HEADER STRUCTURAL GENOMICS, ALDOLASE 07-OCT-02 1MZH
TITLE QR15, AN ALDOLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEOXYRIBOSE-PHOSPHATE ALDOLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PHOSPHODEOXYRIBOALDOLASE, DEOXYRIBOALDOLASE;
COMPND 5 EC: 4.1.2.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA-BETA BARREL, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, ALDOLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.Y.TAN,P.C.SMITH,J.SHEN,R.XIAO,T.ACTON,B.ROST,G.MONTELIONE,J.F.HUNT,
AUTHOR 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 5 14-FEB-24 1MZH 1 REMARK SEQADV
REVDAT 4 24-FEB-09 1MZH 1 VERSN
REVDAT 3 25-JAN-05 1MZH 1 AUTHOR KEYWDS REMARK
REVDAT 2 13-MAY-03 1MZH 1 AUTHOR REMARK
REVDAT 1 04-FEB-03 1MZH 0
JRNL AUTH A.Y.TAN,P.C.SMITH,J.SHEN,R.XIAO,T.ACTON,B.ROST,G.MONTELIONE,
JRNL AUTH 2 J.F.HUNT
JRNL TITL CRYSTAL STRUCTURE OF AQUIFEX AEOLICUS ALDOLASE, NORTHEAST
JRNL TITL 2 STRUCTURAL GENOMICS CONSORTIUM TARGET QR15
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.7
REMARK 3 NUMBER OF REFLECTIONS : 30184
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1560
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.12
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4541
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE : 0.3000
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 244
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3473
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 391
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 12.73000
REMARK 3 B22 (A**2) : -5.50000
REMARK 3 B33 (A**2) : -7.22000
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.270
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.500 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.250 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 26.080; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 10.600; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 32.68
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PS_PARAM.PRO
REMARK 3 PARAMETER FILE 2 : PARAM19.SOL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MZH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017331.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-02
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 : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798, 0.9799, 0.92
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30534
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 12.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, AMMONIUM SULFATE, PH 7.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.91100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.91100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 24.56950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 61.72900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.56950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 61.72900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 75.91100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.56950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 61.72900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 75.91100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.56950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 61.72900
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 HIS B 1322
REMARK 465 HIS B 1323
REMARK 465 HIS B 1324
REMARK 465 HIS B 1325
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 HIS A 322 85.77 160.27
REMARK 500 HIS A 323 -89.02 -165.64
REMARK 500 HIS A 324 -2.73 -149.82
REMARK 500 ASP B1103 85.09 15.71
REMARK 500 LYS B1152 -71.99 -106.35
REMARK 500 GLU B1225 66.05 62.41
REMARK 500 THR B1251 -74.41 -63.51
REMARK 500 SER B1252 -108.85 -88.79
REMARK 500 THR B1253 -24.05 161.58
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 PO4 B 3001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: QR15 RELATED DB: TARGETDB
DBREF 1MZH A 101 319 UNP O66540 DEOC_AQUAE 1 219
DBREF 1MZH B 1101 1319 UNP O66540 DEOC_AQUAE 1 219
SEQADV 1MZH LEU A 320 UNP O66540 EXPRESSION TAG
SEQADV 1MZH GLU A 321 UNP O66540 EXPRESSION TAG
SEQADV 1MZH HIS A 322 UNP O66540 EXPRESSION TAG
SEQADV 1MZH HIS A 323 UNP O66540 EXPRESSION TAG
SEQADV 1MZH HIS A 324 UNP O66540 EXPRESSION TAG
SEQADV 1MZH HIS A 325 UNP O66540 EXPRESSION TAG
SEQADV 1MZH LEU B 1320 UNP O66540 EXPRESSION TAG
SEQADV 1MZH GLU B 1321 UNP O66540 EXPRESSION TAG
SEQADV 1MZH HIS B 1322 UNP O66540 EXPRESSION TAG
SEQADV 1MZH HIS B 1323 UNP O66540 EXPRESSION TAG
SEQADV 1MZH HIS B 1324 UNP O66540 EXPRESSION TAG
SEQADV 1MZH HIS B 1325 UNP O66540 EXPRESSION TAG
SEQRES 1 A 225 MET ILE ASP VAL ARG LYS TYR ILE ASP ASN ALA ALA LEU
SEQRES 2 A 225 LYS PRO HIS LEU SER GLU LYS GLU ILE GLU GLU PHE VAL
SEQRES 3 A 225 LEU LYS SER GLU GLU LEU GLY ILE TYR ALA VAL CYS VAL
SEQRES 4 A 225 ASN PRO TYR HIS VAL LYS LEU ALA SER SER ILE ALA LYS
SEQRES 5 A 225 LYS VAL LYS VAL CYS CYS VAL ILE GLY PHE PRO LEU GLY
SEQRES 6 A 225 LEU ASN LYS THR SER VAL LYS VAL LYS GLU ALA VAL GLU
SEQRES 7 A 225 ALA VAL ARG ASP GLY ALA GLN GLU LEU ASP ILE VAL TRP
SEQRES 8 A 225 ASN LEU SER ALA PHE LYS SER GLU LYS TYR ASP PHE VAL
SEQRES 9 A 225 VAL GLU GLU LEU LYS GLU ILE PHE ARG GLU THR PRO SER
SEQRES 10 A 225 ALA VAL HIS LYS VAL ILE VAL GLU THR PRO TYR LEU ASN
SEQRES 11 A 225 GLU GLU GLU ILE LYS LYS ALA VAL GLU ILE CYS ILE GLU
SEQRES 12 A 225 ALA GLY ALA ASP PHE ILE LYS THR SER THR GLY PHE ALA
SEQRES 13 A 225 PRO ARG GLY THR THR LEU GLU GLU VAL ARG LEU ILE LYS
SEQRES 14 A 225 SER SER ALA LYS GLY ARG ILE LYS VAL LYS ALA SER GLY
SEQRES 15 A 225 GLY ILE ARG ASP LEU GLU THR ALA ILE SER MET ILE GLU
SEQRES 16 A 225 ALA GLY ALA ASP ARG ILE GLY THR SER SER GLY ILE SER
SEQRES 17 A 225 ILE ALA GLU GLU PHE LEU LYS ARG HIS LEU ILE LEU GLU
SEQRES 18 A 225 HIS HIS HIS HIS
SEQRES 1 B 225 MET ILE ASP VAL ARG LYS TYR ILE ASP ASN ALA ALA LEU
SEQRES 2 B 225 LYS PRO HIS LEU SER GLU LYS GLU ILE GLU GLU PHE VAL
SEQRES 3 B 225 LEU LYS SER GLU GLU LEU GLY ILE TYR ALA VAL CYS VAL
SEQRES 4 B 225 ASN PRO TYR HIS VAL LYS LEU ALA SER SER ILE ALA LYS
SEQRES 5 B 225 LYS VAL LYS VAL CYS CYS VAL ILE GLY PHE PRO LEU GLY
SEQRES 6 B 225 LEU ASN LYS THR SER VAL LYS VAL LYS GLU ALA VAL GLU
SEQRES 7 B 225 ALA VAL ARG ASP GLY ALA GLN GLU LEU ASP ILE VAL TRP
SEQRES 8 B 225 ASN LEU SER ALA PHE LYS SER GLU LYS TYR ASP PHE VAL
SEQRES 9 B 225 VAL GLU GLU LEU LYS GLU ILE PHE ARG GLU THR PRO SER
SEQRES 10 B 225 ALA VAL HIS LYS VAL ILE VAL GLU THR PRO TYR LEU ASN
SEQRES 11 B 225 GLU GLU GLU ILE LYS LYS ALA VAL GLU ILE CYS ILE GLU
SEQRES 12 B 225 ALA GLY ALA ASP PHE ILE LYS THR SER THR GLY PHE ALA
SEQRES 13 B 225 PRO ARG GLY THR THR LEU GLU GLU VAL ARG LEU ILE LYS
SEQRES 14 B 225 SER SER ALA LYS GLY ARG ILE LYS VAL LYS ALA SER GLY
SEQRES 15 B 225 GLY ILE ARG ASP LEU GLU THR ALA ILE SER MET ILE GLU
SEQRES 16 B 225 ALA GLY ALA ASP ARG ILE GLY THR SER SER GLY ILE SER
SEQRES 17 B 225 ILE ALA GLU GLU PHE LEU LYS ARG HIS LEU ILE LEU GLU
SEQRES 18 B 225 HIS HIS HIS HIS
HET PO4 B3001 5
HETNAM PO4 PHOSPHATE ION
FORMUL 3 PO4 O4 P 3-
FORMUL 4 HOH *391(H2 O)
HELIX 1 1 ASP A 103 LYS A 106 5 4
HELIX 2 2 SER A 118 LEU A 132 1 15
HELIX 3 3 HIS A 143 ALA A 151 1 9
HELIX 4 4 LYS A 168 ASP A 182 1 15
HELIX 5 5 ASN A 192 SER A 198 1 7
HELIX 6 6 LYS A 200 GLU A 214 1 15
HELIX 7 7 GLU A 225 LEU A 229 5 5
HELIX 8 8 ASN A 230 GLY A 245 1 16
HELIX 9 9 THR A 261 LYS A 273 1 13
HELIX 10 10 ASP A 286 ALA A 296 1 11
HELIX 11 11 SER A 305 LEU A 320 1 16
HELIX 12 12 ASP B 1103 LYS B 1106 5 4
HELIX 13 13 SER B 1118 LEU B 1132 1 15
HELIX 14 14 HIS B 1143 ALA B 1151 1 9
HELIX 15 15 LYS B 1168 GLY B 1183 1 16
HELIX 16 16 ASN B 1192 SER B 1198 1 7
HELIX 17 17 LYS B 1200 THR B 1215 1 16
HELIX 18 18 GLU B 1225 LEU B 1229 5 5
HELIX 19 19 ASN B 1230 ALA B 1244 1 15
HELIX 20 20 THR B 1261 LYS B 1273 1 13
HELIX 21 21 ASP B 1286 ALA B 1296 1 11
HELIX 22 22 SER B 1305 GLU B 1321 1 17
SHEET 1 A 9 ILE A 108 ALA A 112 0
SHEET 2 A 9 ALA A 136 VAL A 139 1 O CYS A 138 N ASN A 110
SHEET 3 A 9 LYS A 155 ILE A 160 1 O CYS A 157 N VAL A 137
SHEET 4 A 9 GLU A 186 VAL A 190 1 O VAL A 190 N ILE A 160
SHEET 5 A 9 VAL A 219 ILE A 223 1 O VAL A 219 N LEU A 187
SHEET 6 A 9 PHE A 248 LYS A 250 1 O LYS A 250 N VAL A 222
SHEET 7 A 9 LYS A 277 SER A 281 1 O LYS A 279 N ILE A 249
SHEET 8 A 9 ARG A 300 THR A 303 1 O GLY A 302 N ALA A 280
SHEET 9 A 9 ILE A 108 ALA A 112 1 N ASP A 109 O ILE A 301
SHEET 1 B 9 ILE B1108 ALA B1112 0
SHEET 2 B 9 ALA B1136 VAL B1139 1 O CYS B1138 N ASN B1110
SHEET 3 B 9 LYS B1155 ILE B1160 1 O CYS B1157 N VAL B1137
SHEET 4 B 9 GLU B1186 VAL B1190 1 O ASP B1188 N ILE B1160
SHEET 5 B 9 VAL B1219 ILE B1223 1 O LYS B1221 N ILE B1189
SHEET 6 B 9 PHE B1248 LYS B1250 1 O LYS B1250 N VAL B1222
SHEET 7 B 9 LYS B1277 SER B1281 1 O LYS B1279 N ILE B1249
SHEET 8 B 9 ARG B1300 THR B1303 1 O GLY B1302 N ALA B1280
SHEET 9 B 9 ILE B1108 ALA B1112 1 N ASP B1109 O ILE B1301
CISPEP 1 PHE A 162 PRO A 163 0 -0.03
CISPEP 2 PHE B 1162 PRO B 1163 0 -0.17
SITE 1 AC1 6 GLY B1254 GLY B1282 GLY B1283 SER B1304
SITE 2 AC1 6 HOH B2126 HOH B2161
CRYST1 49.139 123.458 151.822 90.00 90.00 90.00 C 2 2 21 16
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 0.020350 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008100 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006587 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
