HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 07-MAY-09 3HE1
TITLE SECRETED PROTEIN HCP3 FROM PSEUDOMONAS AERUGINOSA.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MAJOR EXPORTED HCP3 PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: SECRETED PROTEIN HCP;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 STRAIN: PAO1;
SOURCE 5 GENE: HCPC, PA0263;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B MODIFIED
KEYWDS STRUCTURAL GENOMICS, APC22128, HCP3, HCPC, SECRETION, VIRULENCE, PSI-
KEYWDS 2 2, PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG, SECRETED, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.OSIPIUK,X.XU,H.CUI,A.SAVCHENKO,A.M.EDWARDS,A.JOACHIMIAK,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 4 01-NOV-17 3HE1 1 REMARK
REVDAT 3 25-JUL-12 3HE1 1 JRNL
REVDAT 2 13-JUL-11 3HE1 1 VERSN
REVDAT 1 16-JUN-09 3HE1 0
JRNL AUTH J.OSIPIUK,X.XU,H.CUI,A.SAVCHENKO,A.EDWARDS,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF SECRETORY PROTEIN HCP3 FROM PSEUDOMONAS
JRNL TITL 2 AERUGINOSA.
JRNL REF J.STRUCT.FUNCT.GENOM. V. 12 21 2011
JRNL REFN ISSN 1345-711X
JRNL PMID 21476004
JRNL DOI 10.1007/S10969-011-9107-1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.80
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.890
REMARK 3 COMPLETENESS FOR RANGE (%) : 82.6
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.350
REMARK 3 FREE R VALUE TEST SET COUNT : 6053
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 39.8520 - 5.6910 0.98 5356 266 0.3860 0.4750
REMARK 3 2 5.6910 - 4.5190 0.98 4884 283 0.1770 0.2300
REMARK 3 3 4.5190 - 3.9480 0.98 4875 254 0.1420 0.1630
REMARK 3 4 3.9480 - 3.5880 0.98 4829 241 0.1550 0.1890
REMARK 3 5 3.5880 - 3.3310 0.98 4512 227 0.1610 0.1830
REMARK 3 6 3.3310 - 3.1340 0.98 4715 252 0.1820 0.1980
REMARK 3 7 3.1340 - 2.9770 0.98 4938 257 0.1910 0.2370
REMARK 3 8 2.9770 - 2.8480 0.98 5098 290 0.2190 0.3080
REMARK 3 9 2.8480 - 2.7380 0.98 5400 245 0.2180 0.2720
REMARK 3 10 2.7380 - 2.6440 0.98 5329 278 0.2300 0.2880
REMARK 3 11 2.6440 - 2.5610 0.98 5504 267 0.2340 0.2410
REMARK 3 12 2.5610 - 2.4880 0.98 5476 326 0.2460 0.3130
REMARK 3 13 2.4880 - 2.4220 0.98 5688 289 0.2380 0.2730
REMARK 3 14 2.4220 - 2.3630 0.98 5634 307 0.2340 0.2740
REMARK 3 15 2.3630 - 2.3100 0.98 5895 309 0.2430 0.2700
REMARK 3 16 2.3100 - 2.2600 0.98 5606 297 0.2520 0.3170
REMARK 3 17 2.2600 - 2.2150 0.98 6006 326 0.2510 0.2990
REMARK 3 18 2.2150 - 2.1740 0.98 5911 332 0.2520 0.3010
REMARK 3 19 2.1740 - 2.1350 0.98 5945 314 0.2580 0.3340
REMARK 3 20 2.1350 - 2.0990 0.98 5976 308 0.2600 0.3320
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 : 0.39
REMARK 3 B_SOL : 81.39
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.39800
REMARK 3 B22 (A**2) : -4.39800
REMARK 3 B33 (A**2) : 8.57300
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: 0.5090
REMARK 3 OPERATOR: -K,H+K,L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 7138
REMARK 3 ANGLE : 1.189 9704
REMARK 3 CHIRALITY : 0.076 1110
REMARK 3 PLANARITY : 0.004 1215
REMARK 3 DIHEDRAL : 17.745 2478
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: TWINNED CRYSTAL, TWIN FRACTION: 0.51,
REMARK 3 TWIN OPERATOR: -K,H+K,L. PHENIX PROGRAM TREATS FRIEDEL PAIRS AS
REMARK 3 TWO SEPARATE REFLECTIONS, WHICH GENERATE BIGGER NUMBER OF
REMARK 3 REFLECTIONS USED IN REFINEMENT THAN IN DATA COLLECTION.
REMARK 4
REMARK 4 3HE1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000053018.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69851
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.098
REMARK 200 RESOLUTION RANGE LOW (A) : 39.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.40
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.3920
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.40
REMARK 200 R MERGE FOR SHELL (I) : 0.64700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.090
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD, MLPHARE, DM, SOLVE, RESOLVE, HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS BUFFER, 3.2 M SODIUM
REMARK 280 CHLORIDE, CHYMOTRYPSIN PARTIAL DIGESTION IN CRYSTALLIZATION
REMARK 280 DROPLET, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3 1 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -Y,-X,-Z
REMARK 290 5555 -X+Y,Y,-Z
REMARK 290 6555 X,X-Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: HEXAMER FORMED BY SUBUNITS A AND B AND THEIR SYMMETRY
REMARK 300 RELATED MOLECULES
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -96.0 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 211.82850
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 122.29924
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 244.59848
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 141.21900
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 70.60950
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 122.29924
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 -0.500000 -0.866025 0.000000 70.60950
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 122.29924
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -70.60950
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 122.29924
REMARK 350 BIOMT3 3 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 MSE A -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 ARG A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MSE A 1
REMARK 465 ARG A 52
REMARK 465 ASP A 53
REMARK 465 PRO A 54
REMARK 465 GLN A 55
REMARK 465 SER A 56
REMARK 465 GLY A 57
REMARK 465 GLN A 58
REMARK 465 PRO A 59
REMARK 465 THR A 60
REMARK 465 GLY A 61
REMARK 465 GLN A 62
REMARK 465 ASN A 129
REMARK 465 CYS A 130
REMARK 465 GLN A 131
REMARK 465 ASP A 132
REMARK 465 PRO A 133
REMARK 465 GLY A 134
REMARK 465 ASN A 135
REMARK 465 ALA A 136
REMARK 465 HIS A 137
REMARK 465 PRO A 169
REMARK 465 VAL A 170
REMARK 465 ALA A 171
REMARK 465 GLY A 172
REMARK 465 SER A 173
REMARK 465 MSE B -21
REMARK 465 GLY B -20
REMARK 465 SER B -19
REMARK 465 SER B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 SER B -11
REMARK 465 SER B -10
REMARK 465 GLY B -9
REMARK 465 ARG B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 MSE B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 PRO B 51
REMARK 465 ARG B 52
REMARK 465 ASP B 53
REMARK 465 PRO B 54
REMARK 465 GLN B 55
REMARK 465 SER B 56
REMARK 465 GLY B 57
REMARK 465 GLN B 58
REMARK 465 PRO B 59
REMARK 465 THR B 60
REMARK 465 HIS B 128
REMARK 465 ASN B 129
REMARK 465 CYS B 130
REMARK 465 GLN B 131
REMARK 465 ASP B 132
REMARK 465 PRO B 133
REMARK 465 GLY B 134
REMARK 465 ASN B 135
REMARK 465 ALA B 136
REMARK 465 HIS B 137
REMARK 465 PHE B 138
REMARK 465 SER B 168
REMARK 465 PRO B 169
REMARK 465 VAL B 170
REMARK 465 ALA B 171
REMARK 465 GLY B 172
REMARK 465 SER B 173
REMARK 465 MSE C -21
REMARK 465 GLY C -20
REMARK 465 SER C -19
REMARK 465 SER C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 SER C -11
REMARK 465 SER C -10
REMARK 465 GLY C -9
REMARK 465 ARG C -8
REMARK 465 GLU C -7
REMARK 465 ASN C -6
REMARK 465 LEU C -5
REMARK 465 TYR C -4
REMARK 465 PHE C -3
REMARK 465 GLN C -2
REMARK 465 GLY C -1
REMARK 465 HIS C 0
REMARK 465 MSE C 1
REMARK 465 ARG C 52
REMARK 465 ASP C 53
REMARK 465 PRO C 54
REMARK 465 GLN C 55
REMARK 465 SER C 56
REMARK 465 GLY C 57
REMARK 465 GLN C 58
REMARK 465 PRO C 59
REMARK 465 THR C 60
REMARK 465 GLY C 61
REMARK 465 GLN C 62
REMARK 465 ASN C 129
REMARK 465 CYS C 130
REMARK 465 GLN C 131
REMARK 465 ASP C 132
REMARK 465 PRO C 133
REMARK 465 GLY C 134
REMARK 465 ASN C 135
REMARK 465 ALA C 136
REMARK 465 HIS C 137
REMARK 465 PRO C 169
REMARK 465 VAL C 170
REMARK 465 ALA C 171
REMARK 465 GLY C 172
REMARK 465 SER C 173
REMARK 465 MSE D -21
REMARK 465 GLY D -20
REMARK 465 SER D -19
REMARK 465 SER D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 SER D -11
REMARK 465 SER D -10
REMARK 465 GLY D -9
REMARK 465 ARG D -8
REMARK 465 GLU D -7
REMARK 465 ASN D -6
REMARK 465 LEU D -5
REMARK 465 TYR D -4
REMARK 465 PHE D -3
REMARK 465 GLN D -2
REMARK 465 GLY D -1
REMARK 465 HIS D 0
REMARK 465 MSE D 1
REMARK 465 ALA D 2
REMARK 465 THR D 3
REMARK 465 PRO D 51
REMARK 465 ARG D 52
REMARK 465 ASP D 53
REMARK 465 PRO D 54
REMARK 465 GLN D 55
REMARK 465 SER D 56
REMARK 465 GLY D 57
REMARK 465 GLN D 58
REMARK 465 PRO D 59
REMARK 465 THR D 60
REMARK 465 HIS D 128
REMARK 465 ASN D 129
REMARK 465 CYS D 130
REMARK 465 GLN D 131
REMARK 465 ASP D 132
REMARK 465 PRO D 133
REMARK 465 GLY D 134
REMARK 465 ASN D 135
REMARK 465 ALA D 136
REMARK 465 HIS D 137
REMARK 465 PHE D 138
REMARK 465 SER D 168
REMARK 465 PRO D 169
REMARK 465 VAL D 170
REMARK 465 ALA D 171
REMARK 465 GLY D 172
REMARK 465 SER D 173
REMARK 465 MSE E -21
REMARK 465 GLY E -20
REMARK 465 SER E -19
REMARK 465 SER E -18
REMARK 465 HIS E -17
REMARK 465 HIS E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 SER E -11
REMARK 465 SER E -10
REMARK 465 GLY E -9
REMARK 465 ARG E -8
REMARK 465 GLU E -7
REMARK 465 ASN E -6
REMARK 465 LEU E -5
REMARK 465 TYR E -4
REMARK 465 PHE E -3
REMARK 465 GLN E -2
REMARK 465 GLY E -1
REMARK 465 HIS E 0
REMARK 465 MSE E 1
REMARK 465 ARG E 52
REMARK 465 ASP E 53
REMARK 465 PRO E 54
REMARK 465 GLN E 55
REMARK 465 SER E 56
REMARK 465 GLY E 57
REMARK 465 GLN E 58
REMARK 465 PRO E 59
REMARK 465 THR E 60
REMARK 465 GLY E 61
REMARK 465 GLN E 62
REMARK 465 ASN E 129
REMARK 465 CYS E 130
REMARK 465 GLN E 131
REMARK 465 ASP E 132
REMARK 465 PRO E 133
REMARK 465 GLY E 134
REMARK 465 ASN E 135
REMARK 465 ALA E 136
REMARK 465 HIS E 137
REMARK 465 PRO E 169
REMARK 465 VAL E 170
REMARK 465 ALA E 171
REMARK 465 GLY E 172
REMARK 465 SER E 173
REMARK 465 MSE F -21
REMARK 465 GLY F -20
REMARK 465 SER F -19
REMARK 465 SER F -18
REMARK 465 HIS F -17
REMARK 465 HIS F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 HIS F -12
REMARK 465 SER F -11
REMARK 465 SER F -10
REMARK 465 GLY F -9
REMARK 465 ARG F -8
REMARK 465 GLU F -7
REMARK 465 ASN F -6
REMARK 465 LEU F -5
REMARK 465 TYR F -4
REMARK 465 PHE F -3
REMARK 465 GLN F -2
REMARK 465 GLY F -1
REMARK 465 HIS F 0
REMARK 465 MSE F 1
REMARK 465 ALA F 2
REMARK 465 THR F 3
REMARK 465 PRO F 51
REMARK 465 ARG F 52
REMARK 465 ASP F 53
REMARK 465 PRO F 54
REMARK 465 GLN F 55
REMARK 465 SER F 56
REMARK 465 GLY F 57
REMARK 465 GLN F 58
REMARK 465 PRO F 59
REMARK 465 THR F 60
REMARK 465 HIS F 128
REMARK 465 ASN F 129
REMARK 465 CYS F 130
REMARK 465 GLN F 131
REMARK 465 ASP F 132
REMARK 465 PRO F 133
REMARK 465 GLY F 134
REMARK 465 ASN F 135
REMARK 465 ALA F 136
REMARK 465 HIS F 137
REMARK 465 PHE F 138
REMARK 465 SER F 168
REMARK 465 PRO F 169
REMARK 465 VAL F 170
REMARK 465 ALA F 171
REMARK 465 GLY F 172
REMARK 465 SER F 173
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG E 90 CD
REMARK 480 THR F 112 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH E 192 O HOH E 352 2.13
REMARK 500 O HOH A 183 O HOH A 258 2.13
REMARK 500
REMARK 500 REMARK: NULL
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 THR A 3 63.35 -114.85
REMARK 500 HIS A 35 34.96 -146.00
REMARK 500 ASP A 75 -168.16 -164.04
REMARK 500 GLU A 142 111.94 -172.32
REMARK 500 LYS A 150 149.93 -170.07
REMARK 500 HIS B 35 42.11 -141.43
REMARK 500 ASP B 122 135.51 -173.49
REMARK 500 THR C 3 63.30 -115.24
REMARK 500 PHE C 22 73.42 -114.66
REMARK 500 HIS C 35 38.21 -140.90
REMARK 500 PHE C 44 133.02 -170.16
REMARK 500 LEU D 16 86.99 -67.21
REMARK 500 HIS D 35 40.54 -141.68
REMARK 500 ASP D 122 135.66 -174.32
REMARK 500 PHE E 22 72.72 -116.59
REMARK 500 HIS E 35 34.14 -145.42
REMARK 500 GLU E 142 112.83 -178.69
REMARK 500 LEU F 16 88.62 -66.89
REMARK 500 HIS F 35 36.70 -142.00
REMARK 500 ASP F 122 137.84 -173.90
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 GOL C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC22128 RELATED DB: TARGETDB
DBREF 3HE1 A 1 172 UNP Q9HI36 MAJE_PSEAE 1 172
DBREF 3HE1 B 1 172 UNP Q9HI36 MAJE_PSEAE 1 172
DBREF 3HE1 C 1 172 UNP Q9HI36 MAJE_PSEAE 1 172
DBREF 3HE1 D 1 172 UNP Q9HI36 MAJE_PSEAE 1 172
DBREF 3HE1 E 1 172 UNP Q9HI36 MAJE_PSEAE 1 172
DBREF 3HE1 F 1 172 UNP Q9HI36 MAJE_PSEAE 1 172
SEQADV 3HE1 MSE A -21 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY A -20 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER A -19 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER A -18 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS A -17 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS A -16 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS A -15 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS A -14 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS A -13 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS A -12 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER A -11 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER A -10 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY A -9 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 ARG A -8 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLU A -7 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 ASN A -6 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 LEU A -5 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 TYR A -4 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 PHE A -3 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLN A -2 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY A -1 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS A 0 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER A 173 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 MSE B -21 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY B -20 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER B -19 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER B -18 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS B -17 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS B -16 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS B -15 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS B -14 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS B -13 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS B -12 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER B -11 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER B -10 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY B -9 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 ARG B -8 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLU B -7 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 ASN B -6 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 LEU B -5 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 TYR B -4 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 PHE B -3 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLN B -2 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY B -1 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS B 0 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER B 173 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 MSE C -21 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY C -20 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER C -19 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER C -18 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS C -17 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS C -16 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS C -15 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS C -14 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS C -13 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS C -12 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER C -11 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER C -10 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY C -9 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 ARG C -8 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLU C -7 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 ASN C -6 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 LEU C -5 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 TYR C -4 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 PHE C -3 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLN C -2 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY C -1 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS C 0 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER C 173 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 MSE D -21 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY D -20 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER D -19 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER D -18 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS D -17 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS D -16 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS D -15 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS D -14 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS D -13 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS D -12 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER D -11 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER D -10 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY D -9 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 ARG D -8 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLU D -7 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 ASN D -6 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 LEU D -5 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 TYR D -4 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 PHE D -3 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLN D -2 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY D -1 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS D 0 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER D 173 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 MSE E -21 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY E -20 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER E -19 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER E -18 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS E -17 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS E -16 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS E -15 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS E -14 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS E -13 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS E -12 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER E -11 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER E -10 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY E -9 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 ARG E -8 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLU E -7 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 ASN E -6 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 LEU E -5 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 TYR E -4 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 PHE E -3 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLN E -2 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY E -1 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS E 0 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER E 173 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 MSE F -21 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY F -20 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER F -19 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER F -18 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS F -17 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS F -16 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS F -15 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS F -14 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS F -13 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS F -12 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER F -11 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER F -10 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY F -9 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 ARG F -8 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLU F -7 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 ASN F -6 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 LEU F -5 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 TYR F -4 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 PHE F -3 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLN F -2 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 GLY F -1 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 HIS F 0 UNP Q9HI36 EXPRESSION TAG
SEQADV 3HE1 SER F 173 UNP Q9HI36 EXPRESSION TAG
SEQRES 1 A 195 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 195 ARG GLU ASN LEU TYR PHE GLN GLY HIS MSE ALA THR PRO
SEQRES 3 A 195 ALA TYR MSE SER ILE THR GLY THR LYS GLN GLY LEU ILE
SEQRES 4 A 195 THR ALA GLY ALA PHE THR GLU ASP SER VAL GLY ASN THR
SEQRES 5 A 195 TYR GLN GLU GLY HIS GLU ASP GLN VAL MSE VAL GLN GLY
SEQRES 6 A 195 PHE ASN HIS GLU VAL ILE ILE PRO ARG ASP PRO GLN SER
SEQRES 7 A 195 GLY GLN PRO THR GLY GLN ARG VAL HIS LYS PRO VAL VAL
SEQRES 8 A 195 ILE THR LYS VAL PHE ASP LYS ALA SER PRO LEU LEU LEU
SEQRES 9 A 195 ALA ALA LEU THR SER GLY GLU ARG LEU THR LYS VAL GLU
SEQRES 10 A 195 ILE GLN TRP TYR ARG THR SER ALA ALA GLY THR GLN GLU
SEQRES 11 A 195 HIS TYR TYR THR THR VAL LEU GLU ASP ALA ILE ILE VAL
SEQRES 12 A 195 ASP ILE LYS ASP TYR MSE HIS ASN CYS GLN ASP PRO GLY
SEQRES 13 A 195 ASN ALA HIS PHE THR HIS LEU GLU ASP VAL HIS PHE THR
SEQRES 14 A 195 TYR ARG LYS ILE THR TRP THR HIS GLU VAL SER GLY THR
SEQRES 15 A 195 SER GLY SER ASP ASP TRP ARG SER PRO VAL ALA GLY SER
SEQRES 1 B 195 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 195 ARG GLU ASN LEU TYR PHE GLN GLY HIS MSE ALA THR PRO
SEQRES 3 B 195 ALA TYR MSE SER ILE THR GLY THR LYS GLN GLY LEU ILE
SEQRES 4 B 195 THR ALA GLY ALA PHE THR GLU ASP SER VAL GLY ASN THR
SEQRES 5 B 195 TYR GLN GLU GLY HIS GLU ASP GLN VAL MSE VAL GLN GLY
SEQRES 6 B 195 PHE ASN HIS GLU VAL ILE ILE PRO ARG ASP PRO GLN SER
SEQRES 7 B 195 GLY GLN PRO THR GLY GLN ARG VAL HIS LYS PRO VAL VAL
SEQRES 8 B 195 ILE THR LYS VAL PHE ASP LYS ALA SER PRO LEU LEU LEU
SEQRES 9 B 195 ALA ALA LEU THR SER GLY GLU ARG LEU THR LYS VAL GLU
SEQRES 10 B 195 ILE GLN TRP TYR ARG THR SER ALA ALA GLY THR GLN GLU
SEQRES 11 B 195 HIS TYR TYR THR THR VAL LEU GLU ASP ALA ILE ILE VAL
SEQRES 12 B 195 ASP ILE LYS ASP TYR MSE HIS ASN CYS GLN ASP PRO GLY
SEQRES 13 B 195 ASN ALA HIS PHE THR HIS LEU GLU ASP VAL HIS PHE THR
SEQRES 14 B 195 TYR ARG LYS ILE THR TRP THR HIS GLU VAL SER GLY THR
SEQRES 15 B 195 SER GLY SER ASP ASP TRP ARG SER PRO VAL ALA GLY SER
SEQRES 1 C 195 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 195 ARG GLU ASN LEU TYR PHE GLN GLY HIS MSE ALA THR PRO
SEQRES 3 C 195 ALA TYR MSE SER ILE THR GLY THR LYS GLN GLY LEU ILE
SEQRES 4 C 195 THR ALA GLY ALA PHE THR GLU ASP SER VAL GLY ASN THR
SEQRES 5 C 195 TYR GLN GLU GLY HIS GLU ASP GLN VAL MSE VAL GLN GLY
SEQRES 6 C 195 PHE ASN HIS GLU VAL ILE ILE PRO ARG ASP PRO GLN SER
SEQRES 7 C 195 GLY GLN PRO THR GLY GLN ARG VAL HIS LYS PRO VAL VAL
SEQRES 8 C 195 ILE THR LYS VAL PHE ASP LYS ALA SER PRO LEU LEU LEU
SEQRES 9 C 195 ALA ALA LEU THR SER GLY GLU ARG LEU THR LYS VAL GLU
SEQRES 10 C 195 ILE GLN TRP TYR ARG THR SER ALA ALA GLY THR GLN GLU
SEQRES 11 C 195 HIS TYR TYR THR THR VAL LEU GLU ASP ALA ILE ILE VAL
SEQRES 12 C 195 ASP ILE LYS ASP TYR MSE HIS ASN CYS GLN ASP PRO GLY
SEQRES 13 C 195 ASN ALA HIS PHE THR HIS LEU GLU ASP VAL HIS PHE THR
SEQRES 14 C 195 TYR ARG LYS ILE THR TRP THR HIS GLU VAL SER GLY THR
SEQRES 15 C 195 SER GLY SER ASP ASP TRP ARG SER PRO VAL ALA GLY SER
SEQRES 1 D 195 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 195 ARG GLU ASN LEU TYR PHE GLN GLY HIS MSE ALA THR PRO
SEQRES 3 D 195 ALA TYR MSE SER ILE THR GLY THR LYS GLN GLY LEU ILE
SEQRES 4 D 195 THR ALA GLY ALA PHE THR GLU ASP SER VAL GLY ASN THR
SEQRES 5 D 195 TYR GLN GLU GLY HIS GLU ASP GLN VAL MSE VAL GLN GLY
SEQRES 6 D 195 PHE ASN HIS GLU VAL ILE ILE PRO ARG ASP PRO GLN SER
SEQRES 7 D 195 GLY GLN PRO THR GLY GLN ARG VAL HIS LYS PRO VAL VAL
SEQRES 8 D 195 ILE THR LYS VAL PHE ASP LYS ALA SER PRO LEU LEU LEU
SEQRES 9 D 195 ALA ALA LEU THR SER GLY GLU ARG LEU THR LYS VAL GLU
SEQRES 10 D 195 ILE GLN TRP TYR ARG THR SER ALA ALA GLY THR GLN GLU
SEQRES 11 D 195 HIS TYR TYR THR THR VAL LEU GLU ASP ALA ILE ILE VAL
SEQRES 12 D 195 ASP ILE LYS ASP TYR MSE HIS ASN CYS GLN ASP PRO GLY
SEQRES 13 D 195 ASN ALA HIS PHE THR HIS LEU GLU ASP VAL HIS PHE THR
SEQRES 14 D 195 TYR ARG LYS ILE THR TRP THR HIS GLU VAL SER GLY THR
SEQRES 15 D 195 SER GLY SER ASP ASP TRP ARG SER PRO VAL ALA GLY SER
SEQRES 1 E 195 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 195 ARG GLU ASN LEU TYR PHE GLN GLY HIS MSE ALA THR PRO
SEQRES 3 E 195 ALA TYR MSE SER ILE THR GLY THR LYS GLN GLY LEU ILE
SEQRES 4 E 195 THR ALA GLY ALA PHE THR GLU ASP SER VAL GLY ASN THR
SEQRES 5 E 195 TYR GLN GLU GLY HIS GLU ASP GLN VAL MSE VAL GLN GLY
SEQRES 6 E 195 PHE ASN HIS GLU VAL ILE ILE PRO ARG ASP PRO GLN SER
SEQRES 7 E 195 GLY GLN PRO THR GLY GLN ARG VAL HIS LYS PRO VAL VAL
SEQRES 8 E 195 ILE THR LYS VAL PHE ASP LYS ALA SER PRO LEU LEU LEU
SEQRES 9 E 195 ALA ALA LEU THR SER GLY GLU ARG LEU THR LYS VAL GLU
SEQRES 10 E 195 ILE GLN TRP TYR ARG THR SER ALA ALA GLY THR GLN GLU
SEQRES 11 E 195 HIS TYR TYR THR THR VAL LEU GLU ASP ALA ILE ILE VAL
SEQRES 12 E 195 ASP ILE LYS ASP TYR MSE HIS ASN CYS GLN ASP PRO GLY
SEQRES 13 E 195 ASN ALA HIS PHE THR HIS LEU GLU ASP VAL HIS PHE THR
SEQRES 14 E 195 TYR ARG LYS ILE THR TRP THR HIS GLU VAL SER GLY THR
SEQRES 15 E 195 SER GLY SER ASP ASP TRP ARG SER PRO VAL ALA GLY SER
SEQRES 1 F 195 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 195 ARG GLU ASN LEU TYR PHE GLN GLY HIS MSE ALA THR PRO
SEQRES 3 F 195 ALA TYR MSE SER ILE THR GLY THR LYS GLN GLY LEU ILE
SEQRES 4 F 195 THR ALA GLY ALA PHE THR GLU ASP SER VAL GLY ASN THR
SEQRES 5 F 195 TYR GLN GLU GLY HIS GLU ASP GLN VAL MSE VAL GLN GLY
SEQRES 6 F 195 PHE ASN HIS GLU VAL ILE ILE PRO ARG ASP PRO GLN SER
SEQRES 7 F 195 GLY GLN PRO THR GLY GLN ARG VAL HIS LYS PRO VAL VAL
SEQRES 8 F 195 ILE THR LYS VAL PHE ASP LYS ALA SER PRO LEU LEU LEU
SEQRES 9 F 195 ALA ALA LEU THR SER GLY GLU ARG LEU THR LYS VAL GLU
SEQRES 10 F 195 ILE GLN TRP TYR ARG THR SER ALA ALA GLY THR GLN GLU
SEQRES 11 F 195 HIS TYR TYR THR THR VAL LEU GLU ASP ALA ILE ILE VAL
SEQRES 12 F 195 ASP ILE LYS ASP TYR MSE HIS ASN CYS GLN ASP PRO GLY
SEQRES 13 F 195 ASN ALA HIS PHE THR HIS LEU GLU ASP VAL HIS PHE THR
SEQRES 14 F 195 TYR ARG LYS ILE THR TRP THR HIS GLU VAL SER GLY THR
SEQRES 15 F 195 SER GLY SER ASP ASP TRP ARG SER PRO VAL ALA GLY SER
MODRES 3HE1 MSE A 7 MET SELENOMETHIONINE
MODRES 3HE1 MSE A 40 MET SELENOMETHIONINE
MODRES 3HE1 MSE A 127 MET SELENOMETHIONINE
MODRES 3HE1 MSE B 7 MET SELENOMETHIONINE
MODRES 3HE1 MSE B 40 MET SELENOMETHIONINE
MODRES 3HE1 MSE B 127 MET SELENOMETHIONINE
MODRES 3HE1 MSE C 7 MET SELENOMETHIONINE
MODRES 3HE1 MSE C 40 MET SELENOMETHIONINE
MODRES 3HE1 MSE C 127 MET SELENOMETHIONINE
MODRES 3HE1 MSE D 7 MET SELENOMETHIONINE
MODRES 3HE1 MSE D 40 MET SELENOMETHIONINE
MODRES 3HE1 MSE D 127 MET SELENOMETHIONINE
MODRES 3HE1 MSE E 7 MET SELENOMETHIONINE
MODRES 3HE1 MSE E 40 MET SELENOMETHIONINE
MODRES 3HE1 MSE E 127 MET SELENOMETHIONINE
MODRES 3HE1 MSE F 7 MET SELENOMETHIONINE
MODRES 3HE1 MSE F 40 MET SELENOMETHIONINE
MODRES 3HE1 MSE F 127 MET SELENOMETHIONINE
HET MSE A 7 8
HET MSE A 40 8
HET MSE A 127 8
HET MSE B 7 8
HET MSE B 40 8
HET MSE B 127 8
HET MSE C 7 8
HET MSE C 40 8
HET MSE C 127 8
HET MSE D 7 8
HET MSE D 40 8
HET MSE D 127 8
HET MSE E 7 8
HET MSE E 40 8
HET MSE E 127 8
HET MSE F 7 8
HET MSE F 40 8
HET MSE F 127 8
HET GOL C 301 6
HET GOL F 302 6
HETNAM MSE SELENOMETHIONINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 18(C5 H11 N O2 SE)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 9 HOH *728(H2 O)
HELIX 1 1 THR A 23 GLY A 28 1 6
HELIX 2 2 ASN A 29 TYR A 31 5 3
HELIX 3 3 ALA A 77 GLY A 88 1 12
HELIX 4 4 THR B 23 GLY B 28 1 6
HELIX 5 5 ASN B 29 TYR B 31 5 3
HELIX 6 6 LYS B 76 GLY B 88 1 13
HELIX 7 7 THR C 23 GLY C 28 1 6
HELIX 8 8 ASN C 29 TYR C 31 5 3
HELIX 9 9 ALA C 77 GLY C 88 1 12
HELIX 10 10 THR D 23 GLY D 28 1 6
HELIX 11 11 ASN D 29 TYR D 31 5 3
HELIX 12 12 ALA D 77 GLY D 88 1 12
HELIX 13 13 THR E 23 GLY E 28 1 6
HELIX 14 14 ASN E 29 TYR E 31 5 3
HELIX 15 15 ALA E 77 GLY E 88 1 12
HELIX 16 16 THR F 23 GLY F 28 1 6
HELIX 17 17 ASN F 29 TYR F 31 5 3
HELIX 18 18 LYS F 76 GLY F 88 1 13
SHEET 1 A 3 VAL A 39 VAL A 41 0
SHEET 2 A 3 ALA A 5 GLY A 11 -1 N ALA A 5 O VAL A 41
SHEET 3 A 3 GLY A 15 LEU A 16 -1 O GLY A 15 N GLY A 11
SHEET 1 B 6 VAL A 39 VAL A 41 0
SHEET 2 B 6 ALA A 5 GLY A 11 -1 N ALA A 5 O VAL A 41
SHEET 3 B 6 ARG A 90 THR A 101 -1 O GLN A 97 N TYR A 6
SHEET 4 B 6 GLN A 107 MSE A 127 -1 O ALA A 118 N LEU A 91
SHEET 5 B 6 LYS A 150 HIS A 155 -1 O THR A 154 N THR A 112
SHEET 6 B 6 SER A 161 ASP A 165 -1 O GLY A 162 N TRP A 153
SHEET 1 C 7 VAL A 39 VAL A 41 0
SHEET 2 C 7 ALA A 5 GLY A 11 -1 N ALA A 5 O VAL A 41
SHEET 3 C 7 ARG A 90 THR A 101 -1 O GLN A 97 N TYR A 6
SHEET 4 C 7 GLN A 107 MSE A 127 -1 O ALA A 118 N LEU A 91
SHEET 5 C 7 HIS A 140 THR A 147 -1 O HIS A 145 N VAL A 121
SHEET 6 C 7 VAL A 68 VAL A 73 -1 N VAL A 68 O PHE A 146
SHEET 7 C 7 GLY A 43 ASN A 45 -1 N ASN A 45 O VAL A 69
SHEET 1 D 6 VAL A 39 VAL A 41 0
SHEET 2 D 6 ALA A 5 GLY A 11 -1 N ALA A 5 O VAL A 41
SHEET 3 D 6 ARG A 90 THR A 101 -1 O GLN A 97 N TYR A 6
SHEET 4 D 6 GLN A 107 MSE A 127 -1 O ALA A 118 N LEU A 91
SHEET 5 D 6 GLY B 43 ILE B 49 -1 O HIS B 46 N ASP A 125
SHEET 6 D 6 VAL B 64 HIS B 65 -1 O VAL B 64 N ILE B 49
SHEET 1 E10 VAL A 39 VAL A 41 0
SHEET 2 E10 ALA A 5 GLY A 11 -1 N ALA A 5 O VAL A 41
SHEET 3 E10 ARG A 90 THR A 101 -1 O GLN A 97 N TYR A 6
SHEET 4 E10 GLN A 107 MSE A 127 -1 O ALA A 118 N LEU A 91
SHEET 5 E10 GLY B 43 ILE B 49 -1 O HIS B 46 N ASP A 125
SHEET 6 E10 VAL B 68 VAL B 73 -1 O VAL B 69 N ASN B 45
SHEET 7 E10 LEU B 141 THR B 147 -1 O VAL B 144 N ILE B 70
SHEET 8 E10 GLN B 107 TYR B 126 -1 N ILE B 119 O THR B 147
SHEET 9 E10 LYS B 150 HIS B 155 -1 O LYS B 150 N GLU B 116
SHEET 10 E10 THR B 160 ASP B 165 -1 O THR B 160 N HIS B 155
SHEET 1 F11 VAL A 39 VAL A 41 0
SHEET 2 F11 ALA A 5 GLY A 11 -1 N ALA A 5 O VAL A 41
SHEET 3 F11 ARG A 90 THR A 101 -1 O GLN A 97 N TYR A 6
SHEET 4 F11 GLN A 107 MSE A 127 -1 O ALA A 118 N LEU A 91
SHEET 5 F11 GLY B 43 ILE B 49 -1 O HIS B 46 N ASP A 125
SHEET 6 F11 VAL B 68 VAL B 73 -1 O VAL B 69 N ASN B 45
SHEET 7 F11 LEU B 141 THR B 147 -1 O VAL B 144 N ILE B 70
SHEET 8 F11 GLN B 107 TYR B 126 -1 N ILE B 119 O THR B 147
SHEET 9 F11 LEU B 91 THR B 101 -1 N VAL B 94 O LEU B 115
SHEET 10 F11 ALA B 5 GLY B 11 -1 N SER B 8 O GLU B 95
SHEET 11 F11 GLY B 15 LEU B 16 -1 O GLY B 15 N GLY B 11
SHEET 1 G11 VAL A 39 VAL A 41 0
SHEET 2 G11 ALA A 5 GLY A 11 -1 N ALA A 5 O VAL A 41
SHEET 3 G11 ARG A 90 THR A 101 -1 O GLN A 97 N TYR A 6
SHEET 4 G11 GLN A 107 MSE A 127 -1 O ALA A 118 N LEU A 91
SHEET 5 G11 GLY B 43 ILE B 49 -1 O HIS B 46 N ASP A 125
SHEET 6 G11 VAL B 68 VAL B 73 -1 O VAL B 69 N ASN B 45
SHEET 7 G11 LEU B 141 THR B 147 -1 O VAL B 144 N ILE B 70
SHEET 8 G11 GLN B 107 TYR B 126 -1 N ILE B 119 O THR B 147
SHEET 9 G11 LEU B 91 THR B 101 -1 N VAL B 94 O LEU B 115
SHEET 10 G11 ALA B 5 GLY B 11 -1 N SER B 8 O GLU B 95
SHEET 11 G11 VAL B 39 VAL B 41 -1 O VAL B 41 N ALA B 5
SHEET 1 H 2 VAL A 48 ILE A 49 0
SHEET 2 H 2 VAL A 64 HIS A 65 -1 O VAL A 64 N ILE A 49
SHEET 1 I 3 GLY C 15 LEU C 16 0
SHEET 2 I 3 ALA C 5 GLY C 11 -1 N GLY C 11 O GLY C 15
SHEET 3 I 3 VAL C 39 VAL C 41 -1 O VAL C 41 N ALA C 5
SHEET 1 J 6 GLY C 15 LEU C 16 0
SHEET 2 J 6 ALA C 5 GLY C 11 -1 N GLY C 11 O GLY C 15
SHEET 3 J 6 ARG C 90 THR C 101 -1 O GLN C 97 N TYR C 6
SHEET 4 J 6 GLN C 107 MSE C 127 -1 O ALA C 118 N LEU C 91
SHEET 5 J 6 LYS C 150 HIS C 155 -1 O THR C 154 N THR C 112
SHEET 6 J 6 SER C 161 ASP C 165 -1 O GLY C 162 N TRP C 153
SHEET 1 K 8 GLY C 15 LEU C 16 0
SHEET 2 K 8 ALA C 5 GLY C 11 -1 N GLY C 11 O GLY C 15
SHEET 3 K 8 ARG C 90 THR C 101 -1 O GLN C 97 N TYR C 6
SHEET 4 K 8 GLN C 107 MSE C 127 -1 O ALA C 118 N LEU C 91
SHEET 5 K 8 HIS C 140 THR C 147 -1 O HIS C 145 N VAL C 121
SHEET 6 K 8 VAL C 68 VAL C 73 -1 N VAL C 68 O PHE C 146
SHEET 7 K 8 GLY C 43 ILE C 49 -1 N ASN C 45 O VAL C 69
SHEET 8 K 8 VAL C 64 HIS C 65 -1 O VAL C 64 N ILE C 49
SHEET 1 L10 GLY C 15 LEU C 16 0
SHEET 2 L10 ALA C 5 GLY C 11 -1 N GLY C 11 O GLY C 15
SHEET 3 L10 ARG C 90 THR C 101 -1 O GLN C 97 N TYR C 6
SHEET 4 L10 GLN C 107 MSE C 127 -1 O ALA C 118 N LEU C 91
SHEET 5 L10 HIS C 140 THR C 147 -1 O HIS C 145 N VAL C 121
SHEET 6 L10 VAL C 68 VAL C 73 -1 N VAL C 68 O PHE C 146
SHEET 7 L10 GLY C 43 ILE C 49 -1 N ASN C 45 O VAL C 69
SHEET 8 L10 GLN D 107 TYR D 126 -1 O ASP D 125 N HIS C 46
SHEET 9 L10 LYS D 150 HIS D 155 -1 O LYS D 150 N GLU D 116
SHEET 10 L10 THR D 160 ASP D 165 -1 O THR D 160 N HIS D 155
SHEET 1 M11 GLY C 15 LEU C 16 0
SHEET 2 M11 ALA C 5 GLY C 11 -1 N GLY C 11 O GLY C 15
SHEET 3 M11 ARG C 90 THR C 101 -1 O GLN C 97 N TYR C 6
SHEET 4 M11 GLN C 107 MSE C 127 -1 O ALA C 118 N LEU C 91
SHEET 5 M11 HIS C 140 THR C 147 -1 O HIS C 145 N VAL C 121
SHEET 6 M11 VAL C 68 VAL C 73 -1 N VAL C 68 O PHE C 146
SHEET 7 M11 GLY C 43 ILE C 49 -1 N ASN C 45 O VAL C 69
SHEET 8 M11 GLN D 107 TYR D 126 -1 O ASP D 125 N HIS C 46
SHEET 9 M11 LEU D 141 THR D 147 -1 O THR D 147 N ILE D 119
SHEET 10 M11 VAL D 68 VAL D 73 -1 N LYS D 72 O GLU D 142
SHEET 11 M11 GLY D 43 ASN D 45 -1 N ASN D 45 O VAL D 69
SHEET 1 N11 GLY C 15 LEU C 16 0
SHEET 2 N11 ALA C 5 GLY C 11 -1 N GLY C 11 O GLY C 15
SHEET 3 N11 ARG C 90 THR C 101 -1 O GLN C 97 N TYR C 6
SHEET 4 N11 GLN C 107 MSE C 127 -1 O ALA C 118 N LEU C 91
SHEET 5 N11 HIS C 140 THR C 147 -1 O HIS C 145 N VAL C 121
SHEET 6 N11 VAL C 68 VAL C 73 -1 N VAL C 68 O PHE C 146
SHEET 7 N11 GLY C 43 ILE C 49 -1 N ASN C 45 O VAL C 69
SHEET 8 N11 GLN D 107 TYR D 126 -1 O ASP D 125 N HIS C 46
SHEET 9 N11 LEU D 91 THR D 101 -1 N LEU D 91 O ALA D 118
SHEET 10 N11 ALA D 5 GLY D 11 -1 N SER D 8 O GLU D 95
SHEET 11 N11 GLY D 15 LEU D 16 -1 O GLY D 15 N GLY D 11
SHEET 1 O11 GLY C 15 LEU C 16 0
SHEET 2 O11 ALA C 5 GLY C 11 -1 N GLY C 11 O GLY C 15
SHEET 3 O11 ARG C 90 THR C 101 -1 O GLN C 97 N TYR C 6
SHEET 4 O11 GLN C 107 MSE C 127 -1 O ALA C 118 N LEU C 91
SHEET 5 O11 HIS C 140 THR C 147 -1 O HIS C 145 N VAL C 121
SHEET 6 O11 VAL C 68 VAL C 73 -1 N VAL C 68 O PHE C 146
SHEET 7 O11 GLY C 43 ILE C 49 -1 N ASN C 45 O VAL C 69
SHEET 8 O11 GLN D 107 TYR D 126 -1 O ASP D 125 N HIS C 46
SHEET 9 O11 LEU D 91 THR D 101 -1 N LEU D 91 O ALA D 118
SHEET 10 O11 ALA D 5 GLY D 11 -1 N SER D 8 O GLU D 95
SHEET 11 O11 VAL D 39 MSE D 40 -1 O VAL D 39 N MSE D 7
SHEET 1 P 2 VAL D 48 ILE D 49 0
SHEET 2 P 2 VAL D 64 HIS D 65 -1 O VAL D 64 N ILE D 49
SHEET 1 Q 3 VAL E 39 VAL E 41 0
SHEET 2 Q 3 ALA E 5 GLY E 11 -1 N ALA E 5 O VAL E 41
SHEET 3 Q 3 GLY E 15 LEU E 16 -1 O GLY E 15 N GLY E 11
SHEET 1 R 6 VAL E 39 VAL E 41 0
SHEET 2 R 6 ALA E 5 GLY E 11 -1 N ALA E 5 O VAL E 41
SHEET 3 R 6 LEU E 91 THR E 101 -1 O GLN E 97 N TYR E 6
SHEET 4 R 6 GLN E 107 MSE E 127 -1 O LEU E 115 N VAL E 94
SHEET 5 R 6 LYS E 150 HIS E 155 -1 O THR E 154 N THR E 112
SHEET 6 R 6 SER E 161 ASP E 165 -1 O GLY E 162 N TRP E 153
SHEET 1 S 7 VAL E 39 VAL E 41 0
SHEET 2 S 7 ALA E 5 GLY E 11 -1 N ALA E 5 O VAL E 41
SHEET 3 S 7 LEU E 91 THR E 101 -1 O GLN E 97 N TYR E 6
SHEET 4 S 7 GLN E 107 MSE E 127 -1 O LEU E 115 N VAL E 94
SHEET 5 S 7 HIS E 140 THR E 147 -1 O HIS E 145 N VAL E 121
SHEET 6 S 7 VAL E 68 VAL E 73 -1 N LYS E 72 O GLU E 142
SHEET 7 S 7 GLY E 43 ASN E 45 -1 N ASN E 45 O VAL E 69
SHEET 1 T 6 VAL E 39 VAL E 41 0
SHEET 2 T 6 ALA E 5 GLY E 11 -1 N ALA E 5 O VAL E 41
SHEET 3 T 6 LEU E 91 THR E 101 -1 O GLN E 97 N TYR E 6
SHEET 4 T 6 GLN E 107 MSE E 127 -1 O LEU E 115 N VAL E 94
SHEET 5 T 6 GLY F 43 ILE F 49 -1 O VAL F 48 N ILE E 123
SHEET 6 T 6 VAL F 64 HIS F 65 -1 O VAL F 64 N ILE F 49
SHEET 1 U10 VAL E 39 VAL E 41 0
SHEET 2 U10 ALA E 5 GLY E 11 -1 N ALA E 5 O VAL E 41
SHEET 3 U10 LEU E 91 THR E 101 -1 O GLN E 97 N TYR E 6
SHEET 4 U10 GLN E 107 MSE E 127 -1 O LEU E 115 N VAL E 94
SHEET 5 U10 GLY F 43 ILE F 49 -1 O VAL F 48 N ILE E 123
SHEET 6 U10 VAL F 68 VAL F 73 -1 O VAL F 69 N ASN F 45
SHEET 7 U10 LEU F 141 THR F 147 -1 O GLU F 142 N LYS F 72
SHEET 8 U10 GLN F 107 TYR F 126 -1 N ILE F 119 O THR F 147
SHEET 9 U10 LYS F 150 HIS F 155 -1 O LYS F 150 N GLU F 116
SHEET 10 U10 THR F 160 ASP F 165 -1 O THR F 160 N HIS F 155
SHEET 1 V11 VAL E 39 VAL E 41 0
SHEET 2 V11 ALA E 5 GLY E 11 -1 N ALA E 5 O VAL E 41
SHEET 3 V11 LEU E 91 THR E 101 -1 O GLN E 97 N TYR E 6
SHEET 4 V11 GLN E 107 MSE E 127 -1 O LEU E 115 N VAL E 94
SHEET 5 V11 GLY F 43 ILE F 49 -1 O VAL F 48 N ILE E 123
SHEET 6 V11 VAL F 68 VAL F 73 -1 O VAL F 69 N ASN F 45
SHEET 7 V11 LEU F 141 THR F 147 -1 O GLU F 142 N LYS F 72
SHEET 8 V11 GLN F 107 TYR F 126 -1 N ILE F 119 O THR F 147
SHEET 9 V11 LEU F 91 THR F 101 -1 N VAL F 94 O LEU F 115
SHEET 10 V11 ALA F 5 GLY F 11 -1 N SER F 8 O GLU F 95
SHEET 11 V11 GLY F 15 LEU F 16 -1 O GLY F 15 N GLY F 11
SHEET 1 W11 VAL E 39 VAL E 41 0
SHEET 2 W11 ALA E 5 GLY E 11 -1 N ALA E 5 O VAL E 41
SHEET 3 W11 LEU E 91 THR E 101 -1 O GLN E 97 N TYR E 6
SHEET 4 W11 GLN E 107 MSE E 127 -1 O LEU E 115 N VAL E 94
SHEET 5 W11 GLY F 43 ILE F 49 -1 O VAL F 48 N ILE E 123
SHEET 6 W11 VAL F 68 VAL F 73 -1 O VAL F 69 N ASN F 45
SHEET 7 W11 LEU F 141 THR F 147 -1 O GLU F 142 N LYS F 72
SHEET 8 W11 GLN F 107 TYR F 126 -1 N ILE F 119 O THR F 147
SHEET 9 W11 LEU F 91 THR F 101 -1 N VAL F 94 O LEU F 115
SHEET 10 W11 ALA F 5 GLY F 11 -1 N SER F 8 O GLU F 95
SHEET 11 W11 VAL F 39 VAL F 41 -1 O VAL F 41 N ALA F 5
SHEET 1 X 2 VAL E 48 ILE E 49 0
SHEET 2 X 2 VAL E 64 HIS E 65 -1 O VAL E 64 N ILE E 49
LINK C TYR A 6 N MSE A 7 1555 1555 1.32
LINK C MSE A 7 N SER A 8 1555 1555 1.32
LINK C VAL A 39 N MSE A 40 1555 1555 1.33
LINK C MSE A 40 N VAL A 41 1555 1555 1.33
LINK C TYR A 126 N MSE A 127 1555 1555 1.34
LINK C MSE A 127 N HIS A 128 1555 1555 1.33
LINK C TYR B 6 N MSE B 7 1555 1555 1.33
LINK C MSE B 7 N SER B 8 1555 1555 1.32
LINK C VAL B 39 N MSE B 40 1555 1555 1.33
LINK C MSE B 40 N VAL B 41 1555 1555 1.33
LINK C TYR B 126 N MSE B 127 1555 1555 1.33
LINK C TYR C 6 N MSE C 7 1555 1555 1.32
LINK C MSE C 7 N SER C 8 1555 1555 1.32
LINK C VAL C 39 N MSE C 40 1555 1555 1.33
LINK C MSE C 40 N VAL C 41 1555 1555 1.33
LINK C TYR C 126 N MSE C 127 1555 1555 1.33
LINK C MSE C 127 N HIS C 128 1555 1555 1.33
LINK C TYR D 6 N MSE D 7 1555 1555 1.33
LINK C MSE D 7 N SER D 8 1555 1555 1.32
LINK C VAL D 39 N MSE D 40 1555 1555 1.33
LINK C MSE D 40 N VAL D 41 1555 1555 1.33
LINK C TYR D 126 N MSE D 127 1555 1555 1.33
LINK C TYR E 6 N MSE E 7 1555 1555 1.33
LINK C MSE E 7 N SER E 8 1555 1555 1.32
LINK C VAL E 39 N MSE E 40 1555 1555 1.33
LINK C MSE E 40 N VAL E 41 1555 1555 1.33
LINK C TYR E 126 N MSE E 127 1555 1555 1.33
LINK C MSE E 127 N HIS E 128 1555 1555 1.33
LINK C TYR F 6 N MSE F 7 1555 1555 1.33
LINK C MSE F 7 N SER F 8 1555 1555 1.32
LINK C VAL F 39 N MSE F 40 1555 1555 1.33
LINK C MSE F 40 N VAL F 41 1555 1555 1.33
LINK C TYR F 126 N MSE F 127 1555 1555 1.33
SITE 1 AC1 4 THR C 160 SER C 161 HOH C 305 HOH C 612
SITE 1 AC2 3 ARG F 63 ASP F 164 ASP F 165
CRYST1 141.219 141.219 105.052 90.00 90.00 120.00 P 3 1 2 36
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 0.007081 0.004088 0.000000 0.00000
SCALE2 0.000000 0.008177 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009519 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
