Header list of 2bkd.pdb file
Complete list - r 22 2 Bytes
HEADER NUCLEAR PROTEIN 15-FEB-05 2BKD TITLE STRUCTURE OF THE N-TERMINAL DOMAIN OF FRAGILE X MENTAL RETARDATION TITLE 2 PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: FRAGILE X MESSENGER RIBONUCLEOPROTEIN 1; COMPND 3 CHAIN: N; COMPND 4 FRAGMENT: RESIDUES 1-134; COMPND 5 SYNONYM: FRAGILE X MESSENGER RIBONUCLEOPROTEIN,FMRP,PROTEIN FMR-1; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: FMR1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET24 KEYWDS FMRP, PROTEIN-PROTEIN INTERACTION, MRNA TRANSPORT, NUCLEAR PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.RAMOS,D.HOLLINGWORTH,S.ADINOLFI,M.CASTETS,G.KELLY,T.A.FRENKIEL, AUTHOR 2 B.BARDONI,A.PASTORE REVDAT 4 01-FEB-23 2BKD 1 COMPND SOURCE REMARK DBREF REVDAT 4 2 1 SEQRES HET HETNAM FORMUL REVDAT 4 3 1 LINK ATOM REVDAT 3 28-MAR-18 2BKD 1 SOURCE JRNL ATOM REVDAT 2 24-FEB-09 2BKD 1 VERSN REVDAT 1 18-JAN-06 2BKD 0 JRNL AUTH A.RAMOS,D.HOLLINGWORTH,S.ADINOLFI,M.CASTETS,G.KELLY, JRNL AUTH 2 T.A.FRENKIEL,B.BARDONI,A.PASTORE JRNL TITL THE STRUCTURE OF THE N-TERMINAL DOMAIN OF THE FRAGILE X JRNL TITL 2 MENTAL RETARDATION PROTEIN: A PLATFORM FOR PROTEIN-PROTEIN JRNL TITL 3 INTERACTION. JRNL REF STRUCTURE V. 14 21 2006 JRNL REFN ISSN 0969-2126 JRNL PMID 16407062 JRNL DOI 10.1016/J.STR.2005.09.018 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XPLOR-NIH REMARK 3 AUTHORS : C.D.SCHWIETERS,J.J.KUSZEWSKI,N.TJ REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE REMARK 3 JRNL CITATION REMARK 4 REMARK 4 2BKD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-FEB-05. REMARK 100 THE DEPOSITION ID IS D_1290022994. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300.0 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 10 REMARK 210 PRESSURE : 1.0 ATM REMARK 210 SAMPLE CONTENTS : 10% D2O/90% H2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-NOESY; 13C-NOESY; HNCO; REMARK 210 HNCA; HNCOCACB; HNCACB REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY REMARK 210 METHOD USED : RMD REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST ENERGY AND LEAST RESTRAINT REMARK 210 VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NONE 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: N 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: 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 VAL N 6 CG1 - CB - CG2 ANGL. DEV. = -10.8 DEGREES REMARK 500 1 ARG N 48 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 2 ARG N 70 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 3 VAL N 6 CG1 - CB - CG2 ANGL. DEV. = -9.8 DEGREES REMARK 500 3 ARG N 9 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 3 PHE N 32 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES REMARK 500 3 TYR N 96 CB - CG - CD2 ANGL. DEV. = -5.4 DEGREES REMARK 500 3 TYR N 96 CB - CG - CD1 ANGL. DEV. = 5.1 DEGREES REMARK 500 3 PHE N 126 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 4 VAL N 6 CG1 - CB - CG2 ANGL. DEV. = -11.1 DEGREES REMARK 500 4 TYR N 96 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES REMARK 500 5 ARG N 48 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 5 ARG N 48 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES REMARK 500 5 TYR N 96 CB - CG - CD2 ANGL. DEV. = -5.9 DEGREES REMARK 500 5 TYR N 96 CB - CG - CD1 ANGL. DEV. = 5.3 DEGREES REMARK 500 6 ARG N 48 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 6 PHE N 126 CB - CG - CD2 ANGL. DEV. = -4.9 DEGREES REMARK 500 6 PHE N 126 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES REMARK 500 7 VAL N 6 CG1 - CB - CG2 ANGL. DEV. = -10.1 DEGREES REMARK 500 7 TYR N 68 CB - CG - CD1 ANGL. DEV. = -3.8 DEGREES REMARK 500 7 ARG N 113 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 8 ARG N 48 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 8 ARG N 48 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES REMARK 500 8 PHE N 126 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES REMARK 500 8 PHE N 126 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES REMARK 500 9 PHE N 126 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES REMARK 500 10 VAL N 6 CG1 - CB - CG2 ANGL. DEV. = -10.6 DEGREES REMARK 500 10 PHE N 32 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES REMARK 500 10 ARG N 113 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 10 PHE N 126 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 10 PHE N 126 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES REMARK 500 11 VAL N 6 CG1 - CB - CG2 ANGL. DEV. = -11.0 DEGREES REMARK 500 11 ARG N 40 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 11 TYR N 96 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES REMARK 500 11 TYR N 96 CB - CG - CD1 ANGL. DEV. = 5.1 DEGREES REMARK 500 11 ARG N 111 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 12 TYR N 96 CB - CG - CD2 ANGL. DEV. = -5.7 DEGREES REMARK 500 12 TYR N 96 CB - CG - CD1 ANGL. DEV. = 5.0 DEGREES REMARK 500 13 TYR N 68 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES REMARK 500 13 ARG N 111 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 14 ARG N 9 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES REMARK 500 14 ARG N 40 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 14 TYR N 55 CB - CG - CD2 ANGL. DEV. = -4.1 DEGREES REMARK 500 14 ARG N 111 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 14 PHE N 126 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES REMARK 500 14 PHE N 126 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES REMARK 500 15 ARG N 9 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 15 ARG N 9 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 15 ARG N 40 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 15 ARG N 48 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 75 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 GLU N 3 -95.49 -139.78 REMARK 500 1 SER N 11 -46.18 74.44 REMARK 500 1 HIS N 24 -154.60 -99.90 REMARK 500 1 ASN N 34 34.48 37.64 REMARK 500 1 TRP N 36 -77.69 -147.60 REMARK 500 1 GLN N 37 112.63 -163.82 REMARK 500 1 ASP N 39 81.66 81.42 REMARK 500 1 ASN N 56 -63.70 -132.54 REMARK 500 1 GLU N 61 109.87 71.42 REMARK 500 1 SER N 62 52.26 70.96 REMARK 500 1 ASP N 63 -155.72 -115.63 REMARK 500 1 GLU N 73 -53.90 73.59 REMARK 500 1 CYS N 78 -86.91 -126.99 REMARK 500 1 TRP N 79 122.82 87.74 REMARK 500 1 ALA N 98 -103.69 60.52 REMARK 500 1 CYS N 99 174.31 70.08 REMARK 500 1 ASP N 100 -120.05 -94.12 REMARK 500 1 TYR N 103 -131.02 -93.65 REMARK 500 1 ASN N 116 107.88 78.88 REMARK 500 1 PRO N 120 -88.81 -73.73 REMARK 500 1 THR N 122 159.65 68.09 REMARK 500 1 LYS N 123 -87.86 69.36 REMARK 500 1 ASP N 132 -115.40 28.15 REMARK 500 2 GLU N 3 -59.25 -142.22 REMARK 500 2 ASN N 34 -7.97 64.61 REMARK 500 2 TRP N 36 92.25 -161.16 REMARK 500 2 GLN N 37 157.74 89.81 REMARK 500 2 PRO N 38 -87.63 -79.58 REMARK 500 2 ASN N 56 -139.54 -116.28 REMARK 500 2 LYS N 57 -112.82 -103.24 REMARK 500 2 ASN N 60 24.28 -141.99 REMARK 500 2 SER N 62 -63.88 -161.75 REMARK 500 2 ALA N 71 46.87 -78.24 REMARK 500 2 ASN N 72 -79.59 -142.40 REMARK 500 2 GLU N 73 125.00 91.05 REMARK 500 2 CYS N 78 135.77 74.24 REMARK 500 2 TRP N 79 78.03 -113.09 REMARK 500 2 MET N 86 -173.82 156.19 REMARK 500 2 ASP N 100 -70.72 -70.95 REMARK 500 2 ALA N 101 133.51 77.25 REMARK 500 2 ILE N 109 90.46 -69.11 REMARK 500 2 GLU N 110 -55.03 -127.69 REMARK 500 2 VAL N 115 101.05 61.17 REMARK 500 2 THR N 122 132.59 76.98 REMARK 500 2 LYS N 123 -68.51 65.49 REMARK 500 2 LYS N 128 63.53 -152.09 REMARK 500 3 GLU N 2 64.55 69.34 REMARK 500 3 GLU N 3 -74.64 -115.52 REMARK 500 3 HIS N 24 -166.26 -111.08 REMARK 500 3 TRP N 36 -53.86 -155.04 REMARK 500 REMARK 500 THIS ENTRY HAS 450 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 GLU N 75 PRO N 76 1 -149.77 REMARK 500 GLU N 33 ASN N 34 3 -146.12 REMARK 500 GLU N 33 ASN N 34 6 -147.77 REMARK 500 TRP N 36 GLN N 37 7 -148.63 REMARK 500 CYS N 77 CYS N 78 8 144.22 REMARK 500 GLU N 33 ASN N 34 10 -146.45 REMARK 500 TRP N 79 TRP N 80 10 -149.61 REMARK 500 ASN N 35 TRP N 36 11 -146.46 REMARK 500 HIS N 24 GLU N 25 12 -147.11 REMARK 500 ASN N 34 ASN N 35 12 147.96 REMARK 500 ASN N 72 GLU N 73 16 147.27 REMARK 500 ASN N 72 GLU N 73 17 141.22 REMARK 500 LYS N 74 GLU N 75 19 -146.67 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 N 19 0.11 SIDE CHAIN REMARK 500 1 ARG N 40 0.09 SIDE CHAIN REMARK 500 1 HIS N 45 0.11 SIDE CHAIN REMARK 500 1 ARG N 85 0.10 SIDE CHAIN REMARK 500 2 ARG N 9 0.10 SIDE CHAIN REMARK 500 2 PHE N 19 0.10 SIDE CHAIN REMARK 500 2 ARG N 111 0.09 SIDE CHAIN REMARK 500 3 PHE N 19 0.10 SIDE CHAIN REMARK 500 3 HIS N 45 0.09 SIDE CHAIN REMARK 500 4 PHE N 19 0.08 SIDE CHAIN REMARK 500 4 HIS N 45 0.10 SIDE CHAIN REMARK 500 4 ARG N 70 0.08 SIDE CHAIN REMARK 500 5 ARG N 9 0.07 SIDE CHAIN REMARK 500 5 PHE N 19 0.11 SIDE CHAIN REMARK 500 5 HIS N 45 0.09 SIDE CHAIN REMARK 500 5 TYR N 55 0.07 SIDE CHAIN REMARK 500 5 ARG N 70 0.09 SIDE CHAIN REMARK 500 6 PHE N 19 0.08 SIDE CHAIN REMARK 500 6 TYR N 55 0.09 SIDE CHAIN REMARK 500 6 ARG N 111 0.10 SIDE CHAIN REMARK 500 6 ARG N 113 0.12 SIDE CHAIN REMARK 500 7 PHE N 19 0.10 SIDE CHAIN REMARK 500 7 HIS N 45 0.10 SIDE CHAIN REMARK 500 7 TYR N 55 0.12 SIDE CHAIN REMARK 500 7 ARG N 85 0.13 SIDE CHAIN REMARK 500 7 TYR N 103 0.08 SIDE CHAIN REMARK 500 7 ARG N 111 0.07 SIDE CHAIN REMARK 500 8 ARG N 9 0.19 SIDE CHAIN REMARK 500 8 PHE N 19 0.10 SIDE CHAIN REMARK 500 8 ARG N 48 0.08 SIDE CHAIN REMARK 500 8 TYR N 68 0.08 SIDE CHAIN REMARK 500 8 ARG N 70 0.15 SIDE CHAIN REMARK 500 8 ARG N 111 0.12 SIDE CHAIN REMARK 500 8 ARG N 113 0.10 SIDE CHAIN REMARK 500 9 PHE N 19 0.10 SIDE CHAIN REMARK 500 10 HIS N 45 0.10 SIDE CHAIN REMARK 500 10 TYR N 55 0.07 SIDE CHAIN REMARK 500 10 TYR N 68 0.08 SIDE CHAIN REMARK 500 10 ARG N 85 0.09 SIDE CHAIN REMARK 500 10 ARG N 111 0.12 SIDE CHAIN REMARK 500 11 PHE N 19 0.07 SIDE CHAIN REMARK 500 11 ARG N 40 0.09 SIDE CHAIN REMARK 500 11 HIS N 45 0.11 SIDE CHAIN REMARK 500 11 TYR N 68 0.12 SIDE CHAIN REMARK 500 12 ARG N 9 0.10 SIDE CHAIN REMARK 500 12 PHE N 19 0.10 SIDE CHAIN REMARK 500 12 ARG N 40 0.09 SIDE CHAIN REMARK 500 12 ARG N 48 0.12 SIDE CHAIN REMARK 500 12 TYR N 55 0.09 SIDE CHAIN REMARK 500 13 ARG N 9 0.13 SIDE CHAIN REMARK 500 REMARK 500 THIS ENTRY HAS 78 PLANE DEVIATIONS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2FMR RELATED DB: PDB REMARK 900 KH1 FROM THE FRAGILE X PROTEIN FMR1, NMR , 18 STRUCTURES DBREF 2BKD N 1 134 UNP Q06787 FMR1_HUMAN 1 134 SEQRES 1 N 134 MET GLU GLU LEU VAL VAL GLU VAL ARG GLY SER ASN GLY SEQRES 2 N 134 ALA PHE TYR LYS ALA PHE VAL LYS ASP VAL HIS GLU ASP SEQRES 3 N 134 SER ILE THR VAL ALA PHE GLU ASN ASN TRP GLN PRO ASP SEQRES 4 N 134 ARG GLN ILE PRO PHE HIS ASP VAL ARG PHE PRO PRO PRO SEQRES 5 N 134 VAL GLY TYR ASN LYS ASP ILE ASN GLU SER ASP GLU VAL SEQRES 6 N 134 GLU VAL TYR SER ARG ALA ASN GLU LYS GLU PRO CYS CYS SEQRES 7 N 134 TRP TRP LEU ALA LYS VAL ARG MET ILE LYS GLY GLU PHE SEQRES 8 N 134 TYR VAL ILE GLU TYR ALA ALA CYS ASP ALA THR TYR ASN SEQRES 9 N 134 GLU ILE VAL THR ILE GLU ARG LEU ARG SER VAL ASN PRO SEQRES 10 N 134 ASN LYS PRO ALA THR LYS ASP THR PHE HIS LYS ILE LYS SEQRES 11 N 134 LEU ASP VAL PRO MODRES 2BKD HIS N 24 HIS L-HISTIDINOL MODRES 2BKD HIS N 45 HIS L-HISTIDINOL MODRES 2BKD HIS N 127 HIS L-HISTIDINOL SHEET 1 NA 5 ARG N 40 PRO N 43 0 SHEET 2 NA 5 SER N 27 ALA N 31 -1 O ILE N 28 N ILE N 42 SHEET 3 NA 5 PHE N 15 VAL N 23 -1 O PHE N 19 N ALA N 31 SHEET 4 NA 5 VAL N 5 ARG N 9 -1 O VAL N 6 N ALA N 18 SHEET 5 NA 5 VAL N 47 ARG N 48 -1 O ARG N 48 N GLU N 7 SHEET 1 NB 5 GLU N 105 THR N 108 0 SHEET 2 NB 5 PHE N 91 TYR N 96 -1 O TYR N 92 N VAL N 107 SHEET 3 NB 5 TRP N 80 LYS N 88 -1 O LYS N 83 N GLU N 95 SHEET 4 NB 5 GLU N 64 VAL N 67 -1 O VAL N 65 N ALA N 82 SHEET 5 NB 5 LEU N 112 ARG N 113 -1 O ARG N 113 N GLU N 66 LINK C VAL N 23 N HIS N 24 1555 1555 1.34 LINK C HIS N 24 N GLU N 25 1555 1555 1.35 LINK C PHE N 44 N HIS N 45 1555 1555 1.35 LINK C HIS N 45 N ASP N 46 1555 1555 1.35 LINK C PHE N 126 N HIS N 127 1555 1555 1.35 LINK C HIS N 127 N LYS N 128 1555 1555 1.35 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 22 2 Bytes