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HEADER HYDROLASE 04-SEP-17 6AVY
TITLE CRYSTAL STRUCTURE OF ZEA MAYS ACYL-PROTEIN THIOESTERASE 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYL-PROTEIN THIOESTERASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZEA MAYS;
SOURCE 3 ORGANISM_COMMON: MAIZE;
SOURCE 4 ORGANISM_TAXID: 4577;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX4T3
KEYWDS ALPHA/BETA HYDROLASE, ACYL-PROTEIN THIOESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.BURGER,B.C.WILLIGE,J.CHORY
REVDAT 1 27-DEC-17 6AVY 0
JRNL AUTH M.BURGER,B.C.WILLIGE,J.CHORY
JRNL TITL A HYDROPHOBIC ANCHOR MECHANISM DEFINES A DEACETYLASE FAMILY
JRNL TITL 2 THAT SUPPRESSES HOST RESPONSE AGAINST YOPJ EFFECTORS.
JRNL REF NAT COMMUN V. 8 2201 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 29259199
JRNL DOI 10.1038/S41467-017-02347-W
REMARK 2
REMARK 2 RESOLUTION. 2.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10.1_2155
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 21333
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1066
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 42.9146 - 4.4786 0.94 2708 143 0.1805 0.2022
REMARK 3 2 4.4786 - 3.5553 0.97 2674 141 0.1511 0.1886
REMARK 3 3 3.5553 - 3.1061 0.98 2645 140 0.1750 0.1991
REMARK 3 4 3.1061 - 2.8221 0.98 2650 139 0.1913 0.2562
REMARK 3 5 2.8221 - 2.6199 0.98 2652 138 0.2027 0.2792
REMARK 3 6 2.6199 - 2.4655 0.97 2598 137 0.2143 0.3015
REMARK 3 7 2.4655 - 2.3420 0.88 2351 125 0.2158 0.2623
REMARK 3 8 2.3420 - 2.2400 0.74 1989 103 0.2128 0.2525
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.420
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.003 3583
REMARK 3 ANGLE : 0.687 4892
REMARK 3 CHIRALITY : 0.044 543
REMARK 3 PLANARITY : 0.005 632
REMARK 3 DIHEDRAL : 14.286 2092
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 : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: (CHAIN A AND (RESSEQ 19 OR (RESID 20 AND
REMARK 3 (NAME N OR NAME CA OR NAME C )) OR RESSEQ
REMARK 3 22:27 OR RESSEQ 29:83 OR (RESID 84 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB OR NAME CG OR NAME CD1 OR NAME
REMARK 3 CE1 OR NAME CZ )) OR RESSEQ 85:88 OR
REMARK 3 RESSEQ 90 OR RESSEQ 92:133 OR (RESID 134
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB OR NAME CG OR NAME CD1 OR
REMARK 3 NAME CE1 OR NAME CZ OR NAME OH )) OR
REMARK 3 RESSEQ 135:138 OR (RESID 139 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 OR NAME CG OR NAME CD1 OR NAME CE1 OR
REMARK 3 NAME CE2)) OR RESSEQ 140:149 OR (RESID
REMARK 3 150 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB OR NAME CG OR NAME CD1
REMARK 3 OR NAME CE1 OR NAME CZ OR NAME OH )) OR
REMARK 3 RESSEQ 151:234 OR RESSEQ 236:249))
REMARK 3 SELECTION : (CHAIN B AND (RESSEQ 19 OR (RESID 20 AND
REMARK 3 (NAME O OR NAME N OR NAME CA )) OR RESSEQ
REMARK 3 22:27 OR RESSEQ 29:83 OR (RESID 84 AND
REMARK 3 (NAME N OR NAME CA OR NAME C OR NAME O OR
REMARK 3 NAME CB OR NAME CG OR NAME CD1 OR NAME
REMARK 3 CE1 OR NAME CZ )) OR RESSEQ 85:88 OR
REMARK 3 RESSEQ 90 OR RESSEQ 92:133 OR (RESID 134
REMARK 3 AND (NAME N OR NAME CA OR NAME C OR NAME
REMARK 3 O OR NAME CB OR NAME CG OR NAME CD1 OR
REMARK 3 NAME CE1 OR NAME CZ OR NAME OH )) OR
REMARK 3 RESSEQ 135:138 OR (RESID 139 AND (NAME N
REMARK 3 OR NAME CA OR NAME C OR NAME O OR NAME CB
REMARK 3 OR NAME CG OR NAME CD1 OR NAME CE1 OR
REMARK 3 NAME CE2)) OR RESSEQ 140:149 OR (RESID
REMARK 3 150 AND (NAME N OR NAME CA OR NAME C OR
REMARK 3 NAME O OR NAME CB OR NAME CG OR NAME CD1
REMARK 3 OR NAME CE1 OR NAME CZ OR NAME OH )) OR
REMARK 3 RESSEQ 151:234 OR RESSEQ 236:249))
REMARK 3 ATOM PAIRS NUMBER : 1999
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6AVY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1000229859.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21370
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.240
REMARK 200 RESOLUTION RANGE LOW (A) : 42.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.05712
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.21550
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.920
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: 1FJ2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5, 1% (V/V) PEG
REMARK 280 3350, 1 M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 24.44000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.60500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.78500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.60500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.44000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.78500
REMARK 290 SMTRY3 4 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: 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 GLY A -1
REMARK 465 PRO A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 TYR A 3
REMARK 465 GLY A 4
REMARK 465 GLY A 5
REMARK 465 SER A 6
REMARK 465 SER A 7
REMARK 465 SER A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 PRO A 11
REMARK 465 GLY A 12
REMARK 465 ALA A 13
REMARK 465 LYS A 14
REMARK 465 ARG A 15
REMARK 465 PRO A 16
REMARK 465 PHE A 17
REMARK 465 GLU A 18
REMARK 465 LEU A 250
REMARK 465 GLY A 251
REMARK 465 THR A 252
REMARK 465 SER A 253
REMARK 465 SER A 254
REMARK 465 SER A 255
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 TYR B 3
REMARK 465 GLY B 4
REMARK 465 GLY B 5
REMARK 465 SER B 6
REMARK 465 SER B 7
REMARK 465 SER B 8
REMARK 465 LEU B 9
REMARK 465 ALA B 10
REMARK 465 PRO B 11
REMARK 465 GLY B 12
REMARK 465 ALA B 13
REMARK 465 LYS B 14
REMARK 465 ARG B 15
REMARK 465 PRO B 16
REMARK 465 PHE B 17
REMARK 465 LEU B 250
REMARK 465 GLY B 251
REMARK 465 THR B 252
REMARK 465 SER B 253
REMARK 465 SER B 254
REMARK 465 SER B 255
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 B 301 O HOH B 303 2.11
REMARK 500 N GLY B 29 O HOH B 301 2.15
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 ASN A 59 -6.07 76.09
REMARK 500 ASP A 88 152.45 70.27
REMARK 500 SER A 126 -119.73 57.56
REMARK 500 TYR B 19 149.95 70.57
REMARK 500 ASN B 59 -2.71 72.78
REMARK 500 ASP B 92 -23.63 -142.60
REMARK 500 SER B 126 -120.26 56.68
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6AVY A 1 255 UNP B6T1C9 B6T1C9_MAIZE 1 255
DBREF 6AVY B 1 255 UNP B6T1C9 B6T1C9_MAIZE 1 255
SEQADV 6AVY GLY A -1 UNP B6T1C9 EXPRESSION TAG
SEQADV 6AVY PRO A 0 UNP B6T1C9 EXPRESSION TAG
SEQADV 6AVY GLY B -1 UNP B6T1C9 EXPRESSION TAG
SEQADV 6AVY PRO B 0 UNP B6T1C9 EXPRESSION TAG
SEQRES 1 A 257 GLY PRO MET SER TYR GLY GLY SER SER SER LEU ALA PRO
SEQRES 2 A 257 GLY ALA LYS ARG PRO PHE GLU TYR GLY ARG THR HIS VAL
SEQRES 3 A 257 VAL ARG PRO LYS GLY THR HIS LYS ALA THR ILE VAL TRP
SEQRES 4 A 257 LEU HIS GLY LEU GLY ASP ASN GLY THR SER TRP SER GLN
SEQRES 5 A 257 LEU LEU GLU THR LEU PRO LEU PRO ASN ILE LYS TRP ILE
SEQRES 6 A 257 CYS PRO THR ALA PRO SER ARG PRO VAL SER LEU PHE GLY
SEQRES 7 A 257 GLY PHE PRO CYS THR ALA TRP PHE ASP VAL ALA ASP LEU
SEQRES 8 A 257 SER GLU ASP ALA PRO ASP ASP THR GLU GLY MET ASP ALA
SEQRES 9 A 257 SER ALA ALA HIS VAL ALA ASN LEU LEU SER THR GLU PRO
SEQRES 10 A 257 ALA ASP ILE LYS LEU GLY VAL GLY GLY PHE SER MET GLY
SEQRES 11 A 257 ALA ALA THR ALA LEU TYR SER ALA THR CYS PHE ALA HIS
SEQRES 12 A 257 GLY LYS TYR GLY ASN GLY ASN PRO TYR PRO VAL ASN LEU
SEQRES 13 A 257 SER LEU ALA VAL GLY LEU SER GLY TRP LEU PRO CYS ALA
SEQRES 14 A 257 ARG THR LEU LYS ASN ARG ILE GLU ALA SER PRO GLU ALA
SEQRES 15 A 257 ALA GLN ARG ALA SER THR ILE PRO LEU LEU LEU CYS HIS
SEQRES 16 A 257 GLY LYS ALA ASP ASP VAL VAL LEU TYR LYS HIS GLY GLN
SEQRES 17 A 257 ARG SER THR ASP ALA LEU LYS ALA ASN GLY PHE SER ASN
SEQRES 18 A 257 VAL LEU PHE LYS SER TYR ASN SER LEU GLY HIS TYR THR
SEQRES 19 A 257 VAL PRO GLU GLU MET ASP GLU VAL CYS LYS TRP LEU THR
SEQRES 20 A 257 ALA ASN LEU GLY LEU GLY THR SER SER SER
SEQRES 1 B 257 GLY PRO MET SER TYR GLY GLY SER SER SER LEU ALA PRO
SEQRES 2 B 257 GLY ALA LYS ARG PRO PHE GLU TYR GLY ARG THR HIS VAL
SEQRES 3 B 257 VAL ARG PRO LYS GLY THR HIS LYS ALA THR ILE VAL TRP
SEQRES 4 B 257 LEU HIS GLY LEU GLY ASP ASN GLY THR SER TRP SER GLN
SEQRES 5 B 257 LEU LEU GLU THR LEU PRO LEU PRO ASN ILE LYS TRP ILE
SEQRES 6 B 257 CYS PRO THR ALA PRO SER ARG PRO VAL SER LEU PHE GLY
SEQRES 7 B 257 GLY PHE PRO CYS THR ALA TRP PHE ASP VAL ALA ASP LEU
SEQRES 8 B 257 SER GLU ASP ALA PRO ASP ASP THR GLU GLY MET ASP ALA
SEQRES 9 B 257 SER ALA ALA HIS VAL ALA ASN LEU LEU SER THR GLU PRO
SEQRES 10 B 257 ALA ASP ILE LYS LEU GLY VAL GLY GLY PHE SER MET GLY
SEQRES 11 B 257 ALA ALA THR ALA LEU TYR SER ALA THR CYS PHE ALA HIS
SEQRES 12 B 257 GLY LYS TYR GLY ASN GLY ASN PRO TYR PRO VAL ASN LEU
SEQRES 13 B 257 SER LEU ALA VAL GLY LEU SER GLY TRP LEU PRO CYS ALA
SEQRES 14 B 257 ARG THR LEU LYS ASN ARG ILE GLU ALA SER PRO GLU ALA
SEQRES 15 B 257 ALA GLN ARG ALA SER THR ILE PRO LEU LEU LEU CYS HIS
SEQRES 16 B 257 GLY LYS ALA ASP ASP VAL VAL LEU TYR LYS HIS GLY GLN
SEQRES 17 B 257 ARG SER THR ASP ALA LEU LYS ALA ASN GLY PHE SER ASN
SEQRES 18 B 257 VAL LEU PHE LYS SER TYR ASN SER LEU GLY HIS TYR THR
SEQRES 19 B 257 VAL PRO GLU GLU MET ASP GLU VAL CYS LYS TRP LEU THR
SEQRES 20 B 257 ALA ASN LEU GLY LEU GLY THR SER SER SER
FORMUL 3 HOH *202(H2 O)
HELIX 1 AA1 ASN A 44 GLU A 53 1 10
HELIX 2 AA2 SER A 73 GLY A 76 5 4
HELIX 3 AA3 ASP A 96 SER A 112 1 17
HELIX 4 AA4 SER A 126 GLY A 142 1 17
HELIX 5 AA5 THR A 169 GLU A 175 1 7
HELIX 6 AA6 SER A 177 ILE A 187 1 11
HELIX 7 AA7 LEU A 201 ASN A 215 1 15
HELIX 8 AA8 VAL A 233 LEU A 248 1 16
HELIX 9 AA9 ASN B 44 GLU B 53 1 10
HELIX 10 AB1 SER B 73 GLY B 76 5 4
HELIX 11 AB2 ASP B 96 SER B 112 1 17
HELIX 12 AB3 SER B 126 GLY B 142 1 17
HELIX 13 AB4 CYS B 166 ARG B 168 5 3
HELIX 14 AB5 THR B 169 GLU B 175 1 7
HELIX 15 AB6 SER B 177 ILE B 187 1 11
HELIX 16 AB7 LEU B 201 ASN B 215 1 15
HELIX 17 AB8 VAL B 233 GLY B 249 1 17
SHEET 1 AA1 7 HIS A 23 VAL A 25 0
SHEET 2 AA1 7 ILE A 60 CYS A 64 -1 O TRP A 62 N VAL A 25
SHEET 3 AA1 7 ALA A 33 LEU A 38 1 N ALA A 33 O LYS A 61
SHEET 4 AA1 7 LYS A 119 PHE A 125 1 O LYS A 119 N THR A 34
SHEET 5 AA1 7 LEU A 156 LEU A 160 1 O LEU A 160 N GLY A 124
SHEET 6 AA1 7 LEU A 189 GLY A 194 1 O LEU A 190 N GLY A 159
SHEET 7 AA1 7 VAL A 220 TYR A 225 1 O LEU A 221 N LEU A 191
SHEET 1 AA2 2 SER A 69 PRO A 71 0
SHEET 2 AA2 2 PRO A 79 THR A 81 -1 O CYS A 80 N ARG A 70
SHEET 1 AA3 7 HIS B 23 VAL B 25 0
SHEET 2 AA3 7 ILE B 60 CYS B 64 -1 O TRP B 62 N VAL B 25
SHEET 3 AA3 7 ALA B 33 LEU B 38 1 N ALA B 33 O LYS B 61
SHEET 4 AA3 7 LYS B 119 PHE B 125 1 O LYS B 119 N THR B 34
SHEET 5 AA3 7 LEU B 156 LEU B 160 1 O LEU B 160 N GLY B 124
SHEET 6 AA3 7 LEU B 189 GLY B 194 1 O LEU B 190 N GLY B 159
SHEET 7 AA3 7 VAL B 220 TYR B 225 1 O LEU B 221 N LEU B 191
SHEET 1 AA4 2 SER B 69 PRO B 71 0
SHEET 2 AA4 2 PRO B 79 THR B 81 -1 O CYS B 80 N ARG B 70
CISPEP 1 TYR B 19 GLY B 20 0 4.65
CRYST1 48.880 89.570 105.210 90.00 90.00 90.00 P 21 21 21 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 0.020458 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009505 0.00000
TER 1740 GLY A 249
TER 3489 GLY B 249
MASTER 339 0 0 17 18 0 0 6 3689 2 0 40
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