HEADER BIOSYNTHETIC PROTEIN 01-MAR-10 3LZC
TITLE CRYSTAL STRUCTURE OF DPH2 FROM PYROCOCCUS HORIKOSHII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DPH2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII;
SOURCE 3 ORGANISM_TAXID: 53953;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PDESTF1
KEYWDS DIPHTHAMIDE BIOSYNTHESIS, RADICAL SAM ENZYME, GENE TRIPLICATION,
KEYWDS 2 BIOSYNTHETIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHANG,X.ZHU,A.T.TORELLI,M.LEE,B.DZIKOVSKI,R.M.KORALEWSKI,E.WANG,
AUTHOR 2 J.FREED,C.KREBS,H.LIN,S.E.EALICK
REVDAT 4 21-FEB-24 3LZC 1 SEQADV
REVDAT 3 08-NOV-17 3LZC 1 REMARK
REVDAT 2 14-JUL-10 3LZC 1 JRNL
REVDAT 1 23-JUN-10 3LZC 0
JRNL AUTH Y.ZHANG,X.ZHU,A.T.TORELLI,M.LEE,B.DZIKOVSKI,R.M.KORALEWSKI,
JRNL AUTH 2 E.WANG,J.FREED,C.KREBS,S.E.EALICK,H.LIN
JRNL TITL DIPHTHAMIDE BIOSYNTHESIS REQUIRES AN ORGANIC RADICAL
JRNL TITL 2 GENERATED BY AN IRON-SULPHUR ENZYME.
JRNL REF NATURE V. 465 891 2010
JRNL REFN ISSN 0028-0836
JRNL PMID 20559380
JRNL DOI 10.1038/NATURE09138
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.5_2
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 36367
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1848
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 40.1950 - 5.3140 0.99 2880 184 0.1730 0.2040
REMARK 3 2 5.3140 - 4.2190 1.00 2787 141 0.1560 0.1570
REMARK 3 3 4.2190 - 3.6860 0.99 2770 140 0.1690 0.1900
REMARK 3 4 3.6860 - 3.3490 0.99 2743 131 0.2040 0.2620
REMARK 3 5 3.3490 - 3.1090 0.99 2697 167 0.2200 0.2690
REMARK 3 6 3.1090 - 2.9260 0.99 2696 135 0.2410 0.2860
REMARK 3 7 2.9260 - 2.7800 0.99 2698 138 0.2370 0.3170
REMARK 3 8 2.7800 - 2.6590 0.99 2662 140 0.2320 0.3300
REMARK 3 9 2.6590 - 2.5560 0.99 2683 152 0.2330 0.2980
REMARK 3 10 2.5560 - 2.4680 0.98 2630 161 0.2500 0.3470
REMARK 3 11 2.4680 - 2.3910 0.96 2632 127 0.2460 0.2730
REMARK 3 12 2.3910 - 2.3230 0.92 2487 104 0.2510 0.2880
REMARK 3 13 2.3230 - 2.2610 0.80 2154 128 0.2590 0.3060
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 : 0.34
REMARK 3 B_SOL : 38.98
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 18.92600
REMARK 3 B22 (A**2) : -1.78600
REMARK 3 B33 (A**2) : -17.14000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.008 5382
REMARK 3 ANGLE : 1.035 7283
REMARK 3 CHIRALITY : 0.067 820
REMARK 3 PLANARITY : 0.004 938
REMARK 3 DIHEDRAL : 18.033 1975
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 3LZC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000057913.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-APR-08; 05-AUG-08
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 5.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 24-ID-C; 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97922; 0.97918
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC QUANTUM
REMARK 200 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36367
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : 0.06200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.30900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000, 0.1 M AMMONIUM ACETATE,
REMARK 280 0.05 M SODIUM CITRATE, 0.2 M KCL, 2% ETHYLENE GLYCOL, PH 5.3,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 29.50400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.37650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.29900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.37650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.50400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.29900
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: 3510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 MET A -35
REMARK 465 GLY A -34
REMARK 465 SER A -33
REMARK 465 HIS A -32
REMARK 465 HIS A -31
REMARK 465 HIS A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 ASP A -26
REMARK 465 ILE A -25
REMARK 465 THR A -24
REMARK 465 SER A -23
REMARK 465 LEU A -22
REMARK 465 TYR A -21
REMARK 465 LYS A -20
REMARK 465 LYS A -19
REMARK 465 ALA A -18
REMARK 465 GLY A -17
REMARK 465 SER A -16
REMARK 465 ALA A -15
REMARK 465 ALA A -14
REMARK 465 ALA A -13
REMARK 465 VAL A -12
REMARK 465 LEU A -11
REMARK 465 GLU A -10
REMARK 465 GLU A -9
REMARK 465 ASN A -8
REMARK 465 LEU A -7
REMARK 465 TYR A -6
REMARK 465 PHE A -5
REMARK 465 GLN A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 PHE A -1
REMARK 465 THR A 0
REMARK 465 MET B -35
REMARK 465 GLY B -34
REMARK 465 SER B -33
REMARK 465 HIS B -32
REMARK 465 HIS B -31
REMARK 465 HIS B -30
REMARK 465 HIS B -29
REMARK 465 HIS B -28
REMARK 465 HIS B -27
REMARK 465 ASP B -26
REMARK 465 ILE B -25
REMARK 465 THR B -24
REMARK 465 SER B -23
REMARK 465 LEU B -22
REMARK 465 TYR B -21
REMARK 465 LYS B -20
REMARK 465 LYS B -19
REMARK 465 ALA B -18
REMARK 465 GLY B -17
REMARK 465 SER B -16
REMARK 465 ALA B -15
REMARK 465 ALA B -14
REMARK 465 ALA B -13
REMARK 465 VAL B -12
REMARK 465 LEU B -11
REMARK 465 GLU B -10
REMARK 465 GLU B -9
REMARK 465 ASN B -8
REMARK 465 LEU B -7
REMARK 465 TYR B -6
REMARK 465 PHE B -5
REMARK 465 GLN B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 PHE B -1
REMARK 465 THR B 0
REMARK 465 ASP B 294
REMARK 465 TYR B 295
REMARK 465 ARG B 342
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 MET A 1 CG SD CE
REMARK 470 LYS A 20 CG CD CE NZ
REMARK 470 GLU A 28 CG CD OE1 OE2
REMARK 470 LYS A 132 CG CD CE NZ
REMARK 470 ARG A 171 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 195 CG CD CE NZ
REMARK 470 GLU A 212 CG CD OE1 OE2
REMARK 470 ARG A 213 CG CD NE CZ NH1 NH2
REMARK 470 MET A 226 CG SD CE
REMARK 470 LYS A 229 CG CD CE NZ
REMARK 470 LYS A 252 CG CD CE NZ
REMARK 470 LYS A 256 CG CD CE NZ
REMARK 470 ARG A 289 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 342 CG CD NE CZ NH1 NH2
REMARK 470 MET B 1 CG SD CE
REMARK 470 LYS B 7 CG CD CE NZ
REMARK 470 GLU B 9 CG CD OE1 OE2
REMARK 470 LYS B 12 CG CD CE NZ
REMARK 470 LYS B 15 CG CD CE NZ
REMARK 470 ILE B 17 CG1 CG2 CD1
REMARK 470 LYS B 20 CG CD CE NZ
REMARK 470 ARG B 98 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 171 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 217 CG CD CE NZ
REMARK 470 LYS B 229 CG CD CE NZ
REMARK 470 LYS B 256 CG CD CE NZ
REMARK 470 ARG B 289 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 299 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 329 CG CD OE1 OE2
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 ALA A 62 42.78 -95.81
REMARK 500 ARG A 243 60.08 -109.96
REMARK 500 ASN A 267 -84.82 -99.98
REMARK 500 VAL A 285 77.50 -112.12
REMARK 500 ALA A 286 -109.81 -156.69
REMARK 500 THR A 341 -69.59 -127.91
REMARK 500 ALA B 62 45.90 -89.47
REMARK 500 ASN B 267 -83.20 -105.37
REMARK 500 VAL B 285 62.94 -112.94
REMARK 500 ALA B 286 -112.34 -138.95
REMARK 500 ALA B 297 -1.74 -140.08
REMARK 500 GLU B 329 -74.43 -65.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LZD RELATED DB: PDB
REMARK 900 DIPHTHAMIDE BIOSYNTHESIS REQUIRES A SAM-DEPENDANT [4FE-4S]-
REMARK 900 CONTAINING ENZYME
DBREF 3LZC A 1 342 UNP O58832 O58832_PYRHO 1 342
DBREF 3LZC B 1 342 UNP O58832 O58832_PYRHO 1 342
SEQADV 3LZC MET A -35 UNP O58832 EXPRESSION TAG
SEQADV 3LZC GLY A -34 UNP O58832 EXPRESSION TAG
SEQADV 3LZC SER A -33 UNP O58832 EXPRESSION TAG
SEQADV 3LZC HIS A -32 UNP O58832 EXPRESSION TAG
SEQADV 3LZC HIS A -31 UNP O58832 EXPRESSION TAG
SEQADV 3LZC HIS A -30 UNP O58832 EXPRESSION TAG
SEQADV 3LZC HIS A -29 UNP O58832 EXPRESSION TAG
SEQADV 3LZC HIS A -28 UNP O58832 EXPRESSION TAG
SEQADV 3LZC HIS A -27 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ASP A -26 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ILE A -25 UNP O58832 EXPRESSION TAG
SEQADV 3LZC THR A -24 UNP O58832 EXPRESSION TAG
SEQADV 3LZC SER A -23 UNP O58832 EXPRESSION TAG
SEQADV 3LZC LEU A -22 UNP O58832 EXPRESSION TAG
SEQADV 3LZC TYR A -21 UNP O58832 EXPRESSION TAG
SEQADV 3LZC LYS A -20 UNP O58832 EXPRESSION TAG
SEQADV 3LZC LYS A -19 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ALA A -18 UNP O58832 EXPRESSION TAG
SEQADV 3LZC GLY A -17 UNP O58832 EXPRESSION TAG
SEQADV 3LZC SER A -16 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ALA A -15 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ALA A -14 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ALA A -13 UNP O58832 EXPRESSION TAG
SEQADV 3LZC VAL A -12 UNP O58832 EXPRESSION TAG
SEQADV 3LZC LEU A -11 UNP O58832 EXPRESSION TAG
SEQADV 3LZC GLU A -10 UNP O58832 EXPRESSION TAG
SEQADV 3LZC GLU A -9 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ASN A -8 UNP O58832 EXPRESSION TAG
SEQADV 3LZC LEU A -7 UNP O58832 EXPRESSION TAG
SEQADV 3LZC TYR A -6 UNP O58832 EXPRESSION TAG
SEQADV 3LZC PHE A -5 UNP O58832 EXPRESSION TAG
SEQADV 3LZC GLN A -4 UNP O58832 EXPRESSION TAG
SEQADV 3LZC GLY A -3 UNP O58832 EXPRESSION TAG
SEQADV 3LZC SER A -2 UNP O58832 EXPRESSION TAG
SEQADV 3LZC PHE A -1 UNP O58832 EXPRESSION TAG
SEQADV 3LZC THR A 0 UNP O58832 EXPRESSION TAG
SEQADV 3LZC MET B -35 UNP O58832 EXPRESSION TAG
SEQADV 3LZC GLY B -34 UNP O58832 EXPRESSION TAG
SEQADV 3LZC SER B -33 UNP O58832 EXPRESSION TAG
SEQADV 3LZC HIS B -32 UNP O58832 EXPRESSION TAG
SEQADV 3LZC HIS B -31 UNP O58832 EXPRESSION TAG
SEQADV 3LZC HIS B -30 UNP O58832 EXPRESSION TAG
SEQADV 3LZC HIS B -29 UNP O58832 EXPRESSION TAG
SEQADV 3LZC HIS B -28 UNP O58832 EXPRESSION TAG
SEQADV 3LZC HIS B -27 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ASP B -26 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ILE B -25 UNP O58832 EXPRESSION TAG
SEQADV 3LZC THR B -24 UNP O58832 EXPRESSION TAG
SEQADV 3LZC SER B -23 UNP O58832 EXPRESSION TAG
SEQADV 3LZC LEU B -22 UNP O58832 EXPRESSION TAG
SEQADV 3LZC TYR B -21 UNP O58832 EXPRESSION TAG
SEQADV 3LZC LYS B -20 UNP O58832 EXPRESSION TAG
SEQADV 3LZC LYS B -19 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ALA B -18 UNP O58832 EXPRESSION TAG
SEQADV 3LZC GLY B -17 UNP O58832 EXPRESSION TAG
SEQADV 3LZC SER B -16 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ALA B -15 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ALA B -14 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ALA B -13 UNP O58832 EXPRESSION TAG
SEQADV 3LZC VAL B -12 UNP O58832 EXPRESSION TAG
SEQADV 3LZC LEU B -11 UNP O58832 EXPRESSION TAG
SEQADV 3LZC GLU B -10 UNP O58832 EXPRESSION TAG
SEQADV 3LZC GLU B -9 UNP O58832 EXPRESSION TAG
SEQADV 3LZC ASN B -8 UNP O58832 EXPRESSION TAG
SEQADV 3LZC LEU B -7 UNP O58832 EXPRESSION TAG
SEQADV 3LZC TYR B -6 UNP O58832 EXPRESSION TAG
SEQADV 3LZC PHE B -5 UNP O58832 EXPRESSION TAG
SEQADV 3LZC GLN B -4 UNP O58832 EXPRESSION TAG
SEQADV 3LZC GLY B -3 UNP O58832 EXPRESSION TAG
SEQADV 3LZC SER B -2 UNP O58832 EXPRESSION TAG
SEQADV 3LZC PHE B -1 UNP O58832 EXPRESSION TAG
SEQADV 3LZC THR B 0 UNP O58832 EXPRESSION TAG
SEQRES 1 A 378 MET GLY SER HIS HIS HIS HIS HIS HIS ASP ILE THR SER
SEQRES 2 A 378 LEU TYR LYS LYS ALA GLY SER ALA ALA ALA VAL LEU GLU
SEQRES 3 A 378 GLU ASN LEU TYR PHE GLN GLY SER PHE THR MET LEU HIS
SEQRES 4 A 378 GLU ILE PRO LYS SER GLU ILE LEU LYS GLU LEU LYS ARG
SEQRES 5 A 378 ILE GLY ALA LYS ARG VAL LEU ILE GLN SER PRO GLU GLY
SEQRES 6 A 378 LEU ARG ARG GLU ALA GLU GLU LEU ALA GLY PHE LEU GLU
SEQRES 7 A 378 GLU ASN ASN ILE GLU VAL PHE LEU HIS GLY GLU ILE ASN
SEQRES 8 A 378 TYR GLY ALA CYS ASP PRO ALA ASP ARG GLU ALA LYS LEU
SEQRES 9 A 378 VAL GLY CYS ASP ALA LEU ILE HIS LEU GLY HIS SER TYR
SEQRES 10 A 378 MET LYS LEU PRO LEU GLU VAL PRO THR ILE PHE VAL PRO
SEQRES 11 A 378 ALA PHE ALA ARG VAL SER VAL VAL GLU ALA LEU LYS GLU
SEQRES 12 A 378 ASN ILE GLY GLU ILE LYS LYS LEU GLY ARG LYS ILE ILE
SEQRES 13 A 378 VAL THR THR THR ALA GLN HIS ILE HIS GLN LEU LYS GLU
SEQRES 14 A 378 ALA LYS GLU PHE LEU GLU SER GLU GLY PHE GLU VAL SER
SEQRES 15 A 378 ILE GLY ARG GLY ASP SER ARG ILE SER TRP PRO GLY GLN
SEQRES 16 A 378 VAL LEU GLY CYS ASN TYR SER VAL ALA LYS VAL ARG GLY
SEQRES 17 A 378 GLU GLY ILE LEU PHE ILE GLY SER GLY ILE PHE HIS PRO
SEQRES 18 A 378 LEU GLY LEU ALA VAL ALA THR ARG LYS LYS VAL LEU ALA
SEQRES 19 A 378 ILE ASP PRO TYR THR LYS ALA PHE SER TRP ILE ASP PRO
SEQRES 20 A 378 GLU ARG PHE ILE ARG LYS ARG TRP ALA GLN ILE ALA LYS
SEQRES 21 A 378 ALA MET ASP ALA LYS LYS PHE GLY VAL ILE VAL SER ILE
SEQRES 22 A 378 LYS LYS GLY GLN LEU ARG LEU ALA GLU ALA LYS ARG ILE
SEQRES 23 A 378 VAL LYS LEU LEU LYS LYS HIS GLY ARG GLU ALA ARG LEU
SEQRES 24 A 378 ILE VAL MET ASN ASP VAL ASN TYR HIS LYS LEU GLU GLY
SEQRES 25 A 378 PHE PRO PHE GLU ALA TYR VAL VAL VAL ALA CYS PRO ARG
SEQRES 26 A 378 VAL PRO LEU ASP ASP TYR GLY ALA TRP ARG LYS PRO VAL
SEQRES 27 A 378 LEU THR PRO LYS GLU VAL GLU ILE LEU LEU GLY LEU ARG
SEQRES 28 A 378 GLU GLU TYR GLU PHE ASP GLU ILE LEU GLY GLY PRO ARG
SEQRES 29 A 378 GLU SER ASP GLU PRO PHE GLY ILE SER ILE HIS SER THR
SEQRES 30 A 378 ARG
SEQRES 1 B 378 MET GLY SER HIS HIS HIS HIS HIS HIS ASP ILE THR SER
SEQRES 2 B 378 LEU TYR LYS LYS ALA GLY SER ALA ALA ALA VAL LEU GLU
SEQRES 3 B 378 GLU ASN LEU TYR PHE GLN GLY SER PHE THR MET LEU HIS
SEQRES 4 B 378 GLU ILE PRO LYS SER GLU ILE LEU LYS GLU LEU LYS ARG
SEQRES 5 B 378 ILE GLY ALA LYS ARG VAL LEU ILE GLN SER PRO GLU GLY
SEQRES 6 B 378 LEU ARG ARG GLU ALA GLU GLU LEU ALA GLY PHE LEU GLU
SEQRES 7 B 378 GLU ASN ASN ILE GLU VAL PHE LEU HIS GLY GLU ILE ASN
SEQRES 8 B 378 TYR GLY ALA CYS ASP PRO ALA ASP ARG GLU ALA LYS LEU
SEQRES 9 B 378 VAL GLY CYS ASP ALA LEU ILE HIS LEU GLY HIS SER TYR
SEQRES 10 B 378 MET LYS LEU PRO LEU GLU VAL PRO THR ILE PHE VAL PRO
SEQRES 11 B 378 ALA PHE ALA ARG VAL SER VAL VAL GLU ALA LEU LYS GLU
SEQRES 12 B 378 ASN ILE GLY GLU ILE LYS LYS LEU GLY ARG LYS ILE ILE
SEQRES 13 B 378 VAL THR THR THR ALA GLN HIS ILE HIS GLN LEU LYS GLU
SEQRES 14 B 378 ALA LYS GLU PHE LEU GLU SER GLU GLY PHE GLU VAL SER
SEQRES 15 B 378 ILE GLY ARG GLY ASP SER ARG ILE SER TRP PRO GLY GLN
SEQRES 16 B 378 VAL LEU GLY CYS ASN TYR SER VAL ALA LYS VAL ARG GLY
SEQRES 17 B 378 GLU GLY ILE LEU PHE ILE GLY SER GLY ILE PHE HIS PRO
SEQRES 18 B 378 LEU GLY LEU ALA VAL ALA THR ARG LYS LYS VAL LEU ALA
SEQRES 19 B 378 ILE ASP PRO TYR THR LYS ALA PHE SER TRP ILE ASP PRO
SEQRES 20 B 378 GLU ARG PHE ILE ARG LYS ARG TRP ALA GLN ILE ALA LYS
SEQRES 21 B 378 ALA MET ASP ALA LYS LYS PHE GLY VAL ILE VAL SER ILE
SEQRES 22 B 378 LYS LYS GLY GLN LEU ARG LEU ALA GLU ALA LYS ARG ILE
SEQRES 23 B 378 VAL LYS LEU LEU LYS LYS HIS GLY ARG GLU ALA ARG LEU
SEQRES 24 B 378 ILE VAL MET ASN ASP VAL ASN TYR HIS LYS LEU GLU GLY
SEQRES 25 B 378 PHE PRO PHE GLU ALA TYR VAL VAL VAL ALA CYS PRO ARG
SEQRES 26 B 378 VAL PRO LEU ASP ASP TYR GLY ALA TRP ARG LYS PRO VAL
SEQRES 27 B 378 LEU THR PRO LYS GLU VAL GLU ILE LEU LEU GLY LEU ARG
SEQRES 28 B 378 GLU GLU TYR GLU PHE ASP GLU ILE LEU GLY GLY PRO ARG
SEQRES 29 B 378 GLU SER ASP GLU PRO PHE GLY ILE SER ILE HIS SER THR
SEQRES 30 B 378 ARG
FORMUL 3 HOH *155(H2 O)
HELIX 1 1 PRO A 6 GLY A 18 1 13
HELIX 2 2 PRO A 27 GLY A 29 5 3
HELIX 3 3 LEU A 30 GLU A 43 1 14
HELIX 4 4 ALA A 62 VAL A 69 1 8
HELIX 5 5 VAL A 101 ASN A 108 1 8
HELIX 6 6 ASN A 108 LYS A 114 1 7
HELIX 7 7 ALA A 125 HIS A 129 5 5
HELIX 8 8 GLN A 130 GLU A 141 1 12
HELIX 9 9 TYR A 165 LYS A 169 5 5
HELIX 10 10 ILE A 182 ARG A 193 1 12
HELIX 11 11 PRO A 211 ALA A 225 1 15
HELIX 12 12 ARG A 243 HIS A 257 1 15
HELIX 13 13 ASN A 270 GLU A 275 5 6
HELIX 14 14 PRO A 288 ASP A 293 1 6
HELIX 15 15 THR A 304 LEU A 312 1 9
HELIX 16 16 PRO B 6 GLY B 18 1 13
HELIX 17 17 PRO B 27 GLY B 29 5 3
HELIX 18 18 LEU B 30 ASN B 44 1 15
HELIX 19 19 ALA B 62 VAL B 69 1 8
HELIX 20 20 SER B 100 GLU B 107 1 8
HELIX 21 21 ASN B 108 LYS B 114 1 7
HELIX 22 22 ALA B 125 HIS B 129 5 5
HELIX 23 23 GLN B 130 GLU B 141 1 12
HELIX 24 24 TYR B 165 LYS B 169 5 5
HELIX 25 25 ILE B 182 ARG B 193 1 12
HELIX 26 26 PRO B 211 MET B 226 1 16
HELIX 27 27 ARG B 243 HIS B 257 1 15
HELIX 28 28 ASN B 270 GLU B 275 5 6
HELIX 29 29 PRO B 288 ASP B 293 1 6
HELIX 30 30 THR B 304 LEU B 312 1 9
SHEET 1 A 9 SER A 337 HIS A 339 0
SHEET 2 A 9 THR A 90 PRO A 94 -1 N THR A 90 O HIS A 339
SHEET 3 A 9 ALA A 73 GLY A 78 1 N HIS A 76 O ILE A 91
SHEET 4 A 9 ARG A 21 GLN A 25 1 N LEU A 23 O ILE A 75
SHEET 5 A 9 GLU A 47 HIS A 51 1 O HIS A 51 N ILE A 24
SHEET 6 A 9 GLU B 260 MET B 266 1 O VAL B 265 N LEU A 50
SHEET 7 A 9 LYS B 230 SER B 236 1 N VAL B 233 O ARG B 262
SHEET 8 A 9 ALA B 281 VAL B 284 1 O VAL B 283 N ILE B 234
SHEET 9 A 9 VAL B 302 LEU B 303 1 O LEU B 303 N TYR B 282
SHEET 1 B 5 GLU A 144 SER A 146 0
SHEET 2 B 5 LYS A 118 THR A 123 1 N ILE A 119 O SER A 146
SHEET 3 B 5 GLY A 174 ILE A 178 1 O LEU A 176 N ILE A 120
SHEET 4 B 5 LYS A 195 ILE A 199 1 O LYS A 195 N ILE A 175
SHEET 5 B 5 PHE A 206 TRP A 208 -1 O SER A 207 N ALA A 198
SHEET 1 C 9 VAL A 302 LEU A 303 0
SHEET 2 C 9 ALA A 281 VAL A 284 1 N TYR A 282 O LEU A 303
SHEET 3 C 9 LYS A 230 SER A 236 1 N ILE A 234 O VAL A 283
SHEET 4 C 9 GLU A 260 MET A 266 1 O ARG A 262 N VAL A 233
SHEET 5 C 9 GLU B 47 HIS B 51 1 O LEU B 50 N VAL A 265
SHEET 6 C 9 ARG B 21 GLN B 25 1 N VAL B 22 O PHE B 49
SHEET 7 C 9 ALA B 73 GLY B 78 1 O ILE B 75 N LEU B 23
SHEET 8 C 9 THR B 90 PRO B 94 1 O ILE B 91 N LEU B 74
SHEET 9 C 9 SER B 337 HIS B 339 -1 O HIS B 339 N THR B 90
SHEET 1 D 5 GLU B 144 SER B 146 0
SHEET 2 D 5 LYS B 118 THR B 123 1 N ILE B 119 O SER B 146
SHEET 3 D 5 ILE B 175 ILE B 178 1 O LEU B 176 N ILE B 120
SHEET 4 D 5 VAL B 196 ILE B 199 1 O LEU B 197 N PHE B 177
SHEET 5 D 5 PHE B 206 TRP B 208 -1 O SER B 207 N ALA B 198
CRYST1 59.008 82.598 160.753 90.00 90.00 90.00 P 21 21 21 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 0.016947 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012107 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006221 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
