TRP A 31 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 3 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 3 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 3 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 3 TRP A 104 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 3 TRP A 104 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 3 TRP A 104 NE1 - CE2 - CZ2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 3 TRP A 104 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 3 TRP A 156 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 3 TRP A 156 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 3 TRP A 156 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 3 TRP A 156 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 4 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 4 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 4 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 4 TRP A 104 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 4 TRP A 104 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 4 TRP A 104 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 4 TRP A 104 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 4 TRP A 156 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 4 TRP A 156 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 4 TRP A 156 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 4 TRP A 156 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 5 TRP A 31 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 5 TRP A 31 CG - CD1 - NE1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 5 TRP A 31 NE1 - CE2 - CZ2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 5 TRP A 31 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 162 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 LEU A 17 17.35 -65.01
REMARK 500 1 LYS A 22 -14.98 -46.37
REMARK 500 1 PRO A 40 97.42 -59.45
REMARK 500 1 SER A 41 -57.81 66.77
REMARK 500 1 PRO A 58 -82.25 -64.62
REMARK 500 1 GLU A 59 89.49 -59.44
REMARK 500 1 ALA A 60 5.47 -175.29
REMARK 500 1 ASP A 61 94.55 50.09
REMARK 500 1 PRO A 62 31.00 -64.02
REMARK 500 1 LYS A 63 23.72 -143.96
REMARK 500 1 ALA A 64 -111.00 -111.79
REMARK 500 1 TYR A 65 -90.70 -66.10
REMARK 500 1 ASP A 74 -87.02 163.55
REMARK 500 1 ASN A 76 -100.87 -60.80
REMARK 500 1 ASP A 78 -86.24 73.89
REMARK 500 1 MET A 92 42.38 -67.91
REMARK 500 1 SER A 94 -2.59 -157.07
REMARK 500 1 ALA A 95 -128.52 -80.94
REMARK 500 1 ASN A 99 -70.33 -74.61
REMARK 500 1 LYS A 101 -14.04 -171.51
REMARK 500 1 LEU A 102 -70.11 -79.60
REMARK 500 1 ASP A 110 70.27 -103.85
REMARK 500 1 ASN A 114 27.39 -152.35
REMARK 500 1 ALA A 128 -70.29 -45.22
REMARK 500 1 GLU A 136 -19.03 -43.67
REMARK 500 1 LEU A 141 151.22 -46.53
REMARK 500 1 GLU A 143 -153.69 -75.77
REMARK 500 1 ASP A 144 22.39 40.45
REMARK 500 1 GLU A 145 31.68 -175.80
REMARK 500 1 LYS A 162 -36.60 -134.92
REMARK 500 1 ASP A 163 -79.13 -78.76
REMARK 500 1 ASP A 165 43.58 -60.15
REMARK 500 1 ALA A 178 -83.27 -92.74
REMARK 500 1 ILE A 186 -16.81 -45.33
REMARK 500 1 GLN A 187 101.40 -45.09
REMARK 500 2 LEU A 17 15.96 -67.31
REMARK 500 2 ASP A 61 116.13 -39.99
REMARK 500 2 PRO A 62 12.46 -60.79
REMARK 500 2 ALA A 64 -127.65 -127.96
REMARK 500 2 TYR A 65 -92.64 -43.34
REMARK 500 2 PHE A 73 13.23 -59.86
REMARK 500 2 ASP A 74 -10.09 73.68
REMARK 500 2 ASN A 76 -123.29 16.28
REMARK 500 2 SER A 77 -86.80 -92.97
REMARK 500 2 ASP A 78 156.47 -44.43
REMARK 500 2 HIS A 91 -66.29 -91.55
REMARK 500 2 THR A 93 33.28 -65.85
REMARK 500 2 ALA A 95 -175.48 -171.42
REMARK 500 2 LYS A 97 -138.83 44.99
REMARK 500 2 THR A 98 -98.22 40.76
REMARK 500
REMARK 500 THIS ENTRY HAS 460 RAMACHANDRAN OUTLIERS.
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 46 0.32 SIDE CHAIN
REMARK 500 1 ARG A 71 0.12 SIDE CHAIN
REMARK 500 1 ARG A 151 0.31 SIDE CHAIN
REMARK 500 1 ARG A 184 0.23 SIDE CHAIN
REMARK 500 2 ARG A 43 0.22 SIDE CHAIN
REMARK 500 2 ARG A 46 0.13 SIDE CHAIN
REMARK 500 2 ARG A 71 0.32 SIDE CHAIN
REMARK 500 2 ARG A 151 0.24 SIDE CHAIN
REMARK 500 2 ARG A 184 0.30 SIDE CHAIN
REMARK 500 3 ARG A 43 0.17 SIDE CHAIN
REMARK 500 3 ARG A 46 0.17 SIDE CHAIN
REMARK 500 3 ARG A 71 0.31 SIDE CHAIN
REMARK 500 3 ARG A 151 0.21 SIDE CHAIN
REMARK 500 3 ARG A 184 0.31 SIDE CHAIN
REMARK 500 4 ARG A 46 0.30 SIDE CHAIN
REMARK 500 4 ARG A 71 0.31 SIDE CHAIN
REMARK 500 4 ARG A 151 0.18 SIDE CHAIN
REMARK 500 4 ARG A 184 0.32 SIDE CHAIN
REMARK 500 5 ARG A 43 0.15 SIDE CHAIN
REMARK 500 5 ARG A 46 0.14 SIDE CHAIN
REMARK 500 5 ARG A 71 0.29 SIDE CHAIN
REMARK 500 5 ARG A 151 0.30 SIDE CHAIN
REMARK 500 6 ARG A 43 0.28 SIDE CHAIN
REMARK 500 6 ARG A 46 0.23 SIDE CHAIN
REMARK 500 6 ARG A 71 0.14 SIDE CHAIN
REMARK 500 6 ARG A 151 0.22 SIDE CHAIN
REMARK 500 6 ARG A 184 0.32 SIDE CHAIN
REMARK 500 7 ARG A 43 0.12 SIDE CHAIN
REMARK 500 7 ARG A 46 0.32 SIDE CHAIN
REMARK 500 7 ARG A 71 0.19 SIDE CHAIN
REMARK 500 7 ARG A 151 0.27 SIDE CHAIN
REMARK 500 8 ARG A 43 0.24 SIDE CHAIN
REMARK 500 8 ARG A 46 0.31 SIDE CHAIN
REMARK 500 8 ARG A 71 0.19 SIDE CHAIN
REMARK 500 8 ARG A 151 0.19 SIDE CHAIN
REMARK 500 8 ARG A 184 0.16 SIDE CHAIN
REMARK 500 9 ARG A 43 0.32 SIDE CHAIN
REMARK 500 9 ARG A 46 0.30 SIDE CHAIN
REMARK 500 10 ARG A 43 0.29 SIDE CHAIN
REMARK 500 10 ARG A 46 0.31 SIDE CHAIN
REMARK 500 10 ARG A 71 0.18 SIDE CHAIN
REMARK 500 10 ARG A 151 0.28 SIDE CHAIN
REMARK 500 10 ARG A 184 0.13 SIDE CHAIN
REMARK 500 11 ARG A 43 0.19 SIDE CHAIN
REMARK 500 11 ARG A 46 0.23 SIDE CHAIN
REMARK 500 11 ARG A 71 0.29 SIDE CHAIN
REMARK 500 11 ARG A 151 0.26 SIDE CHAIN
REMARK 500 11 ARG A 184 0.20 SIDE CHAIN
REMARK 500 12 ARG A 43 0.32 SIDE CHAIN
REMARK 500 12 ARG A 71 0.30 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 62 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 110 OD1
REMARK 620 2 ASP A 112 OD1 60.8
REMARK 620 3 ASN A 114 OD1 79.5 58.3
REMARK 620 4 THR A 116 O 96.3 130.1 75.0
REMARK 620 5 GLU A 121 OE1 69.3 125.2 132.9 74.4
REMARK 620 6 GLU A 121 OE2 118.0 143.1 156.1 86.5 52.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5332 RELATED DB: BMRB
REMARK 900 RECOVERIN MUTANT, E85Q
REMARK 900 RELATED ID: 1JSA RELATED DB: PDB
REMARK 900 1JSA CONTAINS CALCIUM-BOUND WILDTYPE RECOVERIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 METHIONINE 1 IS REMOVED FROM THE PROTEIN DURING MYRISTOYLATION
DBREF 1LA3 A 2 202 UNP P21457 RECO_BOVIN 1 201
SEQADV 1LA3 GLN A 85 UNP P21457 GLU 84 ENGINEERED MUTATION
SEQRES 1 A 201 GLY ASN SER LYS SER GLY ALA LEU SER LYS GLU ILE LEU
SEQRES 2 A 201 GLU GLU LEU GLN LEU ASN THR LYS PHE THR GLU GLU GLU
SEQRES 3 A 201 LEU SER SER TRP TYR GLN SER PHE LEU LYS GLU CYS PRO
SEQRES 4 A 201 SER GLY ARG ILE THR ARG GLN GLU PHE GLN THR ILE TYR
SEQRES 5 A 201 SER LYS PHE PHE PRO GLU ALA ASP PRO LYS ALA TYR ALA
SEQRES 6 A 201 GLN HIS VAL PHE ARG SER PHE ASP ALA ASN SER ASP GLY
SEQRES 7 A 201 THR LEU ASP PHE LYS GLN TYR VAL ILE ALA LEU HIS MET
SEQRES 8 A 201 THR SER ALA GLY LYS THR ASN GLN LYS LEU GLU TRP ALA
SEQRES 9 A 201 PHE SER LEU TYR ASP VAL ASP GLY ASN GLY THR ILE SER
SEQRES 10 A 201 LYS ASN GLU VAL LEU GLU ILE VAL THR ALA ILE PHE LYS
SEQRES 11 A 201 MET ILE SER PRO GLU ASP THR LYS HIS LEU PRO GLU ASP
SEQRES 12 A 201 GLU ASN THR PRO GLU LYS ARG ALA GLU LYS ILE TRP GLY
SEQRES 13 A 201 PHE PHE GLY LYS LYS ASP ASP ASP LYS LEU THR GLU LYS
SEQRES 14 A 201 GLU PHE ILE GLU GLY THR LEU ALA ASN LYS GLU ILE LEU
SEQRES 15 A 201 ARG LEU ILE GLN PHE GLU PRO GLN LYS VAL LYS GLU LYS
SEQRES 16 A 201 LEU LYS GLU LYS LYS LEU
HET CA A 501 1
HET MYR A 1 42
HETNAM CA CALCIUM ION
HETNAM MYR MYRISTIC ACID
FORMUL 2 CA CA 2+
FORMUL 3 MYR C14 H28 O2
HELIX 1 1 ASN A 3 LEU A 17 1 15
HELIX 2 2 THR A 24 CYS A 39 1 16
HELIX 3 3 THR A 45 PHE A 57 1 13
HELIX 4 4 ALA A 64 ASP A 74 1 11
HELIX 5 5 PHE A 83 MET A 92 1 10
HELIX 6 6 LYS A 101 ASP A 110 1 10
HELIX 7 7 SER A 118 ILE A 133 1 16
HELIX 8 8 SER A 134 LYS A 139 1 6
HELIX 9 9 THR A 147 GLY A 160 1 14
HELIX 10 10 LYS A 170 ALA A 178 1 9
HELIX 11 11 GLU A 181 ILE A 186 1 6
SHEET 1 A 2 ARG A 43 ILE A 44 0
SHEET 2 A 2 LEU A 81 ASP A 82 -1 O LEU A 81 N ILE A 44
LINK C1 MYR A 1 N GLY A 2 1555 1555 1.30
LINK OD1 ASP A 110 CA CA A 501 1555 1555 2.52
LINK OD1 ASP A 112 CA CA A 501 1555 1555 2.49
LINK OD1 ASN A 114 CA CA A 501 1555 1555 2.49
LINK O THR A 116 CA CA A 501 1555 1555 2.48
LINK OE1 GLU A 121 CA CA A 501 1555 1555 2.51
LINK OE2 GLU A 121 CA CA A 501 1555 1555 2.48
SITE 1 AC1 5 ASP A 110 ASP A 112 ASN A 114 THR A 116
SITE 2 AC1 5 GLU A 121
SITE 1 AC2 6 GLY A 2 ASN A 3 SER A 10 TYR A 32
SITE 2 AC2 6 PHE A 57 PHE A 83
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 - t 27 2 Bytes