Header list of 1g91.pdb file
Complete list - c 21 2 Bytes
HEADER CYTOKINE 21-NOV-00 1G91
TITLE SOLUTION STRUCTURE OF MYELOID PROGENITOR INHIBITORY FACTOR-1 (MPIF-1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYELOID PROGENITOR INHIBITORY FACTOR-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MPIF-1;
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_STRAIN: K12-DERIVED STRAIN SGI3009;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PHE4
KEYWDS CHEMOKINE, CYTOKINE, MPIF-1, CKB8, CCL23
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR K.RAJARATHNAM,Y.LI,T.ROHRER,R.GENTZ
REVDAT 4 21-DEC-22 1G91 1 SEQADV
REVDAT 3 23-FEB-22 1G91 1 REMARK
REVDAT 2 24-FEB-09 1G91 1 VERSN
REVDAT 1 07-MAR-01 1G91 0
JRNL AUTH K.RAJARATHNAM,Y.LI,T.ROHRER,R.GENTZ
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF MYELOID PROGENITOR
JRNL TITL 2 INHIBITORY FACTOR-1 (MPIF-1), A NOVEL MONOMERIC CC
JRNL TITL 3 CHEMOKINE.
JRNL REF J.BIOL.CHEM. V. 276 4909 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11060285
JRNL DOI 10.1074/JBC.M005085200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 711 NOE, 82 DIHEDRAL, AND 36 H-BONDING RESTRAINTS
REMARK 4
REMARK 4 1G91 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000012384.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 5.2
REMARK 210 IONIC STRENGTH : 20 MM SODIUM ACETATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM MPIF-1 U-13C,15N; 2 MM MPIF
REMARK 210 -1 U-15N; 2 MM MPIF-1
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; HNCACB;
REMARK 210 CBCA(CO)NH; HCCH-TOCSY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHA; 2D NOESY;
REMARK 210 DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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
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 2 64.73 -110.44
REMARK 500 1 PHE A 4 50.05 -117.73
REMARK 500 1 ALA A 6 -161.55 50.94
REMARK 500 1 SER A 14 127.96 -170.53
REMARK 500 1 THR A 70 -67.61 67.05
REMARK 500 1 ARG A 71 -74.06 175.19
REMARK 500 1 LYS A 73 91.13 52.67
REMARK 500 1 ARG A 75 -159.98 65.89
REMARK 500 1 LYS A 76 -49.75 -144.79
REMARK 500 2 ASP A 2 70.28 50.31
REMARK 500 2 HIS A 5 -71.26 -104.25
REMARK 500 2 SER A 8 -81.26 -92.32
REMARK 500 2 ALA A 9 -176.55 -55.14
REMARK 500 2 ASP A 10 -88.61 -142.39
REMARK 500 2 THR A 16 103.72 -44.58
REMARK 500 2 SER A 27 -174.79 -176.06
REMARK 500 2 LYS A 67 -151.07 -74.81
REMARK 500 2 ASP A 69 56.88 -94.55
REMARK 500 2 THR A 70 67.89 -114.92
REMARK 500 2 ARG A 75 35.07 -162.73
REMARK 500 3 ASP A 2 119.97 61.04
REMARK 500 3 ASP A 10 -66.87 -137.14
REMARK 500 3 SER A 27 -176.65 -176.52
REMARK 500 3 ASN A 32 109.68 -49.32
REMARK 500 3 PRO A 38 -169.54 -78.16
REMARK 500 3 ARG A 71 100.87 -168.09
REMARK 500 3 LYS A 73 -89.27 -56.95
REMARK 500 3 THR A 74 81.33 -153.49
REMARK 500 3 ARG A 75 -85.64 -120.23
REMARK 500 3 LYS A 76 23.83 -149.45
REMARK 500 4 PHE A 4 -40.17 -148.15
REMARK 500 4 SER A 19 96.59 -67.48
REMARK 500 4 SER A 27 -173.04 -174.87
REMARK 500 4 ASN A 32 96.21 -63.40
REMARK 500 4 PRO A 38 -169.07 -78.00
REMARK 500 4 ARG A 71 65.09 72.37
REMARK 500 4 LYS A 73 51.77 -142.01
REMARK 500 4 ARG A 75 73.52 -164.81
REMARK 500 4 LYS A 76 -39.59 -163.42
REMARK 500 5 HIS A 5 37.82 -99.41
REMARK 500 5 ALA A 6 -159.27 -99.47
REMARK 500 5 ASP A 10 81.98 -153.65
REMARK 500 5 THR A 31 -174.33 -67.79
REMARK 500 5 LYS A 67 167.58 -43.91
REMARK 500 5 ASP A 69 79.04 -67.54
REMARK 500 5 ILE A 72 56.08 -140.75
REMARK 500 5 THR A 74 74.99 50.69
REMARK 500 5 LYS A 76 40.67 -166.79
REMARK 500 6 PHE A 4 46.38 -145.38
REMARK 500 6 THR A 31 -176.74 -63.10
REMARK 500
REMARK 500 THIS ENTRY HAS 242 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 1 ARG A 3 0.30 SIDE CHAIN
REMARK 500 1 ARG A 18 0.26 SIDE CHAIN
REMARK 500 1 ARG A 48 0.23 SIDE CHAIN
REMARK 500 1 ARG A 49 0.28 SIDE CHAIN
REMARK 500 1 ARG A 64 0.20 SIDE CHAIN
REMARK 500 1 ARG A 71 0.29 SIDE CHAIN
REMARK 500 1 ARG A 75 0.12 SIDE CHAIN
REMARK 500 2 ARG A 3 0.28 SIDE CHAIN
REMARK 500 2 ARG A 18 0.28 SIDE CHAIN
REMARK 500 2 ARG A 48 0.29 SIDE CHAIN
REMARK 500 2 ARG A 49 0.28 SIDE CHAIN
REMARK 500 2 ARG A 64 0.28 SIDE CHAIN
REMARK 500 2 ARG A 71 0.23 SIDE CHAIN
REMARK 500 2 ARG A 75 0.30 SIDE CHAIN
REMARK 500 3 ARG A 3 0.28 SIDE CHAIN
REMARK 500 3 ARG A 18 0.30 SIDE CHAIN
REMARK 500 3 ARG A 48 0.30 SIDE CHAIN
REMARK 500 3 ARG A 64 0.18 SIDE CHAIN
REMARK 500 3 ARG A 71 0.19 SIDE CHAIN
REMARK 500 3 ARG A 75 0.29 SIDE CHAIN
REMARK 500 4 ARG A 3 0.25 SIDE CHAIN
REMARK 500 4 ARG A 18 0.28 SIDE CHAIN
REMARK 500 4 ARG A 48 0.31 SIDE CHAIN
REMARK 500 4 ARG A 49 0.28 SIDE CHAIN
REMARK 500 4 ARG A 64 0.14 SIDE CHAIN
REMARK 500 4 ARG A 71 0.22 SIDE CHAIN
REMARK 500 4 ARG A 75 0.31 SIDE CHAIN
REMARK 500 5 ARG A 18 0.13 SIDE CHAIN
REMARK 500 5 ARG A 48 0.24 SIDE CHAIN
REMARK 500 5 ARG A 49 0.32 SIDE CHAIN
REMARK 500 5 ARG A 64 0.26 SIDE CHAIN
REMARK 500 5 ARG A 71 0.23 SIDE CHAIN
REMARK 500 5 ARG A 75 0.18 SIDE CHAIN
REMARK 500 6 ARG A 3 0.14 SIDE CHAIN
REMARK 500 6 ARG A 18 0.31 SIDE CHAIN
REMARK 500 6 ARG A 48 0.23 SIDE CHAIN
REMARK 500 6 ARG A 49 0.09 SIDE CHAIN
REMARK 500 6 ARG A 64 0.20 SIDE CHAIN
REMARK 500 6 ARG A 71 0.26 SIDE CHAIN
REMARK 500 6 ARG A 75 0.12 SIDE CHAIN
REMARK 500 7 ARG A 3 0.32 SIDE CHAIN
REMARK 500 7 ARG A 18 0.31 SIDE CHAIN
REMARK 500 7 ARG A 48 0.26 SIDE CHAIN
REMARK 500 7 ARG A 49 0.26 SIDE CHAIN
REMARK 500 7 ARG A 64 0.31 SIDE CHAIN
REMARK 500 7 ARG A 71 0.22 SIDE CHAIN
REMARK 500 7 ARG A 75 0.18 SIDE CHAIN
REMARK 500 8 ARG A 3 0.32 SIDE CHAIN
REMARK 500 8 ARG A 18 0.29 SIDE CHAIN
REMARK 500 8 ARG A 48 0.26 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 203 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1G91 A 2 77 UNP P55773 CCL23_HUMAN 45 120
SEQADV 1G91 MET A 1 UNP P55773 INITIATING METHIONINE
SEQRES 1 A 77 MET ASP ARG PHE HIS ALA THR SER ALA ASP CYS CYS ILE
SEQRES 2 A 77 SER TYR THR PRO ARG SER ILE PRO CYS SER LEU LEU GLU
SEQRES 3 A 77 SER TYR PHE GLU THR ASN SER GLU CYS SER LYS PRO GLY
SEQRES 4 A 77 VAL ILE PHE LEU THR LYS LYS GLY ARG ARG PHE CYS ALA
SEQRES 5 A 77 ASN PRO SER ASP LYS GLN VAL GLN VAL CYS MET ARG MET
SEQRES 6 A 77 LEU LYS LEU ASP THR ARG ILE LYS THR ARG LYS ASN
HELIX 1 1 PRO A 21 LEU A 25 5 5
HELIX 2 2 ASP A 56 LYS A 67 1 12
SHEET 1 A 3 SER A 27 GLU A 30 0
SHEET 2 A 3 VAL A 40 LEU A 43 -1 N ILE A 41 O PHE A 29
SHEET 3 A 3 ARG A 49 ALA A 52 -1 O PHE A 50 N PHE A 42
SSBOND 1 CYS A 11 CYS A 35 1555 1555 2.02
SSBOND 2 CYS A 12 CYS A 51 1555 1555 2.02
SSBOND 3 CYS A 22 CYS A 62 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 - c 21 2 Bytes