HEADER METAL BINDING PROTEIN 12-DEC-11 2LMV
TITLE ANDROCAM AT HIGH CALCIUM WITH THREE EXPLICIT CA2+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN-RELATED PROTEIN 97A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROTEIN ANDROCAM;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: AND, ANDROCAM, CAMR97A, CG17769;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET15B
KEYWDS HIGH CALCIUM, SPERMATOGENESIS, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.K.JOSHI,S.T.MORAN,K.M.BECKINGHAM,K.R.MACKENZIE
REVDAT 2 05-SEP-12 2LMV 1 JRNL
REVDAT 1 22-AUG-12 2LMV 0
JRNL AUTH M.K.JOSHI,S.MORAN,K.M.BECKINGHAM,K.R.MACKENZIE
JRNL TITL STRUCTURE OF ANDROCAM SUPPORTS SPECIALIZED INTERACTIONS WITH
JRNL TITL 2 MYOSIN VI.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 13290 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22851764
JRNL DOI 10.1073/PNAS.1209730109
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA
REMARK 3 AUTHORS : LINGE, O'DONOGHUE AND NILGES
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2LMV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-11.
REMARK 100 THE RCSB ID CODE IS RCSB102577.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 10
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.8 MM [U-100% 13C; U-100% 15N]
REMARK 210 ANDROCAM, 10 MM CALCIUM CHLORIDE,
REMARK 210 10 % D2O, 10 MM POTASSIUM
REMARK 210 CHLORIDE, 10 MM TRIS, 10 MM DTT,
REMARK 210 0.1 MM TSP, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCO; 3D
REMARK 210 CBCA(CO)NH; 2D 1H-13C HSQC
REMARK 210 ALIPHATIC; 3D HCCH-COSY; 3D HCCH-
REMARK 210 TOCSY; 2D 1H-13C HSQC AROMATIC;
REMARK 210 3D HCACO; 3D HNCACB
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, SPARKY, ARIA
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE C TERMINAL LOBES IN ALL 20 MODELS ALSO SUPERIMPOSE
REMARK 210 WITH VERY SIMILAR RMSD VALUES AS THE N TERMINAL LOBES.
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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
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 GLU A 3 51.58 -159.29
REMARK 500 1 PHE A 19 44.16 -105.91
REMARK 500 1 ASN A 42 67.91 -173.01
REMARK 500 1 ASN A 59 27.18 -140.46
REMARK 500 1 ASN A 60 -85.18 62.01
REMARK 500 1 ASP A 80 38.03 -93.00
REMARK 500 1 ASP A 93 99.08 -55.32
REMARK 500 1 ASP A 133 -9.64 -147.66
REMARK 500 1 TYR A 138 -25.45 -39.12
REMARK 500 2 LEU A 4 89.77 -67.75
REMARK 500 2 GLN A 41 -80.68 -93.58
REMARK 500 2 ASN A 42 74.89 56.81
REMARK 500 2 ASN A 57 43.68 -89.65
REMARK 500 2 ASN A 58 -15.66 -155.16
REMARK 500 2 ASN A 59 21.39 -144.21
REMARK 500 2 ASN A 60 -83.24 64.49
REMARK 500 2 GLU A 78 -80.70 60.22
REMARK 500 2 THR A 79 40.53 -147.25
REMARK 500 2 ASP A 133 -35.40 -143.05
REMARK 500 2 TYR A 138 -23.72 -39.21
REMARK 500 3 THR A 5 177.32 -59.10
REMARK 500 3 PHE A 19 37.34 -88.14
REMARK 500 3 ASN A 42 71.87 -155.28
REMARK 500 3 THR A 79 -1.36 -173.39
REMARK 500 3 THR A 81 57.06 36.11
REMARK 500 3 ASP A 93 93.82 -60.83
REMARK 500 3 ASP A 133 6.66 -155.66
REMARK 500 3 TYR A 138 -24.21 -38.49
REMARK 500 4 ASN A 42 64.35 -170.27
REMARK 500 4 ASN A 57 59.64 -111.53
REMARK 500 4 ASN A 58 -55.17 -170.81
REMARK 500 4 ASN A 60 -81.75 62.66
REMARK 500 4 ASP A 80 29.41 -157.39
REMARK 500 4 THR A 81 117.21 -38.26
REMARK 500 4 ASP A 133 -6.68 -151.68
REMARK 500 5 GLU A 3 69.79 -168.69
REMARK 500 5 LEU A 4 81.17 47.05
REMARK 500 5 ASN A 42 82.61 -172.13
REMARK 500 5 ASN A 57 36.57 -98.50
REMARK 500 5 ASN A 58 -27.39 -159.54
REMARK 500 5 ASN A 60 -81.34 64.13
REMARK 500 5 GLU A 78 -84.89 62.76
REMARK 500 5 THR A 81 90.15 -47.23
REMARK 500 5 LYS A 115 90.00 52.70
REMARK 500 5 ASP A 133 -23.84 -155.70
REMARK 500 6 LEU A 4 89.84 -67.12
REMARK 500 6 GLN A 41 -68.12 -91.65
REMARK 500 6 ASN A 42 78.32 54.42
REMARK 500 6 ASN A 57 52.76 -93.81
REMARK 500 6 ASN A 58 -63.24 -162.33
REMARK 500
REMARK 500 THIS ENTRY HAS 172 RAMACHANDRAN OUTLIERS.
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 1 CA A 150 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD2
REMARK 620 2 MET A 135 O 98.1
REMARK 620 3 ASP A 133 OD2 104.7 73.4
REMARK 620 4 GLU A 140 OE2 89.7 120.1 159.1
REMARK 620 5 ASP A 131 OD2 107.1 154.7 100.8 59.9
REMARK 620 6 ASP A 129 OD1 10.7 108.2 110.5 81.7 96.9
REMARK 620 7 ASP A 133 OD1 71.0 77.0 33.8 156.5 112.2 77.4
REMARK 620 8 GLU A 140 OE1 119.7 73.5 127.2 52.1 92.4 118.3 149.7
REMARK 620 9 ASP A 131 OD1 76.7 141.7 71.4 98.0 49.9 71.2 65.3 142.2
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 CA A 151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 26 O
REMARK 620 2 THR A 24 OG1 113.7
REMARK 620 3 GLN A 62 OE1 93.0 81.1
REMARK 620 4 ASP A 20 OD1 68.6 92.7 156.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 1 CA A 149 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD2
REMARK 620 2 PHE A 99 O 53.5
REMARK 620 3 ASP A 97 OD2 72.2 62.5
REMARK 620 4 GLU A 104 OE2 129.2 88.8 123.5
REMARK 620 5 ASP A 95 OD2 146.5 159.0 121.7 71.8
REMARK 620 6 ASP A 93 OD1 31.8 74.1 103.3 114.6 120.8
REMARK 620 7 ASP A 97 OD1 76.1 88.2 28.7 142.6 102.2 100.4
REMARK 620 8 GLU A 104 OE1 103.9 108.3 170.7 52.2 66.3 74.0 159.7
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 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 17354 RELATED DB: BMRB
REMARK 900 RELATED ID: 2LMT RELATED DB: PDB
REMARK 900 RELATED ID: 2LMU RELATED DB: PDB
DBREF 2LMV A 1 148 UNP P49258 CALL_DROME 1 148
SEQRES 1 A 148 MET SER GLU LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 ASP ALA PHE VAL GLN PHE ASP LYS GLU GLY THR GLY LYS
SEQRES 3 A 148 ILE ALA THR ARG GLU LEU GLY THR LEU MET ARG THR LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP LEU ILE
SEQRES 5 A 148 ALA GLU ALA GLU ASN ASN ASN ASN GLY GLN LEU ASN PHE
SEQRES 6 A 148 THR GLU PHE CYS GLY ILE MET ALA LYS GLN MET ARG GLU
SEQRES 7 A 148 THR ASP THR GLU GLU GLU MET ARG GLU ALA PHE LYS ILE
SEQRES 8 A 148 PHE ASP ARG ASP GLY ASP GLY PHE ILE SER PRO ALA GLU
SEQRES 9 A 148 LEU ARG PHE VAL MET ILE ASN LEU GLY GLU LYS VAL THR
SEQRES 10 A 148 ASP GLU GLU ILE ASP GLU MET ILE ARG GLU ALA ASP PHE
SEQRES 11 A 148 ASP GLY ASP GLY MET ILE ASN TYR GLU GLU PHE VAL TRP
SEQRES 12 A 148 MET ILE SER GLN LYS
HET CA A 149 1
HET CA A 150 1
HET CA A 151 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 3(CA 2+)
HELIX 1 1 THR A 5 GLN A 18 1 14
HELIX 2 2 GLU A 31 LEU A 39 1 9
HELIX 3 3 THR A 44 ASN A 59 1 16
HELIX 4 4 PHE A 65 ARG A 77 1 13
HELIX 5 5 THR A 81 ASP A 93 1 13
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 LYS A 148 1 12
SHEET 1 A 2 LYS A 26 ALA A 28 0
SHEET 2 A 2 GLN A 62 ASN A 64 -1 O LEU A 63 N ILE A 27
LINK OD2 ASP A 129 CA CA A 150 1555 1555 4.40
LINK O LYS A 26 CA CA A 151 1555 1555 2.30
LINK OD2 ASP A 93 CA CA A 149 1555 1555 3.80
LINK O PHE A 99 CA CA A 149 1555 1555 2.33
LINK O MET A 135 CA CA A 150 1555 1555 2.33
LINK OD2 ASP A 133 CA CA A 150 1555 1555 3.73
LINK OD2 ASP A 97 CA CA A 149 1555 1555 3.97
LINK OG1 THR A 24 CA CA A 151 1555 1555 2.40
LINK OE1 GLN A 62 CA CA A 151 1555 1555 2.44
LINK OD1 ASP A 20 CA CA A 151 1555 1555 2.44
LINK OE2 GLU A 140 CA CA A 150 1555 1555 2.54
LINK OE2 GLU A 104 CA CA A 149 1555 1555 2.47
LINK OD2 ASP A 131 CA CA A 150 1555 1555 2.71
LINK OD2 ASP A 95 CA CA A 149 1555 1555 2.48
LINK OD1 ASP A 129 CA CA A 150 1555 1555 2.29
LINK OD1 ASP A 93 CA CA A 149 1555 1555 2.31
LINK OD1 ASP A 133 CA CA A 150 1555 1555 2.37
LINK OD1 ASP A 97 CA CA A 149 1555 1555 2.38
LINK OE1 GLU A 140 CA CA A 150 1555 1555 2.45
LINK OD1 ASP A 131 CA CA A 150 1555 1555 2.48
LINK OE1 GLU A 104 CA CA A 149 1555 1555 2.52
SITE 1 AC1 5 ASP A 93 ASP A 95 ASP A 97 PHE A 99
SITE 2 AC1 5 GLU A 104
SITE 1 AC2 5 ASP A 129 ASP A 131 ASP A 133 MET A 135
SITE 2 AC2 5 GLU A 140
SITE 1 AC3 5 ASP A 20 GLU A 22 THR A 24 LYS A 26
SITE 2 AC3 5 GLN A 62
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
(ATOM LINES ARE NOT SHOWN.)
END