HEADER TRANSFERASE 18-MAY-11 3S40
TITLE THE CRYSTAL STRUCTURE OF A DIACYLGLYCEROL KINASES FROM BACILLUS
TITLE 2 ANTHRACIS STR. STERNE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIACYLGLYCEROL KINASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;
SOURCE 4 ORGANISM_TAXID: 260799;
SOURCE 5 STRAIN: STERNE;
SOURCE 6 GENE: BAS4713, BA_5075, GBAA_5075;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS DIACYLGLYCEROL KINASES, STRUCTURAL GENOMICS, THE CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,R.ZHANG,X.XU,H.CUI,S.PETERSON,A.SAVCHENKO,W.F.ANDERSON,
AUTHOR 2 A.JOACHIMIAK,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID)
REVDAT 3 06-DEC-23 3S40 1 REMARK
REVDAT 2 13-SEP-23 3S40 1 SEQADV LINK
REVDAT 1 01-JUN-11 3S40 0
JRNL AUTH K.TAN,R.ZHANG,X.XU,H.CUI,S.PETERSON,A.SAVCHENKO,
JRNL AUTH 2 W.F.ANDERSON,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF A DIACYLGLYCEROL KINASES FROM
JRNL TITL 2 BACILLUS ANTHRACIS STR. STERNE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 3 NUMBER OF REFLECTIONS : 58777
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2979
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 43.2406 - 5.7886 0.99 2891 130 0.1638 0.2179
REMARK 3 2 5.7886 - 4.5963 1.00 2880 140 0.1435 0.1949
REMARK 3 3 4.5963 - 4.0158 1.00 2848 158 0.1419 0.1778
REMARK 3 4 4.0158 - 3.6488 1.00 2820 144 0.1473 0.2078
REMARK 3 5 3.6488 - 3.3874 1.00 2847 156 0.1643 0.2192
REMARK 3 6 3.3874 - 3.1877 0.99 2769 167 0.1826 0.2218
REMARK 3 7 3.1877 - 3.0281 0.98 2818 132 0.1885 0.2823
REMARK 3 8 3.0281 - 2.8963 0.98 2793 143 0.2161 0.3072
REMARK 3 9 2.8963 - 2.7849 0.97 2764 153 0.1955 0.2901
REMARK 3 10 2.7849 - 2.6888 0.96 2704 156 0.1978 0.2454
REMARK 3 11 2.6888 - 2.6047 0.95 2717 128 0.1962 0.3247
REMARK 3 12 2.6047 - 2.5303 0.95 2667 156 0.1933 0.2513
REMARK 3 13 2.5303 - 2.4637 0.93 2617 139 0.1900 0.2835
REMARK 3 14 2.4637 - 2.4036 0.92 2624 138 0.1905 0.2605
REMARK 3 15 2.4036 - 2.3489 0.90 2523 149 0.1952 0.2895
REMARK 3 16 2.3489 - 2.2989 0.90 2581 127 0.1854 0.2448
REMARK 3 17 2.2989 - 2.2530 0.89 2491 143 0.1931 0.2222
REMARK 3 18 2.2530 - 2.2104 0.87 2453 134 0.1974 0.3054
REMARK 3 19 2.2104 - 2.1710 0.86 2432 122 0.2094 0.3139
REMARK 3 20 2.1710 - 2.1342 0.84 2378 134 0.2380 0.2971
REMARK 3 21 2.1342 - 2.0997 0.77 2181 130 0.2604 0.3527
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 : 43.94
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.480
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) : -4.19460
REMARK 3 B22 (A**2) : 0.26840
REMARK 3 B33 (A**2) : 3.92620
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.49340
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 : 0.007 8776
REMARK 3 ANGLE : 1.077 11902
REMARK 3 CHIRALITY : 0.075 1382
REMARK 3 PLANARITY : 0.005 1528
REMARK 3 DIHEDRAL : 15.333 3171
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7048 33.0817 37.1669
REMARK 3 T TENSOR
REMARK 3 T11: 0.1217 T22: 0.0942
REMARK 3 T33: 0.0958 T12: -0.0028
REMARK 3 T13: -0.0224 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 0.5572 L22: 0.1781
REMARK 3 L33: 0.3274 L12: 0.0478
REMARK 3 L13: -0.1427 L23: -0.0095
REMARK 3 S TENSOR
REMARK 3 S11: 0.0603 S12: -0.0160 S13: -0.0759
REMARK 3 S21: 0.0355 S22: -0.0313 S23: -0.0081
REMARK 3 S31: -0.0823 S32: 0.0137 S33: -0.0009
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 3S40 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000065732.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
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) : 0.97924
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : MIRROR
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 : 62575
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 44.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.65600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2QVL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS, 0.4M NH4CL, 16% PEG
REMARK 280 3350, 4% JEFFAMINE M-600, PH 5.8, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 65.37900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
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 300 REMARK: EXPERIMENTALLY UNKNOWN. IT IS PREDICTED THAT THE MOLECULE
REMARK 300 IS MONOMERIC.
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 THR A 2
REMARK 465 LEU A 144
REMARK 465 VAL A 145
REMARK 465 SER A 146
REMARK 465 GLU A 147
REMARK 465 VAL A 148
REMARK 465 SER A 149
REMARK 465 ASN A 150
REMARK 465 ASN A 151
REMARK 465 ILE A 152
REMARK 465 ASP A 153
REMARK 465 ALA A 154
REMARK 465 GLU A 155
REMARK 465 GLU A 156
REMARK 465 LYS A 157
REMARK 465 ALA A 158
REMARK 465 LYS A 159
REMARK 465 LEU A 160
REMARK 465 GLY A 161
REMARK 465 ARG A 171
REMARK 465 THR A 172
REMARK 465 VAL A 173
REMARK 465 LYS A 174
REMARK 465 ASN A 175
REMARK 465 ALA A 176
REMARK 465 GLY A 274
REMARK 465 GLU A 275
REMARK 465 GLY A 301
REMARK 465 SER A 302
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MSE B 1
REMARK 465 LYS B 174
REMARK 465 SER B 247
REMARK 465 ASN B 248
REMARK 465 GLU B 249
REMARK 465 ASN B 250
REMARK 465 ASP B 251
REMARK 465 GLY B 301
REMARK 465 SER B 302
REMARK 465 GLY C -1
REMARK 465 HIS C 0
REMARK 465 MSE C 1
REMARK 465 THR C 2
REMARK 465 LEU C 144
REMARK 465 VAL C 145
REMARK 465 SER C 146
REMARK 465 GLU C 147
REMARK 465 VAL C 148
REMARK 465 SER C 149
REMARK 465 ASN C 150
REMARK 465 ASN C 151
REMARK 465 ILE C 152
REMARK 465 LYS C 174
REMARK 465 ASN C 175
REMARK 465 GLY C 301
REMARK 465 SER C 302
REMARK 465 GLY D -1
REMARK 465 HIS D 0
REMARK 465 MSE D 1
REMARK 465 THR D 2
REMARK 465 SER D 146
REMARK 465 GLU D 147
REMARK 465 VAL D 148
REMARK 465 SER D 149
REMARK 465 ASN D 150
REMARK 465 ASN D 151
REMARK 465 ILE D 152
REMARK 465 ASP D 153
REMARK 465 ALA D 154
REMARK 465 GLU D 155
REMARK 465 GLU D 156
REMARK 465 LYS D 157
REMARK 465 ALA D 158
REMARK 465 LYS D 159
REMARK 465 LEU D 160
REMARK 465 ILE D 170
REMARK 465 ARG D 171
REMARK 465 THR D 172
REMARK 465 VAL D 173
REMARK 465 LYS D 174
REMARK 465 ASN D 175
REMARK 465 GLY D 187
REMARK 465 GLY D 240
REMARK 465 LYS D 241
REMARK 465 LYS D 242
REMARK 465 LEU D 243
REMARK 465 PHE D 244
REMARK 465 GLU D 245
REMARK 465 ASP D 246
REMARK 465 SER D 247
REMARK 465 ASN D 248
REMARK 465 GLU D 249
REMARK 465 ASN D 250
REMARK 465 ASP D 251
REMARK 465 GLY D 301
REMARK 465 SER D 302
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 LYS A 162 CG CD CE NZ
REMARK 470 ILE A 163 CG1 CG2 CD1
REMARK 470 ARG B 171 CG CD NE CZ NH1 NH2
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 ASN A 138 -60.98 -107.51
REMARK 500 ASP A 192 -177.84 -175.04
REMARK 500 ASN A 201 -40.97 -130.25
REMARK 500 ASN A 214 28.87 47.73
REMARK 500 ASN A 248 72.64 -108.34
REMARK 500 GLU A 249 -14.88 -49.73
REMARK 500 ASN B 132 56.49 36.86
REMARK 500 ASN B 138 -63.01 -102.80
REMARK 500 ASP B 192 -176.95 173.29
REMARK 500 PHE B 244 48.31 -106.52
REMARK 500 ASN C 132 63.63 32.54
REMARK 500 ASN C 138 -65.84 -98.12
REMARK 500 LYS C 241 47.87 -97.38
REMARK 500 ASP C 246 -76.80 -96.73
REMARK 500 GLU C 267 93.78 -55.05
REMARK 500 GLU C 275 107.86 -49.08
REMARK 500 ASN D 132 66.36 34.98
REMARK 500 ASN D 138 -73.55 -95.74
REMARK 500 PHE D 179 130.54 -179.33
REMARK 500 ASP D 192 -179.24 -176.95
REMARK 500 THR D 230 26.89 -75.43
REMARK 500 GLU D 265 -84.32 -36.99
REMARK 500 GLU D 267 164.68 -47.91
REMARK 500 SER D 277 54.16 -107.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP90228 RELATED DB: TARGETDB
DBREF 3S40 A 1 300 UNP Q81KC6 Q81KC6_BACAN 1 300
DBREF 3S40 B 1 300 UNP Q81KC6 Q81KC6_BACAN 1 300
DBREF 3S40 C 1 300 UNP Q81KC6 Q81KC6_BACAN 1 300
DBREF 3S40 D 1 300 UNP Q81KC6 Q81KC6_BACAN 1 300
SEQADV 3S40 GLY A -1 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 HIS A 0 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 GLY A 301 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 SER A 302 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 GLY B -1 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 HIS B 0 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 GLY B 301 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 SER B 302 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 GLY C -1 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 HIS C 0 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 GLY C 301 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 SER C 302 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 GLY D -1 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 HIS D 0 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 GLY D 301 UNP Q81KC6 EXPRESSION TAG
SEQADV 3S40 SER D 302 UNP Q81KC6 EXPRESSION TAG
SEQRES 1 A 304 GLY HIS MSE THR LYS THR LYS PHE GLU LYS VAL LEU LEU
SEQRES 2 A 304 ILE VAL ASN PRO LYS ALA GLY GLN GLY ASP LEU HIS THR
SEQRES 3 A 304 ASN LEU THR LYS ILE VAL PRO PRO LEU ALA ALA ALA PHE
SEQRES 4 A 304 PRO ASP LEU HIS ILE LEU HIS THR LYS GLU GLN GLY ASP
SEQRES 5 A 304 ALA THR LYS TYR CYS GLN GLU PHE ALA SER LYS VAL ASP
SEQRES 6 A 304 LEU ILE ILE VAL PHE GLY GLY ASP GLY THR VAL PHE GLU
SEQRES 7 A 304 CYS THR ASN GLY LEU ALA PRO LEU GLU ILE ARG PRO THR
SEQRES 8 A 304 LEU ALA ILE ILE PRO GLY GLY THR CYS ASN ASP PHE SER
SEQRES 9 A 304 ARG THR LEU GLY VAL PRO GLN ASN ILE ALA GLU ALA ALA
SEQRES 10 A 304 LYS LEU ILE THR LYS GLU HIS VAL LYS PRO VAL ASP VAL
SEQRES 11 A 304 ALA LYS ALA ASN GLY GLN HIS PHE LEU ASN PHE TRP GLY
SEQRES 12 A 304 ILE GLY LEU VAL SER GLU VAL SER ASN ASN ILE ASP ALA
SEQRES 13 A 304 GLU GLU LYS ALA LYS LEU GLY LYS ILE GLY TYR TYR LEU
SEQRES 14 A 304 SER THR ILE ARG THR VAL LYS ASN ALA GLU THR PHE PRO
SEQRES 15 A 304 VAL LYS ILE THR TYR ASP GLY GLN VAL TYR GLU ASP GLU
SEQRES 16 A 304 ALA VAL LEU VAL MSE VAL GLY ASN GLY GLU TYR LEU GLY
SEQRES 17 A 304 GLY ILE PRO SER PHE ILE PRO ASN VAL LYS CYS ASP ASP
SEQRES 18 A 304 GLY THR LEU ASP ILE PHE VAL VAL LYS SER THR GLY ILE
SEQRES 19 A 304 GLN ALA PHE LYS ASP TYR ILE GLY LYS LYS LEU PHE GLU
SEQRES 20 A 304 ASP SER ASN GLU ASN ASP ILE PHE HIS VAL LYS ALA LYS
SEQRES 21 A 304 SER ILE HIS ILE GLU THR GLU GLU GLU LYS GLU VAL ASP
SEQRES 22 A 304 THR ASP GLY GLU SER SER LEU HIS THR PRO CYS GLN ILE
SEQRES 23 A 304 GLU LEU LEU GLN GLY HIS PHE THR MSE ILE TYR ASN PRO
SEQRES 24 A 304 ALA VAL VAL GLY SER
SEQRES 1 B 304 GLY HIS MSE THR LYS THR LYS PHE GLU LYS VAL LEU LEU
SEQRES 2 B 304 ILE VAL ASN PRO LYS ALA GLY GLN GLY ASP LEU HIS THR
SEQRES 3 B 304 ASN LEU THR LYS ILE VAL PRO PRO LEU ALA ALA ALA PHE
SEQRES 4 B 304 PRO ASP LEU HIS ILE LEU HIS THR LYS GLU GLN GLY ASP
SEQRES 5 B 304 ALA THR LYS TYR CYS GLN GLU PHE ALA SER LYS VAL ASP
SEQRES 6 B 304 LEU ILE ILE VAL PHE GLY GLY ASP GLY THR VAL PHE GLU
SEQRES 7 B 304 CYS THR ASN GLY LEU ALA PRO LEU GLU ILE ARG PRO THR
SEQRES 8 B 304 LEU ALA ILE ILE PRO GLY GLY THR CYS ASN ASP PHE SER
SEQRES 9 B 304 ARG THR LEU GLY VAL PRO GLN ASN ILE ALA GLU ALA ALA
SEQRES 10 B 304 LYS LEU ILE THR LYS GLU HIS VAL LYS PRO VAL ASP VAL
SEQRES 11 B 304 ALA LYS ALA ASN GLY GLN HIS PHE LEU ASN PHE TRP GLY
SEQRES 12 B 304 ILE GLY LEU VAL SER GLU VAL SER ASN ASN ILE ASP ALA
SEQRES 13 B 304 GLU GLU LYS ALA LYS LEU GLY LYS ILE GLY TYR TYR LEU
SEQRES 14 B 304 SER THR ILE ARG THR VAL LYS ASN ALA GLU THR PHE PRO
SEQRES 15 B 304 VAL LYS ILE THR TYR ASP GLY GLN VAL TYR GLU ASP GLU
SEQRES 16 B 304 ALA VAL LEU VAL MSE VAL GLY ASN GLY GLU TYR LEU GLY
SEQRES 17 B 304 GLY ILE PRO SER PHE ILE PRO ASN VAL LYS CYS ASP ASP
SEQRES 18 B 304 GLY THR LEU ASP ILE PHE VAL VAL LYS SER THR GLY ILE
SEQRES 19 B 304 GLN ALA PHE LYS ASP TYR ILE GLY LYS LYS LEU PHE GLU
SEQRES 20 B 304 ASP SER ASN GLU ASN ASP ILE PHE HIS VAL LYS ALA LYS
SEQRES 21 B 304 SER ILE HIS ILE GLU THR GLU GLU GLU LYS GLU VAL ASP
SEQRES 22 B 304 THR ASP GLY GLU SER SER LEU HIS THR PRO CYS GLN ILE
SEQRES 23 B 304 GLU LEU LEU GLN GLY HIS PHE THR MSE ILE TYR ASN PRO
SEQRES 24 B 304 ALA VAL VAL GLY SER
SEQRES 1 C 304 GLY HIS MSE THR LYS THR LYS PHE GLU LYS VAL LEU LEU
SEQRES 2 C 304 ILE VAL ASN PRO LYS ALA GLY GLN GLY ASP LEU HIS THR
SEQRES 3 C 304 ASN LEU THR LYS ILE VAL PRO PRO LEU ALA ALA ALA PHE
SEQRES 4 C 304 PRO ASP LEU HIS ILE LEU HIS THR LYS GLU GLN GLY ASP
SEQRES 5 C 304 ALA THR LYS TYR CYS GLN GLU PHE ALA SER LYS VAL ASP
SEQRES 6 C 304 LEU ILE ILE VAL PHE GLY GLY ASP GLY THR VAL PHE GLU
SEQRES 7 C 304 CYS THR ASN GLY LEU ALA PRO LEU GLU ILE ARG PRO THR
SEQRES 8 C 304 LEU ALA ILE ILE PRO GLY GLY THR CYS ASN ASP PHE SER
SEQRES 9 C 304 ARG THR LEU GLY VAL PRO GLN ASN ILE ALA GLU ALA ALA
SEQRES 10 C 304 LYS LEU ILE THR LYS GLU HIS VAL LYS PRO VAL ASP VAL
SEQRES 11 C 304 ALA LYS ALA ASN GLY GLN HIS PHE LEU ASN PHE TRP GLY
SEQRES 12 C 304 ILE GLY LEU VAL SER GLU VAL SER ASN ASN ILE ASP ALA
SEQRES 13 C 304 GLU GLU LYS ALA LYS LEU GLY LYS ILE GLY TYR TYR LEU
SEQRES 14 C 304 SER THR ILE ARG THR VAL LYS ASN ALA GLU THR PHE PRO
SEQRES 15 C 304 VAL LYS ILE THR TYR ASP GLY GLN VAL TYR GLU ASP GLU
SEQRES 16 C 304 ALA VAL LEU VAL MSE VAL GLY ASN GLY GLU TYR LEU GLY
SEQRES 17 C 304 GLY ILE PRO SER PHE ILE PRO ASN VAL LYS CYS ASP ASP
SEQRES 18 C 304 GLY THR LEU ASP ILE PHE VAL VAL LYS SER THR GLY ILE
SEQRES 19 C 304 GLN ALA PHE LYS ASP TYR ILE GLY LYS LYS LEU PHE GLU
SEQRES 20 C 304 ASP SER ASN GLU ASN ASP ILE PHE HIS VAL LYS ALA LYS
SEQRES 21 C 304 SER ILE HIS ILE GLU THR GLU GLU GLU LYS GLU VAL ASP
SEQRES 22 C 304 THR ASP GLY GLU SER SER LEU HIS THR PRO CYS GLN ILE
SEQRES 23 C 304 GLU LEU LEU GLN GLY HIS PHE THR MSE ILE TYR ASN PRO
SEQRES 24 C 304 ALA VAL VAL GLY SER
SEQRES 1 D 304 GLY HIS MSE THR LYS THR LYS PHE GLU LYS VAL LEU LEU
SEQRES 2 D 304 ILE VAL ASN PRO LYS ALA GLY GLN GLY ASP LEU HIS THR
SEQRES 3 D 304 ASN LEU THR LYS ILE VAL PRO PRO LEU ALA ALA ALA PHE
SEQRES 4 D 304 PRO ASP LEU HIS ILE LEU HIS THR LYS GLU GLN GLY ASP
SEQRES 5 D 304 ALA THR LYS TYR CYS GLN GLU PHE ALA SER LYS VAL ASP
SEQRES 6 D 304 LEU ILE ILE VAL PHE GLY GLY ASP GLY THR VAL PHE GLU
SEQRES 7 D 304 CYS THR ASN GLY LEU ALA PRO LEU GLU ILE ARG PRO THR
SEQRES 8 D 304 LEU ALA ILE ILE PRO GLY GLY THR CYS ASN ASP PHE SER
SEQRES 9 D 304 ARG THR LEU GLY VAL PRO GLN ASN ILE ALA GLU ALA ALA
SEQRES 10 D 304 LYS LEU ILE THR LYS GLU HIS VAL LYS PRO VAL ASP VAL
SEQRES 11 D 304 ALA LYS ALA ASN GLY GLN HIS PHE LEU ASN PHE TRP GLY
SEQRES 12 D 304 ILE GLY LEU VAL SER GLU VAL SER ASN ASN ILE ASP ALA
SEQRES 13 D 304 GLU GLU LYS ALA LYS LEU GLY LYS ILE GLY TYR TYR LEU
SEQRES 14 D 304 SER THR ILE ARG THR VAL LYS ASN ALA GLU THR PHE PRO
SEQRES 15 D 304 VAL LYS ILE THR TYR ASP GLY GLN VAL TYR GLU ASP GLU
SEQRES 16 D 304 ALA VAL LEU VAL MSE VAL GLY ASN GLY GLU TYR LEU GLY
SEQRES 17 D 304 GLY ILE PRO SER PHE ILE PRO ASN VAL LYS CYS ASP ASP
SEQRES 18 D 304 GLY THR LEU ASP ILE PHE VAL VAL LYS SER THR GLY ILE
SEQRES 19 D 304 GLN ALA PHE LYS ASP TYR ILE GLY LYS LYS LEU PHE GLU
SEQRES 20 D 304 ASP SER ASN GLU ASN ASP ILE PHE HIS VAL LYS ALA LYS
SEQRES 21 D 304 SER ILE HIS ILE GLU THR GLU GLU GLU LYS GLU VAL ASP
SEQRES 22 D 304 THR ASP GLY GLU SER SER LEU HIS THR PRO CYS GLN ILE
SEQRES 23 D 304 GLU LEU LEU GLN GLY HIS PHE THR MSE ILE TYR ASN PRO
SEQRES 24 D 304 ALA VAL VAL GLY SER
MODRES 3S40 MSE A 198 MET SELENOMETHIONINE
MODRES 3S40 MSE A 293 MET SELENOMETHIONINE
MODRES 3S40 MSE B 198 MET SELENOMETHIONINE
MODRES 3S40 MSE B 293 MET SELENOMETHIONINE
MODRES 3S40 MSE C 198 MET SELENOMETHIONINE
MODRES 3S40 MSE C 293 MET SELENOMETHIONINE
MODRES 3S40 MSE D 198 MET SELENOMETHIONINE
MODRES 3S40 MSE D 293 MET SELENOMETHIONINE
HET MSE A 198 8
HET MSE A 293 8
HET MSE B 198 8
HET MSE B 293 8
HET MSE C 198 8
HET MSE C 293 8
HET MSE D 198 8
HET MSE D 293 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 5 HOH *329(H2 O)
HELIX 1 1 ASP A 21 PHE A 37 1 17
HELIX 2 2 GLY A 49 ALA A 59 1 11
HELIX 3 3 GLY A 70 ALA A 82 1 13
HELIX 4 4 ASN A 99 LEU A 105 1 7
HELIX 5 5 ASN A 110 THR A 119 1 10
HELIX 6 6 LYS A 162 LEU A 167 1 6
HELIX 7 7 GLY A 231 ILE A 239 1 9
HELIX 8 8 ASP B 21 PHE B 37 1 17
HELIX 9 9 GLY B 49 ALA B 59 1 11
HELIX 10 10 GLY B 70 ALA B 82 1 13
HELIX 11 11 ASN B 99 LEU B 105 1 7
HELIX 12 12 ASN B 110 GLU B 121 1 12
HELIX 13 13 ASN B 150 THR B 169 1 20
HELIX 14 14 GLY B 231 LYS B 242 1 12
HELIX 15 15 ASP C 21 PHE C 37 1 17
HELIX 16 16 GLY C 49 ALA C 59 1 11
HELIX 17 17 GLY C 70 ALA C 82 1 13
HELIX 18 18 ASN C 99 LEU C 105 1 7
HELIX 19 19 ASN C 110 LYS C 120 1 11
HELIX 20 20 ASP C 153 GLY C 161 1 9
HELIX 21 21 GLY C 161 VAL C 173 1 13
HELIX 22 22 GLY C 231 LYS C 241 1 11
HELIX 23 23 ASP D 21 PHE D 37 1 17
HELIX 24 24 GLY D 49 ALA D 59 1 11
HELIX 25 25 GLY D 70 ALA D 82 1 13
HELIX 26 26 ASN D 99 LEU D 105 1 7
HELIX 27 27 ASN D 110 THR D 119 1 10
HELIX 28 28 ILE D 163 THR D 169 1 7
HELIX 29 29 GLY D 231 ILE D 239 1 9
SHEET 1 A 8 THR A 89 PRO A 94 0
SHEET 2 A 8 LEU A 64 GLY A 69 1 N VAL A 67 O ILE A 93
SHEET 3 A 8 VAL A 9 VAL A 13 1 N LEU A 10 O ILE A 66
SHEET 4 A 8 ASP A 39 HIS A 44 1 O HIS A 41 N LEU A 11
SHEET 5 A 8 ASP B 39 HIS B 44 -1 O LEU B 40 N ILE A 42
SHEET 6 A 8 VAL B 9 VAL B 13 1 N LEU B 11 O HIS B 41
SHEET 7 A 8 LEU B 64 GLY B 69 1 O ILE B 66 N ILE B 12
SHEET 8 A 8 THR B 89 PRO B 94 1 O ILE B 93 N VAL B 67
SHEET 1 B 8 GLN A 134 PHE A 136 0
SHEET 2 B 8 VAL A 123 ALA A 131 -1 N ALA A 131 O GLN A 134
SHEET 3 B 8 CYS A 282 ILE A 294 -1 O LEU A 287 N VAL A 128
SHEET 4 B 8 SER A 259 THR A 264 -1 N ILE A 260 O ILE A 284
SHEET 5 B 8 PHE A 179 TYR A 185 -1 N THR A 184 O HIS A 261
SHEET 6 B 8 GLN A 188 GLY A 200 -1 O TYR A 190 N ILE A 183
SHEET 7 B 8 LEU A 222 LYS A 228 -1 O PHE A 225 N MSE A 198
SHEET 8 B 8 ILE A 252 ALA A 257 -1 O PHE A 253 N VAL A 226
SHEET 1 C 9 GLN A 134 PHE A 136 0
SHEET 2 C 9 VAL A 123 ALA A 131 -1 N ALA A 131 O GLN A 134
SHEET 3 C 9 CYS A 282 ILE A 294 -1 O LEU A 287 N VAL A 128
SHEET 4 C 9 SER A 259 THR A 264 -1 N ILE A 260 O ILE A 284
SHEET 5 C 9 PHE A 179 TYR A 185 -1 N THR A 184 O HIS A 261
SHEET 6 C 9 GLN A 188 GLY A 200 -1 O TYR A 190 N ILE A 183
SHEET 7 C 9 PHE A 139 ILE A 142 -1 N TRP A 140 O VAL A 199
SHEET 8 C 9 GLU A 269 THR A 272 -1 O ASP A 271 N GLY A 141
SHEET 9 C 9 LEU A 278 HIS A 279 -1 O LEU A 278 N VAL A 270
SHEET 1 D 2 TYR A 204 LEU A 205 0
SHEET 2 D 2 ILE A 208 PRO A 209 -1 O ILE A 208 N LEU A 205
SHEET 1 E 7 GLN B 134 PHE B 136 0
SHEET 2 E 7 VAL B 123 ALA B 131 -1 N ALA B 131 O GLN B 134
SHEET 3 E 7 CYS B 282 ILE B 294 -1 O GLU B 285 N LYS B 130
SHEET 4 E 7 SER B 259 THR B 264 -1 N ILE B 260 O ILE B 284
SHEET 5 E 7 PHE B 179 TYR B 185 -1 N LYS B 182 O GLU B 263
SHEET 6 E 7 VAL B 189 GLY B 200 -1 O ASP B 192 N VAL B 181
SHEET 7 E 7 PHE B 139 ILE B 142 -1 N TRP B 140 O VAL B 199
SHEET 1 F 8 GLN B 134 PHE B 136 0
SHEET 2 F 8 VAL B 123 ALA B 131 -1 N ALA B 131 O GLN B 134
SHEET 3 F 8 CYS B 282 ILE B 294 -1 O GLU B 285 N LYS B 130
SHEET 4 F 8 SER B 259 THR B 264 -1 N ILE B 260 O ILE B 284
SHEET 5 F 8 PHE B 179 TYR B 185 -1 N LYS B 182 O GLU B 263
SHEET 6 F 8 VAL B 189 GLY B 200 -1 O ASP B 192 N VAL B 181
SHEET 7 F 8 LEU B 222 LYS B 228 -1 O PHE B 225 N MSE B 198
SHEET 8 F 8 PHE B 253 ALA B 257 -1 O VAL B 255 N ILE B 224
SHEET 1 G 2 TYR B 204 LEU B 205 0
SHEET 2 G 2 ILE B 208 PRO B 209 -1 O ILE B 208 N LEU B 205
SHEET 1 H 8 THR C 89 PRO C 94 0
SHEET 2 H 8 LEU C 64 GLY C 69 1 N VAL C 67 O ILE C 93
SHEET 3 H 8 VAL C 9 VAL C 13 1 N ILE C 12 O ILE C 66
SHEET 4 H 8 ASP C 39 HIS C 44 1 O HIS C 41 N LEU C 11
SHEET 5 H 8 ASP D 39 HIS D 44 -1 O LEU D 40 N ILE C 42
SHEET 6 H 8 VAL D 9 VAL D 13 1 N VAL D 13 O LEU D 43
SHEET 7 H 8 LEU D 64 GLY D 69 1 O ILE D 66 N ILE D 12
SHEET 8 H 8 THR D 89 PRO D 94 1 O ILE D 93 N VAL D 67
SHEET 1 I 8 GLN C 134 PHE C 136 0
SHEET 2 I 8 VAL C 123 ALA C 131 -1 N ALA C 131 O GLN C 134
SHEET 3 I 8 CYS C 282 ILE C 294 -1 O GLU C 285 N LYS C 130
SHEET 4 I 8 SER C 259 THR C 264 -1 N ILE C 260 O ILE C 284
SHEET 5 I 8 PHE C 179 TYR C 185 -1 N LYS C 182 O GLU C 263
SHEET 6 I 8 GLN C 188 GLY C 200 -1 O TYR C 190 N ILE C 183
SHEET 7 I 8 LEU C 222 LYS C 228 -1 O PHE C 225 N MSE C 198
SHEET 8 I 8 PHE C 253 ALA C 257 -1 O VAL C 255 N ILE C 224
SHEET 1 J 8 GLN C 134 PHE C 136 0
SHEET 2 J 8 VAL C 123 ALA C 131 -1 N ALA C 131 O GLN C 134
SHEET 3 J 8 CYS C 282 ILE C 294 -1 O GLU C 285 N LYS C 130
SHEET 4 J 8 SER C 259 THR C 264 -1 N ILE C 260 O ILE C 284
SHEET 5 J 8 PHE C 179 TYR C 185 -1 N LYS C 182 O GLU C 263
SHEET 6 J 8 GLN C 188 GLY C 200 -1 O TYR C 190 N ILE C 183
SHEET 7 J 8 PHE C 139 ILE C 142 -1 N TRP C 140 O VAL C 199
SHEET 8 J 8 ASP C 271 THR C 272 -1 O ASP C 271 N GLY C 141
SHEET 1 K 2 TYR C 204 LEU C 205 0
SHEET 2 K 2 ILE C 208 PRO C 209 -1 O ILE C 208 N LEU C 205
SHEET 1 L 8 GLN D 134 PHE D 136 0
SHEET 2 L 8 VAL D 123 ALA D 131 -1 N ALA D 131 O GLN D 134
SHEET 3 L 8 CYS D 282 ILE D 294 -1 O GLU D 285 N LYS D 130
SHEET 4 L 8 SER D 259 THR D 264 -1 N ILE D 260 O ILE D 284
SHEET 5 L 8 PHE D 179 TYR D 185 -1 N THR D 184 O HIS D 261
SHEET 6 L 8 VAL D 189 GLY D 200 -1 O ASP D 192 N VAL D 181
SHEET 7 L 8 LEU D 222 LYS D 228 -1 O PHE D 225 N MSE D 198
SHEET 8 L 8 PHE D 253 ALA D 257 -1 O ALA D 257 N LEU D 222
SHEET 1 M 8 GLN D 134 PHE D 136 0
SHEET 2 M 8 VAL D 123 ALA D 131 -1 N ALA D 131 O GLN D 134
SHEET 3 M 8 CYS D 282 ILE D 294 -1 O GLU D 285 N LYS D 130
SHEET 4 M 8 SER D 259 THR D 264 -1 N ILE D 260 O ILE D 284
SHEET 5 M 8 PHE D 179 TYR D 185 -1 N THR D 184 O HIS D 261
SHEET 6 M 8 VAL D 189 GLY D 200 -1 O ASP D 192 N VAL D 181
SHEET 7 M 8 PHE D 139 ILE D 142 -1 N TRP D 140 O VAL D 199
SHEET 8 M 8 ASP D 271 THR D 272 -1 O ASP D 271 N GLY D 141
SHEET 1 N 2 TYR D 204 LEU D 205 0
SHEET 2 N 2 ILE D 208 PRO D 209 -1 O ILE D 208 N LEU D 205
LINK C VAL A 197 N MSE A 198 1555 1555 1.32
LINK C MSE A 198 N VAL A 199 1555 1555 1.33
LINK C THR A 292 N MSE A 293 1555 1555 1.33
LINK C MSE A 293 N ILE A 294 1555 1555 1.32
LINK C VAL B 197 N MSE B 198 1555 1555 1.33
LINK C MSE B 198 N VAL B 199 1555 1555 1.33
LINK C THR B 292 N MSE B 293 1555 1555 1.33
LINK C MSE B 293 N ILE B 294 1555 1555 1.33
LINK C VAL C 197 N MSE C 198 1555 1555 1.33
LINK C MSE C 198 N VAL C 199 1555 1555 1.33
LINK C THR C 292 N MSE C 293 1555 1555 1.33
LINK C MSE C 293 N ILE C 294 1555 1555 1.33
LINK C VAL D 197 N MSE D 198 1555 1555 1.33
LINK C MSE D 198 N VAL D 199 1555 1555 1.33
LINK C THR D 292 N MSE D 293 1555 1555 1.33
LINK C MSE D 293 N ILE D 294 1555 1555 1.32
CISPEP 1 THR A 280 PRO A 281 0 -4.65
CISPEP 2 THR B 280 PRO B 281 0 -1.69
CISPEP 3 THR C 280 PRO C 281 0 -2.67
CISPEP 4 THR D 280 PRO D 281 0 -2.49
CRYST1 63.608 130.758 72.794 90.00 115.04 90.00 P 1 21 1 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 0.015721 0.000000 0.007344 0.00000
SCALE2 0.000000 0.007648 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015162 0.00000
(ATOM LINES ARE NOT SHOWN.)
END