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HEADER LYASE 10-JUL-08 3DQZ
TITLE STRUCTURE OF THE HYDROXYNITRILE LYASE FROM ARABIDOPSIS
TITLE 2 THALIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-HYDROXYNITRILE LYASE-LIKE PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ATHNL, AT5G10300/F18D22_70;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: F18D22_70, AT5G10300;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS A/B-HYDRLOASE FOLD, CYANOGENESIS, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.ANDEXER,N.STAUNIG,K.GRUBER
REVDAT 1 14-JUL-09 3DQZ 0
JRNL AUTH J.ANDEXER,N.STAUNIG,T.EGGERT,C.KRATKY,M.POHL,
JRNL AUTH 2 K.GRUBER
JRNL TITL THE CRYSTAL STRUCTURE OF THE R-SELECTIVE
JRNL TITL 2 HYDROXYNITRILE LYASE FROM ARABIDOPSIS THALIANA:
JRNL TITL 3 MECHANISTIC IMPLICATIONS AND EXPLANATIONS FOR THE
JRNL TITL 4 STEREOSELECTIVITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.17
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.3
REMARK 3 NUMBER OF REFLECTIONS : 33106
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.720
REMARK 3 FREE R VALUE TEST SET COUNT : 1561
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
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 : 0.35
REMARK 3 B_SOL : 24.79
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) : 28.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.17900
REMARK 3 B22 (A**2) : 1.95800
REMARK 3 B33 (A**2) : -0.77900
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : -2.06200
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.4810
REMARK 3 OPERATOR: L,-K,H
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 NULL
REMARK 3 ANGLE : 0.899 NULL
REMARK 3 CHIRALITY : 0.063 NULL
REMARK 3 PLANARITY : 0.004 NULL
REMARK 3 DIHEDRAL : 16.596 NULL
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: THIS IS A TWINNED STRUCTURE, THE
REMARK 3 DETWIN FRACTION IS 0.481 AND OPERATOR IS 'L,-K,H'.
REMARK 4
REMARK 4 3DQZ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JUL-08.
REMARK 100 THE RCSB ID CODE IS RCSB048379.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8081
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33151
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07100
REMARK 200 FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.21000
REMARK 200 FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1QJ4, 1DWP, 1XKL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-18% PEG3350, 100MM BISTRIS,
REMARK 280 PH6.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 111.65650
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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 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 MET A 1
REMARK 465 GLU A 2
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 MET B 258
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 MET D 258
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 TYR A 14 -2.33 73.86
REMARK 500 HIS A 15 -166.58 -123.72
REMARK 500 ALA A 41 16.46 58.83
REMARK 500 ASN A 72 -1.94 74.85
REMARK 500 SER A 81 -112.60 64.89
REMARK 500 ASN A 105 39.35 38.39
REMARK 500 ASP A 110 -163.99 -100.31
REMARK 500 LEU A 129 44.07 -148.28
REMARK 500 PHE A 223 95.49 -166.22
REMARK 500 TYR A 257 63.12 -118.66
REMARK 500 TYR B 14 -0.78 73.13
REMARK 500 HIS B 15 -166.79 -126.36
REMARK 500 ALA B 41 18.23 58.29
REMARK 500 ASN B 72 -5.68 88.18
REMARK 500 SER B 81 -111.87 62.40
REMARK 500 ASN B 105 37.63 39.97
REMARK 500 ASP B 110 -162.34 -100.03
REMARK 500 PHE B 223 94.40 -164.94
REMARK 500 TYR C 14 -2.34 73.48
REMARK 500 HIS C 15 -165.90 -124.49
REMARK 500 ALA C 41 16.82 57.96
REMARK 500 ASN C 72 -2.00 76.11
REMARK 500 SER C 81 -112.46 63.23
REMARK 500 ASN C 105 38.13 38.99
REMARK 500 ASP C 110 -163.81 -100.91
REMARK 500 PHE C 223 95.71 -166.37
REMARK 500 TYR D 14 -1.10 72.39
REMARK 500 HIS D 15 -165.25 -125.72
REMARK 500 ALA D 41 17.01 57.94
REMARK 500 ASN D 72 -4.40 65.03
REMARK 500 SER D 81 -111.86 64.52
REMARK 500 ASN D 105 38.19 38.77
REMARK 500 ASP D 110 -162.84 -101.09
REMARK 500 PHE D 223 95.05 -165.04
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 CL D 259
DBREF 3DQZ A 1 258 UNP Q9LFT6 Q9LFT6_ARATH 1 258
DBREF 3DQZ B 1 258 UNP Q9LFT6 Q9LFT6_ARATH 1 258
DBREF 3DQZ C 1 258 UNP Q9LFT6 Q9LFT6_ARATH 1 258
DBREF 3DQZ D 1 258 UNP Q9LFT6 Q9LFT6_ARATH 1 258
SEQRES 1 A 258 MET GLU ARG LYS HIS HIS PHE VAL LEU VAL HIS ASN ALA
SEQRES 2 A 258 TYR HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 A 258 LEU GLU SER ALA GLY HIS ARG VAL THR ALA VAL GLU LEU
SEQRES 4 A 258 ALA ALA SER GLY ILE ASP PRO ARG PRO ILE GLN ALA VAL
SEQRES 5 A 258 GLU THR VAL ASP GLU TYR SER LYS PRO LEU ILE GLU THR
SEQRES 6 A 258 LEU LYS SER LEU PRO GLU ASN GLU GLU VAL ILE LEU VAL
SEQRES 7 A 258 GLY PHE SER PHE GLY GLY ILE ASN ILE ALA LEU ALA ALA
SEQRES 8 A 258 ASP ILE PHE PRO ALA LYS ILE LYS VAL LEU VAL PHE LEU
SEQRES 9 A 258 ASN ALA PHE LEU PRO ASP THR THR HIS VAL PRO SER HIS
SEQRES 10 A 258 VAL LEU ASP LYS TYR MET GLU MET PRO GLY GLY LEU GLY
SEQRES 11 A 258 ASP CYS GLU PHE SER SER HIS GLU THR ARG ASN GLY THR
SEQRES 12 A 258 MET SER LEU LEU LYS MET GLY PRO LYS PHE MET LYS ALA
SEQRES 13 A 258 ARG LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU
SEQRES 14 A 258 ALA LYS MET LEU HIS ARG GLN GLY SER PHE PHE THR GLU
SEQRES 15 A 258 ASP LEU SER LYS LYS GLU LYS PHE SER GLU GLU GLY TYR
SEQRES 16 A 258 GLY SER VAL GLN ARG VAL TYR VAL MET SER SER GLU ASP
SEQRES 17 A 258 LYS ALA ILE PRO CYS ASP PHE ILE ARG TRP MET ILE ASP
SEQRES 18 A 258 ASN PHE ASN VAL SER LYS VAL TYR GLU ILE ASP GLY GLY
SEQRES 19 A 258 ASP HIS MET VAL MET LEU SER LYS PRO GLN LYS LEU PHE
SEQRES 20 A 258 ASP SER LEU SER ALA ILE ALA THR ASP TYR MET
SEQRES 1 B 258 MET GLU ARG LYS HIS HIS PHE VAL LEU VAL HIS ASN ALA
SEQRES 2 B 258 TYR HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 B 258 LEU GLU SER ALA GLY HIS ARG VAL THR ALA VAL GLU LEU
SEQRES 4 B 258 ALA ALA SER GLY ILE ASP PRO ARG PRO ILE GLN ALA VAL
SEQRES 5 B 258 GLU THR VAL ASP GLU TYR SER LYS PRO LEU ILE GLU THR
SEQRES 6 B 258 LEU LYS SER LEU PRO GLU ASN GLU GLU VAL ILE LEU VAL
SEQRES 7 B 258 GLY PHE SER PHE GLY GLY ILE ASN ILE ALA LEU ALA ALA
SEQRES 8 B 258 ASP ILE PHE PRO ALA LYS ILE LYS VAL LEU VAL PHE LEU
SEQRES 9 B 258 ASN ALA PHE LEU PRO ASP THR THR HIS VAL PRO SER HIS
SEQRES 10 B 258 VAL LEU ASP LYS TYR MET GLU MET PRO GLY GLY LEU GLY
SEQRES 11 B 258 ASP CYS GLU PHE SER SER HIS GLU THR ARG ASN GLY THR
SEQRES 12 B 258 MET SER LEU LEU LYS MET GLY PRO LYS PHE MET LYS ALA
SEQRES 13 B 258 ARG LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU
SEQRES 14 B 258 ALA LYS MET LEU HIS ARG GLN GLY SER PHE PHE THR GLU
SEQRES 15 B 258 ASP LEU SER LYS LYS GLU LYS PHE SER GLU GLU GLY TYR
SEQRES 16 B 258 GLY SER VAL GLN ARG VAL TYR VAL MET SER SER GLU ASP
SEQRES 17 B 258 LYS ALA ILE PRO CYS ASP PHE ILE ARG TRP MET ILE ASP
SEQRES 18 B 258 ASN PHE ASN VAL SER LYS VAL TYR GLU ILE ASP GLY GLY
SEQRES 19 B 258 ASP HIS MET VAL MET LEU SER LYS PRO GLN LYS LEU PHE
SEQRES 20 B 258 ASP SER LEU SER ALA ILE ALA THR ASP TYR MET
SEQRES 1 C 258 MET GLU ARG LYS HIS HIS PHE VAL LEU VAL HIS ASN ALA
SEQRES 2 C 258 TYR HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 C 258 LEU GLU SER ALA GLY HIS ARG VAL THR ALA VAL GLU LEU
SEQRES 4 C 258 ALA ALA SER GLY ILE ASP PRO ARG PRO ILE GLN ALA VAL
SEQRES 5 C 258 GLU THR VAL ASP GLU TYR SER LYS PRO LEU ILE GLU THR
SEQRES 6 C 258 LEU LYS SER LEU PRO GLU ASN GLU GLU VAL ILE LEU VAL
SEQRES 7 C 258 GLY PHE SER PHE GLY GLY ILE ASN ILE ALA LEU ALA ALA
SEQRES 8 C 258 ASP ILE PHE PRO ALA LYS ILE LYS VAL LEU VAL PHE LEU
SEQRES 9 C 258 ASN ALA PHE LEU PRO ASP THR THR HIS VAL PRO SER HIS
SEQRES 10 C 258 VAL LEU ASP LYS TYR MET GLU MET PRO GLY GLY LEU GLY
SEQRES 11 C 258 ASP CYS GLU PHE SER SER HIS GLU THR ARG ASN GLY THR
SEQRES 12 C 258 MET SER LEU LEU LYS MET GLY PRO LYS PHE MET LYS ALA
SEQRES 13 C 258 ARG LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU
SEQRES 14 C 258 ALA LYS MET LEU HIS ARG GLN GLY SER PHE PHE THR GLU
SEQRES 15 C 258 ASP LEU SER LYS LYS GLU LYS PHE SER GLU GLU GLY TYR
SEQRES 16 C 258 GLY SER VAL GLN ARG VAL TYR VAL MET SER SER GLU ASP
SEQRES 17 C 258 LYS ALA ILE PRO CYS ASP PHE ILE ARG TRP MET ILE ASP
SEQRES 18 C 258 ASN PHE ASN VAL SER LYS VAL TYR GLU ILE ASP GLY GLY
SEQRES 19 C 258 ASP HIS MET VAL MET LEU SER LYS PRO GLN LYS LEU PHE
SEQRES 20 C 258 ASP SER LEU SER ALA ILE ALA THR ASP TYR MET
SEQRES 1 D 258 MET GLU ARG LYS HIS HIS PHE VAL LEU VAL HIS ASN ALA
SEQRES 2 D 258 TYR HIS GLY ALA TRP ILE TRP TYR LYS LEU LYS PRO LEU
SEQRES 3 D 258 LEU GLU SER ALA GLY HIS ARG VAL THR ALA VAL GLU LEU
SEQRES 4 D 258 ALA ALA SER GLY ILE ASP PRO ARG PRO ILE GLN ALA VAL
SEQRES 5 D 258 GLU THR VAL ASP GLU TYR SER LYS PRO LEU ILE GLU THR
SEQRES 6 D 258 LEU LYS SER LEU PRO GLU ASN GLU GLU VAL ILE LEU VAL
SEQRES 7 D 258 GLY PHE SER PHE GLY GLY ILE ASN ILE ALA LEU ALA ALA
SEQRES 8 D 258 ASP ILE PHE PRO ALA LYS ILE LYS VAL LEU VAL PHE LEU
SEQRES 9 D 258 ASN ALA PHE LEU PRO ASP THR THR HIS VAL PRO SER HIS
SEQRES 10 D 258 VAL LEU ASP LYS TYR MET GLU MET PRO GLY GLY LEU GLY
SEQRES 11 D 258 ASP CYS GLU PHE SER SER HIS GLU THR ARG ASN GLY THR
SEQRES 12 D 258 MET SER LEU LEU LYS MET GLY PRO LYS PHE MET LYS ALA
SEQRES 13 D 258 ARG LEU TYR GLN ASN CYS PRO ILE GLU ASP TYR GLU LEU
SEQRES 14 D 258 ALA LYS MET LEU HIS ARG GLN GLY SER PHE PHE THR GLU
SEQRES 15 D 258 ASP LEU SER LYS LYS GLU LYS PHE SER GLU GLU GLY TYR
SEQRES 16 D 258 GLY SER VAL GLN ARG VAL TYR VAL MET SER SER GLU ASP
SEQRES 17 D 258 LYS ALA ILE PRO CYS ASP PHE ILE ARG TRP MET ILE ASP
SEQRES 18 D 258 ASN PHE ASN VAL SER LYS VAL TYR GLU ILE ASP GLY GLY
SEQRES 19 D 258 ASP HIS MET VAL MET LEU SER LYS PRO GLN LYS LEU PHE
SEQRES 20 D 258 ASP SER LEU SER ALA ILE ALA THR ASP TYR MET
HET CL D 259 1
HETNAM CL CHLORIDE ION
FORMUL 5 CL CL 1-
FORMUL 6 HOH *69(H2 O)
HELIX 1 1 GLY A 16 TYR A 21 5 6
HELIX 2 2 LYS A 22 ALA A 30 1 9
HELIX 3 3 PRO A 48 VAL A 52 5 5
HELIX 4 4 THR A 54 SER A 68 1 15
HELIX 5 5 PHE A 82 ASP A 92 1 11
HELIX 6 6 PHE A 94 ALA A 96 5 3
HELIX 7 7 SER A 116 GLU A 124 1 9
HELIX 8 8 GLY A 150 LEU A 158 1 9
HELIX 9 9 PRO A 163 HIS A 174 1 12
HELIX 10 10 PHE A 180 LYS A 186 1 7
HELIX 11 11 GLY A 194 VAL A 198 5 5
HELIX 12 12 PRO A 212 PHE A 223 1 12
HELIX 13 13 MET A 237 LYS A 242 1 6
HELIX 14 14 LYS A 242 TYR A 257 1 16
HELIX 15 15 GLY B 16 TYR B 21 5 6
HELIX 16 16 LYS B 22 ALA B 30 1 9
HELIX 17 17 PRO B 48 VAL B 52 5 5
HELIX 18 18 THR B 54 SER B 68 1 15
HELIX 19 19 PHE B 82 ASP B 92 1 11
HELIX 20 20 ILE B 93 ALA B 96 5 4
HELIX 21 21 SER B 116 GLU B 124 1 9
HELIX 22 22 GLY B 150 LEU B 158 1 9
HELIX 23 23 PRO B 163 MET B 172 1 10
HELIX 24 24 PHE B 180 LYS B 186 1 7
HELIX 25 25 GLY B 194 VAL B 198 5 5
HELIX 26 26 PRO B 212 PHE B 223 1 12
HELIX 27 27 MET B 237 LYS B 242 1 6
HELIX 28 28 LYS B 242 TYR B 257 1 16
HELIX 29 29 GLY C 16 TYR C 21 5 6
HELIX 30 30 LYS C 22 ALA C 30 1 9
HELIX 31 31 PRO C 48 VAL C 52 5 5
HELIX 32 32 THR C 54 SER C 68 1 15
HELIX 33 33 PHE C 82 ASP C 92 1 11
HELIX 34 34 PHE C 94 ALA C 96 5 3
HELIX 35 35 SER C 116 GLU C 124 1 9
HELIX 36 36 GLY C 150 LEU C 158 1 9
HELIX 37 37 PRO C 163 HIS C 174 1 12
HELIX 38 38 PHE C 180 LYS C 186 1 7
HELIX 39 39 GLY C 194 VAL C 198 5 5
HELIX 40 40 PRO C 212 PHE C 223 1 12
HELIX 41 41 MET C 237 LYS C 242 1 6
HELIX 42 42 LYS C 242 TYR C 257 1 16
HELIX 43 43 GLY D 16 TYR D 21 5 6
HELIX 44 44 LYS D 22 ALA D 30 1 9
HELIX 45 45 PRO D 48 VAL D 52 5 5
HELIX 46 46 THR D 54 SER D 68 1 15
HELIX 47 47 PHE D 82 ASP D 92 1 11
HELIX 48 48 PHE D 94 ALA D 96 5 3
HELIX 49 49 SER D 116 GLU D 124 1 9
HELIX 50 50 GLY D 150 LEU D 158 1 9
HELIX 51 51 PRO D 163 MET D 172 1 10
HELIX 52 52 PHE D 180 LYS D 186 1 7
HELIX 53 53 GLY D 194 VAL D 198 5 5
HELIX 54 54 PRO D 212 PHE D 223 1 12
HELIX 55 55 MET D 237 LYS D 242 1 6
HELIX 56 56 LYS D 242 TYR D 257 1 16
SHEET 1 A 6 ARG A 33 VAL A 37 0
SHEET 2 A 6 HIS A 6 VAL A 10 1 N LEU A 9 O THR A 35
SHEET 3 A 6 VAL A 75 PHE A 80 1 O VAL A 78 N VAL A 8
SHEET 4 A 6 ILE A 98 LEU A 104 1 O VAL A 102 N LEU A 77
SHEET 5 A 6 ARG A 200 SER A 205 1 O VAL A 203 N PHE A 103
SHEET 6 A 6 VAL A 228 ILE A 231 1 O TYR A 229 N TYR A 202
SHEET 1 B 3 GLU A 133 THR A 139 0
SHEET 2 B 3 GLY A 142 LYS A 148 -1 O LYS A 148 N GLU A 133
SHEET 3 B 3 GLY A 177 SER A 178 -1 O GLY A 177 N LEU A 147
SHEET 1 C 6 ARG B 33 VAL B 37 0
SHEET 2 C 6 HIS B 6 VAL B 10 1 N PHE B 7 O ARG B 33
SHEET 3 C 6 VAL B 75 PHE B 80 1 O VAL B 78 N VAL B 8
SHEET 4 C 6 ILE B 98 LEU B 104 1 O VAL B 102 N LEU B 77
SHEET 5 C 6 GLN B 199 SER B 205 1 O GLN B 199 N LEU B 101
SHEET 6 C 6 VAL B 228 ILE B 231 1 O TYR B 229 N TYR B 202
SHEET 1 D 3 GLU B 133 THR B 139 0
SHEET 2 D 3 GLY B 142 LYS B 148 -1 O LYS B 148 N GLU B 133
SHEET 3 D 3 GLY B 177 SER B 178 -1 O GLY B 177 N LEU B 147
SHEET 1 E 6 ARG C 33 VAL C 37 0
SHEET 2 E 6 HIS C 6 VAL C 10 1 N LEU C 9 O THR C 35
SHEET 3 E 6 VAL C 75 PHE C 80 1 O VAL C 78 N VAL C 8
SHEET 4 E 6 ILE C 98 LEU C 104 1 O VAL C 102 N LEU C 77
SHEET 5 E 6 ARG C 200 SER C 205 1 O VAL C 203 N PHE C 103
SHEET 6 E 6 VAL C 228 ILE C 231 1 O TYR C 229 N TYR C 202
SHEET 1 F 3 GLU C 133 THR C 139 0
SHEET 2 F 3 GLY C 142 LYS C 148 -1 O LYS C 148 N GLU C 133
SHEET 3 F 3 GLY C 177 SER C 178 -1 O GLY C 177 N LEU C 147
SHEET 1 G 6 ARG D 33 VAL D 37 0
SHEET 2 G 6 HIS D 6 VAL D 10 1 N LEU D 9 O THR D 35
SHEET 3 G 6 VAL D 75 PHE D 80 1 O VAL D 78 N VAL D 8
SHEET 4 G 6 ILE D 98 LEU D 104 1 O VAL D 102 N LEU D 77
SHEET 5 G 6 ARG D 200 SER D 205 1 O VAL D 203 N PHE D 103
SHEET 6 G 6 VAL D 228 ILE D 231 1 O TYR D 229 N TYR D 202
SHEET 1 H 3 GLU D 133 THR D 139 0
SHEET 2 H 3 GLY D 142 LYS D 148 -1 O LYS D 148 N GLU D 133
SHEET 3 H 3 GLY D 177 SER D 178 -1 O GLY D 177 N LEU D 147
SITE 1 AC1 2 ARG D 175 GLN D 176
CRYST1 50.248 223.313 50.201 90.00 101.47 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019901 0.000000 0.004038 0.00000
SCALE2 0.000000 0.004478 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020326 0.00000
MTRIX1 1 -0.892166 -0.224244 -0.392115 -12.09170
MTRIX2 1 -0.243977 -0.491335 0.836101 6.46592
MTRIX3 1 -0.380151 0.841608 0.383642 -7.37886
MTRIX1 2 0.194955 -0.002658 -0.980809 -16.27400
MTRIX2 2 -0.005533 -0.999983 0.001611 -56.47510
MTRIX3 2 -0.980797 0.005113 -0.194967 -27.60680
MTRIX1 3 0.203611 0.223737 0.953144 25.73530
MTRIX2 3 -0.869170 0.489421 0.070787 14.54750
MTRIX3 3 -0.450651 -0.842857 0.294117 -59.55490
TER 2038 MET A 258
TER 4067 TYR B 257
TER 6105 MET C 258
TER 8134 TYR D 257
MASTER 261 0 1 56 36 0 1 15 8200 4 0 80
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