Header list of 2f2d.pdb file
Complete list - r 9 2 Bytes
HEADER ISOMERASE 16-NOV-05 2F2D TITLE SOLUTION STRUCTURE OF THE FK506-BINDING DOMAIN OF HUMAN FKBP38 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 38 KDA FK-506 BINDING PROTEIN HOMOLOG, FKBP38; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: FK506-BINDING DOMAIN, RESIDUES 35-153; COMPND 5 SYNONYM: FKBPR38, FK506-BINDING PROTEIN 8; 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: FKBP8, FKBP38; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A KEYWDS BETA HALF-BARREL, PPIASE, IMMUNOPHILIN, ISOMERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR M.MAESTRE-MARTINEZ,F.EDLICH,F.JARCZOWSKI,M.WEIWAD,G.FISCHER,C.LUECKE REVDAT 3 09-MAR-22 2F2D 1 REMARK SEQADV REVDAT 2 24-FEB-09 2F2D 1 VERSN REVDAT 1 02-MAY-06 2F2D 0 JRNL AUTH M.MAESTRE-MARTINEZ,F.EDLICH,F.JARCZOWSKI,M.WEIWAD,G.FISCHER, JRNL AUTH 2 C.LUECKE JRNL TITL SOLUTION STRUCTURE OF THE FK506-BINDING DOMAIN OF HUMAN JRNL TITL 2 FKBP38 JRNL REF J.BIOMOL.NMR V. 34 197 2006 JRNL REFN ISSN 0925-2738 JRNL PMID 16604427 JRNL DOI 10.1007/S10858-006-0018-6 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, DISCOVER 2000 REMARK 3 AUTHORS : BRUKER (XWINNMR), ACCELRYS (DISCOVER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 1585 NOE REMARK 3 -DERIVED DISTANTS RESTRAINTS REMARK 4 REMARK 4 2F2D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-05. REMARK 100 THE DEPOSITION ID IS D_1000035366. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.7 REMARK 210 IONIC STRENGTH : 20 MM SODIUM PHOSPHATE REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.3 MM HFKBP38D, 20 MM PHOSPHATE REMARK 210 BUFFER, 0.05% AZIDE, 95% H2O, 5% REMARK 210 D2O; 1.3 MM HFKBP38D U-15N, 20 REMARK 210 MM PHOSPHATE BUFFER, 0.05% AZIDE, REMARK 210 95% H2O, 5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; 2D_15N REMARK 210 -SEPARATED_HSQC; 2D_15N- REMARK 210 SEPARATED_HTQC; 3D_15N-SEPARATED_ REMARK 210 TOCSY; 3D_15N-SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 700 MHZ REMARK 210 SPECTROMETER MODEL : DRX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : AURELIA 2.5.9, FELIX 2000, DYANA REMARK 210 1.5 REMARK 210 METHOD USED : SIMULATED ANNEALING COMBINED REMARK 210 WITH TORSION ANGLE DYNAMICS REMARK 210 FOLLOWED BY ENERGY MINIMIZATION REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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 OE1 GLU A 85 HZ1 LYS A 144 1.55 REMARK 500 HZ1 LYS A 47 OE2 GLU A 110 1.56 REMARK 500 OE1 GLU A 35 HE ARG A 46 1.58 REMARK 500 OE2 GLU A 35 HH21 ARG A 46 1.59 REMARK 500 OE2 GLU A 83 HH22 ARG A 127 1.59 REMARK 500 HE ARG A 79 OE1 GLU A 82 1.59 REMARK 500 HH21 ARG A 79 OE2 GLU A 82 1.59 REMARK 500 REMARK 500 REMARK: NULL 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 1 HIS A 69 CG HIS A 69 CD2 0.063 REMARK 500 2 HIS A 69 CG HIS A 69 CD2 0.058 REMARK 500 3 HIS A 69 CG HIS A 69 CD2 0.059 REMARK 500 4 HIS A 69 CG HIS A 69 CD2 0.058 REMARK 500 5 HIS A 69 CG HIS A 69 CD2 0.061 REMARK 500 5 HIS A 134 CG HIS A 134 CD2 0.054 REMARK 500 6 HIS A 69 CG HIS A 69 CD2 0.057 REMARK 500 6 HIS A 134 CG HIS A 134 CD2 0.055 REMARK 500 7 HIS A 69 CG HIS A 69 CD2 0.060 REMARK 500 8 HIS A 69 CG HIS A 69 CD2 0.061 REMARK 500 9 HIS A 69 CG HIS A 69 CD2 0.055 REMARK 500 9 HIS A 134 CG HIS A 134 CD2 0.055 REMARK 500 10 HIS A 69 CG HIS A 69 CD2 0.060 REMARK 500 10 HIS A 134 CG HIS A 134 CD2 0.056 REMARK 500 11 HIS A 69 CG HIS A 69 CD2 0.061 REMARK 500 11 HIS A 134 CG HIS A 134 CD2 0.055 REMARK 500 12 HIS A 69 CG HIS A 69 CD2 0.058 REMARK 500 13 HIS A 69 CG HIS A 69 CD2 0.058 REMARK 500 13 HIS A 134 CG HIS A 134 CD2 0.060 REMARK 500 15 HIS A 69 CG HIS A 69 CD2 0.058 REMARK 500 16 HIS A 69 CG HIS A 69 CD2 0.056 REMARK 500 17 HIS A 69 CG HIS A 69 CD2 0.057 REMARK 500 17 HIS A 134 CG HIS A 134 CD2 0.054 REMARK 500 18 HIS A 69 CG HIS A 69 CD2 0.057 REMARK 500 18 HIS A 134 CG HIS A 134 CD2 0.059 REMARK 500 19 HIS A 69 CG HIS A 69 CD2 0.055 REMARK 500 20 HIS A 134 CG HIS A 134 CD2 0.060 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 34 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 1 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 1 ARG A 59 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 1 HIS A 69 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES REMARK 500 1 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 1 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 1 HIS A 134 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES REMARK 500 2 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 2 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 2 ARG A 59 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES REMARK 500 2 HIS A 69 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 2 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 2 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES REMARK 500 2 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 2 HIS A 134 ND1 - CE1 - NE2 ANGL. DEV. = 8.7 DEGREES REMARK 500 3 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 3 ARG A 59 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 3 HIS A 69 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES REMARK 500 3 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 3 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 3 HIS A 134 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES REMARK 500 4 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 4 ARG A 34 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES REMARK 500 4 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES REMARK 500 4 ARG A 59 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 4 HIS A 69 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 4 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 4 GLU A 85 N - CA - CB ANGL. DEV. = 11.3 DEGREES REMARK 500 4 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 4 HIS A 134 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 5 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 5 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 5 ARG A 46 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES REMARK 500 5 ARG A 59 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 5 HIS A 69 ND1 - CE1 - NE2 ANGL. DEV. = 8.8 DEGREES REMARK 500 5 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 5 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 5 HIS A 134 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 6 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 6 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 6 ARG A 59 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES REMARK 500 6 HIS A 69 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 6 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES REMARK 500 6 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 6 HIS A 134 ND1 - CE1 - NE2 ANGL. DEV. = 8.9 DEGREES REMARK 500 7 ARG A 34 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES REMARK 500 7 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 7 ARG A 59 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES REMARK 500 7 HIS A 69 ND1 - CE1 - NE2 ANGL. DEV. = 9.0 DEGREES REMARK 500 7 ARG A 79 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 140 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 ARG A 34 61.90 64.71 REMARK 500 1 GLU A 35 -173.24 64.49 REMARK 500 1 LEU A 40 -70.30 -66.22 REMARK 500 1 LEU A 44 -80.59 72.93 REMARK 500 1 ASP A 94 -65.27 -148.49 REMARK 500 1 LEU A 105 70.66 -100.49 REMARK 500 1 HIS A 134 174.65 71.13 REMARK 500 1 ALA A 135 118.39 78.72 REMARK 500 2 ARG A 34 -73.55 -77.30 REMARK 500 2 TRP A 36 134.05 72.57 REMARK 500 2 ASN A 42 -72.70 -66.62 REMARK 500 2 LEU A 44 -72.98 -121.82 REMARK 500 2 CYS A 93 78.08 58.90 REMARK 500 2 ASP A 94 -66.71 -149.78 REMARK 500 2 PRO A 104 1.08 -67.99 REMARK 500 2 LYS A 119 -51.91 -172.17 REMARK 500 2 GLN A 125 -66.92 -144.67 REMARK 500 2 HIS A 134 172.18 70.00 REMARK 500 2 ALA A 135 111.22 74.18 REMARK 500 2 LYS A 144 -74.10 -73.07 REMARK 500 3 ARG A 34 -76.43 -132.12 REMARK 500 3 TRP A 36 -135.94 68.92 REMARK 500 3 ILE A 39 45.29 -104.29 REMARK 500 3 LEU A 40 -58.45 -175.02 REMARK 500 3 LEU A 44 63.70 15.82 REMARK 500 3 SER A 57 85.19 53.96 REMARK 500 3 THR A 78 -157.13 50.92 REMARK 500 3 VAL A 80 -71.31 -87.20 REMARK 500 3 ASP A 94 -66.44 -151.39 REMARK 500 3 SER A 102 61.57 -104.54 REMARK 500 3 VAL A 103 -61.02 -94.96 REMARK 500 3 ASP A 117 42.91 -91.45 REMARK 500 3 SER A 118 54.79 35.34 REMARK 500 3 LYS A 119 -58.86 -151.86 REMARK 500 3 GLN A 125 -70.69 -160.54 REMARK 500 3 ARG A 127 52.42 -111.34 REMARK 500 3 SER A 128 143.77 65.46 REMARK 500 3 ALA A 135 21.30 -158.19 REMARK 500 3 ALA A 136 134.93 72.68 REMARK 500 4 TRP A 36 106.25 86.54 REMARK 500 4 ASN A 42 -70.62 -69.56 REMARK 500 4 LEU A 44 -78.74 -137.04 REMARK 500 4 GLU A 85 94.69 133.36 REMARK 500 4 ASP A 92 -16.71 -146.32 REMARK 500 4 CYS A 93 86.61 76.20 REMARK 500 4 ASP A 94 -70.63 -132.84 REMARK 500 4 MET A 106 109.65 -160.23 REMARK 500 4 SER A 118 64.09 33.35 REMARK 500 4 LYS A 119 -61.28 -176.60 REMARK 500 4 TYR A 122 -69.41 -137.16 REMARK 500 REMARK 500 THIS ENTRY HAS 277 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 LEU A 37 ASP A 38 7 149.59 REMARK 500 SER A 118 LYS A 119 9 -142.71 REMARK 500 SER A 118 LYS A 119 15 -147.52 REMARK 500 ARG A 34 GLU A 35 17 -149.04 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 3 ARG A 34 0.11 SIDE CHAIN REMARK 500 3 ARG A 46 0.10 SIDE CHAIN REMARK 500 6 TYR A 120 0.08 SIDE CHAIN REMARK 500 7 TYR A 122 0.06 SIDE CHAIN REMARK 500 8 ARG A 79 0.10 SIDE CHAIN REMARK 500 9 ARG A 46 0.14 SIDE CHAIN REMARK 500 11 TYR A 120 0.06 SIDE CHAIN REMARK 500 13 ARG A 46 0.08 SIDE CHAIN REMARK 500 15 ARG A 46 0.11 SIDE CHAIN REMARK 500 16 ARG A 46 0.11 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 2F2D A 35 153 UNP Q14318 FKBP8_HUMAN 35 153 SEQADV 2F2D MET A 33 UNP Q14318 CLONING ARTIFACT SEQADV 2F2D ARG A 34 UNP Q14318 CLONING ARTIFACT SEQRES 1 A 121 MET ARG GLU TRP LEU ASP ILE LEU GLY ASN GLY LEU LEU SEQRES 2 A 121 ARG LYS LYS THR LEU VAL PRO GLY PRO PRO GLY SER SER SEQRES 3 A 121 ARG PRO VAL LYS GLY GLN VAL VAL THR VAL HIS LEU GLN SEQRES 4 A 121 THR SER LEU GLU ASN GLY THR ARG VAL GLN GLU GLU PRO SEQRES 5 A 121 GLU LEU VAL PHE THR LEU GLY ASP CYS ASP VAL ILE GLN SEQRES 6 A 121 ALA LEU ASP LEU SER VAL PRO LEU MET ASP VAL GLY GLU SEQRES 7 A 121 THR ALA MET VAL THR ALA ASP SER LYS TYR CYS TYR GLY SEQRES 8 A 121 PRO GLN GLY ARG SER PRO TYR ILE PRO PRO HIS ALA ALA SEQRES 9 A 121 LEU CYS LEU GLU VAL THR LEU LYS THR ALA VAL ASP GLY SEQRES 10 A 121 PRO ASP LEU GLU HELIX 1 1 ILE A 96 VAL A 103 1 8 SHEET 1 A 5 LEU A 45 VAL A 51 0 SHEET 2 A 5 THR A 111 ALA A 116 -1 O THR A 115 N ARG A 46 SHEET 3 A 5 CYS A 138 VAL A 147 -1 O VAL A 141 N ALA A 112 SHEET 4 A 5 VAL A 65 SER A 73 -1 N SER A 73 O CYS A 138 SHEET 5 A 5 ARG A 79 THR A 89 -1 O LEU A 86 N VAL A 68 CISPEP 1 SER A 128 PRO A 129 1 11.60 CISPEP 2 SER A 128 PRO A 129 2 11.60 CISPEP 3 SER A 128 PRO A 129 3 -1.22 CISPEP 4 SER A 128 PRO A 129 4 10.21 CISPEP 5 SER A 128 PRO A 129 5 7.46 CISPEP 6 SER A 128 PRO A 129 6 10.64 CISPEP 7 SER A 128 PRO A 129 7 8.77 CISPEP 8 SER A 128 PRO A 129 8 -3.77 CISPEP 9 SER A 128 PRO A 129 9 4.83 CISPEP 10 SER A 128 PRO A 129 10 3.38 CISPEP 11 SER A 128 PRO A 129 11 9.28 CISPEP 12 SER A 128 PRO A 129 12 8.10 CISPEP 13 SER A 128 PRO A 129 13 6.37 CISPEP 14 SER A 128 PRO A 129 14 9.08 CISPEP 15 SER A 128 PRO A 129 15 10.99 CISPEP 16 SER A 128 PRO A 129 16 9.56 CISPEP 17 SER A 128 PRO A 129 17 -1.47 CISPEP 18 SER A 128 PRO A 129 18 2.58 CISPEP 19 SER A 128 PRO A 129 19 9.83 CISPEP 20 SER A 128 PRO A 129 20 8.42 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 9 2 Bytes