Header list of 1jba.pdb file
Complete list - b 23 2 Bytes
HEADER LYASE 03-APR-99 1JBA
TITLE UNMYRISTOYLATED GCAP-2 WITH THREE CALCIUM IONS BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (GUANYLATE CYCLASE ACTIVATING PROTEIN 2);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GCAP-2;
COMPND 5 EC: 4.6.1.2;
COMPND 6 ENGINEERED: 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 CELL: ROD;
SOURCE 7 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 11 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3);
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET11B
KEYWDS EF-HAND, CALCIUM-BINDING PROTEIN, GUANYLYL CYCLASE REGULATION, LYASE
EXPDTA SOLUTION NMR
NUMMDL 22
AUTHOR J.B.AMES,A.M.DIZHOOR,M.IKURA,K.PALCZEWSKI,L.STRYER
REVDAT 4 23-FEB-22 1JBA 1 REMARK LINK
REVDAT 3 24-FEB-09 1JBA 1 VERSN
REVDAT 2 21-APR-00 1JBA 1 REMARK DBREF
REVDAT 1 10-DEC-99 1JBA 0
JRNL AUTH J.B.AMES,A.M.DIZHOOR,M.IKURA,K.PALCZEWSKI,L.STRYER
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF GUANYLYL CYCLASE ACTIVATING
JRNL TITL 2 PROTEIN-2, A CALCIUM-SENSITIVE MODULATOR OF PHOTORECEPTOR
JRNL TITL 3 GUANYLYL CYCLASES.
JRNL REF J.BIOL.CHEM. V. 274 19329 1999
JRNL REFN ISSN 0021-9258
JRNL PMID 10383444
JRNL DOI 10.1074/JBC.274.27.19329
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JBA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000783.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 0.1 M
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 95% WATER/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCO; HNCACB; CBCACONH; NOESY;
REMARK 210 TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 22
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
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 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 1-22
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 191
REMARK 465 SER A 192
REMARK 465 TRP A 193
REMARK 465 ILE A 194
REMARK 465 SER A 195
REMARK 465 GLN A 196
REMARK 465 GLN A 197
REMARK 465 ARG A 198
REMARK 465 ARG A 199
REMARK 465 LYS A 200
REMARK 465 SER A 201
REMARK 465 ALA A 202
REMARK 465 MET A 203
REMARK 465 PHE A 204
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 O ALA A 21 H GLN A 25 1.44
REMARK 500 O LEU A 85 H VAL A 88 1.50
REMARK 500 O LYS A 29 H GLU A 33 1.57
REMARK 500 O LEU A 167 H VAL A 171 1.58
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 7 CG TRP A 7 CD2 -0.127
REMARK 500 1 TRP A 27 CG TRP A 27 CD2 -0.132
REMARK 500 1 HIS A 43 CG HIS A 43 ND1 -0.121
REMARK 500 1 HIS A 95 CG HIS A 95 ND1 -0.121
REMARK 500 1 TRP A 99 CG TRP A 99 CD2 -0.117
REMARK 500 1 TRP A 179 CG TRP A 179 CD2 -0.113
REMARK 500 2 TRP A 7 CG TRP A 7 CD2 -0.124
REMARK 500 2 TRP A 27 CG TRP A 27 CD2 -0.125
REMARK 500 2 HIS A 43 CG HIS A 43 ND1 -0.120
REMARK 500 2 HIS A 95 CG HIS A 95 ND1 -0.119
REMARK 500 2 TRP A 99 CG TRP A 99 CD2 -0.125
REMARK 500 2 TRP A 179 CG TRP A 179 CD2 -0.116
REMARK 500 3 TRP A 7 CG TRP A 7 CD2 -0.114
REMARK 500 3 TRP A 27 CG TRP A 27 CD2 -0.126
REMARK 500 3 HIS A 43 CG HIS A 43 ND1 -0.122
REMARK 500 3 HIS A 95 CG HIS A 95 ND1 -0.124
REMARK 500 3 TRP A 99 CG TRP A 99 CD2 -0.119
REMARK 500 3 TRP A 179 CG TRP A 179 CD2 -0.118
REMARK 500 4 TRP A 7 CG TRP A 7 CD2 -0.125
REMARK 500 4 TRP A 27 CG TRP A 27 CD2 -0.128
REMARK 500 4 HIS A 43 CG HIS A 43 ND1 -0.121
REMARK 500 4 HIS A 95 CG HIS A 95 ND1 -0.124
REMARK 500 4 TRP A 99 CG TRP A 99 CD2 -0.123
REMARK 500 4 TRP A 179 CG TRP A 179 CD2 -0.121
REMARK 500 5 TRP A 7 CG TRP A 7 CD2 -0.124
REMARK 500 5 TRP A 27 CG TRP A 27 CD2 -0.125
REMARK 500 5 HIS A 43 CG HIS A 43 ND1 -0.120
REMARK 500 5 HIS A 95 CG HIS A 95 ND1 -0.121
REMARK 500 5 TRP A 99 CG TRP A 99 CD2 -0.127
REMARK 500 5 TRP A 179 CG TRP A 179 CD2 -0.116
REMARK 500 6 TRP A 7 CG TRP A 7 CD2 -0.134
REMARK 500 6 TRP A 27 CG TRP A 27 CD2 -0.131
REMARK 500 6 HIS A 43 CG HIS A 43 ND1 -0.120
REMARK 500 6 HIS A 95 CG HIS A 95 ND1 -0.120
REMARK 500 6 TRP A 99 CG TRP A 99 CD2 -0.116
REMARK 500 6 TRP A 179 CG TRP A 179 CD2 -0.110
REMARK 500 7 TRP A 7 CG TRP A 7 CD2 -0.129
REMARK 500 7 TRP A 27 CG TRP A 27 CD2 -0.128
REMARK 500 7 HIS A 43 CG HIS A 43 ND1 -0.122
REMARK 500 7 HIS A 95 CG HIS A 95 ND1 -0.121
REMARK 500 7 TRP A 99 CG TRP A 99 CD2 -0.116
REMARK 500 7 TRP A 179 CG TRP A 179 CD2 -0.117
REMARK 500 8 TRP A 7 CG TRP A 7 CD2 -0.137
REMARK 500 8 TRP A 27 CG TRP A 27 CD2 -0.130
REMARK 500 8 HIS A 43 CG HIS A 43 ND1 -0.122
REMARK 500 8 HIS A 95 CG HIS A 95 ND1 -0.123
REMARK 500 8 TRP A 99 CG TRP A 99 CD2 -0.120
REMARK 500 8 TRP A 179 CG TRP A 179 CD2 -0.112
REMARK 500 9 TRP A 7 CG TRP A 7 CD2 -0.114
REMARK 500 9 TRP A 27 CG TRP A 27 CD2 -0.127
REMARK 500
REMARK 500 THIS ENTRY HAS 132 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 7 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 TRP A 7 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 1 TRP A 7 NE1 - CE2 - CZ2 ANGL. DEV. = 9.9 DEGREES
REMARK 500 1 TRP A 7 NE1 - CE2 - CD2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 1 TRP A 27 CD1 - CG - CD2 ANGL. DEV. = 5.0 DEGREES
REMARK 500 1 TRP A 27 CG - CD1 - NE1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 1 TRP A 27 NE1 - CE2 - CZ2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 1 TRP A 27 NE1 - CE2 - CD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 1 TRP A 27 CE2 - CD2 - CG ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 TRP A 27 CG - CD2 - CE3 ANGL. DEV. = -6.6 DEGREES
REMARK 500 1 TRP A 99 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 1 TRP A 99 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 1 TRP A 99 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 1 TRP A 99 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 1 TRP A 179 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 1 TRP A 179 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 1 TRP A 179 NE1 - CE2 - CZ2 ANGL. DEV. = 9.1 DEGREES
REMARK 500 1 TRP A 179 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 2 TRP A 7 CD1 - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 2 TRP A 7 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 TRP A 7 NE1 - CE2 - CZ2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 2 TRP A 7 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 2 TRP A 27 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 2 TRP A 27 NE1 - CE2 - CZ2 ANGL. DEV. = 10.1 DEGREES
REMARK 500 2 TRP A 27 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 2 TRP A 27 CG - CD2 - CE3 ANGL. DEV. = -6.1 DEGREES
REMARK 500 2 TRP A 99 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 2 TRP A 99 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 2 TRP A 99 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 2 TRP A 99 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 2 TRP A 179 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 2 TRP A 179 NE1 - CE2 - CZ2 ANGL. DEV. = 9.5 DEGREES
REMARK 500 2 TRP A 179 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 3 TRP A 7 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 3 TRP A 7 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 3 TRP A 7 NE1 - CE2 - CZ2 ANGL. DEV. = 9.3 DEGREES
REMARK 500 3 TRP A 7 NE1 - CE2 - CD2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 3 TRP A 27 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 3 TRP A 27 CG - CD1 - NE1 ANGL. DEV. = -6.6 DEGREES
REMARK 500 3 TRP A 27 NE1 - CE2 - CZ2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 3 TRP A 27 NE1 - CE2 - CD2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 3 TRP A 99 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 3 TRP A 99 CG - CD1 - NE1 ANGL. DEV. = -6.3 DEGREES
REMARK 500 3 TRP A 99 NE1 - CE2 - CZ2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 3 TRP A 99 NE1 - CE2 - CD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 3 TRP A 179 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 3 TRP A 179 CG - CD1 - NE1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 3 TRP A 179 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 3 TRP A 179 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 4 TRP A 7 CD1 - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 356 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 GLN A 3 -135.40 48.28
REMARK 500 1 GLN A 4 -158.09 -151.78
REMARK 500 1 SER A 6 -159.60 -166.74
REMARK 500 1 GLU A 12 -76.69 -75.80
REMARK 500 1 ALA A 15 33.38 -151.26
REMARK 500 1 VAL A 16 -120.19 44.01
REMARK 500 1 ALA A 18 168.38 60.36
REMARK 500 1 ASP A 20 -79.62 -64.64
REMARK 500 1 CYS A 35 102.01 -163.73
REMARK 500 1 ARG A 47 -74.06 -75.07
REMARK 500 1 PHE A 48 -9.39 -46.71
REMARK 500 1 PHE A 49 -74.79 -99.57
REMARK 500 1 VAL A 51 66.24 20.04
REMARK 500 1 PRO A 52 -164.36 -66.22
REMARK 500 1 ASP A 53 -59.12 -132.10
REMARK 500 1 GLU A 55 -34.27 68.88
REMARK 500 1 ALA A 57 32.97 -73.47
REMARK 500 1 ASN A 74 -13.73 63.42
REMARK 500 1 LEU A 79 -70.08 -43.77
REMARK 500 1 VAL A 88 -60.09 -136.79
REMARK 500 1 LEU A 89 -77.33 -40.09
REMARK 500 1 ASP A 105 81.59 -59.04
REMARK 500 1 ARG A 108 86.73 49.87
REMARK 500 1 ASN A 109 -18.59 -147.58
REMARK 500 1 ARG A 114 -13.40 -46.26
REMARK 500 1 CYS A 131 -154.36 -82.99
REMARK 500 1 SER A 132 30.50 -90.12
REMARK 500 1 VAL A 135 31.62 36.55
REMARK 500 1 GLU A 136 73.83 -8.21
REMARK 500 1 ALA A 137 -63.17 -14.65
REMARK 500 1 GLU A 138 -104.17 -54.82
REMARK 500 1 GLN A 139 85.52 -54.63
REMARK 500 1 GLN A 140 0.20 -173.56
REMARK 500 1 LYS A 142 105.15 62.25
REMARK 500 1 GLU A 159 -31.04 -171.72
REMARK 500 1 ARG A 176 -59.28 -158.31
REMARK 500 1 ASP A 177 -145.17 49.66
REMARK 500 1 TRP A 179 -7.48 -167.67
REMARK 500 1 MET A 183 -81.17 -60.76
REMARK 500 1 LEU A 184 -33.20 -39.34
REMARK 500 1 MET A 186 -73.25 69.18
REMARK 500 1 LEU A 188 -50.61 78.60
REMARK 500 1 ASN A 189 -51.13 176.88
REMARK 500 2 GLN A 3 29.83 -150.27
REMARK 500 2 TRP A 7 -130.12 -110.05
REMARK 500 2 GLU A 9 -85.12 -44.51
REMARK 500 2 ALA A 19 -62.54 -148.07
REMARK 500 2 ASP A 20 -74.07 -57.47
REMARK 500 2 GLU A 33 -35.30 66.75
REMARK 500 2 GLU A 34 14.33 -165.31
REMARK 500
REMARK 500 THIS ENTRY HAS 960 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 47 0.16 SIDE CHAIN
REMARK 500 1 ARG A 66 0.32 SIDE CHAIN
REMARK 500 1 ARG A 90 0.12 SIDE CHAIN
REMARK 500 1 ARG A 108 0.32 SIDE CHAIN
REMARK 500 1 ARG A 114 0.29 SIDE CHAIN
REMARK 500 1 ARG A 152 0.17 SIDE CHAIN
REMARK 500 1 ARG A 175 0.29 SIDE CHAIN
REMARK 500 1 ARG A 176 0.09 SIDE CHAIN
REMARK 500 2 ARG A 47 0.25 SIDE CHAIN
REMARK 500 2 ARG A 66 0.23 SIDE CHAIN
REMARK 500 2 ARG A 90 0.20 SIDE CHAIN
REMARK 500 2 ARG A 108 0.32 SIDE CHAIN
REMARK 500 2 ARG A 114 0.11 SIDE CHAIN
REMARK 500 2 ARG A 152 0.32 SIDE CHAIN
REMARK 500 2 ARG A 175 0.20 SIDE CHAIN
REMARK 500 2 ARG A 176 0.29 SIDE CHAIN
REMARK 500 3 ARG A 66 0.32 SIDE CHAIN
REMARK 500 3 ARG A 90 0.31 SIDE CHAIN
REMARK 500 3 ARG A 108 0.21 SIDE CHAIN
REMARK 500 3 ARG A 114 0.30 SIDE CHAIN
REMARK 500 3 ARG A 152 0.14 SIDE CHAIN
REMARK 500 3 ARG A 175 0.17 SIDE CHAIN
REMARK 500 3 ARG A 176 0.18 SIDE CHAIN
REMARK 500 4 ARG A 47 0.26 SIDE CHAIN
REMARK 500 4 ARG A 66 0.32 SIDE CHAIN
REMARK 500 4 ARG A 90 0.27 SIDE CHAIN
REMARK 500 4 ARG A 108 0.25 SIDE CHAIN
REMARK 500 4 ARG A 114 0.24 SIDE CHAIN
REMARK 500 4 ARG A 152 0.18 SIDE CHAIN
REMARK 500 4 ARG A 175 0.15 SIDE CHAIN
REMARK 500 4 ARG A 176 0.29 SIDE CHAIN
REMARK 500 5 ARG A 47 0.31 SIDE CHAIN
REMARK 500 5 ARG A 66 0.32 SIDE CHAIN
REMARK 500 5 ARG A 90 0.10 SIDE CHAIN
REMARK 500 5 ARG A 114 0.16 SIDE CHAIN
REMARK 500 5 ARG A 152 0.32 SIDE CHAIN
REMARK 500 5 ARG A 175 0.26 SIDE CHAIN
REMARK 500 5 ARG A 176 0.32 SIDE CHAIN
REMARK 500 6 ARG A 47 0.32 SIDE CHAIN
REMARK 500 6 ARG A 66 0.30 SIDE CHAIN
REMARK 500 6 ARG A 90 0.13 SIDE CHAIN
REMARK 500 6 ARG A 108 0.32 SIDE CHAIN
REMARK 500 6 ARG A 114 0.28 SIDE CHAIN
REMARK 500 6 ARG A 152 0.28 SIDE CHAIN
REMARK 500 6 ARG A 175 0.20 SIDE CHAIN
REMARK 500 6 ARG A 176 0.25 SIDE CHAIN
REMARK 500 7 ARG A 47 0.32 SIDE CHAIN
REMARK 500 7 ARG A 66 0.29 SIDE CHAIN
REMARK 500 7 ARG A 90 0.32 SIDE CHAIN
REMARK 500 7 ARG A 108 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 162 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 500 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 69 OD1
REMARK 620 2 ASN A 71 OD1 121.7
REMARK 620 3 ASP A 73 OD2 134.3 94.3
REMARK 620 4 THR A 75 O 80.6 157.6 67.5
REMARK 620 5 GLU A 80 OE1 64.3 63.3 157.6 134.4
REMARK 620 6 GLU A 80 OE2 100.8 63.2 121.4 114.2 51.4
REMARK 620 N 1 2 3 4 5
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 105 OD1
REMARK 620 2 ASP A 107 OD1 69.6
REMARK 620 3 ASN A 109 OD1 80.7 69.0
REMARK 620 4 CYS A 111 O 144.7 113.9 69.3
REMARK 620 5 GLU A 116 OE1 111.9 110.9 166.9 99.8
REMARK 620 6 GLU A 116 OE2 138.7 81.4 116.1 73.8 52.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 158 OD2
REMARK 620 2 ASN A 160 OD1 76.8
REMARK 620 3 ASP A 162 OD1 95.8 85.5
REMARK 620 4 ASP A 162 OD2 147.7 114.7 57.4
REMARK 620 5 GLN A 164 O 101.7 168.7 83.6 60.9
REMARK 620 6 GLU A 169 OE1 89.6 126.0 148.4 104.5 64.9
REMARK 620 7 GLU A 169 OE2 100.8 79.5 154.3 110.8 111.7 51.8
REMARK 620 N 1 2 3 4 5 6
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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502
DBREF 1JBA A 1 204 UNP P51177 GUC1B_BOVIN 1 204
SEQRES 1 A 204 MET GLY GLN GLN PHE SER TRP GLU GLU ALA GLU GLU ASN
SEQRES 2 A 204 GLY ALA VAL GLY ALA ALA ASP ALA ALA GLN LEU GLN GLU
SEQRES 3 A 204 TRP TYR LYS LYS PHE LEU GLU GLU CYS PRO SER GLY THR
SEQRES 4 A 204 LEU PHE MET HIS GLU PHE LYS ARG PHE PHE LYS VAL PRO
SEQRES 5 A 204 ASP ASN GLU GLU ALA THR GLN TYR VAL GLU ALA MET PHE
SEQRES 6 A 204 ARG ALA PHE ASP THR ASN GLY ASP ASN THR ILE ASP PHE
SEQRES 7 A 204 LEU GLU TYR VAL ALA ALA LEU ASN LEU VAL LEU ARG GLY
SEQRES 8 A 204 THR LEU GLU HIS LYS LEU LYS TRP THR PHE LYS ILE TYR
SEQRES 9 A 204 ASP LYS ASP ARG ASN GLY CYS ILE ASP ARG GLN GLU LEU
SEQRES 10 A 204 LEU ASP ILE VAL GLU SER ILE TYR LYS LEU LYS LYS ALA
SEQRES 11 A 204 CYS SER VAL GLU VAL GLU ALA GLU GLN GLN GLY LYS LEU
SEQRES 12 A 204 LEU THR PRO GLU GLU VAL VAL ASP ARG ILE PHE LEU LEU
SEQRES 13 A 204 VAL ASP GLU ASN GLY ASP GLY GLN LEU SER LEU ASN GLU
SEQRES 14 A 204 PHE VAL GLU GLY ALA ARG ARG ASP LYS TRP VAL MET LYS
SEQRES 15 A 204 MET LEU GLN MET ASP LEU ASN PRO SER SER TRP ILE SER
SEQRES 16 A 204 GLN GLN ARG ARG LYS SER ALA MET PHE
HET CA A 500 1
HET CA A 501 1
HET CA A 502 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 3(CA 2+)
HELIX 1 H1 TRP A 7 ASN A 13 1 7
HELIX 2 H2 ALA A 21 LEU A 32 1 12
HELIX 3 H3 MET A 42 VAL A 88 1 47
HELIX 4 H5 PHE A 78 VAL A 88 1 11
HELIX 5 H6 LYS A 96 TYR A 104 1 9
HELIX 6 H7 ARG A 114 LEU A 127 1 14
HELIX 7 H8 GLU A 147 LEU A 156 1 10
HELIX 8 H9 LEU A 167 ARG A 176 1 10
HELIX 9 H10 TRP A 179 ASN A 189 1 11
SHEET 1 S1 1 THR A 39 PHE A 41 0
SHEET 1 S2 1 THR A 75 ASP A 77 0
SHEET 1 S3 1 CYS A 111 ASP A 113 0
SHEET 1 S4 1 GLN A 164 SER A 166 0
LINK OD1 ASP A 69 CA CA A 500 1555 1555 2.48
LINK OD1 ASN A 71 CA CA A 500 1555 1555 2.48
LINK OD2 ASP A 73 CA CA A 500 1555 1555 2.54
LINK O THR A 75 CA CA A 500 1555 1555 2.50
LINK OE1 GLU A 80 CA CA A 500 1555 1555 2.53
LINK OE2 GLU A 80 CA CA A 500 1555 1555 2.51
LINK OD1 ASP A 105 CA CA A 501 1555 1555 2.50
LINK OD1 ASP A 107 CA CA A 501 1555 1555 2.50
LINK OD1 ASN A 109 CA CA A 501 1555 1555 2.46
LINK O CYS A 111 CA CA A 501 1555 1555 2.52
LINK OE1 GLU A 116 CA CA A 501 1555 1555 2.48
LINK OE2 GLU A 116 CA CA A 501 1555 1555 2.50
LINK OD2 ASP A 158 CA CA A 502 1555 1555 2.50
LINK OD1 ASN A 160 CA CA A 502 1555 1555 2.49
LINK OD1 ASP A 162 CA CA A 502 1555 1555 1.84
LINK OD2 ASP A 162 CA CA A 502 1555 1555 2.53
LINK O GLN A 164 CA CA A 502 1555 1555 2.49
LINK OE1 GLU A 169 CA CA A 502 1555 1555 2.49
LINK OE2 GLU A 169 CA CA A 502 1555 1555 2.52
SITE 1 AC1 5 ASP A 69 ASN A 71 ASP A 73 THR A 75
SITE 2 AC1 5 GLU A 80
SITE 1 AC2 5 ASP A 105 ASP A 107 ASN A 109 CYS A 111
SITE 2 AC2 5 GLU A 116
SITE 1 AC3 5 ASP A 158 ASN A 160 ASP A 162 GLN A 164
SITE 2 AC3 5 GLU A 169
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