HEADER TRANSFERASE 29-JUL-12 4GC5
TITLE CRYSTAL STRUCTURE OF MURINE TFB1M
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIMETHYLADENOSINE TRANSFERASE 1, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MITOCHONDRIAL 12S RRNA DIMETHYLASE 1, MITOCHONDRIAL
COMPND 5 TRANSCRIPTION FACTOR B1, MTTFB1, S-ADENOSYLMETHIONINE-6-N', N'-
COMPND 6 ADENOSYL(RRNA) DIMETHYLTRANSFERASE 1;
COMPND 7 EC: 2.1.1.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: TFB1M;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ARCTIC EXPRESS RIL (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS METHYLTRANSFERASE FOLD, RRNA METHYLTRANSFERASE, S-ADENOSYL-L-
KEYWDS 2 METHIONINE (SAM) BINDING, METHYLATION, MITOCHONDRIA, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.E.GUJA,E.YAKUBOVSKAYA,H.SHI,E.MEJIA,E.HAMBARDJIEVA,K.VENKATARAMAN,
AUTHOR 2 A.W.KARZAI,M.GARCIA-DIAZ
REVDAT 2 02-OCT-13 4GC5 1 JRNL
REVDAT 1 10-JUL-13 4GC5 0
JRNL AUTH K.E.GUJA,K.VENKATARAMAN,E.YAKUBOVSKAYA,H.SHI,E.MEJIA,
JRNL AUTH 2 E.HAMBARDJIEVA,A.W.KARZAI,M.GARCIA-DIAZ
JRNL TITL STRUCTURAL BASIS FOR S-ADENOSYLMETHIONINE BINDING AND
JRNL TITL 2 METHYLTRANSFERASE ACTIVITY BY MITOCHONDRIAL TRANSCRIPTION
JRNL TITL 3 FACTOR B1.
JRNL REF NUCLEIC ACIDS RES. V. 41 7947 2013
JRNL REFN ISSN 0305-1048
JRNL PMID 23804760
JRNL DOI 10.1093/NAR/GKT547
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.42
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 69.2
REMARK 3 NUMBER OF REFLECTIONS : 33212
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 1678
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.4180 - 4.1204 0.96 3879 209 0.1356 0.1662
REMARK 3 2 4.1204 - 3.2714 1.00 3816 230 0.1359 0.1908
REMARK 3 3 3.2714 - 2.8581 1.00 3833 189 0.1905 0.2420
REMARK 3 4 2.8581 - 2.5969 1.00 3794 208 0.2181 0.2661
REMARK 3 5 2.5969 - 2.4108 0.92 3472 180 0.2384 0.2638
REMARK 3 6 2.4108 - 2.2687 0.79 2981 148 0.2364 0.2692
REMARK 3 7 2.2687 - 2.1551 0.68 2543 142 0.2842 0.3138
REMARK 3 8 2.1551 - 2.0613 0.58 2187 99 0.2474 0.2480
REMARK 3 9 2.0613 - 1.9820 0.49 1824 103 0.2581 0.2973
REMARK 3 10 1.9820 - 1.9136 0.40 1506 74 0.2753 0.3458
REMARK 3 11 1.9136 - 1.8538 0.30 1104 59 0.2838 0.3406
REMARK 3 12 1.8538 - 1.8010 0.16 595 37 0.2838 0.2949
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.013 2616
REMARK 3 ANGLE : 1.515 3557
REMARK 3 CHIRALITY : 0.101 410
REMARK 3 PLANARITY : 0.007 457
REMARK 3 DIHEDRAL : 15.212 997
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resid 10 through 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2652 -9.3591 97.7419
REMARK 3 T TENSOR
REMARK 3 T11: 0.6875 T22: 0.6641
REMARK 3 T33: 0.4112 T12: -0.2178
REMARK 3 T13: -0.0377 T23: -0.1124
REMARK 3 L TENSOR
REMARK 3 L11: 1.3230 L22: 7.4911
REMARK 3 L33: 1.7888 L12: -0.6896
REMARK 3 L13: -0.2437 L23: -1.2405
REMARK 3 S TENSOR
REMARK 3 S11: -0.1394 S12: 0.1530 S13: 0.1089
REMARK 3 S21: -0.2150 S22: 0.5503 S23: -0.5756
REMARK 3 S31: -0.4418 S32: 0.7643 S33: -0.4533
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resid 32 through 241 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8912 26.1370 83.9696
REMARK 3 T TENSOR
REMARK 3 T11: 0.3314 T22: 0.3437
REMARK 3 T33: 0.2902 T12: -0.1141
REMARK 3 T13: 0.0310 T23: -0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 2.5086 L22: 1.5097
REMARK 3 L33: 5.3254 L12: -0.1377
REMARK 3 L13: -0.8431 L23: -1.1723
REMARK 3 S TENSOR
REMARK 3 S11: 0.0628 S12: -0.4367 S13: 0.0707
REMARK 3 S21: 0.2070 S22: 0.0857 S23: 0.1185
REMARK 3 S31: -0.0259 S32: -0.2738 S33: -0.1415
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resid 242 through 328 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1348 24.9449 59.1993
REMARK 3 T TENSOR
REMARK 3 T11: 0.2774 T22: 0.2784
REMARK 3 T33: 0.3272 T12: -0.0704
REMARK 3 T13: -0.0003 T23: 0.1034
REMARK 3 L TENSOR
REMARK 3 L11: 3.8386 L22: 0.9475
REMARK 3 L33: 3.4005 L12: -0.2808
REMARK 3 L13: -0.7336 L23: 0.2836
REMARK 3 S TENSOR
REMARK 3 S11: 0.1569 S12: -0.2999 S13: -0.0163
REMARK 3 S21: -0.0070 S22: -0.1055 S23: -0.0316
REMARK 3 S31: 0.0820 S32: 0.2241 S33: -0.0396
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4GC5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-12.
REMARK 100 THE RCSB ID CODE IS RCSB073999.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33212
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.801
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.9 M SODIUM ACETATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 23.81500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 50.63500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 105.83000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 23.81500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 50.63500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 105.83000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 23.81500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 50.63500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 105.83000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 23.81500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 50.63500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 105.83000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MSE A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 SER A 4
REMARK 465 GLY A 5
REMARK 465 LYS A 6
REMARK 465 LEU A 7
REMARK 465 GLY A 8
REMARK 465 THR A 9
REMARK 465 LYS A 329
REMARK 465 LYS A 330
REMARK 465 SER A 331
REMARK 465 LYS A 332
REMARK 465 GLY A 333
REMARK 465 GLN A 334
REMARK 465 GLU A 335
REMARK 465 LYS A 336
REMARK 465 ASP A 337
REMARK 465 GLY A 338
REMARK 465 ASP A 339
REMARK 465 PRO A 340
REMARK 465 GLU A 341
REMARK 465 SER A 342
REMARK 465 CYS A 343
REMARK 465 GLY A 344
REMARK 465 PHE A 345
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE A 10 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 18 CD1
REMARK 470 ARG A 19 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 32 CG CD OE1 NE2
REMARK 470 ASN A 77 CG OD1 ND2
REMARK 470 GLU A 179 CG CD OE1 OE2
REMARK 470 ARG A 183 CZ NH1 NH2
REMARK 470 LYS A 191 CD CE NZ
REMARK 470 LYS A 215 CG CD CE NZ
REMARK 470 LYS A 220 CE NZ
REMARK 470 ARG A 257 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 291 NE CZ NH1 NH2
REMARK 470 LYS A 309 CG CD CE NZ
REMARK 470 GLU A 313 CG CD OE1 OE2
REMARK 470 LYS A 327 CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 GLY A 63 O HOH A 635 2.02
REMARK 500 OE1 GLN A 282 O HOH A 570 2.12
REMARK 500 O HOH A 520 O HOH A 630 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 614 O HOH A 614 3556 2.01
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 ARG A 11 100.36 -168.98
REMARK 500 LYS A 31 -4.37 -59.27
REMARK 500 GLN A 32 -132.01 -90.65
REMARK 500 LEU A 33 -27.41 38.46
REMARK 500 ASN A 135 47.94 -72.16
REMARK 500 ASP A 162 -164.56 -127.35
REMARK 500 LYS A 239 78.18 -116.76
REMARK 500 LYS A 327 59.46 -68.87
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 LEU A 33 24.2 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GC9 RELATED DB: PDB
DBREF 4GC5 A 1 345 UNP Q8JZM0 TFB1M_MOUSE 1 345
SEQRES 1 A 345 MSE ALA ALA SER GLY LYS LEU GLY THR PHE ARG LEU PRO
SEQRES 2 A 345 PRO LEU PRO THR ILE ARG GLU ILE ILE LYS LEU PHE GLY
SEQRES 3 A 345 LEU ARG ALA VAL LYS GLN LEU SER GLN ASN PHE LEU LEU
SEQRES 4 A 345 ASP LEU ARG LEU THR ASP LYS ILE VAL ARG LYS ALA GLY
SEQRES 5 A 345 SER LEU ALA ASP VAL TYR VAL TYR GLU VAL GLY PRO GLY
SEQRES 6 A 345 PRO GLY GLY ILE THR ARG SER ILE LEU ASN ALA ASN VAL
SEQRES 7 A 345 ALA GLU LEU LEU VAL VAL GLU LYS ASP THR ARG PHE ILE
SEQRES 8 A 345 PRO GLY LEU GLN MSE LEU SER ASP ALA ALA PRO GLY LYS
SEQRES 9 A 345 LEU ARG ILE VAL HIS GLY ASP VAL LEU THR TYR LYS ILE
SEQRES 10 A 345 GLU LYS ALA PHE PRO GLY ASN ILE ARG ARG GLN TRP GLU
SEQRES 11 A 345 ASP ASP PRO PRO ASN VAL HIS ILE ILE GLY ASN LEU PRO
SEQRES 12 A 345 PHE SER VAL SER THR PRO LEU ILE ILE LYS TRP LEU GLU
SEQRES 13 A 345 ASN ILE SER LEU LYS ASP GLY PRO PHE VAL TYR GLY ARG
SEQRES 14 A 345 THR LYS MSE THR LEU THR PHE GLN LYS GLU VAL ALA GLU
SEQRES 15 A 345 ARG LEU VAL ALA THR THR GLY SER LYS GLN HIS SER ARG
SEQRES 16 A 345 LEU SER ILE MSE ALA GLN TYR LEU CYS ASN VAL GLU HIS
SEQRES 17 A 345 LEU PHE THR ILE PRO GLY LYS ALA PHE VAL PRO LYS PRO
SEQRES 18 A 345 LYS VAL ASP VAL GLY VAL VAL HIS LEU THR PRO LEU ILE
SEQRES 19 A 345 GLU PRO LYS ILE LYS GLN PRO PHE LYS LEU VAL GLU LYS
SEQRES 20 A 345 VAL VAL GLN ASN ALA PHE GLN PHE ARG ARG LYS TYR CYS
SEQRES 21 A 345 HIS ARG GLY LEU GLY MSE LEU PHE PRO GLU ALA GLN ARG
SEQRES 22 A 345 LEU GLU SER THR GLY ARG LEU LEU GLN LEU ALA ASP ILE
SEQRES 23 A 345 ASP PRO THR LEU ARG PRO THR HIS LEU SER LEU MSE HIS
SEQRES 24 A 345 PHE LYS SER LEU CYS ASP VAL TYR ARG LYS MSE CYS ASP
SEQRES 25 A 345 GLU ASP PRO GLN LEU PHE THR TYR ASN PHE ARG GLU GLU
SEQRES 26 A 345 LEU LYS GLN LYS LYS SER LYS GLY GLN GLU LYS ASP GLY
SEQRES 27 A 345 ASP PRO GLU SER CYS GLY PHE
MODRES 4GC5 MSE A 96 MET SELENOMETHIONINE
MODRES 4GC5 MSE A 172 MET SELENOMETHIONINE
MODRES 4GC5 MSE A 199 MET SELENOMETHIONINE
MODRES 4GC5 MSE A 266 MET SELENOMETHIONINE
MODRES 4GC5 MSE A 298 MET SELENOMETHIONINE
MODRES 4GC5 MSE A 310 MET SELENOMETHIONINE
HET MSE A 96 13
HET MSE A 172 8
HET MSE A 199 8
HET MSE A 266 8
HET MSE A 298 8
HET MSE A 310 8
HET ACT A 401 4
HET ACT A 402 4
HETNAM MSE SELENOMETHIONINE
HETNAM ACT ACETATE ION
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 ACT 2(C2 H3 O2 1-)
FORMUL 4 HOH *233(H2 O)
HELIX 1 1 THR A 17 LYS A 31 1 15
HELIX 2 2 ASP A 40 GLY A 52 1 13
HELIX 3 3 GLY A 67 ASN A 75 1 9
HELIX 4 4 ASP A 87 ARG A 89 5 3
HELIX 5 5 PHE A 90 ALA A 101 1 12
HELIX 6 6 PRO A 122 ARG A 126 5 5
HELIX 7 7 PRO A 143 LYS A 161 1 19
HELIX 8 8 ASP A 162 GLY A 168 5 7
HELIX 9 9 LYS A 178 ALA A 186 1 9
HELIX 10 10 SER A 194 TYR A 202 1 9
HELIX 11 11 PRO A 213 PHE A 217 5 5
HELIX 12 12 PRO A 241 GLN A 254 1 14
HELIX 13 13 TYR A 259 GLY A 265 1 7
HELIX 14 14 MSE A 266 PHE A 268 5 3
HELIX 15 15 PRO A 269 ALA A 271 5 3
HELIX 16 16 GLN A 272 ASP A 285 1 14
HELIX 17 17 ARG A 291 LEU A 295 5 5
HELIX 18 18 SER A 296 ASP A 314 1 19
HELIX 19 19 GLN A 316 TYR A 320 5 5
HELIX 20 20 ASN A 321 LYS A 327 1 7
SHEET 1 A 7 LEU A 105 VAL A 108 0
SHEET 2 A 7 GLU A 80 VAL A 84 1 N VAL A 83 O ARG A 106
SHEET 3 A 7 TYR A 58 VAL A 62 1 N VAL A 59 O LEU A 82
SHEET 4 A 7 VAL A 136 GLY A 140 1 O HIS A 137 N TYR A 60
SHEET 5 A 7 LYS A 171 GLN A 177 1 O LYS A 171 N ILE A 138
SHEET 6 A 7 VAL A 225 PRO A 232 -1 O GLY A 226 N PHE A 176
SHEET 7 A 7 CYS A 204 ILE A 212 -1 N ILE A 212 O VAL A 225
LINK C GLN A 95 N MSE A 96 1555 1555 1.33
LINK C MSE A 96 N LEU A 97 1555 1555 1.32
LINK C LYS A 171 N MSE A 172 1555 1555 1.32
LINK C MSE A 172 N THR A 173 1555 1555 1.33
LINK C ILE A 198 N MSE A 199 1555 1555 1.35
LINK C MSE A 199 N ALA A 200 1555 1555 1.33
LINK C GLY A 265 N MSE A 266 1555 1555 1.35
LINK C MSE A 266 N LEU A 267 1555 1555 1.33
LINK C LEU A 297 N MSE A 298 1555 1555 1.32
LINK C MSE A 298 N HIS A 299 1555 1555 1.32
LINK C LYS A 309 N MSE A 310 1555 1555 1.33
LINK C MSE A 310 N CYS A 311 1555 1555 1.32
CISPEP 1 VAL A 218 PRO A 219 0 -9.03
SITE 1 AC1 3 LYS A 258 TYR A 259 ARG A 262
SITE 1 AC2 5 GLN A 35 GLY A 63 GLU A 85 LYS A 86
SITE 2 AC2 5 HOH A 594
CRYST1 47.630 101.270 211.660 90.00 90.00 90.00 I 2 2 2 8
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 0.020995 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009875 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004725 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
