HEADER LIPID BINDING PROTEIN 02-OCT-12 4HDE
TITLE THE CRYSTAL STRUCTURE OF A SCO1/SENC FAMILY LIPOPROTEIN FROM BACILLUS
TITLE 2 ANTHRACIS STR. AMES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SCO1/SENC FAMILY LIPOPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 29-195;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;
SOURCE 3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;
SOURCE 4 ORGANISM_TAXID: 1392;
SOURCE 5 STRAIN: AMES;
SOURCE 6 GENE: BAS2093, BA_2249, GBAA_2249;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MAGIC;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, THE CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS 2 DISEASES, CSGID, NIAID, NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS
KEYWDS 3 DISEASES, LIPID BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,M.ZHOU,K.KWON,W.F.ANDERSON,A.JOACHIMIAK,CENTER FOR STRUCTURAL
AUTHOR 2 GENOMICS OF INFECTIOUS DISEASES (CSGID)
REVDAT 1 24-OCT-12 4HDE 0
JRNL AUTH K.TAN,M.ZHOU,K.KWON,W.F.ANDERSON,A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF A SCO1/SENC FAMILY LIPOPROTEIN FROM
JRNL TITL 2 BACILLUS ANTHRACIS STR. AMES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.32 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.32
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 35718
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1791
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 22.5634 - 3.0947 0.94 2677 144 0.1427 0.1467
REMARK 3 2 3.0947 - 2.4573 0.97 2596 159 0.1648 0.2068
REMARK 3 3 2.4573 - 2.1470 0.98 2629 139 0.1625 0.1913
REMARK 3 4 2.1470 - 1.9508 0.99 2627 128 0.1626 0.1878
REMARK 3 5 1.9508 - 1.8111 0.99 2596 158 0.1633 0.1960
REMARK 3 6 1.8111 - 1.7043 0.99 2630 149 0.1575 0.1824
REMARK 3 7 1.7043 - 1.6190 1.00 2619 139 0.1590 0.1939
REMARK 3 8 1.6190 - 1.5485 0.99 2649 123 0.1663 0.1946
REMARK 3 9 1.5485 - 1.4889 1.00 2641 115 0.1755 0.2046
REMARK 3 10 1.4889 - 1.4376 1.00 2647 132 0.1920 0.2346
REMARK 3 11 1.4376 - 1.3926 1.00 2575 125 0.2096 0.2269
REMARK 3 12 1.3926 - 1.3528 1.00 2618 149 0.2280 0.2276
REMARK 3 13 1.3528 - 1.3172 0.93 2423 131 0.2512 0.2704
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 36.77
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.380
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) : 2.51970
REMARK 3 B22 (A**2) : -2.90940
REMARK 3 B33 (A**2) : 0.38970
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 : 0.006 1423
REMARK 3 ANGLE : 1.042 1930
REMARK 3 CHIRALITY : 0.075 211
REMARK 3 PLANARITY : 0.006 250
REMARK 3 DIHEDRAL : 11.799 548
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resseq 28:55)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8879 25.3580 -18.8147
REMARK 3 T TENSOR
REMARK 3 T11: 0.0620 T22: 0.0728
REMARK 3 T33: 0.0669 T12: 0.0210
REMARK 3 T13: 0.0017 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 3.6442 L22: 2.2887
REMARK 3 L33: 1.8292 L12: 1.9794
REMARK 3 L13: -1.1531 L23: -0.7712
REMARK 3 S TENSOR
REMARK 3 S11: -0.0626 S12: -0.0016 S13: -0.0957
REMARK 3 S21: -0.0274 S22: 0.0266 S23: 0.0056
REMARK 3 S31: 0.0157 S32: -0.0545 S33: 0.0528
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 56:100)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6121 24.9109 -8.0228
REMARK 3 T TENSOR
REMARK 3 T11: 0.0877 T22: 0.1294
REMARK 3 T33: 0.1057 T12: -0.0016
REMARK 3 T13: 0.0141 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 1.1227 L22: 2.3491
REMARK 3 L33: 1.7921 L12: 0.0639
REMARK 3 L13: 0.4250 L23: -0.0999
REMARK 3 S TENSOR
REMARK 3 S11: -0.0341 S12: -0.0291 S13: 0.0448
REMARK 3 S21: 0.1710 S22: 0.0056 S23: -0.0218
REMARK 3 S31: -0.0415 S32: 0.0095 S33: 0.0229
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resseq 101:165)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.4560 34.8519 -10.9488
REMARK 3 T TENSOR
REMARK 3 T11: 0.1204 T22: 0.1216
REMARK 3 T33: 0.0800 T12: -0.0016
REMARK 3 T13: 0.0019 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.1332 L22: 1.7623
REMARK 3 L33: 0.7884 L12: 0.0805
REMARK 3 L13: -0.0509 L23: 0.1860
REMARK 3 S TENSOR
REMARK 3 S11: -0.0011 S12: 0.0221 S13: 0.1252
REMARK 3 S21: 0.0355 S22: 0.0051 S23: 0.0396
REMARK 3 S31: -0.1157 S32: -0.0229 S33: 0.0023
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resseq 166:195)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4781 16.0233 -7.6433
REMARK 3 T TENSOR
REMARK 3 T11: 0.1153 T22: 0.1333
REMARK 3 T33: 0.1365 T12: -0.0154
REMARK 3 T13: 0.0236 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 2.4496 L22: 2.0906
REMARK 3 L33: 5.2730 L12: 0.4252
REMARK 3 L13: 1.5112 L23: 0.4956
REMARK 3 S TENSOR
REMARK 3 S11: 0.0333 S12: -0.0714 S13: -0.1040
REMARK 3 S21: 0.0524 S22: -0.0126 S23: -0.0733
REMARK 3 S31: 0.1504 S32: -0.0924 S33: -0.0067
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 4HDE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-12.
REMARK 100 THE RCSB ID CODE IS RCSB075325.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 0.97937
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35792
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.317
REMARK 200 RESOLUTION RANGE LOW (A) : 23.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.10500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.32
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.65300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD/MLPHARE/DM/ARP/WARP/HKL3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M MAGNESSIUM CHLORIDE, 0.1M HEPES:
REMARK 280 NAOH, 30%(W/V)PEG MME550, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 17.49250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.27550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.23400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.27550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.49250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.23400
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 300 REMARK: THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN
REMARK 300 IS EXPERIMENTALLY UNKNOWN. IT IS PREDICTED TO BE A MONOMER.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 26
REMARK 465 ASN A 27
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 PHE A 42 -164.03 -113.65
REMARK 500 THR A 71 -93.10 -125.32
REMARK 500 THR A 129 -163.93 -164.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP05583 RELATED DB: TARGETTRACK
DBREF 4HDE A 29 195 UNP Q81R11 Q81R11_BACAN 29 195
SEQADV 4HDE SER A 26 UNP Q81R11 EXPRESSION TAG
SEQADV 4HDE ASN A 27 UNP Q81R11 EXPRESSION TAG
SEQADV 4HDE ALA A 28 UNP Q81R11 EXPRESSION TAG
SEQRES 1 A 170 SER ASN ALA LEU ARG LYS PRO LEU ASN TRP ASP LEU GLU
SEQRES 2 A 170 THR PHE GLN PHE THR ASN GLN ASP GLY LYS PRO PHE GLY
SEQRES 3 A 170 THR LYS ASP LEU LYS GLY LYS VAL TRP VAL ALA ASP PHE
SEQRES 4 A 170 MSE PHE THR ASN CYS GLN THR VAL CYS PRO PRO MSE THR
SEQRES 5 A 170 ALA ASN MSE ALA LYS LEU GLN LYS MSE ALA LYS GLU GLU
SEQRES 6 A 170 LYS LEU ASP VAL GLN PHE VAL SER PHE SER VAL ASP PRO
SEQRES 7 A 170 ASP LEU ASP LYS PRO GLU ASN LEU LYS ALA PHE ILE GLN
SEQRES 8 A 170 LYS PHE THR GLU ASP THR SER ASN TRP ASN LEU LEU THR
SEQRES 9 A 170 GLY TYR SER LEU GLU ASP ILE THR LYS PHE SER LYS ASP
SEQRES 10 A 170 ASN PHE GLN SER LEU VAL ASP LYS PRO GLU ASN GLY GLN
SEQRES 11 A 170 VAL ILE HIS GLY THR SER PHE TYR LEU ILE ASP GLN ASN
SEQRES 12 A 170 GLY LYS VAL MSE LYS LYS TYR SER GLY ILE SER ASN THR
SEQRES 13 A 170 PRO TYR GLU ASP ILE ILE ARG ASP MSE LYS ARG LEU ALA
SEQRES 14 A 170 GLU
MODRES 4HDE MSE A 65 MET SELENOMETHIONINE
MODRES 4HDE MSE A 76 MET SELENOMETHIONINE
MODRES 4HDE MSE A 80 MET SELENOMETHIONINE
MODRES 4HDE MSE A 86 MET SELENOMETHIONINE
MODRES 4HDE MSE A 172 MET SELENOMETHIONINE
MODRES 4HDE MSE A 190 MET SELENOMETHIONINE
HET MSE A 65 13
HET MSE A 76 8
HET MSE A 80 8
HET MSE A 86 8
HET MSE A 172 8
HET MSE A 190 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 HOH *249(H2 O)
HELIX 1 1 THR A 52 LYS A 56 1 5
HELIX 2 2 VAL A 72 GLU A 90 1 19
HELIX 3 3 LYS A 107 GLN A 116 1 10
HELIX 4 4 SER A 132 GLN A 145 1 14
HELIX 5 5 PRO A 182 GLU A 195 1 14
SHEET 1 A 2 GLN A 41 THR A 43 0
SHEET 2 A 2 PRO A 49 GLY A 51 -1 O PHE A 50 N PHE A 42
SHEET 1 B 5 TRP A 125 LEU A 128 0
SHEET 2 B 5 GLN A 95 SER A 100 1 N SER A 98 O LEU A 128
SHEET 3 B 5 TRP A 60 MSE A 65 1 N ASP A 63 O PHE A 99
SHEET 4 B 5 SER A 161 ILE A 165 -1 O ILE A 165 N TRP A 60
SHEET 5 B 5 VAL A 171 SER A 176 -1 O MSE A 172 N LEU A 164
LINK C PHE A 64 N MSE A 65 1555 1555 1.33
LINK C MSE A 65 N PHE A 66 1555 1555 1.33
LINK C PRO A 75 N MSE A 76 1555 1555 1.33
LINK C MSE A 76 N THR A 77 1555 1555 1.33
LINK C ASN A 79 N MSE A 80 1555 1555 1.32
LINK C MSE A 80 N ALA A 81 1555 1555 1.33
LINK C LYS A 85 N MSE A 86 1555 1555 1.33
LINK C MSE A 86 N ALA A 87 1555 1555 1.33
LINK C VAL A 171 N MSE A 172 1555 1555 1.33
LINK C MSE A 172 N LYS A 173 1555 1555 1.33
LINK C ASP A 189 N MSE A 190 1555 1555 1.33
LINK C MSE A 190 N LYS A 191 1555 1555 1.33
CRYST1 34.985 48.468 88.551 90.00 90.00 90.00 P 21 21 21 4
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 0.028584 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020632 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011293 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
