Header list of 1rw5.pdb file
Complete list - r 2 2 Bytes
HEADER HORMONE/GROWTH FACTOR 16-DEC-03 1RW5
TITLE SOLUTION STRUCTURE OF HUMAN PROLACTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLACTIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PRL;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PT7
KEYWDS FOUR HELIX BUNDLE, CYTOKINE, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.TEILUM,J.HOCH,J.A.MARTIAL,B.B.KRAGELUND
REVDAT 4 02-MAR-22 1RW5 1 REMARK
REVDAT 3 24-FEB-09 1RW5 1 VERSN
REVDAT 2 23-AUG-05 1RW5 1 JRNL REMARK
REVDAT 1 22-FEB-05 1RW5 0
JRNL AUTH K.TEILUM,J.C.HOCH,V.GOFFIN,S.KINET,J.A.MARTIAL,B.B.KRAGELUND
JRNL TITL SOLUTION STRUCTURE OF HUMAN PROLACTIN
JRNL REF J.MOL.BIOL. V. 351 810 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16045928
JRNL DOI 10.1016/J.JMB.2005.06.042
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, XPLOR-NIH 2.9
REMARK 3 AUTHORS : VARIAN (VNMR), SCHWIETERS,KUSZEWSKI,TJANDRA,CLORE
REMARK 3 (XPLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 2149 NOE
REMARK 3 DISTANCE CONTRAINTS, 320 DIHEDRAL ANGLE CONSTRAINTS, AND 81
REMARK 3 RESIDUAL DIPOLAR COUPLINGS
REMARK 4
REMARK 4 1RW5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000021082.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 8.05
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM HUMAN PROLACTIN, C-13, N-15,
REMARK 210 0.02% NAN3, 10% D2O, 90% H2O;
REMARK 210 1MM HUMAN PROLACTIN, C-13, N-15,
REMARK 210 0.02% NAN3, 100% D2O; 0.3MM
REMARK 210 HUMAN PROLACTIN, C-13, N-15,
REMARK 210 0.02% NAN3, 20% D2O, 80% H2O;
REMARK 210 0.3MM HUMAN PROLACTIN, C-13, N-
REMARK 210 15, 0.02% NAN3, 20% D2O, 80% H2O,
REMARK 210 6.2MG/ML PF1-PHAGE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPATATED_NOESY_ALIPHATIC_REGION; 3D_13C-SEPATATED_NOESY_
REMARK 210 AROMATIC_REGION; S3CT
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.2, PRONTO3D 20020517,
REMARK 210 CYANA 1.0.6, XPLOR-NIH 2.9
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 20 WITH THE LOWEST
REMARK 210 ENERGY OF THE STRUCTURES WITH NO
REMARK 210 RESTRAINT VIOLATIONS LARGER THAN
REMARK 210 0.4 A, 5 DEG, AND 1 HZ FOR NOE'S,
REMARK 210 TORSION ANGLES AND RDC'S
REMARK 210 RESPECTIVELY
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
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 11 -164.05 51.69
REMARK 500 1 HIS A 46 95.72 -52.41
REMARK 500 1 ALA A 54 86.83 -66.87
REMARK 500 1 CYS A 58 92.72 50.34
REMARK 500 1 MET A 75 -81.58 -62.29
REMARK 500 1 ALA A 111 -70.88 -55.37
REMARK 500 1 GLU A 145 54.25 -146.23
REMARK 500 1 PRO A 148 -172.66 -61.71
REMARK 500 1 VAL A 149 -169.98 -115.01
REMARK 500 1 MET A 158 97.20 -53.02
REMARK 500 1 ILE A 194 -52.49 -125.32
REMARK 500 1 ASN A 198 -164.42 -167.73
REMARK 500 2 CYS A 4 -53.40 168.02
REMARK 500 2 PRO A 5 154.81 -46.71
REMARK 500 2 ASP A 17 -72.33 -104.03
REMARK 500 2 ASN A 76 31.55 -162.84
REMARK 500 2 GLN A 77 -155.03 -120.64
REMARK 500 2 ALA A 111 -70.47 -53.43
REMARK 500 2 PRO A 148 -175.60 -60.45
REMARK 500 2 SER A 151 -42.96 -159.02
REMARK 500 2 SER A 155 88.47 51.37
REMARK 500 3 HIS A 46 97.51 -57.57
REMARK 500 3 ALA A 54 88.00 -65.29
REMARK 500 3 MET A 75 -72.04 -54.23
REMARK 500 3 ASN A 76 -168.82 52.50
REMARK 500 3 GLN A 77 -163.53 65.45
REMARK 500 3 ALA A 111 -71.44 -105.57
REMARK 500 3 PRO A 148 175.42 -56.90
REMARK 500 3 SER A 151 38.53 -169.99
REMARK 500 3 PRO A 154 108.27 -48.71
REMARK 500 3 SER A 155 98.30 59.52
REMARK 500 3 ASN A 198 43.65 -167.64
REMARK 500 4 CYS A 4 97.55 -171.58
REMARK 500 4 ARG A 43 -65.17 -99.82
REMARK 500 4 HIS A 46 95.62 -53.92
REMARK 500 4 ALA A 54 89.05 -65.45
REMARK 500 4 ALA A 64 43.59 -93.41
REMARK 500 4 ALA A 111 -70.54 -57.87
REMARK 500 4 ASN A 144 17.18 -141.10
REMARK 500 4 MET A 158 99.53 -49.50
REMARK 500 4 ASN A 197 94.36 -69.59
REMARK 500 4 ASN A 198 30.77 -145.32
REMARK 500 5 HIS A 46 88.48 -59.82
REMARK 500 5 ALA A 54 89.55 -65.95
REMARK 500 5 ALA A 64 30.08 -98.01
REMARK 500 5 PRO A 109 -71.13 -86.63
REMARK 500 5 ALA A 111 -70.60 -88.59
REMARK 500 5 SER A 155 90.56 52.32
REMARK 500 5 GLU A 161 -72.96 -71.37
REMARK 500 5 ASN A 198 31.62 -167.40
REMARK 500
REMARK 500 THIS ENTRY HAS 214 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6643 RELATED DB: BMRB
DBREF 1RW5 A 1 199 UNP P01236 PRL_HUMAN 29 227
SEQRES 1 A 199 LEU PRO ILE CYS PRO GLY GLY ALA ALA ARG CYS GLN VAL
SEQRES 2 A 199 THR LEU ARG ASP LEU PHE ASP ARG ALA VAL VAL LEU SER
SEQRES 3 A 199 HIS TYR ILE HIS ASN LEU SER SER GLU MET PHE SER GLU
SEQRES 4 A 199 PHE ASP LYS ARG TYR THR HIS GLY ARG GLY PHE ILE THR
SEQRES 5 A 199 LYS ALA ILE ASN SER CYS HIS THR SER SER LEU ALA THR
SEQRES 6 A 199 PRO GLU ASP LYS GLU GLN ALA GLN GLN MET ASN GLN LYS
SEQRES 7 A 199 ASP PHE LEU SER LEU ILE VAL SER ILE LEU ARG SER TRP
SEQRES 8 A 199 ASN GLU PRO LEU TYR HIS LEU VAL THR GLU VAL ARG GLY
SEQRES 9 A 199 MET GLN GLU ALA PRO GLU ALA ILE LEU SER LYS ALA VAL
SEQRES 10 A 199 GLU ILE GLU GLU GLN THR LYS ARG LEU LEU GLU GLY MET
SEQRES 11 A 199 GLU LEU ILE VAL SER GLN VAL HIS PRO GLU THR LYS GLU
SEQRES 12 A 199 ASN GLU ILE TYR PRO VAL TRP SER GLY LEU PRO SER LEU
SEQRES 13 A 199 GLN MET ALA ASP GLU GLU SER ARG LEU SER ALA TYR TYR
SEQRES 14 A 199 ASN LEU LEU HIS CYS LEU ARG ARG ASP SER HIS LYS ILE
SEQRES 15 A 199 ASP ASN TYR LEU LYS LEU LEU LYS CYS ARG ILE ILE HIS
SEQRES 16 A 199 ASN ASN ASN CYS
HELIX 1 1 THR A 14 LYS A 42 1 29
HELIX 2 2 CYS A 58 LEU A 63 5 6
HELIX 3 3 ASP A 68 ASN A 76 1 9
HELIX 4 4 LYS A 78 GLY A 104 1 27
HELIX 5 5 GLU A 110 HIS A 138 1 29
HELIX 6 6 ASP A 160 ILE A 194 1 35
SSBOND 1 CYS A 4 CYS A 11 1555 1555 2.02
SSBOND 2 CYS A 58 CYS A 174 1555 1555 2.02
SSBOND 3 CYS A 191 CYS A 199 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