HEADER LIGASE 12-MAR-11 3R23
TITLE CRYSTAL STRUCTURE OF D-ALANINE--D-ALANINE LIGASE FROM BACILLUS
TITLE 2 ANTHRACIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: D-ALA-D-ALA LIGASE, D-ALANYLALANINE SYNTHETASE;
COMPND 5 EC: 6.3.2.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;
SOURCE 4 ORGANISM_TAXID: 198094;
SOURCE 5 STRAIN: AMES;
SOURCE 6 GENE: BAS2435, BA_2610, DDL, DDLB, GBAA_2610;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS 2 DISEASES, CSGID, ALPHA-BETA STRUCTURE, LIGASE, CYTOSOL
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,R.MULLIGAN,J.HASSEMAN,W.F.ANDERSON,A.JOACHIMIAK,CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 2 06-APR-11 3R23 1 AUTHOR
REVDAT 1 30-MAR-11 3R23 0
JRNL AUTH Y.KIM,R.MULLIGAN,J.HASSEMAN,W.F.ANDERSON,A.JOACHIMIAK,
JRNL AUTH 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 3 (CSGID)
JRNL TITL CRYSTAL STRUCTURE OF D-ALANINE--D-ALANINE LIGASE FROM
JRNL TITL 2 BACILLUS ANTHRACIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.24
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 24525
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.150
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 40.2434 - 5.3651 0.99 2445 217 0.2044 0.2594
REMARK 3 2 5.3651 - 4.2599 0.99 2353 210 0.1493 0.1868
REMARK 3 3 4.2599 - 3.7219 0.99 2327 206 0.1513 0.2053
REMARK 3 4 3.7219 - 3.3818 0.99 2285 202 0.1982 0.2686
REMARK 3 5 3.3818 - 3.1395 0.98 2248 200 0.2128 0.2949
REMARK 3 6 3.1395 - 2.9545 0.97 2253 200 0.2148 0.2783
REMARK 3 7 2.9545 - 2.8065 0.96 2203 196 0.2159 0.3163
REMARK 3 8 2.8065 - 2.6844 0.96 2188 194 0.2284 0.3297
REMARK 3 9 2.6844 - 2.5811 0.94 2155 191 0.2346 0.3080
REMARK 3 10 2.5811 - 2.4920 0.90 2068 184 0.2228 0.3376
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.29
REMARK 3 B_SOL : 20.11
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.600
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.17
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 16.49710
REMARK 3 B22 (A**2) : 8.36930
REMARK 3 B33 (A**2) : 7.67160
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 : 0.012 4826
REMARK 3 ANGLE : 1.518 6500
REMARK 3 CHIRALITY : 0.103 746
REMARK 3 PLANARITY : 0.008 825
REMARK 3 DIHEDRAL : 16.891 1846
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1696 36.8127 66.3870
REMARK 3 T TENSOR
REMARK 3 T11: 0.0209 T22: 0.0958
REMARK 3 T33: 0.0835 T12: -0.0302
REMARK 3 T13: 0.0109 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 0.0067 L22: 0.1432
REMARK 3 L33: 0.0889 L12: -0.0016
REMARK 3 L13: 0.0031 L23: 0.1077
REMARK 3 S TENSOR
REMARK 3 S11: -0.0175 S12: 0.0243 S13: -0.0187
REMARK 3 S21: -0.0447 S22: -0.0522 S23: 0.1368
REMARK 3 S31: -0.0535 S32: -0.0381 S33: 0.0301
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2806 50.9485 91.3041
REMARK 3 T TENSOR
REMARK 3 T11: 0.1773 T22: 0.0249
REMARK 3 T33: 0.1026 T12: 0.0134
REMARK 3 T13: 0.1478 T23: -0.1217
REMARK 3 L TENSOR
REMARK 3 L11: 0.0518 L22: 0.0097
REMARK 3 L33: 0.0542 L12: -0.0274
REMARK 3 L13: 0.0053 L23: 0.0018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0230 S12: -0.0240 S13: -0.0267
REMARK 3 S21: 0.0420 S22: 0.0148 S23: 0.0141
REMARK 3 S31: -0.1429 S32: 0.0110 S33: -0.0189
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 3R23 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064391.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUN-10
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 : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25302
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY : 44.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.15700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.81700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.040
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL3000, PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 20% W/V POLYETHYLENE
REMARK 280 GLYCOL MONOMETHYL ETHER 5,000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 100K, PH 6.5, TEMPERATURE 289K
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 32.93900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.19000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.59350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.19000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.93900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.59350
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: 3110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 -2
REMARK 465 ASN A -1
REMARK 465 PHE A 304
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 GLY B 141
REMARK 465 SER B 142
REMARK 465 SER B 143
REMARK 465 VAL B 144
REMARK 465 PHE B 304
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 ASP B 151 CG OD1 OD2
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 SER A 11 -127.54 46.03
REMARK 500 LEU A 121 73.22 62.64
REMARK 500 SER A 143 -70.79 -51.06
REMARK 500 VAL A 243 -32.47 72.15
REMARK 500 TYR A 244 156.72 179.26
REMARK 500 SER B 11 -124.31 60.05
REMARK 500 VAL B 243 -29.91 72.21
REMARK 500 TYR B 244 156.51 174.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL A 243 -10.98
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 EDO A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 312
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP01207 RELATED DB: TARGETDB
DBREF 3R23 A 1 304 UNP Q81Q29 DDL_BACAN 1 304
DBREF 3R23 B 1 304 UNP Q81Q29 DDL_BACAN 1 304
SEQADV 3R23 SER A -2 UNP Q81Q29 EXPRESSION TAG
SEQADV 3R23 ASN A -1 UNP Q81Q29 EXPRESSION TAG
SEQADV 3R23 ALA A 0 UNP Q81Q29 EXPRESSION TAG
SEQADV 3R23 SER B -2 UNP Q81Q29 EXPRESSION TAG
SEQADV 3R23 ASN B -1 UNP Q81Q29 EXPRESSION TAG
SEQADV 3R23 ALA B 0 UNP Q81Q29 EXPRESSION TAG
SEQRES 1 A 307 SER ASN ALA MSE ARG ILE GLY VAL ILE MSE GLY GLY VAL
SEQRES 2 A 307 SER SER GLU LYS GLN VAL SER ILE MSE THR GLY ASN GLU
SEQRES 3 A 307 MSE ILE ALA ASN LEU ASP LYS ASN LYS TYR GLU ILE VAL
SEQRES 4 A 307 PRO ILE THR LEU ASN GLU LYS MSE ASP LEU ILE GLU LYS
SEQRES 5 A 307 ALA LYS ASP ILE ASP PHE ALA LEU LEU ALA LEU HIS GLY
SEQRES 6 A 307 LYS TYR GLY GLU ASP GLY THR VAL GLN GLY THR LEU GLU
SEQRES 7 A 307 SER LEU GLY ILE PRO TYR SER GLY SER ASN MSE LEU SER
SEQRES 8 A 307 SER GLY ILE CYS MSE ASP LYS ASN ILE SER LYS LYS ILE
SEQRES 9 A 307 LEU ARG TYR GLU GLY ILE GLU THR PRO ASP TRP ILE GLU
SEQRES 10 A 307 LEU THR LYS MSE GLU ASP LEU ASN PHE ASP GLU LEU ASP
SEQRES 11 A 307 LYS LEU GLY PHE PRO LEU VAL VAL LYS PRO ASN SER GLY
SEQRES 12 A 307 GLY SER SER VAL GLY VAL LYS ILE VAL TYR ASP LYS ASP
SEQRES 13 A 307 GLU LEU ILE SER MSE LEU GLU THR VAL PHE GLU TRP ASP
SEQRES 14 A 307 SER GLU VAL VAL ILE GLU LYS TYR ILE LYS GLY GLU GLU
SEQRES 15 A 307 ILE THR CYS SER ILE PHE ASP GLY LYS GLN LEU PRO ILE
SEQRES 16 A 307 ILE SER ILE ARG HIS ALA ALA GLU PHE PHE ASP TYR ASN
SEQRES 17 A 307 ALA LYS TYR ASP ASP ALA SER THR ILE GLU GLU VAL ILE
SEQRES 18 A 307 GLU LEU PRO ALA GLU LEU LYS GLU ARG VAL ASN LYS ALA
SEQRES 19 A 307 SER LEU ALA CYS TYR LYS ALA LEU LYS CYS SER VAL TYR
SEQRES 20 A 307 ALA ARG VAL ASP MSE MSE VAL LYS ASP GLY ILE PRO TYR
SEQRES 21 A 307 VAL MSE GLU VAL ASN THR LEU PRO GLY MSE THR GLN ALA
SEQRES 22 A 307 SER LEU LEU PRO LYS SER ALA ASP ALA ALA GLY ILE HIS
SEQRES 23 A 307 TYR SER LYS LEU LEU ASP MSE ILE ILE GLU THR SER LEU
SEQRES 24 A 307 ARG VAL ARG LYS GLU GLU GLY PHE
SEQRES 1 B 307 SER ASN ALA MSE ARG ILE GLY VAL ILE MSE GLY GLY VAL
SEQRES 2 B 307 SER SER GLU LYS GLN VAL SER ILE MSE THR GLY ASN GLU
SEQRES 3 B 307 MSE ILE ALA ASN LEU ASP LYS ASN LYS TYR GLU ILE VAL
SEQRES 4 B 307 PRO ILE THR LEU ASN GLU LYS MSE ASP LEU ILE GLU LYS
SEQRES 5 B 307 ALA LYS ASP ILE ASP PHE ALA LEU LEU ALA LEU HIS GLY
SEQRES 6 B 307 LYS TYR GLY GLU ASP GLY THR VAL GLN GLY THR LEU GLU
SEQRES 7 B 307 SER LEU GLY ILE PRO TYR SER GLY SER ASN MSE LEU SER
SEQRES 8 B 307 SER GLY ILE CYS MSE ASP LYS ASN ILE SER LYS LYS ILE
SEQRES 9 B 307 LEU ARG TYR GLU GLY ILE GLU THR PRO ASP TRP ILE GLU
SEQRES 10 B 307 LEU THR LYS MSE GLU ASP LEU ASN PHE ASP GLU LEU ASP
SEQRES 11 B 307 LYS LEU GLY PHE PRO LEU VAL VAL LYS PRO ASN SER GLY
SEQRES 12 B 307 GLY SER SER VAL GLY VAL LYS ILE VAL TYR ASP LYS ASP
SEQRES 13 B 307 GLU LEU ILE SER MSE LEU GLU THR VAL PHE GLU TRP ASP
SEQRES 14 B 307 SER GLU VAL VAL ILE GLU LYS TYR ILE LYS GLY GLU GLU
SEQRES 15 B 307 ILE THR CYS SER ILE PHE ASP GLY LYS GLN LEU PRO ILE
SEQRES 16 B 307 ILE SER ILE ARG HIS ALA ALA GLU PHE PHE ASP TYR ASN
SEQRES 17 B 307 ALA LYS TYR ASP ASP ALA SER THR ILE GLU GLU VAL ILE
SEQRES 18 B 307 GLU LEU PRO ALA GLU LEU LYS GLU ARG VAL ASN LYS ALA
SEQRES 19 B 307 SER LEU ALA CYS TYR LYS ALA LEU LYS CYS SER VAL TYR
SEQRES 20 B 307 ALA ARG VAL ASP MSE MSE VAL LYS ASP GLY ILE PRO TYR
SEQRES 21 B 307 VAL MSE GLU VAL ASN THR LEU PRO GLY MSE THR GLN ALA
SEQRES 22 B 307 SER LEU LEU PRO LYS SER ALA ASP ALA ALA GLY ILE HIS
SEQRES 23 B 307 TYR SER LYS LEU LEU ASP MSE ILE ILE GLU THR SER LEU
SEQRES 24 B 307 ARG VAL ARG LYS GLU GLU GLY PHE
MODRES 3R23 MSE A 1 MET SELENOMETHIONINE
MODRES 3R23 MSE A 7 MET SELENOMETHIONINE
MODRES 3R23 MSE A 19 MET SELENOMETHIONINE
MODRES 3R23 MSE A 24 MET SELENOMETHIONINE
MODRES 3R23 MSE A 44 MET SELENOMETHIONINE
MODRES 3R23 MSE A 86 MET SELENOMETHIONINE
MODRES 3R23 MSE A 93 MET SELENOMETHIONINE
MODRES 3R23 MSE A 118 MET SELENOMETHIONINE
MODRES 3R23 MSE A 158 MET SELENOMETHIONINE
MODRES 3R23 MSE A 249 MET SELENOMETHIONINE
MODRES 3R23 MSE A 250 MET SELENOMETHIONINE
MODRES 3R23 MSE A 259 MET SELENOMETHIONINE
MODRES 3R23 MSE A 267 MET SELENOMETHIONINE
MODRES 3R23 MSE A 290 MET SELENOMETHIONINE
MODRES 3R23 MSE B 1 MET SELENOMETHIONINE
MODRES 3R23 MSE B 7 MET SELENOMETHIONINE
MODRES 3R23 MSE B 19 MET SELENOMETHIONINE
MODRES 3R23 MSE B 24 MET SELENOMETHIONINE
MODRES 3R23 MSE B 44 MET SELENOMETHIONINE
MODRES 3R23 MSE B 86 MET SELENOMETHIONINE
MODRES 3R23 MSE B 93 MET SELENOMETHIONINE
MODRES 3R23 MSE B 118 MET SELENOMETHIONINE
MODRES 3R23 MSE B 158 MET SELENOMETHIONINE
MODRES 3R23 MSE B 249 MET SELENOMETHIONINE
MODRES 3R23 MSE B 250 MET SELENOMETHIONINE
MODRES 3R23 MSE B 259 MET SELENOMETHIONINE
MODRES 3R23 MSE B 267 MET SELENOMETHIONINE
MODRES 3R23 MSE B 290 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 7 8
HET MSE A 19 8
HET MSE A 24 8
HET MSE A 44 8
HET MSE A 86 8
HET MSE A 93 8
HET MSE A 118 8
HET MSE A 158 8
HET MSE A 249 8
HET MSE A 250 8
HET MSE A 259 8
HET MSE A 267 8
HET MSE A 290 8
HET MSE B 1 8
HET MSE B 7 8
HET MSE B 19 8
HET MSE B 24 8
HET MSE B 44 8
HET MSE B 86 8
HET MSE B 93 8
HET MSE B 118 8
HET MSE B 158 8
HET MSE B 249 8
HET MSE B 250 8
HET MSE B 259 8
HET MSE B 267 8
HET MSE B 290 8
HET EDO A 311 4
HET EDO A 312 4
HET EDO B 311 4
HET EDO B 312 4
HETNAM MSE SELENOMETHIONINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 28(C5 H11 N O2 SE)
FORMUL 3 EDO 4(C2 H6 O2)
FORMUL 7 HOH *234(H2 O)
HELIX 1 1 VAL A 10 LEU A 28 1 19
HELIX 2 2 GLU A 42 MSE A 44 5 3
HELIX 3 3 ASP A 45 ALA A 50 1 6
HELIX 4 4 GLY A 62 ASP A 67 1 6
HELIX 5 5 GLY A 68 GLY A 78 1 11
HELIX 6 6 ASN A 85 MSE A 93 1 9
HELIX 7 7 ASP A 94 GLU A 105 1 12
HELIX 8 8 ASP A 151 GLU A 164 1 14
HELIX 9 9 PRO A 221 LEU A 239 1 19
HELIX 10 10 SER A 271 ALA A 280 1 10
HELIX 11 11 HIS A 283 GLU A 302 1 20
HELIX 12 12 VAL B 10 LEU B 28 1 19
HELIX 13 13 GLU B 42 MSE B 44 5 3
HELIX 14 14 ASP B 45 ALA B 50 1 6
HELIX 15 15 LYS B 51 ILE B 53 5 3
HELIX 16 16 GLY B 62 ASP B 67 1 6
HELIX 17 17 GLY B 68 LEU B 77 1 10
HELIX 18 18 ASN B 85 ASP B 94 1 10
HELIX 19 19 ASP B 94 GLU B 105 1 12
HELIX 20 20 ASN B 122 ASP B 127 1 6
HELIX 21 21 ASP B 153 ASP B 166 1 14
HELIX 22 22 PRO B 221 LEU B 239 1 19
HELIX 23 23 SER B 271 ALA B 280 1 10
HELIX 24 24 HIS B 283 GLY B 303 1 21
SHEET 1 A 3 TYR A 33 THR A 39 0
SHEET 2 A 3 MSE A 1 MSE A 7 1 N MSE A 7 O ILE A 38
SHEET 3 A 3 PHE A 55 LEU A 58 1 O LEU A 57 N GLY A 4
SHEET 1 B 4 TRP A 112 THR A 116 0
SHEET 2 B 4 GLU A 168 LYS A 173 -1 O ILE A 171 N ILE A 113
SHEET 3 B 4 LEU A 133 PRO A 137 -1 N LYS A 136 O VAL A 170
SHEET 4 B 4 LYS A 147 VAL A 149 -1 O VAL A 149 N LEU A 133
SHEET 1 C 4 LYS A 188 GLN A 189 0
SHEET 2 C 4 GLU A 178 PHE A 185 -1 N PHE A 185 O LYS A 188
SHEET 3 C 4 ILE A 193 HIS A 197 -1 O ILE A 193 N THR A 181
SHEET 4 C 4 THR A 213 VAL A 217 -1 O ILE A 214 N ARG A 196
SHEET 1 D 4 LYS A 188 GLN A 189 0
SHEET 2 D 4 GLU A 178 PHE A 185 -1 N PHE A 185 O LYS A 188
SHEET 3 D 4 TYR A 244 LYS A 252 -1 O MSE A 249 N ILE A 180
SHEET 4 D 4 ILE A 255 ASN A 262 -1 O ASN A 262 N ARG A 246
SHEET 1 E 2 GLU A 200 PHE A 202 0
SHEET 2 E 2 LYS A 207 ASP A 209 -1 O LYS A 207 N PHE A 202
SHEET 1 F 3 TYR B 33 THR B 39 0
SHEET 2 F 3 MSE B 1 MSE B 7 1 N ILE B 3 O VAL B 36
SHEET 3 F 3 PHE B 55 LEU B 58 1 O LEU B 57 N GLY B 4
SHEET 1 G 4 TRP B 112 THR B 116 0
SHEET 2 G 4 GLU B 168 LYS B 173 -1 O ILE B 171 N ILE B 113
SHEET 3 G 4 LEU B 133 PRO B 137 -1 N LYS B 136 O VAL B 170
SHEET 4 G 4 LYS B 147 VAL B 149 -1 O VAL B 149 N LEU B 133
SHEET 1 H 4 LYS B 188 GLN B 189 0
SHEET 2 H 4 GLU B 178 PHE B 185 -1 N PHE B 185 O LYS B 188
SHEET 3 H 4 ILE B 193 HIS B 197 -1 O ILE B 195 N GLU B 179
SHEET 4 H 4 THR B 213 GLU B 216 -1 O GLU B 216 N SER B 194
SHEET 1 I 4 LYS B 188 GLN B 189 0
SHEET 2 I 4 GLU B 178 PHE B 185 -1 N PHE B 185 O LYS B 188
SHEET 3 I 4 ALA B 245 LYS B 252 -1 O VAL B 247 N CYS B 182
SHEET 4 I 4 ILE B 255 ASN B 262 -1 O MSE B 259 N ASP B 248
SHEET 1 J 2 GLU B 200 PHE B 202 0
SHEET 2 J 2 LYS B 207 ASP B 209 -1 O LYS B 207 N PHE B 202
LINK C ALA A 0 N MSE A 1 1555 1555 1.32
LINK C MSE A 1 N ARG A 2 1555 1555 1.32
LINK C ILE A 6 N MSE A 7 1555 1555 1.33
LINK C MSE A 7 N GLY A 8 1555 1555 1.32
LINK C ILE A 18 N MSE A 19 1555 1555 1.32
LINK C MSE A 19 N THR A 20 1555 1555 1.33
LINK C GLU A 23 N MSE A 24 1555 1555 1.34
LINK C MSE A 24 N ILE A 25 1555 1555 1.33
LINK C LYS A 43 N MSE A 44 1555 1555 1.32
LINK C MSE A 44 N ASP A 45 1555 1555 1.33
LINK C ASN A 85 N MSE A 86 1555 1555 1.32
LINK C MSE A 86 N LEU A 87 1555 1555 1.33
LINK C CYS A 92 N MSE A 93 1555 1555 1.33
LINK C MSE A 93 N ASP A 94 1555 1555 1.33
LINK C LYS A 117 N MSE A 118 1555 1555 1.33
LINK C MSE A 118 N GLU A 119 1555 1555 1.34
LINK C SER A 157 N MSE A 158 1555 1555 1.34
LINK C MSE A 158 N LEU A 159 1555 1555 1.34
LINK C ASP A 248 N MSE A 249 1555 1555 1.34
LINK C MSE A 249 N MSE A 250 1555 1555 1.34
LINK C MSE A 250 N VAL A 251 1555 1555 1.33
LINK C VAL A 258 N MSE A 259 1555 1555 1.33
LINK C MSE A 259 N GLU A 260 1555 1555 1.33
LINK C GLY A 266 N MSE A 267 1555 1555 1.32
LINK C MSE A 267 N THR A 268 1555 1555 1.33
LINK C ASP A 289 N MSE A 290 1555 1555 1.32
LINK C MSE A 290 N ILE A 291 1555 1555 1.33
LINK C ALA B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N ARG B 2 1555 1555 1.33
LINK C ILE B 6 N MSE B 7 1555 1555 1.33
LINK C MSE B 7 N GLY B 8 1555 1555 1.33
LINK C ILE B 18 N MSE B 19 1555 1555 1.33
LINK C MSE B 19 N THR B 20 1555 1555 1.33
LINK C GLU B 23 N MSE B 24 1555 1555 1.33
LINK C MSE B 24 N ILE B 25 1555 1555 1.33
LINK C LYS B 43 N MSE B 44 1555 1555 1.33
LINK C MSE B 44 N ASP B 45 1555 1555 1.33
LINK C ASN B 85 N MSE B 86 1555 1555 1.33
LINK C MSE B 86 N LEU B 87 1555 1555 1.32
LINK C CYS B 92 N MSE B 93 1555 1555 1.32
LINK C MSE B 93 N ASP B 94 1555 1555 1.33
LINK C LYS B 117 N MSE B 118 1555 1555 1.33
LINK C MSE B 118 N GLU B 119 1555 1555 1.33
LINK C SER B 157 N MSE B 158 1555 1555 1.33
LINK C MSE B 158 N LEU B 159 1555 1555 1.33
LINK C ASP B 248 N MSE B 249 1555 1555 1.33
LINK C MSE B 249 N MSE B 250 1555 1555 1.33
LINK C MSE B 250 N VAL B 251 1555 1555 1.33
LINK C VAL B 258 N MSE B 259 1555 1555 1.32
LINK C MSE B 259 N GLU B 260 1555 1555 1.33
LINK C GLY B 266 N MSE B 267 1555 1555 1.32
LINK C MSE B 267 N THR B 268 1555 1555 1.33
LINK C ASP B 289 N MSE B 290 1555 1555 1.33
LINK C MSE B 290 N ILE B 291 1555 1555 1.33
CISPEP 1 PHE A 131 PRO A 132 0 -3.55
CISPEP 2 PHE B 131 PRO B 132 0 0.05
SITE 1 AC1 5 LYS A 95 LYS A 136 MSE A 259 GLU A 260
SITE 2 AC1 5 HOH A 401
SITE 1 AC2 4 LYS A 32 TYR A 33 ASP A 289 GLU A 293
SITE 1 AC3 6 CYS B 92 LYS B 95 SER B 98 LYS B 99
SITE 2 AC3 6 MSE B 259 VAL B 261
SITE 1 AC4 2 TYR A 204 GLU B 260
CRYST1 65.878 83.187 128.380 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 0.015180 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012021 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007789 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
