Header list of 1sy9.pdb file
Complete list - r 2 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 01-APR-04 1SY9
TITLE STRUCTURE OF CALMODULIN COMPLEXED WITH A FRAGMENT OF THE OLFACTORY CNG
TITLE 2 CHANNEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CYCLIC-NUCLEOTIDE-GATED OLFACTORY CHANNEL;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: RESIDUES 151-176;
COMPND 9 SYNONYM: CYCLIC-NUCLEOTIDE-GATED CATION CHANNEL 2, CNG CHANNEL 2,
COMPND 10 CNG-2, CNG2;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 10 OF THE PROTEIN IS NATURALLY FOUND IN BOS TAURUS (BOVINE).
KEYWDS 4 HELIX-TURN-HELIX, CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR G.M.CONTESSA,M.ORSALE,S.MELINO,V.TORRE,M.PACI,A.DESIDERI,D.O.CICERO
REVDAT 3 02-MAR-22 1SY9 1 REMARK LINK
REVDAT 2 24-FEB-09 1SY9 1 VERSN
REVDAT 1 12-APR-05 1SY9 0
JRNL AUTH G.M.CONTESSA,M.ORSALE,S.MELINO,V.TORRE,M.PACI,A.DESIDERI,
JRNL AUTH 2 D.O.CICERO
JRNL TITL STRUCTURE OF CALMODULIN COMPLEXED WITH AN OLFACTORY CNG
JRNL TITL 2 CHANNEL FRAGMENT AND ROLE OF THE CENTRAL LINKER: RESIDUAL
JRNL TITL 3 DIPOLAR COUPLINGS TO EVALUATE CALMODULIN BINDING MODES
JRNL TITL 4 OUTSIDE THE KINASE FAMILY.
JRNL REF J.BIOMOL.NMR V. 31 185 2005
JRNL REFN ISSN 0925-2738
JRNL PMID 15803393
JRNL DOI 10.1007/S10858-005-0165-1
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.ORSALE,S.MELINO,G.M.CONTESSA,V.TORRE,G.ANDREOTTI,A.MOTTA,
REMARK 1 AUTH 2 M.PACI,A.DESIDERI,D.O.CICERO
REMARK 1 TITL TWO DISTINCT CA2+-CALMODULIN INTERACTIONS WITH N-TERMINAL
REMARK 1 TITL 2 REGIONS OF THE OLFACTORY AND ROD CYCLIC NUCLEOTIDE GATED
REMARK 1 TITL 3 CHANNELS CHARACTERIZED BY NMR SPECTROSCOPY
REMARK 1 REF FEBS LETT. V. 548 11 2003
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/S0014-5793(03)00716-6
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, X-PLOR 3.85
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 3935 RESTRAINTS: 3050 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 591
REMARK 3 ARE DIHEDRAL ANGLE RESTRAINTS, 133 ARE DISTANCE RESTRAINTS FROM
REMARK 3 HYDROGEN BONDS. 68 SCALAR J COUPLING CONSTANTS AND 93 RESIDUAL
REMARK 3 DIPOLAR COUPLING CONSTANTS WERE INCLUDED AS EXPERIMENTAL
REMARK 3 RESTRAINTS NECESSARY TO OBTAIN THE FINAL STRUCTURES.
REMARK 4
REMARK 4 1SY9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022090.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308; 308
REMARK 210 PH : 6.7; 6.7
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : NULL; NULL
REMARK 210 SAMPLE CONTENTS : 1.2 MM COMPLEX U-15N,13C, 6 MM
REMARK 210 CACL2, 140 MM KCL, D2O; 1.2 MM
REMARK 210 COMPLEX U-15N,13C, 6 MM CACL2,
REMARK 210 140 MM KCL, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLN B 151
REMARK 465 GLN B 152
REMARK 465 ARG B 153
REMARK 465 ARG B 154
REMARK 465 ASN B 174
REMARK 465 PHE B 175
REMARK 465 ARG B 176
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 THR A 44 H LEU A 48 1.60
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 PRO A 43 -147.18 -68.75
REMARK 500 1 ILE A 100 -129.29 -89.07
REMARK 500 1 SER A 101 159.87 168.71
REMARK 500 2 PRO A 43 -143.08 -61.15
REMARK 500 2 THR A 79 -160.71 -111.34
REMARK 500 3 THR A 29 -34.32 -39.49
REMARK 500 3 PRO A 43 -152.24 -67.18
REMARK 500 3 ASP A 56 93.97 -68.99
REMARK 500 3 ASP A 129 78.27 -103.38
REMARK 500 4 THR A 29 -34.79 -39.56
REMARK 500 4 PRO A 43 -147.84 -66.30
REMARK 500 4 ASP A 56 99.01 -69.12
REMARK 500 5 PRO A 43 -148.97 -68.36
REMARK 500 5 THR A 79 -165.33 -107.29
REMARK 500 6 GLN A 3 -159.71 -56.52
REMARK 500 6 PRO A 43 -151.89 -62.23
REMARK 500 7 PRO A 43 -148.43 -63.83
REMARK 500 8 ASP A 2 30.35 -99.97
REMARK 500 8 PRO A 43 -151.39 -64.58
REMARK 500 8 THR A 79 -159.65 -117.97
REMARK 500 9 PRO A 43 -148.84 -68.38
REMARK 500 9 THR A 79 -164.32 -125.63
REMARK 500 10 PRO A 43 -149.52 -70.65
REMARK 500 11 PRO A 43 -149.54 -61.36
REMARK 500 12 GLN A 3 -174.06 -64.85
REMARK 500 12 PRO A 43 -143.67 -68.60
REMARK 500 12 ASP A 56 97.63 -69.44
REMARK 500 12 THR A 79 -166.82 -118.20
REMARK 500 13 PRO A 43 -150.37 -68.63
REMARK 500 14 PRO A 43 -146.05 -61.78
REMARK 500 14 THR A 79 -162.94 -121.93
REMARK 500 15 PRO A 43 -147.56 -69.48
REMARK 500 16 GLN A 3 -89.96 -122.05
REMARK 500 16 LEU A 4 -78.01 -103.69
REMARK 500 16 PRO A 43 -146.99 -66.08
REMARK 500 17 LEU A 4 -89.54 -114.28
REMARK 500 17 PRO A 43 -150.54 -67.30
REMARK 500 17 THR A 79 -160.05 -101.07
REMARK 500 18 THR A 29 -34.98 -39.07
REMARK 500 18 PRO A 43 -150.89 -70.69
REMARK 500 18 THR A 79 -164.45 -112.22
REMARK 500 19 PRO A 43 -148.47 -69.07
REMARK 500 20 PRO A 43 -148.59 -64.18
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 37 0.28 SIDE CHAIN
REMARK 500 1 ARG A 74 0.16 SIDE CHAIN
REMARK 500 1 ARG A 86 0.31 SIDE CHAIN
REMARK 500 1 ARG A 90 0.25 SIDE CHAIN
REMARK 500 1 ARG A 106 0.30 SIDE CHAIN
REMARK 500 1 ARG A 126 0.24 SIDE CHAIN
REMARK 500 1 ARG B 158 0.30 SIDE CHAIN
REMARK 500 1 ARG B 159 0.32 SIDE CHAIN
REMARK 500 1 ARG B 162 0.24 SIDE CHAIN
REMARK 500 1 ARG B 168 0.32 SIDE CHAIN
REMARK 500 1 ARG B 173 0.32 SIDE CHAIN
REMARK 500 2 ARG A 37 0.32 SIDE CHAIN
REMARK 500 2 ARG A 74 0.29 SIDE CHAIN
REMARK 500 2 ARG A 86 0.26 SIDE CHAIN
REMARK 500 2 ARG A 90 0.22 SIDE CHAIN
REMARK 500 2 ARG A 106 0.21 SIDE CHAIN
REMARK 500 2 ARG A 126 0.31 SIDE CHAIN
REMARK 500 2 ARG B 158 0.31 SIDE CHAIN
REMARK 500 2 ARG B 159 0.32 SIDE CHAIN
REMARK 500 2 ARG B 162 0.25 SIDE CHAIN
REMARK 500 2 ARG B 168 0.23 SIDE CHAIN
REMARK 500 2 ARG B 173 0.31 SIDE CHAIN
REMARK 500 3 ARG A 37 0.30 SIDE CHAIN
REMARK 500 3 ARG A 74 0.28 SIDE CHAIN
REMARK 500 3 ARG A 86 0.26 SIDE CHAIN
REMARK 500 3 ARG A 90 0.30 SIDE CHAIN
REMARK 500 3 ARG A 106 0.27 SIDE CHAIN
REMARK 500 3 ARG A 126 0.28 SIDE CHAIN
REMARK 500 3 ARG B 158 0.20 SIDE CHAIN
REMARK 500 3 ARG B 159 0.32 SIDE CHAIN
REMARK 500 3 ARG B 162 0.27 SIDE CHAIN
REMARK 500 3 ARG B 168 0.26 SIDE CHAIN
REMARK 500 3 ARG B 173 0.30 SIDE CHAIN
REMARK 500 4 ARG A 37 0.31 SIDE CHAIN
REMARK 500 4 ARG A 74 0.27 SIDE CHAIN
REMARK 500 4 ARG A 86 0.28 SIDE CHAIN
REMARK 500 4 ARG A 90 0.25 SIDE CHAIN
REMARK 500 4 ARG A 106 0.27 SIDE CHAIN
REMARK 500 4 ARG A 126 0.29 SIDE CHAIN
REMARK 500 4 ARG B 158 0.28 SIDE CHAIN
REMARK 500 4 ARG B 159 0.18 SIDE CHAIN
REMARK 500 4 ARG B 162 0.31 SIDE CHAIN
REMARK 500 4 ARG B 168 0.30 SIDE CHAIN
REMARK 500 4 ARG B 173 0.30 SIDE CHAIN
REMARK 500 5 ARG A 37 0.25 SIDE CHAIN
REMARK 500 5 ARG A 74 0.32 SIDE CHAIN
REMARK 500 5 ARG A 86 0.20 SIDE CHAIN
REMARK 500 5 ARG A 90 0.31 SIDE CHAIN
REMARK 500 5 ARG A 106 0.31 SIDE CHAIN
REMARK 500 5 ARG A 126 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 220 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 149 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD2 107.3
REMARK 620 3 ASP A 24 OD1 60.8 101.5
REMARK 620 4 THR A 26 O 69.2 174.7 73.4
REMARK 620 5 GLU A 31 OE1 84.8 83.9 145.4 99.5
REMARK 620 6 GLU A 31 OE2 138.5 59.9 154.2 125.3 55.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 150 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 105.0
REMARK 620 3 ASN A 60 OD1 82.7 66.5
REMARK 620 4 THR A 62 O 77.8 149.5 84.1
REMARK 620 5 GLU A 67 OE1 103.7 82.7 149.0 126.8
REMARK 620 6 GLU A 67 OE2 74.5 132.5 153.4 77.9 53.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 74.8
REMARK 620 3 ASP A 95 OD2 119.7 55.0
REMARK 620 4 ASN A 97 OD1 65.1 85.5 78.9
REMARK 620 5 TYR A 99 O 70.9 136.1 124.3 55.5
REMARK 620 6 GLU A 104 OE1 109.8 125.1 125.0 147.8 92.3
REMARK 620 7 GLU A 104 OE2 166.6 107.0 69.7 128.1 112.8 57.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 152 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD2 105.5
REMARK 620 3 ASP A 131 OD1 63.9 50.6
REMARK 620 4 ASP A 133 OD1 66.6 73.6 83.0
REMARK 620 5 ASP A 133 OD2 108.6 61.6 101.8 42.0
REMARK 620 6 GLN A 135 O 107.6 116.5 155.1 72.3 57.1
REMARK 620 7 GLU A 140 OE1 142.0 91.5 106.7 151.3 109.4 93.9
REMARK 620 8 GLU A 140 OE2 99.7 89.8 70.8 153.7 143.9 134.0 45.7
REMARK 620 N 1 2 3 4 5 6 7
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 149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 152
DBREF 1SY9 A 1 148 UNP P62155 CALM_XENLA 1 148
DBREF 1SY9 B 151 176 UNP Q03041 CNGA2_BOVIN 60 85
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 A 148 MET MET THR ALA LYS
SEQRES 1 B 26 GLN GLN ARG ARG GLY GLY PHE ARG ARG ILE ALA ARG LEU
SEQRES 2 B 26 VAL GLY VAL LEU ARG GLU TRP ALA TYR ARG ASN PHE ARG
HET CA A 149 1
HET CA A 150 1
HET CA A 151 1
HET CA A 152 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 THR A 28 GLY A 40 1 13
HELIX 3 3 THR A 44 ASP A 56 1 13
HELIX 4 4 ASP A 64 THR A 79 1 16
HELIX 5 5 ASP A 80 ASP A 93 1 14
HELIX 6 6 SER A 101 GLY A 113 1 13
HELIX 7 7 THR A 117 ASP A 129 1 13
HELIX 8 8 ASN A 137 THR A 146 1 10
HELIX 9 9 GLY B 156 ARG B 173 1 18
LINK OD1 ASP A 20 CA CA A 149 1555 1555 2.43
LINK OD2 ASP A 22 CA CA A 149 1555 1555 2.58
LINK OD1 ASP A 24 CA CA A 149 1555 1555 2.72
LINK O THR A 26 CA CA A 149 1555 1555 2.52
LINK OE1 GLU A 31 CA CA A 149 1555 1555 2.29
LINK OE2 GLU A 31 CA CA A 149 1555 1555 2.31
LINK OD1 ASP A 56 CA CA A 150 1555 1555 2.32
LINK OD1 ASP A 58 CA CA A 150 1555 1555 2.59
LINK OD1 ASN A 60 CA CA A 150 1555 1555 2.51
LINK O THR A 62 CA CA A 150 1555 1555 2.09
LINK OE1 GLU A 67 CA CA A 150 1555 1555 2.41
LINK OE2 GLU A 67 CA CA A 150 1555 1555 2.42
LINK OD1 ASP A 93 CA CA A 151 1555 1555 2.22
LINK OD1 ASP A 95 CA CA A 151 1555 1555 1.88
LINK OD2 ASP A 95 CA CA A 151 1555 1555 2.58
LINK OD1 ASN A 97 CA CA A 151 1555 1555 2.48
LINK O TYR A 99 CA CA A 151 1555 1555 2.80
LINK OE1 GLU A 104 CA CA A 151 1555 1555 2.35
LINK OE2 GLU A 104 CA CA A 151 1555 1555 2.07
LINK OD1 ASP A 129 CA CA A 152 1555 1555 2.73
LINK OD2 ASP A 131 CA CA A 152 1555 1555 2.79
LINK OD1 ASP A 131 CA CA A 152 1555 1555 1.82
LINK OD1 ASP A 133 CA CA A 152 1555 1555 1.94
LINK OD2 ASP A 133 CA CA A 152 1555 1555 3.16
LINK O GLN A 135 CA CA A 152 1555 1555 2.53
LINK OE1 GLU A 140 CA CA A 152 1555 1555 2.05
LINK OE2 GLU A 140 CA CA A 152 1555 1555 3.01
SITE 1 AC1 5 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 5 GLU A 31
SITE 1 AC2 5 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 5 GLU A 67
SITE 1 AC3 5 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 5 GLU A 104
SITE 1 AC4 5 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 5 GLU A 140
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 - r 2 2 Bytes