Header list of 1l5c.pdb file
Complete list - t 27 2 Bytes
HEADER HORMONE/GROWTH FACTOR 06-MAR-02 1L5C
TITLE SOLUTION STRUCTURE OF THE MONOMERIC FORM OF A MUTANT UNLIGANDED BOVINE
TITLE 2 NEUROPHYSIN, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NEUROPHYSIN 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE)PLYS-S;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: T7
KEYWDS NMR ANALYSIS NEUROPHYSIN MONOMER, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.L.NGUYEN,E.BRESLOW
REVDAT 4 27-OCT-21 1L5C 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1L5C 1 VERSN
REVDAT 2 15-MAY-02 1L5C 1 JRNL
REVDAT 1 20-MAR-02 1L5C 0
JRNL AUTH T.L.NGUYEN,E.BRESLOW
JRNL TITL NMR ANALYSIS OF THE MONOMERIC FORM OF A MUTANT UNLIGANDED
JRNL TITL 2 BOVINE NEUROPHYSIN: COMPARISON WITH THE CRYSTAL STRUCTURE OF
JRNL TITL 3 A NEUROPHYSIN DIMER.
JRNL REF BIOCHEMISTRY V. 41 5920 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11980496
JRNL DOI 10.1021/BI012067K
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, CNS 0.9
REMARK 3 AUTHORS : BAX (NMRPIPE), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 811 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS, 50 HYDROGEN BOND DISTANCE
REMARK 3 RESTRAINTS, 72 TORSION ANGLE CONSTRAINTS, 46 JNHA COUPLING
REMARK 3 CONSTANTS, 157 CA/CB AND 108 1H CHEMICAL SHIFT RESTRAINTS AND
REMARK 3 THE PAIRING OF THE PROTEIN'S 7 DISULFIDES.
REMARK 4
REMARK 4 1L5C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015654.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283; 298; 303
REMARK 210 PH : 7.5; 7.5; 7.5
REMARK 210 IONIC STRENGTH : NULL; NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.4 MM H80E OF BOVINE
REMARK 210 NEUROPHYSIN I U-15N; 90% H2O, 10%
REMARK 210 D20; 1.4 MM H80E OF BOVINE
REMARK 210 NEUROPHYSIN I U-15N, 13C; 90%
REMARK 210 H20, 10% D2O; 0.7 MM DES1-5 H80E
REMARK 210 OF BOVINE NEUROPHYSIN I U-15N;
REMARK 210 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 4.1, CNS 0.9, TALOS
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 : 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 O LYS A 59 H CYS A 67 1.48
REMARK 500 O ALA A 69 H ILE A 72 1.56
REMARK 500 O ALA A 90 H SER A 92 1.59
REMARK 500 O GLU A 80 OD2 ASP A 82 2.07
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 ASP A 4 -76.57 -83.18
REMARK 500 1 LEU A 5 -136.56 -146.35
REMARK 500 1 ARG A 8 -164.76 -67.65
REMARK 500 1 THR A 9 98.30 46.75
REMARK 500 1 CYS A 10 -169.89 -50.56
REMARK 500 1 PRO A 12 -169.75 -62.55
REMARK 500 1 PHE A 22 -101.98 -120.96
REMARK 500 1 PRO A 24 -119.12 -99.70
REMARK 500 1 LEU A 32 33.17 -157.84
REMARK 500 1 LEU A 42 -19.15 -47.87
REMARK 500 1 ASN A 48 20.35 -141.14
REMARK 500 1 PRO A 51 100.16 -45.69
REMARK 500 1 PRO A 60 159.41 -40.01
REMARK 500 1 SER A 63 57.29 -90.27
REMARK 500 1 ALA A 68 -96.10 -159.97
REMARK 500 1 ALA A 69 -169.81 -75.90
REMARK 500 1 ALA A 70 97.46 -38.16
REMARK 500 1 GLU A 81 94.29 -61.92
REMARK 500 1 PRO A 83 -3.25 -59.83
REMARK 500 1 ASP A 86 -26.15 171.18
REMARK 500 1 PRO A 87 -70.46 -103.10
REMARK 500 1 ALA A 89 -157.60 -75.67
REMARK 500 1 ALA A 90 -178.32 -69.79
REMARK 500 2 ASP A 4 -122.69 -81.33
REMARK 500 2 LEU A 5 -139.44 -94.97
REMARK 500 2 THR A 9 74.38 -173.35
REMARK 500 2 CYS A 10 -75.15 -65.49
REMARK 500 2 PHE A 22 -69.52 -138.99
REMARK 500 2 LEU A 32 35.72 -154.24
REMARK 500 2 TYR A 49 44.88 -160.30
REMARK 500 2 PRO A 51 179.24 -48.43
REMARK 500 2 CYS A 54 -164.54 -119.33
REMARK 500 2 GLN A 55 175.32 53.03
REMARK 500 2 PRO A 60 155.61 -37.23
REMARK 500 2 SER A 63 54.55 -90.34
REMARK 500 2 ALA A 68 -94.57 -165.76
REMARK 500 2 ALA A 69 -169.70 -77.46
REMARK 500 2 ALA A 70 96.21 -39.07
REMARK 500 2 GLU A 81 93.14 -65.89
REMARK 500 2 ASP A 86 -26.33 171.67
REMARK 500 2 PRO A 87 -70.31 -102.18
REMARK 500 2 ALA A 89 -157.81 -76.19
REMARK 500 3 ASP A 4 -136.27 -82.04
REMARK 500 3 LEU A 5 -124.50 -94.87
REMARK 500 3 ARG A 8 -162.98 -74.80
REMARK 500 3 THR A 9 103.07 41.38
REMARK 500 3 CYS A 10 -83.84 -63.66
REMARK 500 3 PRO A 12 -175.75 -68.69
REMARK 500 3 LEU A 32 31.49 -144.16
REMARK 500 3 THR A 38 -168.24 -70.13
REMARK 500
REMARK 500 THIS ENTRY HAS 413 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1NPO RELATED DB: PDB
REMARK 900 BOVINE NEUROPHYSIN II COMPLEX WITH OXYTOCIN
REMARK 900 RELATED ID: 2BN2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BOVINE NEUROPHYSIN II COMPLEXED WITH THE
REMARK 900 VASOPRESSIN ANALOGUE PHE-TYR AMIDE
REMARK 900 RELATED ID: 1L5D RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE MONOMERIC FORM OF A MUTANT UNLIGANDED
REMARK 900 BOVINE NEUROPHYSIN, MINIMIZED AVERAGE STRUCTURE
DBREF 1L5C A 1 92 UNP P01175 NEU1_BOVIN 32 123
SEQADV 1L5C GLU A 80 UNP P01175 HIS 111 ENGINEERED MUTATION
SEQRES 1 A 92 ALA VAL LEU ASP LEU ASP VAL ARG THR CYS LEU PRO CYS
SEQRES 2 A 92 GLY PRO GLY GLY LYS GLY ARG CYS PHE GLY PRO SER ILE
SEQRES 3 A 92 CYS CYS GLY ASP GLU LEU GLY CYS PHE VAL GLY THR ALA
SEQRES 4 A 92 GLU ALA LEU ARG CYS GLN GLU GLU ASN TYR LEU PRO SER
SEQRES 5 A 92 PRO CYS GLN SER GLY GLN LYS PRO CYS GLY SER GLY GLY
SEQRES 6 A 92 ARG CYS ALA ALA ALA GLY ILE CYS CYS SER PRO ASP GLY
SEQRES 7 A 92 CYS GLU GLU ASP PRO ALA CYS ASP PRO GLU ALA ALA PHE
SEQRES 8 A 92 SER
HELIX 1 1 THR A 38 TYR A 49 5 12
SHEET 1 A 2 PRO A 12 CYS A 13 0
SHEET 2 A 2 GLY A 19 ARG A 20 -1 O GLY A 19 N CYS A 13
SHEET 1 B 2 CYS A 27 GLY A 29 0
SHEET 2 B 2 LEU A 32 PHE A 35 -1 O GLY A 33 N GLY A 29
SHEET 1 C 4 PRO A 60 CYS A 61 0
SHEET 2 C 4 GLY A 65 CYS A 67 -1 O GLY A 65 N CYS A 61
SHEET 3 C 4 GLY A 71 CYS A 74 -1 O CYS A 74 N ARG A 66
SHEET 4 C 4 CYS A 79 CYS A 85 -1 O GLU A 80 N CYS A 73
SSBOND 1 CYS A 10 CYS A 54 1555 1555 2.03
SSBOND 2 CYS A 13 CYS A 27 1555 1555 2.02
SSBOND 3 CYS A 21 CYS A 44 1555 1555 2.03
SSBOND 4 CYS A 28 CYS A 34 1555 1555 2.02
SSBOND 5 CYS A 61 CYS A 73 1555 1555 2.03
SSBOND 6 CYS A 67 CYS A 85 1555 1555 2.03
SSBOND 7 CYS A 74 CYS A 79 1555 1555 2.03
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 - t 27 2 Bytes