Header list of 1psy.pdb file
Complete list - r 2 2 Bytes
HEADER PLANT PROTEIN 22-JUN-03 1PSY
TITLE STRUCTURE OF RICC3, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2S ALBUMIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RICC3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RICINUS COMMUNIS;
SOURCE 3 ORGANISM_COMMON: CASTOR BEAN;
SOURCE 4 ORGANISM_TAXID: 3988
KEYWDS RICC3, ALBUMIN SEED PROTEIN, SEED STORAGE PROTEIN, PLANT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.PANTOJA-UCEDA,M.BRUIX,G.GIMENEZ-GALLEGO,M.RICO,J.SANTORO
REVDAT 3 02-MAR-22 1PSY 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1PSY 1 VERSN
REVDAT 1 13-JAN-04 1PSY 0
JRNL AUTH D.PANTOJA-UCEDA,M.BRUIX,G.GIMENEZ-GALLEGO,M.RICO,J.SANTORO
JRNL TITL SOLUTION STRUCTURE OF RICC3, A 2S ALBUMIN STORAGE PROTEIN
JRNL TITL 2 FROM RICINUS COMMUNIS.
JRNL REF BIOCHEMISTRY V. 42 13839 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14636051
JRNL DOI 10.1021/BI0352217
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, AMBER 7
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PSY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019547.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 2MM RICC3 15N; 10MM SODIUM
REMARK 210 PHOSPHATE BUFFER ;95% H2O, 5%
REMARK 210 D2O; 2MM RICC3 10MM SODIUM
REMARK 210 PHOSPHATE BUFFER ;95% H2O, 5%
REMARK 210 D2O; 2MM RICC3 10MM SODIUM
REMARK 210 PHOSPHATE BUFFER ;100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.0.4, DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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 HG SER A 14 H ARG A 19 0.90
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 CYS A 77 CA - CB - SG ANGL. DEV. = 6.6 DEGREES
REMARK 500 2 GLU A 11 OE1 - CD - OE2 ANGL. DEV. = -11.3 DEGREES
REMARK 500 11 ASP A 75 CB - CG - OD2 ANGL. DEV. = -5.7 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 1 PHE A 3 101.15 -172.76
REMARK 500 1 SER A 6 136.81 173.88
REMARK 500 1 SER A 13 -83.55 -116.71
REMARK 500 1 SER A 14 -157.56 -63.73
REMARK 500 1 SER A 15 -153.59 -59.78
REMARK 500 1 GLN A 17 48.93 -161.65
REMARK 500 1 ARG A 19 -36.73 -37.22
REMARK 500 1 GLN A 20 -78.69 -56.02
REMARK 500 1 GLN A 23 32.43 -76.49
REMARK 500 1 ARG A 24 -46.92 -148.03
REMARK 500 1 LYS A 25 -73.78 -115.61
REMARK 500 1 ASP A 26 150.23 -46.13
REMARK 500 1 LEU A 27 84.50 -5.16
REMARK 500 1 SER A 28 25.77 -140.36
REMARK 500 1 SER A 29 -31.91 -174.67
REMARK 500 1 SER A 38 143.40 -171.25
REMARK 500 1 SER A 39 150.93 -45.24
REMARK 500 1 SER A 42 -156.21 -164.27
REMARK 500 1 VAL A 47 59.31 -150.89
REMARK 500 1 GLN A 57 92.28 -64.24
REMARK 500 1 GLN A 58 138.88 177.11
REMARK 500 1 GLU A 59 96.58 -48.59
REMARK 500 1 SER A 60 56.92 -168.48
REMARK 500 1 ASP A 75 -44.80 156.10
REMARK 500 1 TYR A 84 -64.79 -102.19
REMARK 500 1 ALA A 86 48.12 -76.21
REMARK 500 1 GLU A 87 -51.13 -172.93
REMARK 500 1 GLN A 94 47.51 -82.25
REMARK 500 1 GLU A 98 33.13 -165.74
REMARK 500 1 SER A 113 -77.76 -72.29
REMARK 500 1 CYS A 114 34.12 -153.23
REMARK 500 1 VAL A 116 98.22 -69.10
REMARK 500 1 ARG A 117 -93.33 -141.54
REMARK 500 1 ARG A 120 -48.69 -157.11
REMARK 500 1 THR A 124 -47.14 -136.18
REMARK 500 2 MET A 4 131.26 171.51
REMARK 500 2 SER A 6 160.02 167.60
REMARK 500 2 LYS A 7 158.35 173.65
REMARK 500 2 SER A 13 37.29 179.44
REMARK 500 2 SER A 15 -174.85 -61.98
REMARK 500 2 GLN A 17 40.37 -175.86
REMARK 500 2 GLN A 23 37.85 -80.94
REMARK 500 2 ARG A 24 -44.85 -150.28
REMARK 500 2 LYS A 25 -72.69 -126.57
REMARK 500 2 LEU A 27 82.79 -4.17
REMARK 500 2 SER A 28 33.26 -142.87
REMARK 500 2 SER A 29 -32.17 -177.08
REMARK 500 2 GLN A 36 -166.14 -77.88
REMARK 500 2 SER A 37 -150.05 -82.75
REMARK 500 2 SER A 38 51.51 -113.76
REMARK 500
REMARK 500 THIS ENTRY HAS 725 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 2 GLU A 11 0.10 SIDE CHAIN
REMARK 500 8 TYR A 84 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PSY A 1 125 UNP P01089 2SS_RICCO 32 156
SEQADV 1PSY ALA A 1 UNP P01089 ILE 32 CONFLICT
SEQADV 1PSY PHE A 3 UNP P01089 ILE 34 CONFLICT
SEQADV 1PSY MET A 4 UNP P01089 ASP 35 CONFLICT
SEQRES 1 A 125 ALA GLU PHE MET GLU SER LYS GLY GLU ARG GLU GLY SER
SEQRES 2 A 125 SER SER GLN GLN CYS ARG GLN GLU VAL GLN ARG LYS ASP
SEQRES 3 A 125 LEU SER SER CYS GLU ARG TYR LEU ARG GLN SER SER SER
SEQRES 4 A 125 ARG ARG SER THR GLY GLU GLU VAL LEU ARG MET PRO GLY
SEQRES 5 A 125 ASP GLU ASN GLN GLN GLN GLU SER GLN GLN LEU GLN GLN
SEQRES 6 A 125 CYS CYS ASN GLN VAL LYS GLN VAL ARG ASP GLU CYS GLN
SEQRES 7 A 125 CYS GLU ALA ILE LYS TYR ILE ALA GLU ASP GLN ILE GLN
SEQRES 8 A 125 GLN GLY GLN LEU HIS GLY GLU GLU SER GLU ARG VAL ALA
SEQRES 9 A 125 GLN ARG ALA GLY GLU ILE VAL SER SER CYS GLY VAL ARG
SEQRES 10 A 125 CYS MET ARG GLN THR ARG THR ASN
HELIX 1 1 GLN A 17 GLN A 23 1 7
HELIX 2 2 SER A 29 GLN A 36 1 8
HELIX 3 3 SER A 60 LYS A 71 1 12
HELIX 4 4 GLU A 76 GLY A 93 1 18
HELIX 5 5 SER A 100 GLY A 115 1 16
SSBOND 1 CYS A 18 CYS A 77 1555 1555 2.01
SSBOND 2 CYS A 30 CYS A 66 1555 1555 2.01
SSBOND 3 CYS A 67 CYS A 114 1555 1555 2.04
SSBOND 4 CYS A 79 CYS A 118 1555 1555 2.09
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