Header list of 1xhh.pdb file
Complete list - r 2 2 Bytes
HEADER UNKNOWN FUNCTION 20-SEP-04 1XHH
TITLE SOLUTION STRUCTURE OF PORCINE BETA-MICROSEMINOPROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-MICROSEMINOPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS BETA SRANDS, NOVEL FOLD, BETA-MICROSEMINOPROTEIN, PROSTATIC SECRETORY
KEYWDS 2 PROTEIN, SOLUTION STRUCTURE, NA+, K+ ATPASE INHIBITOR, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.WANG,Y.C.LOU,K.P.WU,S.H.WU,W.C.CHANG,C.CHEN
REVDAT 3 02-MAR-22 1XHH 1 REMARK
REVDAT 2 24-FEB-09 1XHH 1 VERSN
REVDAT 1 20-MAR-05 1XHH 0
JRNL AUTH I.WANG,Y.C.LOU,K.P.WU,S.H.WU,W.C.CHANG,C.CHEN
JRNL TITL NOVEL SOLUTION STRUCTURE OF PORCINE BETA-MICROSEMINOPROTEIN
JRNL REF J.MOL.BIOL. V. 346 1071 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15701518
JRNL DOI 10.1016/J.JMB.2004.12.029
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, X-PLOR-NIH 2.9.4A
REMARK 3 AUTHORS : BRUKER (XWINNMR), SCHWIETERS, C.D. (X-PLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XHH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1000030366.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5MM BETA-MICROSEMINOPROTEIN U
REMARK 210 -15N, 13C; 50MM PHOSPHATE, 150MM
REMARK 210 NACL BUFFER; 1.5MM BETA-
REMARK 210 MICROSEMINOPROTEIN U-15N, 13C;
REMARK 210 50MM PHOSPHATE, 150MM NACL BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 3.1.6, X-PLOR-NIH 2.9.4A
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR TECHNIQUES
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 HG1 THR A 31 O GLU A 35 1.42
REMARK 500 O LYS A 11 H ASN A 13 1.48
REMARK 500 OG1 THR A 31 H GLU A 35 1.49
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 CYS A 2 168.83 54.72
REMARK 500 1 ASN A 7 105.57 -53.58
REMARK 500 1 PRO A 12 52.25 -62.42
REMARK 500 1 ASN A 13 39.73 -171.39
REMARK 500 1 LEU A 18 -145.22 51.55
REMARK 500 1 SER A 22 92.78 168.29
REMARK 500 1 ASN A 26 -57.92 -157.13
REMARK 500 1 SER A 27 -160.63 -178.60
REMARK 500 1 ASP A 33 57.43 -172.07
REMARK 500 1 CYS A 34 -52.86 -150.25
REMARK 500 1 GLN A 41 -6.80 -55.82
REMARK 500 1 THR A 58 77.95 -67.00
REMARK 500 1 LYS A 60 54.74 -170.83
REMARK 500 1 CYS A 70 73.76 52.71
REMARK 500 1 ASP A 79 71.11 -158.67
REMARK 500 1 PRO A 80 27.48 -65.08
REMARK 500 1 CYS A 84 -163.44 -77.35
REMARK 500 1 THR A 87 -48.26 -140.65
REMARK 500 2 CYS A 2 173.69 54.66
REMARK 500 2 ASN A 7 157.71 -49.28
REMARK 500 2 PRO A 12 45.94 -62.96
REMARK 500 2 ASN A 13 42.67 -171.81
REMARK 500 2 LEU A 18 -152.30 47.04
REMARK 500 2 SER A 22 110.54 -172.68
REMARK 500 2 ASP A 33 65.08 -170.58
REMARK 500 2 CYS A 34 -50.95 -150.81
REMARK 500 2 LYS A 60 27.41 -175.57
REMARK 500 2 CYS A 70 72.86 51.64
REMARK 500 2 ASP A 79 70.86 -155.15
REMARK 500 2 THR A 87 -34.41 -141.08
REMARK 500 3 CYS A 2 176.14 59.44
REMARK 500 3 SER A 9 175.45 -51.10
REMARK 500 3 PRO A 12 -166.28 -54.89
REMARK 500 3 CYS A 15 74.73 -151.92
REMARK 500 3 LEU A 18 -152.51 50.50
REMARK 500 3 SER A 22 96.95 -176.52
REMARK 500 3 ASN A 26 -71.92 -164.96
REMARK 500 3 SER A 27 -157.03 -167.08
REMARK 500 3 LYS A 32 63.72 -66.20
REMARK 500 3 ASP A 33 7.29 52.86
REMARK 500 3 GLN A 41 -88.30 -49.66
REMARK 500 3 ALA A 51 168.74 52.89
REMARK 500 3 THR A 58 69.44 -68.07
REMARK 500 3 LYS A 60 49.12 -161.21
REMARK 500 3 CYS A 70 71.47 46.68
REMARK 500 3 ASP A 79 71.09 -156.95
REMARK 500 3 PRO A 80 4.63 -65.09
REMARK 500 4 LEU A 10 -74.48 -90.48
REMARK 500 4 LYS A 11 154.81 56.46
REMARK 500 4 ASN A 13 73.19 174.75
REMARK 500
REMARK 500 THIS ENTRY HAS 312 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5565 RELATED DB: BMRB
REMARK 900 THE SAME PROTEIN WITH THE SECONDARY STRUCTURE ASSIGNMENT.
DBREF 1XHH A 1 91 UNP O02826 MSMB_PIG 1 91
SEQADV 1XHH GLN A 1 UNP O02826 PCA 1 SEE REMARK 999
SEQRES 1 A 91 GLN CYS TYR PHE ILE PRO ASN GLN SER LEU LYS PRO ASN
SEQRES 2 A 91 GLU CYS GLN ASP LEU LYS GLY VAL SER HIS PRO LEU ASN
SEQRES 3 A 91 SER VAL TRP LYS THR LYS ASP CYS GLU GLU CYS THR CYS
SEQRES 4 A 91 GLY GLN ASP ALA ILE SER CYS CYS ASN THR ALA ALA ILE
SEQRES 5 A 91 PRO THR GLY TYR ASP THR ASN LYS CYS GLN LYS ILE LEU
SEQRES 6 A 91 ASN LYS LYS THR CYS THR TYR THR VAL VAL GLU LYS LYS
SEQRES 7 A 91 ASP PRO GLY LYS THR CYS ASP VAL THR GLY TRP VAL LEU
SHEET 1 A 4 TYR A 3 PRO A 6 0
SHEET 2 A 4 ALA A 43 ASN A 48 -1 O CYS A 46 N TYR A 3
SHEET 3 A 4 GLU A 35 CYS A 39 -1 N GLU A 36 O CYS A 47
SHEET 4 A 4 TRP A 29 LYS A 30 -1 N TRP A 29 O CYS A 37
SHEET 1 B 2 GLU A 14 ASP A 17 0
SHEET 2 B 2 VAL A 21 PRO A 24 -1 O HIS A 23 N CYS A 15
SHEET 1 C 2 ILE A 52 THR A 54 0
SHEET 2 C 2 GLY A 88 VAL A 90 -1 O VAL A 90 N ILE A 52
SHEET 1 D 3 CYS A 61 ASN A 66 0
SHEET 2 D 3 THR A 71 GLU A 76 -1 O THR A 73 N ILE A 64
SHEET 3 D 3 ASP A 79 THR A 83 -1 O ASP A 79 N GLU A 76
SSBOND 1 CYS A 2 CYS A 47 1555 1555 2.02
SSBOND 2 CYS A 15 CYS A 39 1555 1555 2.02
SSBOND 3 CYS A 34 CYS A 70 1555 1555 2.02
SSBOND 4 CYS A 37 CYS A 46 1555 1555 2.02
SSBOND 5 CYS A 61 CYS A 84 1555 1555 2.02
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