Header list of 1dzc.pdb file
Complete list - n 12 2 Bytes
HEADER CELL CYCLE 24-FEB-00 1DZC
TITLE HIGH RESOLUTION STRUCTURE OF ACIDIC FIBROBLAST GROWTH
TITLE 2 FACTOR. MUTANT FGF-4-ALA-(23-154), 24 NMR STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBROBLAST GROWTH FACTOR 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 25-155;
COMPND 5 SYNONYM: FGF-1, ACIDIC FIBROBLAST GROWTH FACTOR, AFGF, ECGF,HBGF-1,
COMPND 6 ENDOTHELIAL CELL GROWTH FACTOR, HEPARIN-BINDING GROWTH FACTOR 1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: 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_PLASMID: PMG624A
KEYWDS GROWTH FACTOR, CELL CYCLE, ANTITUMORAL
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR R.M.LOZANO,A.PINEDA-LUCENA,C.GONZALEZ,M.A.JIMENEZ,P.CUEVAS,
AUTHOR 2 M.REDONDO-HORCAJO,J.M.SANZ,M.RICO,G.GIMENEZ-GALLEGO
REVDAT 4 15-MAY-13 1DZC 1 HEADER COMPND KEYWDS REMARK
REVDAT 4 2 VERSN
REVDAT 3 24-FEB-09 1DZC 1 VERSN
REVDAT 2 02-JUN-00 1DZC 1 JRNL
REVDAT 1 16-MAR-00 1DZC 0
JRNL AUTH R.M.LOZANO,A.PINEDA-LUCENA,C.GONZALEZ,M.A.JIMENEZ,
JRNL AUTH 2 P.CUEVAS,M.REDONDE-HORCAJO,J.M.SANZ,M.RICO,
JRNL AUTH 3 G.GIMENEZ-GALLEGO
JRNL TITL 1H-NMR STRUCTURAL CHARACTERIZATION OF A NON
JRNL TITL 2 MITOGENIC, VASODILATORY, ISCHEMIA-PROTECTOR AND
JRNL TITL 3 NEUROMODULATORY ACIDIC FIBROBLAST GROWTH FACTOR
JRNL REF BIOCHEMISTRY V. 39 4982 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10819962
JRNL DOI 10.1021/BI992544N
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GROMOS
REMARK 3 AUTHORS : VAN GUNSTEREN,BERENDSEN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE
REMARK 4
REMARK 4 1DZC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-FEB-00.
REMARK 100 THE PDBE ID CODE IS EBI-4653.
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 : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY, TOCSY, COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : GROMOS
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 24
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 CHAIN A:
REMARK 400 MUTATION: RESIDUES 24,25,26 SUBSTITUTED FOR ALA
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 11 GLN A 91 CD GLN A 91 NE2 -0.195
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 1 TYR A 29 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 1 ARG A 49 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 1 PHE A 99 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 1 TYR A 108 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 1 TYR A 111 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 1 TYR A 139 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 2 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 PHE A 99 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 TYR A 108 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 2 ARG A 133 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 TYR A 139 CB - CG - CD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 PHE A 146 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 3 TYR A 29 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 3 TYR A 88 CB - CG - CD1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 4 TYR A 29 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 4 ARG A 51 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 4 PHE A 122 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 4 ARG A 133 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 TYR A 139 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 4 PHE A 146 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 5 TYR A 69 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 5 ARG A 102 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 6 TYR A 29 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 6 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 6 PHE A 99 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 6 TYR A 111 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 6 ARG A 136 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 TYR A 108 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 7 PHE A 122 CB - CG - CD1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 8 TYR A 29 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 8 TYR A 108 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 8 TYR A 139 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 9 TYR A 29 CB - CG - CD2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 10 TYR A 29 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 10 TYR A 108 CB - CG - CD1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 10 TYR A 139 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 11 TYR A 29 CB - CG - CD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 11 TYR A 69 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 11 LYS A 71 CD - CE - NZ ANGL. DEV. = -14.4 DEGREES
REMARK 500 11 GLN A 91 CG - CD - NE2 ANGL. DEV. = -29.4 DEGREES
REMARK 500 11 GLN A 91 CG - CD - OE1 ANGL. DEV. = 13.5 DEGREES
REMARK 500 11 GLN A 91 OE1 - CD - NE2 ANGL. DEV. = -66.9 DEGREES
REMARK 500 11 ARG A 102 NE - CZ - NH1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 11 ARG A 102 NE - CZ - NH2 ANGL. DEV. = 4.1 DEGREES
REMARK 500 11 LYS A 114 CD - CE - NZ ANGL. DEV. = -15.3 DEGREES
REMARK 500 11 TYR A 139 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 11 PHE A 146 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 12 TYR A 29 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 12 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 12 ARG A 102 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 103 ANGLE DEVIATIONS.
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 ALA A 25 -49.62 87.62
REMARK 500 1 ASP A 42 44.99 -74.19
REMARK 500 1 SER A 52 52.26 -101.10
REMARK 500 1 ASP A 53 38.93 -83.50
REMARK 500 1 SER A 61 72.67 -100.95
REMARK 500 1 GLU A 63 44.88 -99.59
REMARK 500 1 SER A 64 -65.68 76.25
REMARK 500 1 GLU A 67 100.00 -55.69
REMARK 500 1 THR A 73 -37.94 -14.44
REMARK 500 1 LEU A 98 94.07 -69.89
REMARK 500 1 GLU A 101 87.53 -57.53
REMARK 500 1 ARG A 102 75.73 -105.85
REMARK 500 1 GLU A 104 37.79 -69.96
REMARK 500 1 GLU A 105 -42.67 62.18
REMARK 500 1 LYS A 114 -58.58 -19.31
REMARK 500 1 ARG A 133 -77.83 -113.03
REMARK 500 1 LEU A 149 77.11 -109.10
REMARK 500 2 ALA A 25 -88.99 -132.33
REMARK 500 2 ASP A 53 -14.47 -48.96
REMARK 500 2 ILE A 56 79.22 -160.28
REMARK 500 2 SER A 61 62.47 -100.86
REMARK 500 2 ALA A 62 127.66 -38.05
REMARK 500 2 GLU A 67 97.60 -68.02
REMARK 500 2 THR A 73 -49.63 -18.01
REMARK 500 2 THR A 83 30.77 -84.79
REMARK 500 2 LEU A 100 95.05 -64.67
REMARK 500 2 GLU A 101 108.32 -53.98
REMARK 500 2 ARG A 102 71.59 -109.39
REMARK 500 2 ASN A 106 38.24 -80.29
REMARK 500 2 HIS A 107 -43.83 65.76
REMARK 500 2 ASN A 120 52.33 39.51
REMARK 500 2 ARG A 133 -89.11 -117.35
REMARK 500 2 HIS A 138 142.55 -14.61
REMARK 500 2 LEU A 145 92.43 -66.03
REMARK 500 2 LEU A 149 79.88 -114.97
REMARK 500 2 SER A 152 -51.20 72.03
REMARK 500 2 SER A 153 59.38 -91.84
REMARK 500 3 SER A 52 69.87 -101.71
REMARK 500 3 SER A 61 73.28 -114.27
REMARK 500 3 GLU A 67 97.74 -63.40
REMARK 500 3 THR A 73 -43.67 -3.13
REMARK 500 3 THR A 83 20.21 -69.81
REMARK 500 3 LEU A 100 97.57 -69.81
REMARK 500 3 GLU A 101 92.72 -62.62
REMARK 500 3 ARG A 102 74.60 -109.69
REMARK 500 3 HIS A 107 -48.92 65.70
REMARK 500 3 ALA A 117 41.33 -80.37
REMARK 500 3 GLU A 118 -37.41 -146.90
REMARK 500 3 ASN A 128 57.55 -92.69
REMARK 500 3 ARG A 133 -122.72 -102.59
REMARK 500
REMARK 500 THIS ENTRY HAS 406 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 129 SER A 130 7 -148.10
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 TYR A 29 0.10 SIDE CHAIN
REMARK 500 1 TYR A 88 0.08 SIDE CHAIN
REMARK 500 1 PHE A 99 0.15 SIDE CHAIN
REMARK 500 1 TYR A 108 0.10 SIDE CHAIN
REMARK 500 1 TYR A 111 0.11 SIDE CHAIN
REMARK 500 1 PHE A 122 0.11 SIDE CHAIN
REMARK 500 1 ARG A 136 0.09 SIDE CHAIN
REMARK 500 2 TYR A 29 0.07 SIDE CHAIN
REMARK 500 2 TYR A 69 0.11 SIDE CHAIN
REMARK 500 2 PHE A 99 0.08 SIDE CHAIN
REMARK 500 2 TYR A 108 0.10 SIDE CHAIN
REMARK 500 2 TRP A 121 0.08 SIDE CHAIN
REMARK 500 2 PHE A 122 0.12 SIDE CHAIN
REMARK 500 3 TYR A 29 0.08 SIDE CHAIN
REMARK 500 3 TYR A 69 0.06 SIDE CHAIN
REMARK 500 3 TYR A 88 0.10 SIDE CHAIN
REMARK 500 3 TYR A 108 0.06 SIDE CHAIN
REMARK 500 3 PHE A 122 0.07 SIDE CHAIN
REMARK 500 3 ARG A 133 0.09 SIDE CHAIN
REMARK 500 3 HIS A 138 0.09 SIDE CHAIN
REMARK 500 3 TYR A 139 0.08 SIDE CHAIN
REMARK 500 4 TYR A 29 0.09 SIDE CHAIN
REMARK 500 4 TYR A 69 0.14 SIDE CHAIN
REMARK 500 4 TYR A 78 0.10 SIDE CHAIN
REMARK 500 4 TYR A 88 0.08 SIDE CHAIN
REMARK 500 4 HIS A 107 0.10 SIDE CHAIN
REMARK 500 4 TYR A 108 0.09 SIDE CHAIN
REMARK 500 4 TYR A 111 0.09 SIDE CHAIN
REMARK 500 4 PHE A 122 0.15 SIDE CHAIN
REMARK 500 4 TYR A 139 0.10 SIDE CHAIN
REMARK 500 5 TYR A 69 0.09 SIDE CHAIN
REMARK 500 5 TYR A 88 0.11 SIDE CHAIN
REMARK 500 5 PHE A 99 0.09 SIDE CHAIN
REMARK 500 5 TYR A 108 0.12 SIDE CHAIN
REMARK 500 5 TYR A 111 0.09 SIDE CHAIN
REMARK 500 5 PHE A 122 0.12 SIDE CHAIN
REMARK 500 5 TYR A 139 0.10 SIDE CHAIN
REMARK 500 6 TYR A 29 0.07 SIDE CHAIN
REMARK 500 6 TYR A 69 0.10 SIDE CHAIN
REMARK 500 6 TYR A 88 0.08 SIDE CHAIN
REMARK 500 6 PHE A 99 0.11 SIDE CHAIN
REMARK 500 6 TYR A 111 0.09 SIDE CHAIN
REMARK 500 6 PHE A 122 0.14 SIDE CHAIN
REMARK 500 7 TYR A 29 0.09 SIDE CHAIN
REMARK 500 7 TYR A 88 0.11 SIDE CHAIN
REMARK 500 7 TYR A 108 0.12 SIDE CHAIN
REMARK 500 7 TYR A 111 0.13 SIDE CHAIN
REMARK 500 7 PHE A 122 0.15 SIDE CHAIN
REMARK 500 8 TYR A 29 0.13 SIDE CHAIN
REMARK 500 8 TYR A 78 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 159 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 1 ASP A 53 12.68
REMARK 500 1 SER A 72 12.53
REMARK 500 1 ARG A 102 11.41
REMARK 500 1 ALA A 117 -10.59
REMARK 500 2 SER A 72 11.07
REMARK 500 3 ASN A 32 11.13
REMARK 500 3 SER A 61 10.65
REMARK 500 3 SER A 72 10.52
REMARK 500 3 LYS A 132 11.81
REMARK 500 4 ASN A 32 11.65
REMARK 500 5 ASP A 53 -10.23
REMARK 500 5 SER A 72 11.82
REMARK 500 6 ALA A 24 13.16
REMARK 500 6 GLU A 118 -10.69
REMARK 500 6 LYS A 119 -10.10
REMARK 500 7 ILE A 56 10.82
REMARK 500 7 SER A 61 12.24
REMARK 500 7 ASP A 82 -11.33
REMARK 500 8 VAL A 65 11.52
REMARK 500 8 SER A 72 10.01
REMARK 500 8 GLY A 85 -12.21
REMARK 500 8 LYS A 119 -10.65
REMARK 500 9 ILE A 56 10.29
REMARK 500 9 SER A 61 11.35
REMARK 500 9 SER A 72 10.24
REMARK 500 9 SER A 90 -11.89
REMARK 500 9 LYS A 132 10.10
REMARK 500 11 ALA A 24 -12.10
REMARK 500 11 ALA A 62 11.14
REMARK 500 11 SER A 72 11.86
REMARK 500 11 MET A 81 10.19
REMARK 500 11 ARG A 102 11.06
REMARK 500 12 ALA A 25 10.10
REMARK 500 12 SER A 61 10.67
REMARK 500 13 ILE A 56 11.99
REMARK 500 13 VAL A 65 10.48
REMARK 500 13 SER A 72 11.99
REMARK 500 13 LEU A 103 10.23
REMARK 500 13 TYR A 108 -11.42
REMARK 500 13 ALA A 143 -10.04
REMARK 500 14 ASP A 42 11.28
REMARK 500 14 SER A 61 13.09
REMARK 500 14 ARG A 102 11.20
REMARK 500 14 LYS A 132 11.29
REMARK 500 14 HIS A 138 10.14
REMARK 500 15 SER A 61 10.38
REMARK 500 15 SER A 64 11.24
REMARK 500 15 MET A 81 11.78
REMARK 500 15 CYS A 131 12.29
REMARK 500 15 LYS A 132 10.73
REMARK 500
REMARK 500 THIS ENTRY HAS 78 MAIN CHAIN PLANARITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 2 ARG A 133 24.0 L L OUTSIDE RANGE
REMARK 500 2 HIS A 138 24.7 L L OUTSIDE RANGE
REMARK 500 7 ALA A 26 24.9 L L OUTSIDE RANGE
REMARK 500 12 ARG A 133 24.1 L L OUTSIDE RANGE
REMARK 500 12 HIS A 138 23.5 L L OUTSIDE RANGE
REMARK 500 17 ARG A 133 23.6 L L OUTSIDE RANGE
REMARK 500 17 HIS A 138 23.8 L L OUTSIDE RANGE
REMARK 500 18 ARG A 133 24.6 L L OUTSIDE RANGE
REMARK 500 18 HIS A 138 24.9 L L OUTSIDE RANGE
REMARK 500 19 ARG A 133 24.2 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AFG RELATED DB: PDB
REMARK 900 RELATED ID: 1AXM RELATED DB: PDB
REMARK 900 RELATED ID: 2AXM RELATED DB: PDB
REMARK 900 RELATED ID: 1RML RELATED DB: PDB
REMARK 900 RELATED ID: 1DZD RELATED DB: PDB
DBREF 1DZC A 24 154 UNP P05230 FGF1_HUMAN 25 155
SEQADV 1DZC ALA A 24 UNP P05230 LYS 25 ENGINEERED MUTATION
SEQADV 1DZC ALA A 25 UNP P05230 PRO 26 ENGINEERED MUTATION
SEQADV 1DZC ALA A 26 UNP P05230 LYS 27 ENGINEERED MUTATION
SEQRES 1 A 131 ALA ALA ALA LEU LEU TYR CYS SER ASN GLY GLY HIS PHE
SEQRES 2 A 131 LEU ARG ILE LEU PRO ASP GLY THR VAL ASP GLY THR ARG
SEQRES 3 A 131 ASP ARG SER ASP GLN HIS ILE GLN LEU GLN LEU SER ALA
SEQRES 4 A 131 GLU SER VAL GLY GLU VAL TYR ILE LYS SER THR GLU THR
SEQRES 5 A 131 GLY GLN TYR LEU ALA MET ASP THR ASP GLY LEU LEU TYR
SEQRES 6 A 131 GLY SER GLN THR PRO ASN GLU GLU CYS LEU PHE LEU GLU
SEQRES 7 A 131 ARG LEU GLU GLU ASN HIS TYR ASN THR TYR ILE SER LYS
SEQRES 8 A 131 LYS HIS ALA GLU LYS ASN TRP PHE VAL GLY LEU LYS LYS
SEQRES 9 A 131 ASN GLY SER CYS LYS ARG GLY PRO ARG THR HIS TYR GLY
SEQRES 10 A 131 GLN LYS ALA ILE LEU PHE LEU PRO LEU PRO VAL SER SER
SEQRES 11 A 131 ASP
HELIX 1 1 LYS A 115 ASN A 120 5 6
HELIX 2 2 GLN A 141 ILE A 144 5 4
SHEET 1 A 2 LEU A 28 CYS A 30 0
SHEET 2 A 2 PHE A 146 PRO A 148 -1 N LEU A 147 O TYR A 29
SHEET 1 B 2 PHE A 36 LEU A 40 0
SHEET 2 B 2 THR A 44 THR A 48 -1 N THR A 48 O PHE A 36
SHEET 1 C 4 GLN A 59 ALA A 62 0
SHEET 2 C 4 GLU A 67 LYS A 71 -1 N LYS A 71 O GLN A 59
SHEET 3 C 4 LEU A 98 LEU A 103 -1 N PHE A 99 O VAL A 68
SHEET 4 C 4 ASN A 109 SER A 113 -1 N ILE A 112 O LEU A 100
SHEET 1 D 3 ILE A 70 SER A 72 0
SHEET 2 D 3 GLN A 77 MET A 81 -1 N LEU A 79 O ILE A 70
SHEET 3 D 3 LEU A 87 SER A 90 -1 N SER A 90 O TYR A 78
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 - n 12 2 Bytes