HEADER TRANSFERASE 12-OCT-18 6MRH
TITLE E. COLI CYSTEINE DESULFURASE SUFS E96A WITH A CYSTEINE PERSULFIDE
TITLE 2 INTERMEDIATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTEINE DESULFURASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SELENOCYSTEINE BETA-LYASE, SCL, SELENOCYSTEINE LYASE,
COMPND 5 SELENOCYSTEINE REDUCTASE;
COMPND 6 EC: 2.8.1.7,4.4.1.16;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: SUFS, CSDB, YNHB, B1680, JW1670;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS CYSTEINE DESULFURASE, SUFS, PERSULFIDE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.DUNKLE,P.A.FRANTOM
REVDAT 5 15-NOV-23 6MRH 1 REMARK
REVDAT 4 11-OCT-23 6MRH 1 LINK
REVDAT 3 01-JAN-20 6MRH 1 REMARK
REVDAT 2 27-FEB-19 6MRH 1 JRNL
REVDAT 1 09-JAN-19 6MRH 0
JRNL AUTH J.A.DUNKLE,M.R.BRUNO,F.W.OUTTEN,P.A.FRANTOM
JRNL TITL STRUCTURAL EVIDENCE FOR DIMER-INTERFACE-DRIVEN REGULATION OF
JRNL TITL 2 THE TYPE II CYSTEINE DESULFURASE, SUFS.
JRNL REF BIOCHEMISTRY V. 58 687 2019
JRNL REFN ISSN 1520-4995
JRNL PMID 30571100
JRNL DOI 10.1021/ACS.BIOCHEM.8B01122
REMARK 2
REMARK 2 RESOLUTION. 2.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.14_3211
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.51
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 72510
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.760
REMARK 3 FREE R VALUE TEST SET COUNT : 2002
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 43.5156 - 4.8625 1.00 5383 153 0.1751 0.1862
REMARK 3 2 4.8625 - 3.8602 1.00 5137 148 0.1621 0.1805
REMARK 3 3 3.8602 - 3.3725 1.00 5098 141 0.1870 0.2062
REMARK 3 4 3.3725 - 3.0642 1.00 5072 140 0.2037 0.2337
REMARK 3 5 3.0642 - 2.8446 1.00 5040 129 0.2116 0.2360
REMARK 3 6 2.8446 - 2.6770 1.00 5025 153 0.2101 0.2486
REMARK 3 7 2.6770 - 2.5429 1.00 5030 139 0.2077 0.2212
REMARK 3 8 2.5429 - 2.4322 1.00 5013 148 0.2106 0.2230
REMARK 3 9 2.4322 - 2.3386 1.00 4972 148 0.2089 0.2252
REMARK 3 10 2.3386 - 2.2579 1.00 4998 135 0.2138 0.2378
REMARK 3 11 2.2579 - 2.1873 0.99 4945 142 0.2359 0.2266
REMARK 3 12 2.1873 - 2.1248 1.00 5006 133 0.2286 0.2436
REMARK 3 13 2.1248 - 2.0688 1.00 4968 144 0.2413 0.2420
REMARK 3 14 2.0688 - 2.0184 0.97 4821 149 0.2919 0.3007
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.43
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 6MRH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237444.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUN-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72610
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 1.40100
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1JF9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 79.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4-4.5 M SODIUM CHLORIDE, 100 MM MES,
REMARK 280 PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 68.47600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 62.98700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 62.98700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 102.71400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 62.98700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 62.98700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 34.23800
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 62.98700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.98700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 102.71400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 62.98700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.98700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.23800
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 68.47600
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: 7730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26800 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 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 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 MET A -13
REMARK 465 ALA A -12
REMARK 465 SER A -11
REMARK 465 MET A -10
REMARK 465 THR A -9
REMARK 465 GLY A -8
REMARK 465 GLY A -7
REMARK 465 GLN A -6
REMARK 465 GLN A -5
REMARK 465 MET A -4
REMARK 465 GLY A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
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 56 50.51 32.18
REMARK 500 ILE A 127 -57.28 -127.86
REMARK 500 LEU A 227 40.72 -101.03
REMARK 500 TRP A 249 -86.71 -118.57
REMARK 500 SER A 254 -23.34 82.85
REMARK 500 ASN A 330 32.42 -89.65
REMARK 500 ALA A 365 57.82 -141.93
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 270 PRO A 271 68.32
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 PLP A 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6MR2 RELATED DB: PDB
REMARK 900 RELATED ID: 6MR6 RELATED DB: PDB
REMARK 900 RELATED ID: 6MRE RELATED DB: PDB
REMARK 900 RELATED ID: 6MRI RELATED DB: PDB
DBREF 6MRH A 1 406 UNP P77444 SUFS_ECOLI 1 406
SEQADV 6MRH MET A -13 UNP P77444 EXPRESSION TAG
SEQADV 6MRH ALA A -12 UNP P77444 EXPRESSION TAG
SEQADV 6MRH SER A -11 UNP P77444 EXPRESSION TAG
SEQADV 6MRH MET A -10 UNP P77444 EXPRESSION TAG
SEQADV 6MRH THR A -9 UNP P77444 EXPRESSION TAG
SEQADV 6MRH GLY A -8 UNP P77444 EXPRESSION TAG
SEQADV 6MRH GLY A -7 UNP P77444 EXPRESSION TAG
SEQADV 6MRH GLN A -6 UNP P77444 EXPRESSION TAG
SEQADV 6MRH GLN A -5 UNP P77444 EXPRESSION TAG
SEQADV 6MRH MET A -4 UNP P77444 EXPRESSION TAG
SEQADV 6MRH GLY A -3 UNP P77444 EXPRESSION TAG
SEQADV 6MRH ARG A -2 UNP P77444 EXPRESSION TAG
SEQADV 6MRH GLY A -1 UNP P77444 EXPRESSION TAG
SEQADV 6MRH SER A 0 UNP P77444 EXPRESSION TAG
SEQADV 6MRH ALA A 96 UNP P77444 GLU 96 ENGINEERED MUTATION
SEQRES 1 A 420 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY
SEQRES 2 A 420 SER MET ILE PHE SER VAL ASP LYS VAL ARG ALA ASP PHE
SEQRES 3 A 420 PRO VAL LEU SER ARG GLU VAL ASN GLY LEU PRO LEU ALA
SEQRES 4 A 420 TYR LEU ASP SER ALA ALA SER ALA GLN LYS PRO SER GLN
SEQRES 5 A 420 VAL ILE ASP ALA GLU ALA GLU PHE TYR ARG HIS GLY TYR
SEQRES 6 A 420 ALA ALA VAL HIS ARG GLY ILE HIS THR LEU SER ALA GLN
SEQRES 7 A 420 ALA THR GLU LYS MET GLU ASN VAL ARG LYS ARG ALA SER
SEQRES 8 A 420 LEU PHE ILE ASN ALA ARG SER ALA GLU GLU LEU VAL PHE
SEQRES 9 A 420 VAL ARG GLY THR THR ALA GLY ILE ASN LEU VAL ALA ASN
SEQRES 10 A 420 SER TRP GLY ASN SER ASN VAL ARG ALA GLY ASP ASN ILE
SEQRES 11 A 420 ILE ILE SER GLN MET GLU HIS HIS ALA ASN ILE VAL PRO
SEQRES 12 A 420 TRP GLN MET LEU CYS ALA ARG VAL GLY ALA GLU LEU ARG
SEQRES 13 A 420 VAL ILE PRO LEU ASN PRO ASP GLY THR LEU GLN LEU GLU
SEQRES 14 A 420 THR LEU PRO THR LEU PHE ASP GLU LYS THR ARG LEU LEU
SEQRES 15 A 420 ALA ILE THR HIS VAL SER ASN VAL LEU GLY THR GLU ASN
SEQRES 16 A 420 PRO LEU ALA GLU MET ILE THR LEU ALA HIS GLN HIS GLY
SEQRES 17 A 420 ALA LYS VAL LEU VAL ASP GLY ALA GLN ALA VAL MET HIS
SEQRES 18 A 420 HIS PRO VAL ASP VAL GLN ALA LEU ASP CYS ASP PHE TYR
SEQRES 19 A 420 VAL PHE SER GLY HIS LYS LEU TYR GLY PRO THR GLY ILE
SEQRES 20 A 420 GLY ILE LEU TYR VAL LYS GLU ALA LEU LEU GLN GLU MET
SEQRES 21 A 420 PRO PRO TRP GLU GLY GLY GLY SER MET ILE ALA THR VAL
SEQRES 22 A 420 SER LEU SER GLU GLY THR THR TRP THR LYS ALA PRO TRP
SEQRES 23 A 420 ARG PHE GLU ALA GLY THR PRO ASN THR GLY GLY ILE ILE
SEQRES 24 A 420 GLY LEU GLY ALA ALA LEU GLU TYR VAL SER ALA LEU GLY
SEQRES 25 A 420 LEU ASN ASN ILE ALA GLU TYR GLU GLN ASN LEU MET HIS
SEQRES 26 A 420 TYR ALA LEU SER GLN LEU GLU SER VAL PRO ASP LEU THR
SEQRES 27 A 420 LEU TYR GLY PRO GLN ASN ARG LEU GLY VAL ILE ALA PHE
SEQRES 28 A 420 ASN LEU GLY LYS HIS HIS ALA TYR ASP VAL GLY SER PHE
SEQRES 29 A 420 LEU ASP ASN TYR GLY ILE ALA VAL ARG THR GLY HIS HIS
SEQRES 30 A 420 CSS ALA MET PRO LEU MET ALA TYR TYR ASN VAL PRO ALA
SEQRES 31 A 420 MET CYS ARG ALA SER LEU ALA MET TYR ASN THR HIS GLU
SEQRES 32 A 420 GLU VAL ASP ARG LEU VAL THR GLY LEU GLN ARG ILE HIS
SEQRES 33 A 420 ARG LEU LEU GLY
MODRES 6MRH CSS A 364 CYS MODIFIED RESIDUE
HET CSS A 364 7
HET PLP A 500 22
HETNAM CSS S-MERCAPTOCYSTEINE
HETNAM PLP PYRIDOXAL-5'-PHOSPHATE
HETSYN PLP VITAMIN B6 PHOSPHATE
FORMUL 1 CSS C3 H7 N O2 S2
FORMUL 2 PLP C8 H10 N O6 P
FORMUL 3 HOH *118(H2 O)
HELIX 1 AA1 SER A 4 ASP A 11 1 8
HELIX 2 AA2 PHE A 12 SER A 16 5 5
HELIX 3 AA3 PRO A 36 GLY A 50 1 15
HELIX 4 AA4 HIS A 59 ILE A 80 1 22
HELIX 5 AA5 SER A 84 GLU A 86 5 3
HELIX 6 AA6 GLY A 93 VAL A 110 1 18
HELIX 7 AA7 HIS A 123 ASN A 126 5 4
HELIX 8 AA8 ILE A 127 GLY A 138 1 12
HELIX 9 AA9 GLN A 153 GLU A 155 5 3
HELIX 10 AB1 THR A 156 PHE A 161 1 6
HELIX 11 AB2 PRO A 182 HIS A 193 1 12
HELIX 12 AB3 ASP A 211 ASP A 216 1 6
HELIX 13 AB4 HIS A 225 LEU A 227 5 3
HELIX 14 AB5 LYS A 239 GLN A 244 1 6
HELIX 15 AB6 PRO A 271 GLU A 275 5 5
HELIX 16 AB7 ASN A 280 GLY A 298 1 19
HELIX 17 AB8 GLY A 298 GLU A 318 1 21
HELIX 18 AB9 HIS A 343 TYR A 354 1 12
HELIX 19 AC1 ALA A 365 TYR A 372 1 8
HELIX 20 AC2 THR A 387 GLY A 406 1 20
SHEET 1 AA1 2 GLU A 18 VAL A 19 0
SHEET 2 AA1 2 LEU A 22 PRO A 23 -1 O LEU A 22 N VAL A 19
SHEET 1 AA2 2 ALA A 25 TYR A 26 0
SHEET 2 AA2 2 ILE A 356 ALA A 357 1 O ALA A 357 N ALA A 25
SHEET 1 AA3 7 LEU A 88 VAL A 91 0
SHEET 2 AA3 7 GLY A 234 VAL A 238 -1 O LEU A 236 N VAL A 89
SHEET 3 AA3 7 PHE A 219 SER A 223 -1 N TYR A 220 O TYR A 237
SHEET 4 AA3 7 LYS A 196 ASP A 200 1 N VAL A 199 O PHE A 219
SHEET 5 AA3 7 THR A 165 THR A 171 1 N LEU A 168 O LYS A 196
SHEET 6 AA3 7 ASN A 115 SER A 119 1 N ILE A 117 O ALA A 169
SHEET 7 AA3 7 GLU A 140 ILE A 144 1 O ARG A 142 N ILE A 116
SHEET 1 AA4 2 ILE A 256 SER A 260 0
SHEET 2 AA4 2 GLY A 264 TRP A 267 -1 O THR A 266 N ALA A 257
SHEET 1 AA5 4 LEU A 323 TYR A 326 0
SHEET 2 AA5 4 VAL A 334 LEU A 339 -1 O ASN A 338 N THR A 324
SHEET 3 AA5 4 MET A 377 SER A 381 -1 O CYS A 378 N PHE A 337
SHEET 4 AA5 4 ARG A 359 GLY A 361 -1 N ARG A 359 O ARG A 379
LINK NZ LYS A 226 C4A PLP A 500 1555 1555 1.43
LINK C HIS A 363 N CSS A 364 1555 1555 1.33
LINK C CSS A 364 N ALA A 365 1555 1555 1.34
SITE 1 AC1 12 THR A 94 THR A 95 HIS A 123 ASN A 175
SITE 2 AC1 12 ASP A 200 ALA A 202 GLN A 203 SER A 223
SITE 3 AC1 12 HIS A 225 LYS A 226 THR A 278 HOH A 615
CRYST1 125.974 125.974 136.952 90.00 90.00 90.00 P 43 21 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 0.007938 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007938 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007302 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
