HEADER PYRIDOXAL PHOSPHATE BINDING 15-JUL-11 3SY1
TITLE CRYSTAL STRUCTURE OF ENGINEERED PROTEIN. NORTHEAST STRUCTURAL GENOMICS
TITLE 2 CONSORTIUM TARGET OR70
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UPF0001 PROTEIN YGGS;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: YGGS, B2951, JW2918
KEYWDS ENGINEERED PROTEIN, STRUCTURAL GENOMICS, PSI-BIOLOGY, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 3 NESG, PYRIDOXAL PHOSPHATE BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.VOROBIEV,M.SU,L.NIVON,J.SEETHARAMAN,S.SAHDEV,R.XIAO,C.CICCOSANTI,
AUTHOR 2 M.MAGLAQUI,D.BAKER,J.K.EVERETT,R.NAIR,T.B.ACTON,B.ROST,
AUTHOR 3 G.T.MONTELIONE,J.F.HUNT,L.TONG,NORTHEAST STRUCTURAL GENOMICS
AUTHOR 4 CONSORTIUM (NESG)
REVDAT 2 13-SEP-23 3SY1 1 REMARK SEQADV
REVDAT 1 03-AUG-11 3SY1 0
JRNL AUTH S.VOROBIEV,M.SU,L.NIVON,J.SEETHARAMAN,S.SAHDEV,R.XIAO,
JRNL AUTH 2 C.CICCOSANTI,M.MAGLAQUI,D.BAKER,J.K.EVERETT,R.NAIR,
JRNL AUTH 3 T.B.ACTON,B.ROST,G.T.MONTELIONE,J.F.HUNT,L.TONG
JRNL TITL CRYSTAL STRUCTURE OF ENGINEERED PROTEIN. NORTHEAST
JRNL TITL 2 STRUCTURAL GENOMICS CONSORTIUM TARGET OR70
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.47 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 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) : 1.47
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.50
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 46117
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2319
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 34.5110 - 3.7660 0.95 2776 127 0.1820 0.2000
REMARK 3 2 3.7660 - 2.9890 0.80 2174 132 0.1690 0.1970
REMARK 3 3 2.9890 - 2.6120 1.00 2744 137 0.1650 0.1890
REMARK 3 4 2.6120 - 2.3730 1.00 2727 139 0.1590 0.1580
REMARK 3 5 2.3730 - 2.2030 0.68 1830 98 0.1640 0.1730
REMARK 3 6 2.2030 - 2.0730 0.98 2648 140 0.1590 0.1800
REMARK 3 7 2.0730 - 1.9690 0.99 2680 127 0.1580 0.1920
REMARK 3 8 1.9690 - 1.8830 0.94 2519 127 0.2400 0.2810
REMARK 3 9 1.8830 - 1.8110 0.96 2542 151 0.1560 0.1830
REMARK 3 10 1.8110 - 1.7480 1.00 2674 137 0.1230 0.1850
REMARK 3 11 1.7480 - 1.6940 1.00 2665 143 0.1170 0.1710
REMARK 3 12 1.6940 - 1.6450 1.00 2678 140 0.1220 0.1610
REMARK 3 13 1.6450 - 1.6020 1.00 2638 148 0.1220 0.1550
REMARK 3 14 1.6020 - 1.5630 1.00 2692 126 0.1260 0.1840
REMARK 3 15 1.5630 - 1.5280 1.00 2639 149 0.1500 0.1850
REMARK 3 16 1.5280 - 1.4950 1.00 2613 169 0.1770 0.2140
REMARK 3 17 1.4950 - 1.4650 0.96 2559 129 0.2040 0.2300
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 : 0.38
REMARK 3 B_SOL : 42.44
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.030
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.51
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.05800
REMARK 3 B22 (A**2) : 1.10100
REMARK 3 B33 (A**2) : -1.15900
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 1827
REMARK 3 ANGLE : 1.129 2481
REMARK 3 CHIRALITY : 0.074 284
REMARK 3 PLANARITY : 0.004 329
REMARK 3 DIHEDRAL : 12.685 690
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3SY1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066793.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46540
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.460
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.1
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : 0.83300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: PDB ENTRY 1W8G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 0.1 M MANGANESE SULFATE,
REMARK 280 0.1 M SODIUM ACETATE, PH 5.0, MICROBATCH CRYSTALLIZATION UNDER
REMARK 280 OIL, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 26.85750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.61700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.84750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.61700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.85750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.84750
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: MONOMER,29.01 KD,98.5%
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 ARG A 230
REMARK 465 ASP A 231
REMARK 465 TYR A 232
REMARK 465 SER A 233
REMARK 465 LYS A 234
REMARK 465 LYS A 235
REMARK 465 GLY A 236
REMARK 465 SER A 237
REMARK 465 LEU A 238
REMARK 465 GLU A 239
REMARK 465 HIS A 240
REMARK 465 HIS A 241
REMARK 465 HIS A 242
REMARK 465 HIS A 243
REMARK 465 HIS A 244
REMARK 465 HIS A 245
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 38 -3.30 71.01
REMARK 500 SER A 133 11.55 -149.06
REMARK 500 GLN A 205 -156.02 -125.74
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 MES A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1W8G RELATED DB: PDB
REMARK 900 THE TEMPLATE FOR THE ENGINEERED PROTEIN
REMARK 900 RELATED ID: OR70 RELATED DB: TARGETDB
DBREF 3SY1 A 2 235 UNP P67080 YGGS_ECOLI 1 234
SEQADV 3SY1 MET A 1 UNP P67080 EXPRESSION TAG
SEQADV 3SY1 VAL A 33 UNP P67080 LEU 32 ENGINEERED MUTATION
SEQADV 3SY1 SER A 56 UNP P67080 GLY 55 ENGINEERED MUTATION
SEQADV 3SY1 HIS A 58 UNP P67080 ASN 57 ENGINEERED MUTATION
SEQADV 3SY1 ASN A 81 UNP P67080 HIS 80 ENGINEERED MUTATION
SEQADV 3SY1 ALA A 83 UNP P67080 ILE 82 ENGINEERED MUTATION
SEQADV 3SY1 ILE A 102 UNP P67080 HIS 101 ENGINEERED MUTATION
SEQADV 3SY1 SER A 165 UNP P67080 MET 164 ENGINEERED MUTATION
SEQADV 3SY1 ALA A 202 UNP P67080 SER 201 ENGINEERED MUTATION
SEQADV 3SY1 GLN A 205 UNP P67080 MET 204 ENGINEERED MUTATION
SEQADV 3SY1 ALA A 221 UNP P67080 ARG 220 ENGINEERED MUTATION
SEQADV 3SY1 GLY A 236 UNP P67080 EXPRESSION TAG
SEQADV 3SY1 SER A 237 UNP P67080 EXPRESSION TAG
SEQADV 3SY1 LEU A 238 UNP P67080 EXPRESSION TAG
SEQADV 3SY1 GLU A 239 UNP P67080 EXPRESSION TAG
SEQADV 3SY1 HIS A 240 UNP P67080 EXPRESSION TAG
SEQADV 3SY1 HIS A 241 UNP P67080 EXPRESSION TAG
SEQADV 3SY1 HIS A 242 UNP P67080 EXPRESSION TAG
SEQADV 3SY1 HIS A 243 UNP P67080 EXPRESSION TAG
SEQADV 3SY1 HIS A 244 UNP P67080 EXPRESSION TAG
SEQADV 3SY1 HIS A 245 UNP P67080 EXPRESSION TAG
SEQRES 1 A 245 MET MET ASN ASP ILE ALA HIS ASN LEU ALA GLN VAL ARG
SEQRES 2 A 245 ASP LYS ILE SER ALA ALA ALA THR ARG CYS GLY ARG SER
SEQRES 3 A 245 PRO GLU GLU ILE THR LEU VAL ALA VAL SER LYS THR LYS
SEQRES 4 A 245 PRO ALA SER ALA ILE ALA GLU ALA ILE ASP ALA GLY GLN
SEQRES 5 A 245 ARG GLN PHE SER GLU HIS TYR VAL GLN GLU GLY VAL ASP
SEQRES 6 A 245 LYS ILE ARG HIS PHE GLN GLU LEU GLY VAL THR GLY LEU
SEQRES 7 A 245 GLU TRP ASN PHE ALA GLY PRO LEU GLN SER ASN LYS SER
SEQRES 8 A 245 ARG LEU VAL ALA GLU HIS PHE ASP TRP CYS ILE THR ILE
SEQRES 9 A 245 ASP ARG LEU ARG ILE ALA THR ARG LEU ASN ASP GLN ARG
SEQRES 10 A 245 PRO ALA GLU LEU PRO PRO LEU ASN VAL LEU ILE GLN ILE
SEQRES 11 A 245 ASN ILE SER ASP GLU ASN SER LYS SER GLY ILE GLN LEU
SEQRES 12 A 245 ALA GLU LEU ASP GLU LEU ALA ALA ALA VAL ALA GLU LEU
SEQRES 13 A 245 PRO ARG LEU ARG LEU ARG GLY LEU SER ALA ILE PRO ALA
SEQRES 14 A 245 PRO GLU SER GLU TYR VAL ARG GLN PHE GLU VAL ALA ARG
SEQRES 15 A 245 GLN MET ALA VAL ALA PHE ALA GLY LEU LYS THR ARG TYR
SEQRES 16 A 245 PRO HIS ILE ASP THR LEU ALA LEU GLY GLN SER ASP ASP
SEQRES 17 A 245 MET GLU ALA ALA ILE ALA ALA GLY SER THR MET VAL ALA
SEQRES 18 A 245 ILE GLY THR ALA ILE PHE GLY ALA ARG ASP TYR SER LYS
SEQRES 19 A 245 LYS GLY SER LEU GLU HIS HIS HIS HIS HIS HIS
HET MES A 301 12
HET ACY A 401 4
HET ACY A 402 4
HET ACY A 403 4
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM ACY ACETIC ACID
FORMUL 2 MES C6 H13 N O4 S
FORMUL 3 ACY 3(C2 H4 O2)
FORMUL 6 HOH *374(H2 O)
HELIX 1 1 ASN A 3 CYS A 23 1 21
HELIX 2 2 SER A 26 ILE A 30 5 5
HELIX 3 3 PRO A 40 ALA A 50 1 11
HELIX 4 4 TYR A 59 GLY A 74 1 16
HELIX 5 5 GLN A 87 ASN A 89 5 3
HELIX 6 6 LYS A 90 PHE A 98 1 9
HELIX 7 7 ARG A 106 ARG A 117 1 12
HELIX 8 8 GLN A 142 ALA A 144 5 3
HELIX 9 9 GLU A 145 GLU A 155 1 11
HELIX 10 10 GLU A 173 THR A 193 1 21
HELIX 11 11 ASP A 208 GLY A 216 1 9
HELIX 12 12 GLY A 223 GLY A 228 1 6
SHEET 1 A 9 THR A 31 VAL A 35 0
SHEET 2 A 9 GLN A 54 GLU A 57 1 O SER A 56 N ALA A 34
SHEET 3 A 9 GLU A 79 PHE A 82 1 O ASN A 81 N PHE A 55
SHEET 4 A 9 TRP A 100 ILE A 104 1 O TRP A 100 N PHE A 82
SHEET 5 A 9 LEU A 124 GLN A 129 1 O ASN A 125 N CYS A 101
SHEET 6 A 9 LEU A 159 SER A 165 1 O ARG A 162 N VAL A 126
SHEET 7 A 9 THR A 200 ALA A 202 1 O ALA A 202 N LEU A 164
SHEET 8 A 9 MET A 219 ILE A 222 1 N MET A 219 O LEU A 201
SHEET 9 A 9 THR A 31 VAL A 35 1 N VAL A 33 O VAL A 220
SITE 1 AC1 6 ASP A 14 TYR A 59 GLN A 61 GLU A 62
SITE 2 AC1 6 HOH A 531 HOH A 562
SITE 1 AC2 7 VAL A 33 SER A 56 ASN A 81 ILE A 102
SITE 2 AC2 7 MET A 219 ALA A 221 HOH A 813
SITE 1 AC3 7 MET A 1 VAL A 35 SER A 56 GLU A 57
SITE 2 AC3 7 HIS A 58 ALA A 83 HOH A 813
SITE 1 AC4 7 ARG A 160 GLU A 173 TYR A 174 HOH A 555
SITE 2 AC4 7 HOH A 876 HOH A 891 HOH A 946
CRYST1 53.715 61.695 83.234 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 0.018617 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016209 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012014 0.00000
(ATOM LINES ARE NOT SHOWN.)
END