Header list of 2pas.pdb file
Complete list - 16 20 Bytes
HEADER BINDING PROTEIN(CALCIUM) 22-MAR-94 2PAS
TITLE COMPARISON BETWEEN THE CRYSTAL AND THE SOLUTION STRUCTURES OF THE EF
TITLE 2 HAND PARVALBUMIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PARVALBUMIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESOX LUCIUS;
SOURCE 3 ORGANISM_COMMON: NORTHERN PIKE;
SOURCE 4 ORGANISM_TAXID: 8010
KEYWDS BINDING PROTEIN(CALCIUM)
EXPDTA SOLUTION NMR
NUMMDL 9
AUTHOR A.PADILLA,A.CAVE,J.PARELLO,G.ETIENNE,C.BALDELLON
REVDAT 3 16-MAR-22 2PAS 1 REMARK LINK
REVDAT 2 24-FEB-09 2PAS 1 VERSN
REVDAT 1 22-JUN-94 2PAS 0
JRNL AUTH A.PADILLA,A.CAVE,J.PARELLO,G.ETIENNE,C.BALDELLON
JRNL TITL COMPARISON BETWEEN THE CRYSTAL AND THE SOLUTION STRUCTURES
JRNL TITL 2 OF THE EF HAND PARVALBUMIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.BLANCUZZI,A.PADILLA,J.PARELLO,A.CAVE
REMARK 1 TITL SYMMETRICAL REARRANGEMENT OF CATION-BINDING SITES OF
REMARK 1 TITL 2 PARVALBUMIN UPON CA2+(SLASH)MG2+ EXCHANGE. A STUDY BY 1H 2D
REMARK 1 TITL 3 NMR
REMARK 1 REF BIOCHEMISTRY V. 32 1302 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH A.PADILLA,G.W.VUISTER,R.BOELENS,G.KLEYWEGT,A.CAVE,J.PARELLO,
REMARK 1 AUTH 2 R.KAPTEIN
REMARK 1 TITL HOMONUCLEAR THREE-DIMENSIONAL 1H NMR SPECTROSCOPY OF PIKE
REMARK 1 TITL 2 PARVALBUMIN. COMPARISON OF SHORT-AND MEDIUM-RANGE NOES FROM
REMARK 1 TITL 3 2D AND 3D NMR
REMARK 1 REF J.AM.CHEM.SOC. V. 112 5024 1990
REMARK 1 REFN ISSN 0002-7863
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.PADILLA,A.CAVE,J.PARELLO
REMARK 1 TITL TWO-DIMENSIONAL 1H NUCLEAR MAGNETIC RESONANCE STUDY OF PIKE
REMARK 1 TITL 2 PI 5.0 PARVALBUMIN (ESOX LUCIUS): SEQUENTIAL RESONANCE
REMARK 1 TITL 3 ASSIGNMENTS AND FOLDING OF THE POLYPEPTIDE CHAIN
REMARK 1 REF J.MOL.BIOL. V. 204 995 1988
REMARK 1 REFN ISSN 0022-2836
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 2PAS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178439.
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 : 9
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: 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 6 -167.80 -115.95
REMARK 500 1 ALA A 8 -75.75 79.28
REMARK 500 1 LYS A 19 -31.84 -32.80
REMARK 500 1 ALA A 20 173.38 -47.06
REMARK 500 1 HIS A 26 -28.11 140.92
REMARK 500 1 ASP A 51 83.98 -60.72
REMARK 500 1 LEU A 67 38.11 -90.44
REMARK 500 1 LEU A 77 150.45 -41.10
REMARK 500 1 ASP A 79 -62.10 105.90
REMARK 500 1 ASP A 90 91.55 -66.08
REMARK 500 1 ILE A 99 -75.49 -72.18
REMARK 500 1 ASP A 100 -37.75 -37.24
REMARK 500 2 ALA A 20 174.07 -55.84
REMARK 500 2 HIS A 26 -39.16 97.68
REMARK 500 2 ALA A 40 -28.36 -36.27
REMARK 500 2 ASP A 51 83.18 -61.40
REMARK 500 2 VAL A 66 -32.75 -39.46
REMARK 500 2 LEU A 67 44.06 -103.77
REMARK 500 2 ALA A 71 117.63 -164.80
REMARK 500 2 ASP A 79 -62.15 121.33
REMARK 500 2 ILE A 99 -72.24 -72.01
REMARK 500 2 ASP A 100 -36.87 -37.53
REMARK 500 3 LYS A 7 37.79 -168.15
REMARK 500 3 ALA A 8 -122.26 -147.86
REMARK 500 3 HIS A 26 -34.97 -31.26
REMARK 500 3 LYS A 36 -27.51 -39.02
REMARK 500 3 ALA A 37 65.68 -177.04
REMARK 500 3 SER A 39 113.75 -172.79
REMARK 500 3 ALA A 40 -33.90 -32.98
REMARK 500 3 ALA A 54 54.00 36.56
REMARK 500 3 VAL A 66 -26.01 -37.46
REMARK 500 3 ALA A 71 125.98 -170.18
REMARK 500 3 ASP A 73 49.22 -149.35
REMARK 500 3 ASP A 76 108.22 66.90
REMARK 500 3 ASP A 79 -61.79 108.26
REMARK 500 3 LYS A 91 -52.99 173.74
REMARK 500 3 ILE A 99 -77.06 -70.03
REMARK 500 3 ASP A 100 -38.12 -39.94
REMARK 500 4 LYS A 7 40.55 162.96
REMARK 500 4 ALA A 8 -132.86 -146.11
REMARK 500 4 VAL A 18 40.73 -142.06
REMARK 500 4 ALA A 20 -172.41 -67.47
REMARK 500 4 ASN A 25 -87.37 -120.86
REMARK 500 4 HIS A 26 -28.33 170.98
REMARK 500 4 LEU A 35 -37.14 -36.69
REMARK 500 4 SER A 39 116.87 60.56
REMARK 500 4 ALA A 40 -25.97 -37.49
REMARK 500 4 ALA A 52 -47.94 -29.11
REMARK 500 4 ASP A 53 39.93 -87.35
REMARK 500 4 ALA A 54 35.60 29.35
REMARK 500
REMARK 500 THIS ENTRY HAS 153 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 75 0.22 SIDE CHAIN
REMARK 500 2 ARG A 75 0.29 SIDE CHAIN
REMARK 500 3 ARG A 75 0.09 SIDE CHAIN
REMARK 500 4 ARG A 75 0.15 SIDE CHAIN
REMARK 500 5 ARG A 75 0.25 SIDE CHAIN
REMARK 500 6 ARG A 75 0.19 SIDE CHAIN
REMARK 500 7 ARG A 75 0.12 SIDE CHAIN
REMARK 500 8 ARG A 75 0.28 SIDE CHAIN
REMARK 500 9 ARG A 75 0.26 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 110 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 51 OD1
REMARK 620 2 ASP A 53 OD1 65.4
REMARK 620 3 ASP A 53 OD2 109.8 44.4
REMARK 620 4 PHE A 57 O 57.2 113.3 146.6
REMARK 620 5 GLU A 62 OE2 78.0 78.5 88.4 59.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 111 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 90 OD1
REMARK 620 2 ASP A 92 OD1 67.7
REMARK 620 3 ASP A 94 OD1 63.3 54.7
REMARK 620 4 LYS A 96 O 94.0 119.4 65.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CD
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: EF
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 111
DBREF 2PAS A 2 109 UNP P02628 PRVA_ESOLU 1 108
SEQRES 1 A 110 ACE ALA ALA LYS ASP LEU LEU LYS ALA ASP ASP ILE LYS
SEQRES 2 A 110 LYS ALA LEU ASP ALA VAL LYS ALA GLU GLY SER PHE ASN
SEQRES 3 A 110 HIS LYS LYS PHE PHE ALA LEU VAL GLY LEU LYS ALA MET
SEQRES 4 A 110 SER ALA ASN ASP VAL LYS LYS VAL PHE LYS ALA ILE ASP
SEQRES 5 A 110 ALA ASP ALA SER GLY PHE ILE GLU GLU GLU GLU LEU LYS
SEQRES 6 A 110 PHE VAL LEU LYS SER PHE ALA ALA ASP GLY ARG ASP LEU
SEQRES 7 A 110 THR ASP ALA GLU THR LYS ALA PHE LEU LYS ALA ALA ASP
SEQRES 8 A 110 LYS ASP GLY ASP GLY LYS ILE GLY ILE ASP GLU PHE GLU
SEQRES 9 A 110 THR LEU VAL HIS GLU ALA
HET ACE A 0 3
HET CA A 110 1
HET CA A 111 1
HETNAM ACE ACETYL GROUP
HETNAM CA CALCIUM ION
FORMUL 1 ACE C2 H4 O
FORMUL 2 CA 2(CA 2+)
HELIX 1 A ASP A 9 VAL A 18 1 10
HELIX 2 B HIS A 26 VAL A 33 1 8
HELIX 3 C ALA A 40 ILE A 50 1 11
HELIX 4 D GLU A 60 ALA A 71 1BENDING AT RESIDUE 65 12
HELIX 5 E ASP A 79 ALA A 89 1 11
HELIX 6 F ILE A 99 GLU A 108 1 10
LINK C ACE A 0 N ALA A 1 1555 1555 1.31
LINK OD1 ASP A 51 CA CA A 110 1555 1555 2.93
LINK OD1 ASP A 53 CA CA A 110 1555 1555 2.47
LINK OD2 ASP A 53 CA CA A 110 1555 1555 3.05
LINK O PHE A 57 CA CA A 110 1555 1555 2.46
LINK OE2 GLU A 62 CA CA A 110 1555 1555 2.97
LINK OD1 ASP A 90 CA CA A 111 1555 1555 2.48
LINK OD1 ASP A 92 CA CA A 111 1555 1555 2.63
LINK OD1 ASP A 94 CA CA A 111 1555 1555 2.71
LINK O LYS A 96 CA CA A 111 1555 1555 2.88
SITE 1 CD 12 ASP A 51 ALA A 52 ASP A 53 ALA A 54
SITE 2 CD 12 SER A 55 GLY A 56 PHE A 57 ILE A 58
SITE 3 CD 12 GLU A 59 GLU A 60 GLU A 61 GLU A 62
SITE 1 EF 12 ASP A 90 LYS A 91 ASP A 92 GLY A 93
SITE 2 EF 12 ASP A 94 GLY A 95 LYS A 96 ILE A 97
SITE 3 EF 12 GLY A 98 ILE A 99 ASP A 100 GLU A 101
SITE 1 AC1 6 ASP A 51 ASP A 53 SER A 55 PHE A 57
SITE 2 AC1 6 GLU A 59 GLU A 62
SITE 1 AC2 6 ASP A 90 ASP A 92 ASP A 94 LYS A 96
SITE 2 AC2 6 ILE A 97 GLU A 101
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 - 16 20 Bytes