HEADER TRANSFERASE 13-FEB-00 1EG5
TITLE NIFS-LIKE PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMINOTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: NIFS-LIKE PROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 STRAIN: ORF 1692;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET22B
KEYWDS PLP-DEPENDENT ENZYMES, IRON-SULFUR-CLUSTER SYNTHESIS, C-S BETA LYASE,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.T.KAISER,T.CLAUSEN,G.P.BOURENKOW,H.-D.BARTUNIK,S.STEINBACHER,
AUTHOR 2 R.HUBER
REVDAT 5 31-JAN-18 1EG5 1 REMARK
REVDAT 4 13-JUL-11 1EG5 1 VERSN
REVDAT 3 24-FEB-09 1EG5 1 VERSN
REVDAT 2 01-APR-03 1EG5 1 JRNL
REVDAT 1 02-APR-00 1EG5 0
JRNL AUTH J.T.KAISER,T.CLAUSEN,G.P.BOURENKOW,H.D.BARTUNIK,
JRNL AUTH 2 S.STEINBACHER,R.HUBER
JRNL TITL CRYSTAL STRUCTURE OF A NIFS-LIKE PROTEIN FROM THERMOTOGA
JRNL TITL 2 MARITIMA: IMPLICATIONS FOR IRON SULPHUR CLUSTER ASSEMBLY.
JRNL REF J.MOL.BIOL. V. 297 451 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10715213
JRNL DOI 10.1006/JMBI.2000.3581
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENG&HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3535820.020
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 78802
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3930
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12186
REMARK 3 BIN R VALUE (WORKING SET) : 0.3400
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 635
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.014
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5717
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 255
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.45000
REMARK 3 B22 (A**2) : 3.45000
REMARK 3 B33 (A**2) : -6.89000
REMARK 3 B12 (A**2) : 5.14000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.41
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.42
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.800
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.910 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.740 ; 2.500
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.830 ; 2.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 6.530 ; 3.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 46.07
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : PLP.CNS.PAR
REMARK 3 PARAMETER FILE 3 : WATER.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : PLP.CNS.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EG5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-00.
REMARK 100 THE DEPOSITION ID IS D_1000010542.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.25
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 78802
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 500.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05400
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) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
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: MAD
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 (%): 63.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, HEPES, DTT, PH 7.8,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 18K, TEMPERATURE
REMARK 280 291.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.32000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 104.64000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 104.64000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 52.32000
REMARK 290
REMARK 290 REMARK: NULL
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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. (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 SER A 321
REMARK 465 SER A 322
REMARK 465 ALA A 323
REMARK 465 CYS A 324
REMARK 465 THR A 325
REMARK 465 SER A 326
REMARK 465 LYS A 327
REMARK 465 ASP A 328
REMARK 465 GLU A 329
REMARK 465 ARG A 330
REMARK 465 LEU A 331
REMARK 465 ARG A 332
REMARK 465 ASP A 377
REMARK 465 LEU A 378
REMARK 465 THR A 379
REMARK 465 GLY A 380
REMARK 465 ASN A 381
REMARK 465 ASN A 382
REMARK 465 ARG A 383
REMARK 465 ARG A 384
REMARK 465 SER B 321
REMARK 465 SER B 322
REMARK 465 ALA B 323
REMARK 465 CYS B 324
REMARK 465 THR B 325
REMARK 465 SER B 326
REMARK 465 LYS B 327
REMARK 465 ASP B 328
REMARK 465 GLU B 329
REMARK 465 ARG B 330
REMARK 465 LEU B 331
REMARK 465 ASP B 377
REMARK 465 LEU B 378
REMARK 465 THR B 379
REMARK 465 GLY B 380
REMARK 465 ASN B 381
REMARK 465 ASN B 382
REMARK 465 ARG B 383
REMARK 465 ARG B 384
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 CYS A 69 164.14 176.22
REMARK 500 ARG A 88 -58.75 -136.63
REMARK 500 ARG A 90 -1.05 -144.24
REMARK 500 ASP A 137 -167.10 -129.94
REMARK 500 ASN A 169 95.98 -161.43
REMARK 500 ILE A 221 143.03 -179.70
REMARK 500 ASN A 278 20.53 -76.04
REMARK 500 LYS B 87 -27.81 72.88
REMARK 500 ARG B 88 -73.03 -87.56
REMARK 500 ARG B 90 -6.77 -146.09
REMARK 500 ILE B 221 144.97 179.32
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 SO4 B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ECX RELATED DB: PDB
REMARK 900 NIFS-LIKE PROTEIN, SUBSTRATE COMPLEX
DBREF 1EG5 A 1 384 UNP Q9X218 Q9X218_THEMA 1 384
DBREF 1EG5 B 1 384 UNP Q9X218 Q9X218_THEMA 1 384
SEQADV 1EG5 MSE A 1 UNP Q9X218 MET 1 MODIFIED RESIDUE
SEQADV 1EG5 MSE A 21 UNP Q9X218 MET 21 MODIFIED RESIDUE
SEQADV 1EG5 MSE A 38 UNP Q9X218 MET 38 MODIFIED RESIDUE
SEQADV 1EG5 MSE A 46 UNP Q9X218 MET 46 MODIFIED RESIDUE
SEQADV 1EG5 MSE A 106 UNP Q9X218 MET 106 MODIFIED RESIDUE
SEQADV 1EG5 MSE A 111 UNP Q9X218 MET 111 MODIFIED RESIDUE
SEQADV 1EG5 MSE A 146 UNP Q9X218 MET 146 MODIFIED RESIDUE
SEQADV 1EG5 MSE A 251 UNP Q9X218 MET 251 MODIFIED RESIDUE
SEQADV 1EG5 MSE A 265 UNP Q9X218 MET 265 MODIFIED RESIDUE
SEQADV 1EG5 MSE A 277 UNP Q9X218 MET 277 MODIFIED RESIDUE
SEQADV 1EG5 ARG A 332 UNP Q9X218 SER 332 SEE REMARK 999
SEQADV 1EG5 MSE A 338 UNP Q9X218 MET 338 MODIFIED RESIDUE
SEQADV 1EG5 MSE B 1 UNP Q9X218 MET 1 MODIFIED RESIDUE
SEQADV 1EG5 MSE B 21 UNP Q9X218 MET 21 MODIFIED RESIDUE
SEQADV 1EG5 MSE B 38 UNP Q9X218 MET 38 MODIFIED RESIDUE
SEQADV 1EG5 MSE B 46 UNP Q9X218 MET 46 MODIFIED RESIDUE
SEQADV 1EG5 MSE B 106 UNP Q9X218 MET 106 MODIFIED RESIDUE
SEQADV 1EG5 MSE B 111 UNP Q9X218 MET 111 MODIFIED RESIDUE
SEQADV 1EG5 MSE B 146 UNP Q9X218 MET 146 MODIFIED RESIDUE
SEQADV 1EG5 MSE B 251 UNP Q9X218 MET 251 MODIFIED RESIDUE
SEQADV 1EG5 MSE B 265 UNP Q9X218 MET 265 MODIFIED RESIDUE
SEQADV 1EG5 MSE B 277 UNP Q9X218 MET 277 MODIFIED RESIDUE
SEQADV 1EG5 ARG B 332 UNP Q9X218 SER 332 SEE REMARK 999
SEQADV 1EG5 MSE B 338 UNP Q9X218 MET 338 MODIFIED RESIDUE
SEQRES 1 A 384 MSE ARG VAL TYR PHE ASP ASN ASN ALA THR THR ARG VAL
SEQRES 2 A 384 ASP ASP ARG VAL LEU GLU GLU MSE ILE VAL PHE TYR ARG
SEQRES 3 A 384 GLU LYS TYR GLY ASN PRO ASN SER ALA HIS GLY MSE GLY
SEQRES 4 A 384 ILE GLU ALA ASN LEU HIS MSE GLU LYS ALA ARG GLU LYS
SEQRES 5 A 384 VAL ALA LYS VAL LEU GLY VAL SER PRO SER GLU ILE PHE
SEQRES 6 A 384 PHE THR SER CYS ALA THR GLU SER ILE ASN TRP ILE LEU
SEQRES 7 A 384 LYS THR VAL ALA GLU THR PHE GLU LYS ARG LYS ARG THR
SEQRES 8 A 384 ILE ILE THR THR PRO ILE GLU HIS LYS ALA VAL LEU GLU
SEQRES 9 A 384 THR MSE LYS TYR LEU SER MSE LYS GLY PHE LYS VAL LYS
SEQRES 10 A 384 TYR VAL PRO VAL ASP SER ARG GLY VAL VAL LYS LEU GLU
SEQRES 11 A 384 GLU LEU GLU LYS LEU VAL ASP GLU ASP THR PHE LEU VAL
SEQRES 12 A 384 SER ILE MSE ALA ALA ASN ASN GLU VAL GLY THR ILE GLN
SEQRES 13 A 384 PRO VAL GLU ASP VAL THR ARG ILE VAL LYS LYS LYS ASN
SEQRES 14 A 384 LYS GLU THR LEU VAL HIS VAL ASP ALA VAL GLN THR ILE
SEQRES 15 A 384 GLY LYS ILE PRO PHE SER LEU GLU LYS LEU GLU VAL ASP
SEQRES 16 A 384 TYR ALA SER PHE SER ALA HIS LYS PHE HIS GLY PRO LYS
SEQRES 17 A 384 GLY VAL GLY ILE THR TYR ILE ARG LYS GLY VAL PRO ILE
SEQRES 18 A 384 ARG PRO LEU ILE HIS GLY GLY GLY GLN GLU ARG GLY LEU
SEQRES 19 A 384 ARG SER GLY THR GLN ASN VAL PRO GLY ILE VAL GLY ALA
SEQRES 20 A 384 ALA ARG ALA MSE GLU ILE ALA VAL GLU GLU LEU SER GLU
SEQRES 21 A 384 ALA ALA LYS HIS MSE GLU LYS LEU ARG SER LYS LEU VAL
SEQRES 22 A 384 SER GLY LEU MSE ASN LEU GLY ALA HIS ILE ILE THR PRO
SEQRES 23 A 384 LEU GLU ILE SER LEU PRO ASN THR LEU SER VAL SER PHE
SEQRES 24 A 384 PRO ASN ILE ARG GLY SER THR LEU GLN ASN LEU LEU SER
SEQRES 25 A 384 GLY TYR GLY ILE TYR VAL SER THR SER SER ALA CYS THR
SEQRES 26 A 384 SER LYS ASP GLU ARG LEU ARG HIS VAL LEU ASP ALA MSE
SEQRES 27 A 384 GLY VAL ASP ARG ARG ILE ALA GLN GLY ALA ILE ARG ILE
SEQRES 28 A 384 SER LEU CYS LYS TYR ASN THR GLU GLU GLU VAL ASP TYR
SEQRES 29 A 384 PHE LEU LYS LYS ILE GLU GLU ILE LEU SER PHE LEU ASP
SEQRES 30 A 384 LEU THR GLY ASN ASN ARG ARG
SEQRES 1 B 384 MSE ARG VAL TYR PHE ASP ASN ASN ALA THR THR ARG VAL
SEQRES 2 B 384 ASP ASP ARG VAL LEU GLU GLU MSE ILE VAL PHE TYR ARG
SEQRES 3 B 384 GLU LYS TYR GLY ASN PRO ASN SER ALA HIS GLY MSE GLY
SEQRES 4 B 384 ILE GLU ALA ASN LEU HIS MSE GLU LYS ALA ARG GLU LYS
SEQRES 5 B 384 VAL ALA LYS VAL LEU GLY VAL SER PRO SER GLU ILE PHE
SEQRES 6 B 384 PHE THR SER CYS ALA THR GLU SER ILE ASN TRP ILE LEU
SEQRES 7 B 384 LYS THR VAL ALA GLU THR PHE GLU LYS ARG LYS ARG THR
SEQRES 8 B 384 ILE ILE THR THR PRO ILE GLU HIS LYS ALA VAL LEU GLU
SEQRES 9 B 384 THR MSE LYS TYR LEU SER MSE LYS GLY PHE LYS VAL LYS
SEQRES 10 B 384 TYR VAL PRO VAL ASP SER ARG GLY VAL VAL LYS LEU GLU
SEQRES 11 B 384 GLU LEU GLU LYS LEU VAL ASP GLU ASP THR PHE LEU VAL
SEQRES 12 B 384 SER ILE MSE ALA ALA ASN ASN GLU VAL GLY THR ILE GLN
SEQRES 13 B 384 PRO VAL GLU ASP VAL THR ARG ILE VAL LYS LYS LYS ASN
SEQRES 14 B 384 LYS GLU THR LEU VAL HIS VAL ASP ALA VAL GLN THR ILE
SEQRES 15 B 384 GLY LYS ILE PRO PHE SER LEU GLU LYS LEU GLU VAL ASP
SEQRES 16 B 384 TYR ALA SER PHE SER ALA HIS LYS PHE HIS GLY PRO LYS
SEQRES 17 B 384 GLY VAL GLY ILE THR TYR ILE ARG LYS GLY VAL PRO ILE
SEQRES 18 B 384 ARG PRO LEU ILE HIS GLY GLY GLY GLN GLU ARG GLY LEU
SEQRES 19 B 384 ARG SER GLY THR GLN ASN VAL PRO GLY ILE VAL GLY ALA
SEQRES 20 B 384 ALA ARG ALA MSE GLU ILE ALA VAL GLU GLU LEU SER GLU
SEQRES 21 B 384 ALA ALA LYS HIS MSE GLU LYS LEU ARG SER LYS LEU VAL
SEQRES 22 B 384 SER GLY LEU MSE ASN LEU GLY ALA HIS ILE ILE THR PRO
SEQRES 23 B 384 LEU GLU ILE SER LEU PRO ASN THR LEU SER VAL SER PHE
SEQRES 24 B 384 PRO ASN ILE ARG GLY SER THR LEU GLN ASN LEU LEU SER
SEQRES 25 B 384 GLY TYR GLY ILE TYR VAL SER THR SER SER ALA CYS THR
SEQRES 26 B 384 SER LYS ASP GLU ARG LEU ARG HIS VAL LEU ASP ALA MSE
SEQRES 27 B 384 GLY VAL ASP ARG ARG ILE ALA GLN GLY ALA ILE ARG ILE
SEQRES 28 B 384 SER LEU CYS LYS TYR ASN THR GLU GLU GLU VAL ASP TYR
SEQRES 29 B 384 PHE LEU LYS LYS ILE GLU GLU ILE LEU SER PHE LEU ASP
SEQRES 30 B 384 LEU THR GLY ASN ASN ARG ARG
MODRES 1EG5 MSE A 1 MET SELENOMETHIONINE
MODRES 1EG5 MSE A 21 MET SELENOMETHIONINE
MODRES 1EG5 MSE A 38 MET SELENOMETHIONINE
MODRES 1EG5 MSE A 46 MET SELENOMETHIONINE
MODRES 1EG5 MSE A 106 MET SELENOMETHIONINE
MODRES 1EG5 MSE A 111 MET SELENOMETHIONINE
MODRES 1EG5 MSE A 146 MET SELENOMETHIONINE
MODRES 1EG5 MSE A 251 MET SELENOMETHIONINE
MODRES 1EG5 MSE A 265 MET SELENOMETHIONINE
MODRES 1EG5 MSE A 277 MET SELENOMETHIONINE
MODRES 1EG5 MSE A 338 MET SELENOMETHIONINE
MODRES 1EG5 MSE B 1 MET SELENOMETHIONINE
MODRES 1EG5 MSE B 21 MET SELENOMETHIONINE
MODRES 1EG5 MSE B 38 MET SELENOMETHIONINE
MODRES 1EG5 MSE B 46 MET SELENOMETHIONINE
MODRES 1EG5 MSE B 106 MET SELENOMETHIONINE
MODRES 1EG5 MSE B 111 MET SELENOMETHIONINE
MODRES 1EG5 MSE B 146 MET SELENOMETHIONINE
MODRES 1EG5 MSE B 251 MET SELENOMETHIONINE
MODRES 1EG5 MSE B 265 MET SELENOMETHIONINE
MODRES 1EG5 MSE B 277 MET SELENOMETHIONINE
MODRES 1EG5 MSE B 338 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 21 8
HET MSE A 38 8
HET MSE A 46 8
HET MSE A 106 8
HET MSE A 111 8
HET MSE A 146 8
HET MSE A 251 8
HET MSE A 265 8
HET MSE A 277 8
HET MSE A 338 8
HET MSE B 1 8
HET MSE B 21 8
HET MSE B 38 8
HET MSE B 46 8
HET MSE B 106 8
HET MSE B 111 8
HET MSE B 146 8
HET MSE B 251 8
HET MSE B 265 8
HET MSE B 277 8
HET MSE B 338 8
HET SO4 A 603 5
HET PLP A 601 15
HET SO4 B 602 5
HET PLP B 600 15
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 1 MSE 22(C5 H11 N O2 SE)
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 PLP 2(C8 H10 N O6 P)
FORMUL 7 HOH *255(H2 O)
HELIX 1 1 ASP A 14 GLU A 27 1 14
HELIX 2 2 HIS A 36 GLY A 58 1 23
HELIX 3 3 SER A 60 SER A 62 5 3
HELIX 4 4 CYS A 69 PHE A 85 1 17
HELIX 5 5 HIS A 99 LYS A 112 1 14
HELIX 6 6 LYS A 128 VAL A 136 1 9
HELIX 7 7 PRO A 157 ASN A 169 1 13
HELIX 8 8 HIS A 202 HIS A 205 5 4
HELIX 9 9 ASN A 240 GLU A 257 1 18
HELIX 10 10 GLU A 257 ASN A 278 1 22
HELIX 11 11 ARG A 303 TYR A 314 1 12
HELIX 12 12 HIS A 333 MSE A 338 1 6
HELIX 13 13 ASP A 341 GLY A 347 1 7
HELIX 14 14 THR A 358 LEU A 376 1 19
HELIX 15 15 ASP B 14 GLU B 27 1 14
HELIX 16 16 HIS B 36 GLY B 58 1 23
HELIX 17 17 SER B 60 SER B 62 5 3
HELIX 18 18 CYS B 69 PHE B 85 1 17
HELIX 19 19 HIS B 99 LYS B 112 1 14
HELIX 20 20 LYS B 128 VAL B 136 1 9
HELIX 21 21 PRO B 157 ASN B 169 1 13
HELIX 22 22 HIS B 202 PHE B 204 5 3
HELIX 23 23 ASN B 240 GLU B 257 1 18
HELIX 24 24 GLU B 257 ASN B 278 1 22
HELIX 25 25 PRO B 286 ILE B 289 5 4
HELIX 26 26 ARG B 303 TYR B 314 1 12
HELIX 27 27 ARG B 332 MSE B 338 1 7
HELIX 28 28 ASP B 341 GLY B 347 1 7
HELIX 29 29 THR B 358 LEU B 376 1 19
SHEET 1 A 2 VAL A 3 TYR A 4 0
SHEET 2 A 2 ILE A 316 TYR A 317 1 N TYR A 317 O VAL A 3
SHEET 1 B 7 ILE A 64 THR A 67 0
SHEET 2 B 7 GLY A 211 ILE A 215 -1 N GLY A 211 O THR A 67
SHEET 3 B 7 TYR A 196 SER A 200 -1 O ALA A 197 N TYR A 214
SHEET 4 B 7 LEU A 173 ASP A 177 1 O VAL A 174 N TYR A 196
SHEET 5 B 7 THR A 140 MSE A 146 1 O PHE A 141 N LEU A 173
SHEET 6 B 7 THR A 91 THR A 94 1 O THR A 91 N PHE A 141
SHEET 7 B 7 LYS A 115 TYR A 118 1 O LYS A 115 N ILE A 92
SHEET 1 C 3 HIS A 282 ILE A 283 0
SHEET 2 C 3 THR A 294 SER A 298 -1 O SER A 298 N HIS A 282
SHEET 3 C 3 ALA A 348 SER A 352 -1 N ILE A 349 O VAL A 297
SHEET 1 D 2 VAL B 3 TYR B 4 0
SHEET 2 D 2 ILE B 316 TYR B 317 1 N TYR B 317 O VAL B 3
SHEET 1 E 7 ILE B 64 THR B 67 0
SHEET 2 E 7 GLY B 211 ILE B 215 -1 N GLY B 211 O THR B 67
SHEET 3 E 7 TYR B 196 SER B 200 -1 O ALA B 197 N TYR B 214
SHEET 4 E 7 LEU B 173 ASP B 177 1 O VAL B 174 N TYR B 196
SHEET 5 E 7 THR B 140 MSE B 146 1 O PHE B 141 N LEU B 173
SHEET 6 E 7 THR B 91 THR B 94 1 O THR B 91 N PHE B 141
SHEET 7 E 7 LYS B 115 TYR B 118 1 O LYS B 115 N ILE B 92
SHEET 1 F 3 HIS B 282 ILE B 283 0
SHEET 2 F 3 THR B 294 SER B 298 -1 O SER B 298 N HIS B 282
SHEET 3 F 3 ALA B 348 SER B 352 -1 N ILE B 349 O VAL B 297
LINK C4A PLP A 601 NZ LYS A 203 1555 1555 1.45
LINK C4A PLP B 600 NZ LYS B 203 1555 1555 1.45
LINK C MSE A 1 N ARG A 2 1555 1555 1.33
LINK C GLU A 20 N MSE A 21 1555 1555 1.33
LINK C MSE A 21 N ILE A 22 1555 1555 1.33
LINK C GLY A 37 N MSE A 38 1555 1555 1.33
LINK C MSE A 38 N GLY A 39 1555 1555 1.33
LINK C HIS A 45 N MSE A 46 1555 1555 1.33
LINK C MSE A 46 N GLU A 47 1555 1555 1.34
LINK C THR A 105 N MSE A 106 1555 1555 1.33
LINK C MSE A 106 N LYS A 107 1555 1555 1.33
LINK C SER A 110 N MSE A 111 1555 1555 1.33
LINK C MSE A 111 N LYS A 112 1555 1555 1.33
LINK C ILE A 145 N MSE A 146 1555 1555 1.33
LINK C MSE A 146 N ALA A 147 1555 1555 1.33
LINK C ALA A 250 N MSE A 251 1555 1555 1.34
LINK C MSE A 251 N GLU A 252 1555 1555 1.33
LINK C HIS A 264 N MSE A 265 1555 1555 1.33
LINK C MSE A 265 N GLU A 266 1555 1555 1.33
LINK C LEU A 276 N MSE A 277 1555 1555 1.33
LINK C MSE A 277 N ASN A 278 1555 1555 1.33
LINK C ALA A 337 N MSE A 338 1555 1555 1.33
LINK C MSE A 338 N GLY A 339 1555 1555 1.33
LINK C MSE B 1 N ARG B 2 1555 1555 1.34
LINK C GLU B 20 N MSE B 21 1555 1555 1.33
LINK C MSE B 21 N ILE B 22 1555 1555 1.33
LINK C GLY B 37 N MSE B 38 1555 1555 1.33
LINK C MSE B 38 N GLY B 39 1555 1555 1.32
LINK C HIS B 45 N MSE B 46 1555 1555 1.33
LINK C MSE B 46 N GLU B 47 1555 1555 1.33
LINK C THR B 105 N MSE B 106 1555 1555 1.33
LINK C MSE B 106 N LYS B 107 1555 1555 1.33
LINK C SER B 110 N MSE B 111 1555 1555 1.33
LINK C MSE B 111 N LYS B 112 1555 1555 1.33
LINK C ILE B 145 N MSE B 146 1555 1555 1.33
LINK C MSE B 146 N ALA B 147 1555 1555 1.33
LINK C ALA B 250 N MSE B 251 1555 1555 1.34
LINK C MSE B 251 N GLU B 252 1555 1555 1.33
LINK C HIS B 264 N MSE B 265 1555 1555 1.33
LINK C MSE B 265 N GLU B 266 1555 1555 1.33
LINK C LEU B 276 N MSE B 277 1555 1555 1.33
LINK C MSE B 277 N ASN B 278 1555 1555 1.33
LINK C ALA B 337 N MSE B 338 1555 1555 1.33
LINK C MSE B 338 N GLY B 339 1555 1555 1.33
SITE 1 AC1 5 ASN B 8 ALA B 9 HIS B 99 ASN B 150
SITE 2 AC1 5 ARG B 350
SITE 1 AC2 5 ASN A 8 ALA A 9 HIS A 99 ASN A 150
SITE 2 AC2 5 ARG A 350
SITE 1 AC3 13 THR A 238 CYS B 69 ALA B 70 THR B 71
SITE 2 AC3 13 HIS B 99 MSE B 146 ASN B 150 ASP B 177
SITE 3 AC3 13 VAL B 179 GLN B 180 SER B 200 HIS B 202
SITE 4 AC3 13 LYS B 203
SITE 1 AC4 12 CYS A 69 ALA A 70 THR A 71 HIS A 99
SITE 2 AC4 12 ASN A 150 ASP A 177 VAL A 179 GLN A 180
SITE 3 AC4 12 SER A 200 HIS A 202 LYS A 203 THR B 238
CRYST1 114.110 114.110 156.960 90.00 90.00 120.00 P 31 2 1 12
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 0.008763 0.005060 0.000000 0.00000
SCALE2 0.000000 0.010119 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006371 0.00000
HETATM 1 N MSE A 1 13.649 75.211 44.643 1.00 55.31 N
HETATM 2 CA MSE A 1 14.740 74.219 44.845 1.00 55.13 C
HETATM 3 C MSE A 1 14.284 72.804 44.486 1.00 52.69 C
HETATM 4 O MSE A 1 13.090 72.554 44.276 1.00 52.87 O
HETATM 5 CB MSE A 1 15.242 74.260 46.301 1.00 56.27 C
HETATM 6 CG MSE A 1 14.178 73.962 47.365 1.00 67.15 C
HETATM 7 SE MSE A 1 14.734 74.064 49.138 1.00 73.02 SE
HETATM 8 CE MSE A 1 14.560 75.873 49.437 1.00 73.44 C
(ATOM LINES ARE NOT SHOWN.)
END
