Header list of 1prr.pdb file
Complete list - 2 20 Bytes
HEADER BINDING PROTEIN 25-MAR-94 1PRR
TITLE NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S
TITLE 2 COMPLEXED WITH CALCIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEVELOPMENT-SPECIFIC PROTEIN S;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYXOCOCCUS XANTHUS;
SOURCE 3 ORGANISM_TAXID: 34
KEYWDS BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR S.BAGBY,T.S.HARVEY,S.G.EAGLE,S.INOUYE,M.IKURA
REVDAT 3 02-MAR-22 1PRR 1 REMARK LINK
REVDAT 2 24-FEB-09 1PRR 1 VERSN
REVDAT 1 31-AUG-94 1PRR 0
JRNL AUTH S.BAGBY,T.S.HARVEY,S.G.EAGLE,S.INOUYE,M.IKURA
JRNL TITL NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN
JRNL TITL 2 S COMPLEXED WITH CALCIUM.
JRNL REF STRUCTURE V. 2 107 1994
JRNL REFN ISSN 0969-2126
JRNL PMID 8081742
JRNL DOI 10.1016/S0969-2126(00)00013-7
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.BAGBY,T.S.HARVEY,S.G.EAGLE,S.INOUYE,M.IKURA
REMARK 1 TITL STRUCTURAL SIMILARITY OF A DEVELOPMENTALLY REGULATED
REMARK 1 TITL 2 BACTERIAL SPORE COAT PROTEIN TO BETAGAMMA-CRYSTALLINS OF THE
REMARK 1 TITL 3 VERTEBRATE EYE LENS
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 4308 1994
REMARK 1 REFN ISSN 0027-8424
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.BAGBY,T.S.HARVEY,L.E.KAY,S.G.EAGLE,S.INOUYE,M.IKURA
REMARK 1 TITL UNUSUAL HELIX-CONTAINING GREEK KEYS IN DEVELOPMENT-SPECIFIC
REMARK 1 TITL 2 CA2+-BINDING PROTEIN S. 1H, 15N AND 13C ASSIGNMENTS AND
REMARK 1 TITL 3 SECONDARY STRUCTURE DETERMINED USING MULTIDIMENSIONAL DOUBLE
REMARK 1 TITL 4 AND TRIPLE RESONANCE HETERONUCLEAR NMR SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 33 2409 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PRR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175811.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 HH22 ARG A 83 H VAL A 84 1.10
REMARK 500 CE2 PHE A 7 NE2 GLN A 16 2.18
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 ASN A 166 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
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 ASN A 3 123.71 179.96
REMARK 500 ASP A 11 34.02 70.97
REMARK 500 PHE A 12 -2.33 60.50
REMARK 500 LYS A 15 143.09 -33.29
REMARK 500 PRO A 21 -167.54 -58.65
REMARK 500 LEU A 32 -73.29 -75.11
REMARK 500 ASN A 36 -137.70 62.87
REMARK 500 THR A 38 -24.54 -154.69
REMARK 500 ILE A 39 44.14 -78.11
REMARK 500 PRO A 46 -178.38 -62.74
REMARK 500 GLN A 54 -84.55 -45.99
REMARK 500 ASP A 56 -177.16 -58.02
REMARK 500 VAL A 66 -12.05 -141.12
REMARK 500 ALA A 67 -156.66 -117.74
REMARK 500 GLU A 70 -75.76 -73.80
REMARK 500 LEU A 72 -81.88 66.74
REMARK 500 ASN A 78 122.43 -170.32
REMARK 500 SER A 80 -40.96 -175.27
REMARK 500 PRO A 91 -162.89 -59.36
REMARK 500 ARG A 92 -161.64 -177.57
REMARK 500 TYR A 97 -80.77 -101.54
REMARK 500 GLU A 99 94.80 -69.67
REMARK 500 GLN A 100 49.73 134.19
REMARK 500 PHE A 101 32.99 32.25
REMARK 500 LYS A 104 139.75 -32.95
REMARK 500 THR A 114 -148.79 -93.04
REMARK 500 ALA A 116 -62.47 -99.61
REMARK 500 LEU A 118 -70.74 -34.49
REMARK 500 ARG A 120 20.70 -75.79
REMARK 500 ILE A 123 -106.57 -139.15
REMARK 500 ASP A 124 -158.78 -172.36
REMARK 500 ASN A 125 -81.02 -58.13
REMARK 500 THR A 127 -0.87 173.97
REMARK 500 ILE A 128 -82.58 -67.95
REMARK 500 SER A 129 -136.59 76.35
REMARK 500 SER A 130 128.98 -38.54
REMARK 500 LYS A 142 -76.99 -63.03
REMARK 500 ASN A 143 -178.92 -56.92
REMARK 500 ASP A 144 -144.26 -64.47
REMARK 500 ASN A 145 73.81 -13.37
REMARK 500 PHE A 146 64.50 31.76
REMARK 500 SER A 155 -178.12 -170.39
REMARK 500 ALA A 157 63.99 -157.21
REMARK 500 PRO A 158 23.45 -65.56
REMARK 500 THR A 159 96.57 -170.00
REMARK 500 LEU A 160 -53.62 -123.79
REMARK 500 MET A 163 -68.38 -142.08
REMARK 500 ASN A 164 -108.45 -91.34
REMARK 500 ASN A 165 -43.25 -153.63
REMARK 500 ASN A 166 95.42 -179.16
REMARK 500
REMARK 500 THIS ENTRY HAS 51 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 ARG A 26 0.23 SIDE CHAIN
REMARK 500 ARG A 83 0.32 SIDE CHAIN
REMARK 500 ARG A 92 0.22 SIDE CHAIN
REMARK 500 ARG A 94 0.28 SIDE CHAIN
REMARK 500 ARG A 120 0.27 SIDE CHAIN
REMARK 500 ARG A 171 0.09 SIDE CHAIN
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 174 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 10 OE1
REMARK 620 2 GLU A 10 OE2 42.4
REMARK 620 3 GLU A 71 OE2 140.7 136.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 175 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 99 OE2
REMARK 620 2 THR A 159 OG1 151.2
REMARK 620 N 1
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 174
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 175
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PRS RELATED DB: PDB
DBREF 1PRR A 1 173 UNP P02966 DESS_MYXXA 1 173
SEQRES 1 A 173 MET ALA ASN ILE THR VAL PHE TYR ASN GLU ASP PHE GLN
SEQRES 2 A 173 GLY LYS GLN VAL ASP LEU PRO PRO GLY ASN TYR THR ARG
SEQRES 3 A 173 ALA GLN LEU ALA ALA LEU GLY ILE GLU ASN ASN THR ILE
SEQRES 4 A 173 SER SER VAL LYS VAL PRO PRO GLY VAL LYS ALA ILE LEU
SEQRES 5 A 173 TYR GLN ASN ASP GLY PHE ALA GLY ASP GLN ILE GLU VAL
SEQRES 6 A 173 VAL ALA ASN ALA GLU GLU LEU GLY PRO LEU ASN ASN ASN
SEQRES 7 A 173 VAL SER SER ILE ARG VAL ILE SER VAL PRO VAL GLN PRO
SEQRES 8 A 173 ARG ALA ARG PHE PHE TYR LYS GLU GLN PHE ASP GLY LYS
SEQRES 9 A 173 GLU VAL ASP LEU PRO PRO GLY GLN TYR THR GLN ALA GLU
SEQRES 10 A 173 LEU GLU ARG TYR GLY ILE ASP ASN ASN THR ILE SER SER
SEQRES 11 A 173 VAL LYS PRO GLN GLY LEU ALA VAL VAL LEU PHE LYS ASN
SEQRES 12 A 173 ASP ASN PHE SER GLY ASP THR LEU PRO VAL ASN SER ASP
SEQRES 13 A 173 ALA PRO THR LEU GLY ALA MET ASN ASN ASN THR SER SER
SEQRES 14 A 173 ILE ARG ILE SER
HET CA A 174 1
HET CA A 175 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
HELIX 1 H1 ARG A 26 GLY A 33 1 8
HELIX 2 H2 GLN A 115 GLY A 122 1 8
SHEET 1 BN1 4 LYS A 15 PRO A 20 0
SHEET 2 BN1 4 ASN A 3 TYR A 8 -1
SHEET 3 BN1 4 SER A 41 VAL A 44 -1
SHEET 4 BN1 4 ASN A 68 GLU A 70 -1
SHEET 1 BN2 4 GLY A 22 TYR A 24 0
SHEET 2 BN2 4 SER A 81 SER A 86 -1
SHEET 3 BN2 4 VAL A 48 TYR A 53 -1
SHEET 4 BN2 4 ASP A 61 VAL A 65 -1
SHEET 1 BC1 4 LYS A 104 PRO A 109 0
SHEET 2 BC1 4 ARG A 92 TYR A 97 -1
SHEET 3 BC1 4 SER A 130 PRO A 133 -1
SHEET 4 BC1 4 ASP A 156 PRO A 158 -1
SHEET 1 BC2 4 GLY A 111 THR A 114 0
SHEET 2 BC2 4 SER A 169 SER A 173 -1
SHEET 3 BC2 4 ALA A 137 PHE A 141 -1
SHEET 4 BC2 4 ASP A 149 ASN A 154 -1
LINK OE1 GLU A 10 CA CA A 174 1555 1555 3.13
LINK OE2 GLU A 10 CA CA A 174 1555 1555 1.76
LINK OE2 GLU A 71 CA CA A 174 1555 1555 3.32
LINK OE2 GLU A 99 CA CA A 175 1555 1555 2.11
LINK OG1 THR A 159 CA CA A 175 1555 1555 2.88
SITE 1 AC1 2 GLU A 10 GLU A 71
SITE 1 AC2 2 GLU A 99 THR A 159
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
Complete list - 2 20 Bytes