Header list of 1fmm.pdb file
Complete list - 23 20 Bytes
HEADER HORMONE/GROWTH FACTOR 18-AUG-00 1FMM
TITLE SOLUTION STRUCTURE OF NFGF-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACIDIC FIBROBLAST GROWTH FACTOR;
COMPND 3 CHAIN: S;
COMPND 4 SYNONYM: NFGF-1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOTOPHTHALMUS VIRIDESCENS;
SOURCE 3 ORGANISM_COMMON: EASTERN NEWT;
SOURCE 4 ORGANISM_TAXID: 8316;
SOURCE 5 CELL: FIBROBLAST;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS GROWTH FACTOR, TRIPLE RESONANCE, MITOGEN, WOUND HEALING, HORMONE-
KEYWDS 2 GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR A.I.ARUNKUMAR,S.SRISAILAM,T.K.S.KUMAR,I.M.CHIU,C.YU
REVDAT 3 23-FEB-22 1FMM 1 REMARK
REVDAT 2 24-FEB-09 1FMM 1 VERSN
REVDAT 1 18-AUG-01 1FMM 0
JRNL AUTH A.I.ARUNKUMAR,S.SRISAILAM,T.K.KUMAR,K.M.KATHIR,Y.H.CHI,
JRNL AUTH 2 H.M.WANG,G.G.CHANG,I.CHIU,C.YU
JRNL TITL STRUCTURE AND STABILITY OF AN ACIDIC FIBROBLAST GROWTH
JRNL TITL 2 FACTOR FROM NOTOPHTHALMUS VIRIDESCENS.
JRNL REF J.BIOL.CHEM. V. 277 46424 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 12205097
JRNL DOI 10.1074/JBC.M207814200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AURELIA 2.7.5
REMARK 3 AUTHORS : A. I. ARUNKUMAR AND S. SRISAILAM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FMM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011718.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 10 MM PHOSPHATE AND 100 MM
REMARK 210 SODIUM CHLORIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: S
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 H2 GLN S 1 OG SER S 130 1.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS S 8 CA - CB - SG ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG S 16 NE - CZ - NH2 ANGL. DEV. = -6.7 DEGREES
REMARK 500 TYR S 56 CB - CA - C ANGL. DEV. = 12.1 DEGREES
REMARK 500 PHE S 77 CB - CG - CD1 ANGL. DEV. = 5.3 DEGREES
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 LYS S 2 -37.33 -173.36
REMARK 500 PRO S 3 -166.80 -77.79
REMARK 500 LYS S 4 126.16 161.06
REMARK 500 LEU S 6 77.84 -111.96
REMARK 500 ASN S 10 54.48 -95.26
REMARK 500 PHE S 18 -106.89 -80.47
REMARK 500 ARG S 27 2.10 -66.74
REMARK 500 TYR S 33 58.66 -167.54
REMARK 500 GLU S 41 -70.40 -100.56
REMARK 500 VAL S 43 -118.06 107.72
REMARK 500 LEU S 51 172.38 62.89
REMARK 500 THR S 53 8.23 -66.82
REMARK 500 GLN S 55 -147.85 -87.97
REMARK 500 TYR S 56 -157.77 -150.00
REMARK 500 ASP S 62 -54.24 179.65
REMARK 500 GLN S 64 -178.08 -69.57
REMARK 500 PRO S 71 -127.70 -70.91
REMARK 500 SER S 72 145.25 63.58
REMARK 500 CYS S 75 49.17 -94.93
REMARK 500 LEU S 76 -162.00 -114.52
REMARK 500 PHE S 77 -166.17 -169.77
REMARK 500 GLU S 82 -114.27 -39.27
REMARK 500 GLU S 83 -81.87 -79.03
REMARK 500 ASN S 84 94.23 -162.43
REMARK 500 ASN S 85 -53.84 -177.03
REMARK 500 THR S 88 -97.63 -36.03
REMARK 500 TYR S 89 169.59 90.54
REMARK 500 LYS S 90 144.65 63.53
REMARK 500 SER S 91 -145.16 158.03
REMARK 500 LYS S 92 -94.37 -169.81
REMARK 500 VAL S 93 -70.32 -115.45
REMARK 500 ASP S 96 -92.16 39.97
REMARK 500 LYS S 97 -14.56 140.62
REMARK 500 ASP S 98 -5.74 -57.96
REMARK 500 TRP S 99 69.25 -150.74
REMARK 500 LYS S 104 -171.39 173.03
REMARK 500 LYS S 105 -62.89 110.39
REMARK 500 ASN S 106 5.25 167.62
REMARK 500 LYS S 108 -0.17 142.15
REMARK 500 THR S 109 -154.51 63.50
REMARK 500 ARG S 114 83.19 -166.80
REMARK 500 HIS S 116 87.75 164.41
REMARK 500 PHE S 117 111.37 -5.29
REMARK 500 GLN S 119 154.52 -45.90
REMARK 500 ILE S 122 -74.41 -44.12
REMARK 500 VAL S 129 -77.79 -8.64
REMARK 500 SER S 130 -91.63 50.69
REMARK 500 SER S 131 -117.15 -150.26
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 ARG S 16 0.23 SIDE CHAIN
REMARK 500 ARG S 27 0.29 SIDE CHAIN
REMARK 500 TYR S 47 0.08 SIDE CHAIN
REMARK 500 TYR S 66 0.09 SIDE CHAIN
REMARK 500 ARG S 80 0.20 SIDE CHAIN
REMARK 500 PHE S 100 0.08 SIDE CHAIN
REMARK 500 ARG S 114 0.22 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FMM S 1 132 UNP Q7SIF8 FGF1_NOTVI 1 132
SEQRES 1 S 132 GLN LYS PRO LYS LEU LEU TYR CYS SER ASN GLY GLY TYR
SEQRES 2 S 132 PHE LEU ARG ILE PHE PRO ASP GLY LYS VAL ASP GLY THR
SEQRES 3 S 132 ARG ASP ARG SER ASP PRO TYR ILE GLN LEU GLN PHE TYR
SEQRES 4 S 132 ALA GLU SER VAL GLY GLU VAL TYR ILE LYS SER LEU GLU
SEQRES 5 S 132 THR GLY GLN TYR LEU ALA MET ASP SER ASP GLY GLN LEU
SEQRES 6 S 132 TYR ALA SER GLN SER PRO SER GLU GLU CYS LEU PHE LEU
SEQRES 7 S 132 GLU ARG LEU GLU GLU ASN ASN TYR ASN THR TYR LYS SER
SEQRES 8 S 132 LYS VAL HIS ALA ASP LYS ASP TRP PHE VAL GLY ILE LYS
SEQRES 9 S 132 LYS ASN GLY LYS THR LYS PRO GLY SER ARG THR HIS PHE
SEQRES 10 S 132 GLY GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL SER
SEQRES 11 S 132 SER ASP
HELIX 1 1 SER S 72 LEU S 76 5 5
SHEET 1 A 4 VAL S 23 THR S 26 0
SHEET 2 A 4 PHE S 14 ILE S 17 -1 O PHE S 14 N THR S 26
SHEET 3 A 4 LEU S 6 CYS S 8 -1 N LEU S 6 O LEU S 15
SHEET 4 A 4 PHE S 124 PRO S 126 -1 O LEU S 125 N TYR S 7
SHEET 1 B 2 LEU S 36 ALA S 40 0
SHEET 2 B 2 VAL S 46 SER S 50 -1 N TYR S 47 O TYR S 39
CRYST1 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
Complete list - 23 20 Bytes