Header list of 1sgo.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 24-FEB-04 1SGO
TITLE NMR STRUCTURE OF THE HUMAN C14ORF129 GENE PRODUCT, HSPC210. NORTHEAST
TITLE 2 STRUCTURAL GENOMICS TARGET HR969.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN C14ORF129;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HSPC210;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: C14ORF129;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(LAMDA DE3)PMGK;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET14
KEYWDS HR969, HUMAN PROTEIN, NESG, STRUCTURAL GENOMICS, HS.4104 HOMO
KEYWDS 2 SAPIENS, NESG CLUSTER ID 18152., PSI, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 3 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.A.RAMELOT,J.R.CORT,R.XIAO,L.-Y.SHIH,L.-C.MA,T.B.ACTON,
AUTHOR 2 G.T.MONTELIONE,M.A.KENNEDY,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (NESG)
REVDAT 4 02-MAR-22 1SGO 1 REMARK
REVDAT 3 24-FEB-09 1SGO 1 VERSN
REVDAT 2 25-JAN-05 1SGO 1 AUTHOR KEYWDS REMARK
REVDAT 1 04-MAY-04 1SGO 0
JRNL AUTH T.A.RAMELOT,J.R.CORT,R.XIAO,L.-Y.SHIH,L.-C.MA,T.B.ACTON,
JRNL AUTH 2 G.T.MONTELIONE,M.A.KENNEDY
JRNL TITL NMR STRUCTURE OF THE HUMAN C14ORF129 GENE PRODUCT, HSPC210.
JRNL TITL 2 NORTHEAST STRUCTURAL GENOMICS TARGET HR969.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SPARKY 3.98, CNS 1.1
REMARK 3 AUTHORS : T.D. GODDARD, D.G. KNELLER (SPARKY), A. BRUNGER
REMARK 3 (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1132 RESTRAINTS. SUMMARY OF
REMARK 3 EXPERIMENTAL CONSTRAINTS: DISTANCE RESTRAINTS: TOTAL = 1000; INTRA-
REMARK 3 RESIDUE [I=J] = 23; SEQUENTIAL [(I-J)=1] = 239; MEDIUM RANGE [1<(I-
REMARK 3 J)<5] = 304; LONG RANGE [(I-J)>=5] = 382; HYDROGEN BOND RESTRAINTS
REMARK 3 = 52 (2 PER H-BOND); NUMBER OF DISTANCE RESTRAINTS PER RESIDUE =
REMARK 3 9.7 (RESIDES 33-135); DIHEDRAL-ANGLE RESTRAINTS = 132 (66 PHI, 66
REMARK 3 PSI); TOTAL NUMBER OF RESTRAINTS PER RESIDUE = 10.3 (RESIDES 33-
REMARK 3 135); NUMBER OF LONG RANGE RESTRA
REMARK 3 NTS PER RESIDUE = 3.7; NUMBER OF STRUCTURES COMPUTED = 20; NUMBER
REMARK 3 OF STRUCTURES USED = 20. AVERAGE DISTANCE VIOLATIONS >0.1 ANG =
REMARK 3 2.3; AVERAGE R.M.S. DISTANCE VIOLATION = 0.011 ANG; MAXIMUM NUMBER
REMARK 3 OF DISTANCE VIOLATIONS 4. AVERAGE DIHEDRAL ANGLE VIOLATIONS: >1
REMARK 3 DEG = 1.5; MAX NUMBER OF DIHEDRAL ANGLE VIOLATIONS = 4; AVERAGE
REMARK 3 R.M.S. ANGLE VIOLATION = 0.17 DEG. RMSD VALUES: BACKBONE ATOMS (N,
REMARK 3 C,C',O, RESIDUES 33-135) = 0.67 ANG; ALL HEAVY ATOMS = 1.21 ANG;
REMARK 3 PROCHECK (RESDIUES 31-135): MOST FAVORED
REMARK 3 EGIONS = 86%; ADDITIONAL ALLOWED REGIONS = 13%; GENEROUSLY ALLOWED
REMARK 3 REGIONS = 1%; DISALLOWED REGIONS = 0%.
REMARK 3
REMARK 3 THE UNSTRUCTURED 10 RESIDUE N-TERMINAL HIS TAG (MGHHHHHHSH) WAS
REMARK 3 NOT INCLUDED IN THE STRUCTURE CALCULATION.
REMARK 4
REMARK 4 1SGO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021693.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM HSPC210, U-15N, 13C; 20 MM
REMARK 210 MES, 100 MM NACL, 10 MM DTT, 5
REMARK 210 MM CACL2, 0.02% NAN3; 1MM
REMARK 210 HSPC210, U-15N, 13C; 20 MM MES,
REMARK 210 100 MM NACL, 10 MM DTT, 5 MM
REMARK 210 CACL2, 0.02% NAN3; 1MM HSPC210,
REMARK 210 U-15N, 5%-13C; 20 MM MES, 100 MM
REMARK 210 NACL, 10 MM DTT, 5 MM CACL2,
REMARK 210 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA; 4D_13C-
REMARK 210 SEPARATED_NOESY; 13C_HSQC; H/D
REMARK 210 EXCHANGE
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, AUTOSTRUCTURE 1.1.2,
REMARK 210 TALOS 199.019.15.27, X-PLOR
REMARK 210 XPLOR-NIH-2.0.6, VNMR 6.1C
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
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: 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 OE1 GLU A 131 HZ3 LYS A 134 1.55
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 PRO A 7 -158.30 -97.53
REMARK 500 1 LEU A 57 -93.82 -135.12
REMARK 500 1 CYS A 59 112.89 -164.88
REMARK 500 1 ASP A 61 -71.28 68.13
REMARK 500 1 GLN A 100 30.46 -94.14
REMARK 500 1 LEU A 110 -60.76 -96.62
REMARK 500 2 PRO A 7 -158.15 -91.48
REMARK 500 2 MET A 8 -149.88 -96.66
REMARK 500 2 LEU A 10 -47.38 75.62
REMARK 500 2 SER A 12 -176.00 67.31
REMARK 500 2 LYS A 31 112.21 -162.41
REMARK 500 2 VAL A 48 -168.20 -122.45
REMARK 500 2 LEU A 57 -102.70 -127.84
REMARK 500 2 ASP A 61 -4.96 74.62
REMARK 500 2 ALA A 91 -155.23 -174.91
REMARK 500 3 ASP A 4 -97.21 -113.54
REMARK 500 3 CYS A 5 -56.99 -167.29
REMARK 500 3 GLU A 17 -80.79 -123.08
REMARK 500 3 GLU A 21 118.67 69.77
REMARK 500 3 LEU A 22 86.31 61.80
REMARK 500 3 VAL A 48 -168.73 -119.30
REMARK 500 3 LEU A 57 -163.56 -122.75
REMARK 500 3 CYS A 59 84.21 -157.75
REMARK 500 3 ASP A 61 -56.54 -166.85
REMARK 500 4 PRO A 7 -73.45 -71.89
REMARK 500 4 SER A 14 102.52 -58.52
REMARK 500 4 LEU A 22 -57.61 -139.94
REMARK 500 4 VAL A 48 -168.63 -122.71
REMARK 500 4 MET A 51 118.62 -164.90
REMARK 500 4 LEU A 57 -157.20 -135.94
REMARK 500 4 ASP A 61 -83.51 61.77
REMARK 500 5 MET A 8 -156.26 -136.52
REMARK 500 5 SER A 11 80.54 -161.31
REMARK 500 5 PHE A 16 18.02 -147.33
REMARK 500 5 ASN A 23 -55.63 71.16
REMARK 500 5 THR A 28 93.30 66.85
REMARK 500 5 MET A 30 -95.51 68.01
REMARK 500 5 VAL A 48 -167.70 -125.54
REMARK 500 5 LEU A 57 -93.34 -120.83
REMARK 500 5 CYS A 59 155.94 176.74
REMARK 500 5 ALA A 60 -80.30 -172.36
REMARK 500 5 ASP A 61 -52.78 -121.95
REMARK 500 5 GLN A 100 42.44 -93.25
REMARK 500 6 ASP A 4 -98.98 64.52
REMARK 500 6 CYS A 5 -31.48 167.78
REMARK 500 6 ASN A 6 65.05 60.63
REMARK 500 6 SER A 14 79.81 59.05
REMARK 500 6 LEU A 22 -79.69 -71.29
REMARK 500 6 THR A 28 -73.26 73.05
REMARK 500 6 VAL A 48 -167.98 -119.89
REMARK 500
REMARK 500 THIS ENTRY HAS 187 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HR969 RELATED DB: TARGETDB
DBREF 1SGO A 1 139 UNP Q9P0R6 CN129_HUMAN 1 139
SEQRES 1 A 139 MET GLU THR ASP CYS ASN PRO MET GLU LEU SER SER MET
SEQRES 2 A 139 SER GLY PHE GLU GLU GLY SER GLU LEU ASN GLY PHE GLU
SEQRES 3 A 139 GLY THR ASP MET LYS ASP MET ARG LEU GLU ALA GLU ALA
SEQRES 4 A 139 VAL VAL ASN ASP VAL LEU PHE ALA VAL ASN ASN MET PHE
SEQRES 5 A 139 VAL SER LYS SER LEU ARG CYS ALA ASP ASP VAL ALA TYR
SEQRES 6 A 139 ILE ASN VAL GLU THR LYS GLU ARG ASN ARG TYR CYS LEU
SEQRES 7 A 139 GLU LEU THR GLU ALA GLY LEU LYS VAL VAL GLY TYR ALA
SEQRES 8 A 139 PHE ASP GLN VAL ASP ASP HIS LEU GLN THR PRO TYR HIS
SEQRES 9 A 139 GLU THR VAL TYR SER LEU LEU ASP THR LEU SER PRO ALA
SEQRES 10 A 139 TYR ARG GLU ALA PHE GLY ASN ALA LEU LEU GLN ARG LEU
SEQRES 11 A 139 GLU ALA LEU LYS ARG ASP GLY GLN SER
HELIX 1 1 ASP A 32 LEU A 45 1 14
HELIX 2 2 PHE A 46 VAL A 48 5 3
HELIX 3 3 VAL A 107 SER A 115 1 9
HELIX 4 4 SER A 115 ASP A 136 1 22
SHEET 1 A 3 ASN A 50 VAL A 53 0
SHEET 2 A 3 VAL A 63 GLU A 69 -1 O ASN A 67 N PHE A 52
SHEET 3 A 3 CYS A 59 ALA A 60 -1 N ALA A 60 O VAL A 63
SHEET 1 B 5 ASN A 50 VAL A 53 0
SHEET 2 B 5 VAL A 63 GLU A 69 -1 O ASN A 67 N PHE A 52
SHEET 3 B 5 ARG A 75 THR A 81 -1 O LEU A 78 N ILE A 66
SHEET 4 B 5 GLY A 84 GLY A 89 -1 O LYS A 86 N GLU A 79
SHEET 5 B 5 TYR A 103 HIS A 104 -1 O HIS A 104 N LEU A 85
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