Header list of 2gf5.pdb file
Complete list - t 20 2 Bytes
HEADER APOPTOSIS 21-MAR-06 2GF5 TITLE STRUCTURE OF INTACT FADD (MORT1) COMPND MOL_ID: 1; COMPND 2 MOLECULE: FADD PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: FAS-ASSOCIATING DEATH DOMAIN-CONTAINING PROTEIN, MEDIATOR OF COMPND 5 RECEPTOR INDUCED TOXICITY; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: FADD, MORT1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE50 KEYWDS DEATH DOMAIN, DEATH EFFECTOR DOMAIN, APOPTOSIS, DEATH-INDUCING KEYWDS 2 SIGNALING COMPLEX EXPDTA SOLUTION NMR NUMMDL 25 AUTHOR P.E.CARRINGTON,C.SANDU,Y.WEI,J.M.HILL,G.MORISAWA,T.HUANG, AUTHOR 2 E.GAVATHIOTIS,Y.WEI,M.H.WERNER REVDAT 3 20-OCT-21 2GF5 1 REMARK SEQADV REVDAT 2 24-FEB-09 2GF5 1 VERSN REVDAT 1 27-JUN-06 2GF5 0 JRNL AUTH P.E.CARRINGTON,C.SANDU,Y.WEI,J.M.HILL,G.MORISAWA,T.HUANG, JRNL AUTH 2 E.GAVATHIOTIS,Y.WEI,M.H.WERNER JRNL TITL THE STRUCTURE OF FADD AND ITS MODE OF INTERACTION WITH JRNL TITL 2 PROCASPASE-8 JRNL REF MOL.CELL V. 22 599 2006 JRNL REFN ISSN 1097-2765 JRNL PMID 16762833 JRNL DOI 10.1016/J.MOLCEL.2006.04.018 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 2.12.2 REMARK 3 AUTHORS : BRUNGER ET AL. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: WATER REFINEMENT REMARK 4 REMARK 4 2GF5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAR-06. REMARK 100 THE DEPOSITION ID IS D_1000037040. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 288 REMARK 210 PH : 7 REMARK 210 IONIC STRENGTH : 200MM PHOSPHATE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 200MM PHOSPHATE BUFFER, 95% H2O REMARK 210 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-EDITED NOESY; 13C-EDITED REMARK 210 NOESY; CBCA(CO)NH; HNCA; C(CO)NH; REMARK 210 H(CCO)NH; HCCH-TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 2.12.2 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25 REMARK 210 CONFORMERS, SELECTION CRITERIA : 25 STRUCTURES FOR LOWEST 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 H ALA A 90 H ALA A 91 1.27 REMARK 500 C ALA A 90 H ALA A 91 1.56 REMARK 500 OE1 GLU A 94 HZ2 LYS A 149 1.58 REMARK 500 OD1 ASP A 111 HH21 ARG A 114 1.60 REMARK 500 HG1 THR A 60 OE2 GLU A 83 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 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 1 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 1 ARG A 77 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 1 ARG A 117 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 1 ARG A 135 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 1 ARG A 140 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 1 ARG A 166 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 1 MET A 170 CG - SD - CE ANGL. DEV. = -13.1 DEGREES REMARK 500 1 ARG A 184 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES REMARK 500 1 ARG A 184 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 2 ARG A 34 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 2 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 2 ARG A 77 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 2 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 2 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 2 ARG A 114 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 2 ARG A 146 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 3 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 3 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 3 ARG A 184 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 4 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 4 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 4 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 4 ARG A 77 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 4 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 4 ARG A 142 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 4 ARG A 166 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 4 MET A 170 CG - SD - CE ANGL. DEV. = -9.9 DEGREES REMARK 500 4 ARG A 189 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 5 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 5 ARG A 64 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 5 ARG A 72 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 5 ARG A 72 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 5 ARG A 77 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 5 ARG A 114 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 5 MET A 170 CG - SD - CE ANGL. DEV. = -10.7 DEGREES REMARK 500 5 ARG A 189 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 6 ARG A 113 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 6 ARG A 132 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 6 ARG A 135 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 6 MET A 170 CG - SD - CE ANGL. DEV. = -10.1 DEGREES REMARK 500 7 ARG A 38 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 7 ARG A 78 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 7 ARG A 132 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 7 ARG A 140 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 7 ARG A 146 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 7 ARG A 166 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 8 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 8 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 8 ARG A 38 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 187 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 CYS A 27 27.60 -70.61 REMARK 500 1 LEU A 28 -58.08 -26.78 REMARK 500 1 GLN A 40 -72.54 -82.48 REMARK 500 1 ASN A 53 64.04 72.82 REMARK 500 1 PRO A 57 28.38 -71.68 REMARK 500 1 ARG A 71 -42.37 86.20 REMARK 500 1 ARG A 72 93.88 -69.22 REMARK 500 1 ALA A 86 30.98 -96.18 REMARK 500 1 ALA A 87 42.43 -71.98 REMARK 500 1 LYS A 120 54.77 76.17 REMARK 500 1 GLU A 152 48.69 -92.24 REMARK 500 1 GLN A 169 45.76 76.67 REMARK 500 2 SER A 16 -154.34 -75.69 REMARK 500 2 ASN A 53 35.42 84.23 REMARK 500 2 HIS A 59 88.18 -69.77 REMARK 500 2 ARG A 71 16.41 81.52 REMARK 500 2 ALA A 87 42.09 -55.84 REMARK 500 2 LYS A 110 27.83 -72.22 REMARK 500 2 ASP A 111 13.37 -145.27 REMARK 500 2 LYS A 120 72.37 67.74 REMARK 500 2 GLU A 152 58.73 -90.77 REMARK 500 2 LYS A 153 -72.90 -70.04 REMARK 500 2 GLN A 169 12.88 93.83 REMARK 500 2 LEU A 172 -75.91 -45.00 REMARK 500 3 LYS A 33 -64.89 -27.40 REMARK 500 3 GLN A 40 -85.80 -90.47 REMARK 500 3 PRO A 57 21.54 -72.95 REMARK 500 3 ALA A 68 -7.17 -48.98 REMARK 500 3 ALA A 87 38.72 -83.84 REMARK 500 3 LYS A 110 30.87 -85.89 REMARK 500 3 LYS A 120 69.13 73.67 REMARK 500 3 GLU A 152 43.76 -102.80 REMARK 500 3 GLU A 154 0.98 -55.86 REMARK 500 4 CYS A 27 35.98 -74.74 REMARK 500 4 ASN A 53 50.88 74.18 REMARK 500 4 ARG A 72 85.13 -60.80 REMARK 500 4 ALA A 87 46.76 -88.64 REMARK 500 4 LYS A 110 25.27 -74.81 REMARK 500 4 LYS A 120 41.00 74.62 REMARK 500 5 ASN A 53 30.55 75.53 REMARK 500 5 SER A 69 -39.55 -34.41 REMARK 500 5 ARG A 71 -11.14 78.66 REMARK 500 5 ALA A 87 44.96 -95.14 REMARK 500 5 LYS A 110 29.08 -68.04 REMARK 500 5 ASP A 111 -32.00 -140.25 REMARK 500 5 LEU A 119 0.73 -65.64 REMARK 500 5 LYS A 120 45.12 74.25 REMARK 500 5 GLU A 152 53.56 -97.29 REMARK 500 5 ASN A 155 51.94 -106.62 REMARK 500 5 GLN A 169 46.58 72.47 REMARK 500 REMARK 500 THIS ENTRY HAS 266 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 ALA A 87 ALA A 88 2 147.18 REMARK 500 LYS A 120 VAL A 121 2 139.15 REMARK 500 SER A 1 ASP A 2 4 -136.54 REMARK 500 GLN A 40 SER A 41 4 -138.28 REMARK 500 GLY A 89 ALA A 90 4 149.71 REMARK 500 LYS A 110 ASP A 111 4 -144.78 REMARK 500 GLU A 152 LYS A 153 4 145.80 REMARK 500 ASP A 2 PRO A 3 5 133.74 REMARK 500 GLN A 40 SER A 41 5 -148.07 REMARK 500 LYS A 110 ASP A 111 5 -144.39 REMARK 500 SER A 1 ASP A 2 6 -142.07 REMARK 500 ALA A 88 GLY A 89 7 -149.59 REMARK 500 GLN A 40 SER A 41 8 -145.08 REMARK 500 ASN A 136 LEU A 137 8 146.22 REMARK 500 LYS A 110 ASP A 111 9 -146.50 REMARK 500 ASP A 111 TRP A 112 11 145.65 REMARK 500 ALA A 91 PRO A 92 12 -149.38 REMARK 500 SER A 1 ASP A 2 13 -149.92 REMARK 500 LYS A 120 VAL A 121 15 148.70 REMARK 500 ASP A 2 PRO A 3 16 145.93 REMARK 500 ALA A 88 GLY A 89 17 -144.75 REMARK 500 LYS A 110 ASP A 111 18 -142.21 REMARK 500 PRO A 57 GLY A 58 19 146.69 REMARK 500 ALA A 91 PRO A 92 19 -145.19 REMARK 500 ALA A 87 ALA A 88 21 147.85 REMARK 500 GLY A 85 ALA A 86 23 -149.47 REMARK 500 LYS A 110 ASP A 111 23 -136.42 REMARK 500 GLN A 40 SER A 41 24 -149.52 REMARK 500 TYR A 133 PRO A 134 24 -148.84 REMARK 500 SER A 1 ASP A 2 25 -149.68 REMARK 500 LYS A 110 ASP A 111 25 -140.18 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 38 0.09 SIDE CHAIN REMARK 500 1 ARG A 71 0.08 SIDE CHAIN REMARK 500 1 ARG A 77 0.19 SIDE CHAIN REMARK 500 1 ARG A 140 0.13 SIDE CHAIN REMARK 500 2 ARG A 38 0.10 SIDE CHAIN REMARK 500 2 ARG A 113 0.09 SIDE CHAIN REMARK 500 2 ARG A 114 0.10 SIDE CHAIN REMARK 500 2 ARG A 132 0.17 SIDE CHAIN REMARK 500 2 TYR A 133 0.09 SIDE CHAIN REMARK 500 2 ARG A 140 0.09 SIDE CHAIN REMARK 500 2 ARG A 142 0.08 SIDE CHAIN REMARK 500 2 ARG A 166 0.09 SIDE CHAIN REMARK 500 2 ARG A 189 0.12 SIDE CHAIN REMARK 500 3 TYR A 25 0.08 SIDE CHAIN REMARK 500 3 ARG A 38 0.14 SIDE CHAIN REMARK 500 3 ARG A 64 0.14 SIDE CHAIN REMARK 500 3 ARG A 140 0.08 SIDE CHAIN REMARK 500 3 ARG A 142 0.08 SIDE CHAIN REMARK 500 3 ARG A 184 0.19 SIDE CHAIN REMARK 500 4 ARG A 30 0.09 SIDE CHAIN REMARK 500 4 ARG A 38 0.09 SIDE CHAIN REMARK 500 4 ARG A 64 0.21 SIDE CHAIN REMARK 500 4 ARG A 71 0.17 SIDE CHAIN REMARK 500 4 ARG A 72 0.14 SIDE CHAIN REMARK 500 4 ARG A 78 0.11 SIDE CHAIN REMARK 500 4 ARG A 114 0.08 SIDE CHAIN REMARK 500 4 ARG A 117 0.11 SIDE CHAIN REMARK 500 4 ARG A 146 0.16 SIDE CHAIN REMARK 500 4 ARG A 166 0.10 SIDE CHAIN REMARK 500 4 ARG A 184 0.24 SIDE CHAIN REMARK 500 4 ARG A 189 0.09 SIDE CHAIN REMARK 500 5 ARG A 30 0.16 SIDE CHAIN REMARK 500 5 ARG A 113 0.09 SIDE CHAIN REMARK 500 5 ARG A 135 0.10 SIDE CHAIN REMARK 500 5 ARG A 166 0.09 SIDE CHAIN REMARK 500 6 ARG A 30 0.17 SIDE CHAIN REMARK 500 6 ARG A 78 0.09 SIDE CHAIN REMARK 500 6 ARG A 114 0.21 SIDE CHAIN REMARK 500 6 ARG A 140 0.11 SIDE CHAIN REMARK 500 6 ARG A 146 0.11 SIDE CHAIN REMARK 500 6 ARG A 166 0.09 SIDE CHAIN REMARK 500 6 ARG A 189 0.11 SIDE CHAIN REMARK 500 7 ARG A 64 0.15 SIDE CHAIN REMARK 500 7 ARG A 77 0.09 SIDE CHAIN REMARK 500 7 ARG A 132 0.08 SIDE CHAIN REMARK 500 7 ARG A 135 0.09 SIDE CHAIN REMARK 500 7 ARG A 146 0.11 SIDE CHAIN REMARK 500 7 ARG A 166 0.11 SIDE CHAIN REMARK 500 8 ARG A 64 0.13 SIDE CHAIN REMARK 500 8 ARG A 78 0.15 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 172 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED DBREF 2GF5 A 2 191 UNP Q13158 FADD_HUMAN 2 191 SEQADV 2GF5 SER A 1 UNP Q13158 CLONING ARTIFACT SEQADV 2GF5 TYR A 25 UNP Q13158 PHE 25 ENGINEERED MUTATION SEQRES 1 A 191 SER ASP PRO PHE LEU VAL LEU LEU HIS SER VAL SER SER SEQRES 2 A 191 SER LEU SER SER SER GLU LEU THR GLU LEU LYS TYR LEU SEQRES 3 A 191 CYS LEU GLY ARG VAL GLY LYS ARG LYS LEU GLU ARG VAL SEQRES 4 A 191 GLN SER GLY LEU ASP LEU PHE SER MET LEU LEU GLU GLN SEQRES 5 A 191 ASN ASP LEU GLU PRO GLY HIS THR GLU LEU LEU ARG GLU SEQRES 6 A 191 LEU LEU ALA SER LEU ARG ARG HIS ASP LEU LEU ARG ARG SEQRES 7 A 191 VAL ASP ASP PHE GLU ALA GLY ALA ALA ALA GLY ALA ALA SEQRES 8 A 191 PRO GLY GLU GLU ASP LEU CYS ALA ALA PHE ASN VAL ILE SEQRES 9 A 191 CYS ASP ASN VAL GLY LYS ASP TRP ARG ARG LEU ALA ARG SEQRES 10 A 191 GLN LEU LYS VAL SER ASP THR LYS ILE ASP SER ILE GLU SEQRES 11 A 191 ASP ARG TYR PRO ARG ASN LEU THR GLU ARG VAL ARG GLU SEQRES 12 A 191 SER LEU ARG ILE TRP LYS ASN THR GLU LYS GLU ASN ALA SEQRES 13 A 191 THR VAL ALA HIS LEU VAL GLY ALA LEU ARG SER CYS GLN SEQRES 14 A 191 MET ASN LEU VAL ALA ASP LEU VAL GLN GLU VAL GLN GLN SEQRES 15 A 191 ALA ARG ASP LEU GLN ASN ARG SER GLY HELIX 1 1 ASP A 2 SER A 13 1 12 HELIX 2 2 SER A 16 CYS A 27 1 12 HELIX 3 3 GLY A 32 VAL A 39 1 8 HELIX 4 4 GLY A 42 GLN A 52 1 11 HELIX 5 5 THR A 60 LEU A 70 1 11 HELIX 6 6 ARG A 72 GLY A 85 1 14 HELIX 7 7 GLY A 93 ASN A 107 1 15 HELIX 8 8 ASP A 111 LEU A 119 1 9 HELIX 9 9 SER A 122 TYR A 133 1 12 HELIX 10 10 LEU A 137 GLU A 152 1 16 HELIX 11 11 THR A 157 GLN A 169 1 13 HELIX 12 12 MET A 170 GLY A 191 1 22 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 20 2 Bytes