Header list of 1rfa.pdb file
Complete list - r 2 2 Bytes
HEADER SERINE/THREONINE-PROTEIN KINASE 26-APR-95 1RFA
TITLE NMR SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAF1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RAS BINDING DOMAIN, RESIDUES 55 - 132 WITH AN ADDITIONAL
COMPND 5 ALA AT THE N-TERMINUS;
COMPND 6 SYNONYM: RAF-RBD, C-RAF-1;
COMPND 7 EC: 2.7.1.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: FETAL LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDW333
KEYWDS SERINE/THREONINE-PROTEIN KINASE, SIGNAL TRANSDUCTION PROTEIN, SERINE-
KEYWDS 2 THREONINE-PROTEIN KINASE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR S.D.EMERSON,V.S.MADISON,R.E.PALERMO,D.S.WAUGH,J.E.SCHEFFLER,K.-
AUTHOR 2 L.TSAO,S.E.KIEFER,S.P.LIU,D.C.FRY
REVDAT 3 02-MAR-22 1RFA 1 REMARK
REVDAT 2 24-FEB-09 1RFA 1 VERSN
REVDAT 1 20-JUN-96 1RFA 0
JRNL AUTH S.D.EMERSON,V.S.MADISON,R.E.PALERMO,D.S.WAUGH,J.E.SCHEFFLER,
JRNL AUTH 2 K.L.TSAO,S.E.KIEFER,S.P.LIU,D.C.FRY
JRNL TITL SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF C-RAF-1 AND
JRNL TITL 2 IDENTIFICATION OF ITS RAS INTERACTION SURFACE.
JRNL REF BIOCHEMISTRY V. 34 6911 1995
JRNL REFN ISSN 0006-2960
JRNL PMID 7766599
JRNL DOI 10.1021/BI00021A001
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.D.EMERSON,D.S.WAUGH,J.E.SCHEFFLER,K.L.TSAO,K.M.PRINZO,
REMARK 1 AUTH 2 D.C.FRY
REMARK 1 TITL CHEMICAL SHIFT ASSIGNMENTS AND FOLDING TOPOLOGY OF THE
REMARK 1 TITL 2 RAS-BINDING DOMAIN OF HUMAN RAF-1 AS DETERMINED BY
REMARK 1 TITL 3 HETERONUCLEAR THREE-DIMENSIONAL NMR SPECTROSCOPY
REMARK 1 REF BIOCHEMISTRY V. 33 7745 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.E.SCHEFFLER,D.S.WAUGH,E.BEKESI,S.E.KIEFER,J.E.LOSARDO,
REMARK 1 AUTH 2 A.NERI,K.M.PRINZO,K.L.TSAO,B.WEGRZYNSKI,S.D.EMERSON,ET AL.
REMARK 1 TITL CHARACTERIZATION OF A 78-RESIDUE FRAGMENT OF C-RAF-1 THAT
REMARK 1 TITL 2 COMPRISES A MINIMAL BINDING DOMAIN FOR THE INTERACTION WITH
REMARK 1 TITL 3 RAS-GTP
REMARK 1 REF J.BIOL.CHEM. V. 269 22340 1994
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CHARMM 22
REMARK 3 AUTHORS : BROOKS ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1RFA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176065.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-30
REMARK 465 RES C SSSEQI
REMARK 465 ALA A 54
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 SER A 77 H CYS A 81 1.54
REMARK 500 HH22 ARG A 100 OE2 GLU A 104 1.56
REMARK 500 HE2 HIS A 103 OE1 GLU A 125 1.57
REMARK 500 HH12 ARG A 111 OD1 ASP A 132 1.58
REMARK 500 HH12 ARG A 100 OE1 GLU A 104 1.58
REMARK 500 HH21 ARG A 59 OE2 GLU A 125 1.59
REMARK 500 HH21 ARG A 100 OE2 GLU A 124 1.59
REMARK 500 HH22 ARG A 111 OD2 ASP A 132 1.60
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 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -6.2 DEGREES
REMARK 500 1 ALA A 119 N - CA - CB ANGL. DEV. = -13.6 DEGREES
REMARK 500 2 ALA A 85 N - CA - CB ANGL. DEV. = -8.9 DEGREES
REMARK 500 2 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -5.8 DEGREES
REMARK 500 2 ALA A 119 N - CA - CB ANGL. DEV. = -13.3 DEGREES
REMARK 500 3 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -6.9 DEGREES
REMARK 500 3 ALA A 119 N - CA - CB ANGL. DEV. = -13.8 DEGREES
REMARK 500 4 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -6.2 DEGREES
REMARK 500 4 ALA A 119 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 5 ALA A 110 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 5 ALA A 118 N - CA - CB ANGL. DEV. = -9.9 DEGREES
REMARK 500 5 ALA A 119 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 6 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -6.4 DEGREES
REMARK 500 6 ALA A 118 N - CA - CB ANGL. DEV. = -8.8 DEGREES
REMARK 500 6 ALA A 119 N - CA - CB ANGL. DEV. = -13.3 DEGREES
REMARK 500 7 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -5.4 DEGREES
REMARK 500 7 ALA A 119 N - CA - CB ANGL. DEV. = -14.0 DEGREES
REMARK 500 8 ALA A 110 N - CA - CB ANGL. DEV. = 10.6 DEGREES
REMARK 500 8 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -6.4 DEGREES
REMARK 500 8 ALA A 119 N - CA - CB ANGL. DEV. = -12.6 DEGREES
REMARK 500 9 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -7.2 DEGREES
REMARK 500 9 ALA A 119 N - CA - CB ANGL. DEV. = -11.9 DEGREES
REMARK 500 10 ALA A 85 N - CA - CB ANGL. DEV. = -9.1 DEGREES
REMARK 500 10 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -7.0 DEGREES
REMARK 500 10 ALA A 119 N - CA - CB ANGL. DEV. = -12.9 DEGREES
REMARK 500 11 VAL A 70 CG1 - CB - CG2 ANGL. DEV. = 11.2 DEGREES
REMARK 500 11 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -6.6 DEGREES
REMARK 500 11 ALA A 118 N - CA - CB ANGL. DEV. = -8.5 DEGREES
REMARK 500 11 ALA A 119 N - CA - CB ANGL. DEV. = -13.8 DEGREES
REMARK 500 12 ALA A 85 N - CA - CB ANGL. DEV. = -8.7 DEGREES
REMARK 500 12 ALA A 110 N - CA - CB ANGL. DEV. = 12.0 DEGREES
REMARK 500 12 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -7.0 DEGREES
REMARK 500 12 ALA A 119 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 13 ALA A 110 N - CA - CB ANGL. DEV. = 10.2 DEGREES
REMARK 500 13 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -5.6 DEGREES
REMARK 500 13 ALA A 119 N - CA - CB ANGL. DEV. = -14.1 DEGREES
REMARK 500 14 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -5.9 DEGREES
REMARK 500 14 ALA A 119 N - CA - CB ANGL. DEV. = -13.9 DEGREES
REMARK 500 15 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -5.9 DEGREES
REMARK 500 15 ALA A 119 N - CA - CB ANGL. DEV. = -12.6 DEGREES
REMARK 500 16 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -5.5 DEGREES
REMARK 500 16 ALA A 119 N - CA - CB ANGL. DEV. = -14.5 DEGREES
REMARK 500 17 ALA A 85 N - CA - CB ANGL. DEV. = -9.1 DEGREES
REMARK 500 17 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -6.7 DEGREES
REMARK 500 17 ALA A 119 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 18 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -6.0 DEGREES
REMARK 500 18 ALA A 119 N - CA - CB ANGL. DEV. = -13.7 DEGREES
REMARK 500 19 VAL A 88 CG1 - CB - CG2 ANGL. DEV. = -10.3 DEGREES
REMARK 500 19 TRP A 114 CG - CD2 - CE3 ANGL. DEV. = -8.1 DEGREES
REMARK 500 19 ALA A 119 N - CA - CB ANGL. DEV. = -15.9 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 80 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 ASN A 56 14.54 -154.55
REMARK 500 1 ARG A 73 -164.30 -119.67
REMARK 500 1 MET A 76 -100.80 -109.01
REMARK 500 1 SER A 77 139.39 74.45
REMARK 500 1 GLU A 104 27.84 -146.49
REMARK 500 1 LEU A 131 -134.48 -78.89
REMARK 500 2 ASN A 56 17.66 -154.87
REMARK 500 2 ARG A 73 -142.65 -101.34
REMARK 500 2 MET A 76 -101.56 44.58
REMARK 500 2 SER A 77 140.30 74.63
REMARK 500 2 LEU A 86 -31.16 -130.64
REMARK 500 2 GLU A 104 29.73 -144.32
REMARK 500 2 LEU A 112 -160.32 -116.96
REMARK 500 3 ASN A 56 21.79 -149.23
REMARK 500 3 LYS A 65 8.82 80.66
REMARK 500 3 THR A 68 168.16 178.64
REMARK 500 3 ASN A 74 -130.99 52.16
REMARK 500 3 GLU A 104 20.57 -141.85
REMARK 500 3 LYS A 108 -148.72 -97.62
REMARK 500 3 LEU A 112 -159.11 -117.59
REMARK 500 4 ASN A 56 22.15 -144.77
REMARK 500 4 LYS A 65 5.82 81.37
REMARK 500 4 ARG A 73 -142.59 -92.13
REMARK 500 4 GLU A 104 32.51 -163.78
REMARK 500 4 LYS A 108 -152.48 -98.12
REMARK 500 4 LEU A 131 -126.51 -77.45
REMARK 500 5 ASN A 56 18.98 -152.54
REMARK 500 5 LYS A 65 3.06 81.13
REMARK 500 5 VAL A 72 -164.56 -122.97
REMARK 500 5 SER A 77 -162.06 -119.48
REMARK 500 5 MET A 83 -47.29 -148.56
REMARK 500 5 GLU A 104 24.86 -146.40
REMARK 500 5 LYS A 108 -147.54 -120.46
REMARK 500 5 LEU A 112 -150.43 -118.00
REMARK 500 6 ASN A 56 23.15 -141.28
REMARK 500 6 LYS A 65 60.23 81.63
REMARK 500 6 GLU A 104 45.59 -158.70
REMARK 500 6 LYS A 108 -147.73 -141.01
REMARK 500 6 LEU A 112 -153.86 -118.70
REMARK 500 6 GLU A 124 -159.83 -138.33
REMARK 500 7 ASN A 56 19.59 -149.65
REMARK 500 7 LYS A 65 -85.27 -127.51
REMARK 500 7 LEU A 101 -167.70 -79.60
REMARK 500 7 GLU A 104 23.32 -143.48
REMARK 500 7 LEU A 112 -162.83 -115.62
REMARK 500 7 LEU A 131 -79.37 57.33
REMARK 500 8 ASN A 56 21.61 -145.03
REMARK 500 8 ASN A 64 -94.87 -174.96
REMARK 500 8 ARG A 73 -167.15 -129.96
REMARK 500 8 GLU A 104 36.28 -155.58
REMARK 500
REMARK 500 THIS ENTRY HAS 210 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 PHE A 99 0.14 SIDE CHAIN
REMARK 500 2 PHE A 99 0.12 SIDE CHAIN
REMARK 500 3 PHE A 99 0.10 SIDE CHAIN
REMARK 500 4 PHE A 99 0.12 SIDE CHAIN
REMARK 500 5 PHE A 99 0.12 SIDE CHAIN
REMARK 500 5 HIS A 103 0.09 SIDE CHAIN
REMARK 500 6 PHE A 99 0.13 SIDE CHAIN
REMARK 500 7 PHE A 99 0.13 SIDE CHAIN
REMARK 500 8 PHE A 99 0.11 SIDE CHAIN
REMARK 500 9 PHE A 99 0.17 SIDE CHAIN
REMARK 500 10 ARG A 59 0.08 SIDE CHAIN
REMARK 500 10 HIS A 79 0.11 SIDE CHAIN
REMARK 500 10 PHE A 99 0.15 SIDE CHAIN
REMARK 500 11 PHE A 99 0.14 SIDE CHAIN
REMARK 500 12 PHE A 99 0.12 SIDE CHAIN
REMARK 500 13 PHE A 99 0.09 SIDE CHAIN
REMARK 500 14 PHE A 99 0.13 SIDE CHAIN
REMARK 500 15 PHE A 99 0.12 SIDE CHAIN
REMARK 500 16 PHE A 99 0.13 SIDE CHAIN
REMARK 500 17 PHE A 99 0.12 SIDE CHAIN
REMARK 500 18 ARG A 59 0.07 SIDE CHAIN
REMARK 500 18 PHE A 99 0.14 SIDE CHAIN
REMARK 500 19 ARG A 59 0.07 SIDE CHAIN
REMARK 500 19 PHE A 99 0.12 SIDE CHAIN
REMARK 500 20 PHE A 99 0.14 SIDE CHAIN
REMARK 500 21 PHE A 99 0.13 SIDE CHAIN
REMARK 500 22 PHE A 99 0.12 SIDE CHAIN
REMARK 500 23 ARG A 59 0.08 SIDE CHAIN
REMARK 500 23 HIS A 79 0.09 SIDE CHAIN
REMARK 500 23 PHE A 99 0.09 SIDE CHAIN
REMARK 500 24 PHE A 99 0.15 SIDE CHAIN
REMARK 500 25 PHE A 99 0.12 SIDE CHAIN
REMARK 500 26 PHE A 99 0.11 SIDE CHAIN
REMARK 500 27 PHE A 99 0.12 SIDE CHAIN
REMARK 500 28 ARG A 59 0.08 SIDE CHAIN
REMARK 500 28 PHE A 99 0.12 SIDE CHAIN
REMARK 500 29 PHE A 99 0.12 SIDE CHAIN
REMARK 500 30 PHE A 99 0.13 SIDE CHAIN
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 SER A 77 -10.12
REMARK 500 6 SER A 77 -12.17
REMARK 500 7 SER A 77 -11.75
REMARK 500 10 SER A 77 -11.95
REMARK 500 13 SER A 77 -10.39
REMARK 500 15 SER A 77 -10.51
REMARK 500 22 SER A 77 -12.13
REMARK 500 23 SER A 77 -10.32
REMARK 500 24 SER A 77 -11.08
REMARK 500 26 SER A 77 -11.57
REMARK 500 29 SER A 77 -12.16
REMARK 500 30 SER A 77 -11.06
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1RFA A 55 132 UNP P04049 RAF1_HUMAN 55 132
SEQRES 1 A 79 ALA SER ASN THR ILE ARG VAL PHE LEU PRO ASN LYS GLN
SEQRES 2 A 79 ARG THR VAL VAL ASN VAL ARG ASN GLY MET SER LEU HIS
SEQRES 3 A 79 ASP CYS LEU MET LYS ALA LEU LYS VAL ARG GLY LEU GLN
SEQRES 4 A 79 PRO GLU CYS CYS ALA VAL PHE ARG LEU LEU HIS GLU HIS
SEQRES 5 A 79 LYS GLY LYS LYS ALA ARG LEU ASP TRP ASN THR ASP ALA
SEQRES 6 A 79 ALA SER LEU ILE GLY GLU GLU LEU GLN VAL ASP PHE LEU
SEQRES 7 A 79 ASP
HELIX 1 1 LEU A 78 ARG A 89 1 12
HELIX 2 2 ALA A 118 SER A 120 5 3
SHEET 1 A 4 VAL A 69 ASN A 71 0
SHEET 2 A 4 THR A 57 PHE A 61 -1 N ILE A 58 O VAL A 70
SHEET 3 A 4 GLU A 125 PHE A 130 1 N LEU A 126 O ARG A 59
SHEET 4 A 4 CYS A 96 ARG A 100 -1 N PHE A 99 O GLN A 127
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