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HEADER HYDROLASE 21-FEB-22 7X0C
TITLE CRYSTAL STRUCTURE OF PHOSPHOLIPASE A1, ATDSEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE A1-IIGAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DAD1-LIKE SEEDLING ESTABLISHMENT-RELATED LIPASE,ATDSEL,
COMPND 5 PHOSPHOLIPASE DSEL;
COMPND 6 EC: 3.1.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: DSEL, AT4G18550, F28J12.210;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOSPHOLIPASE A1, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.HEO,I.LEE,S.MOON,W.LEE
REVDAT 1 13-APR-22 7X0C 0
JRNL AUTH Y.HEO,I.LEE,S.MOON,J.YUN,E.KIM,S.PARK,J.PARK,W.KIM,W.LEE
JRNL TITL CRYSTAL STRUCTURES OF THE PLANT PHOSPHOLIPASE A1 PROTEINS
JRNL TITL 2 REVEAL A UNIQUE DIMERIZATION DOMAIN
JRNL REF MOLECULES 2022
JRNL REFN ESSN 1420-3049
JRNL DOI 10.3390/MOLECULES27072317
REMARK 2
REMARK 2 RESOLUTION. 1.80 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.354
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 98085
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.995
REMARK 3 FREE R VALUE TEST SET COUNT : 4899
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 33.2867 - 5.5817 0.98 3154 158 0.1755 0.1899
REMARK 3 2 5.5817 - 4.4337 0.99 3111 152 0.1642 0.2046
REMARK 3 3 4.4337 - 3.8742 0.98 3108 150 0.1609 0.2006
REMARK 3 4 3.8742 - 3.5204 0.99 3086 158 0.1852 0.1817
REMARK 3 5 3.5204 - 3.2683 1.00 3125 161 0.1828 0.2164
REMARK 3 6 3.2683 - 3.0758 1.00 3123 156 0.1910 0.2262
REMARK 3 7 3.0758 - 2.9218 1.00 3127 166 0.1860 0.2202
REMARK 3 8 2.9218 - 2.7947 1.00 3137 150 0.1881 0.2176
REMARK 3 9 2.7947 - 2.6872 1.00 3115 164 0.1750 0.1935
REMARK 3 10 2.6872 - 2.5945 1.00 3103 186 0.1798 0.1946
REMARK 3 11 2.5945 - 2.5134 1.00 3086 163 0.1788 0.2535
REMARK 3 12 2.5134 - 2.4416 1.00 3102 181 0.1820 0.2041
REMARK 3 13 2.4416 - 2.3773 1.00 3103 170 0.1786 0.2388
REMARK 3 14 2.3773 - 2.3193 1.00 3107 162 0.1760 0.2096
REMARK 3 15 2.3193 - 2.2666 1.00 3128 152 0.1718 0.2237
REMARK 3 16 2.2666 - 2.2184 1.00 3115 153 0.1777 0.2051
REMARK 3 17 2.2184 - 2.1740 1.00 3061 189 0.1766 0.2206
REMARK 3 18 2.1740 - 2.1330 1.00 3134 179 0.1775 0.2288
REMARK 3 19 2.1330 - 2.0949 1.00 3083 194 0.1787 0.2181
REMARK 3 20 2.0949 - 2.0594 1.00 3093 145 0.1833 0.2125
REMARK 3 21 2.0594 - 2.0262 1.00 3120 152 0.1832 0.2414
REMARK 3 22 2.0262 - 1.9950 1.00 3094 178 0.1801 0.2156
REMARK 3 23 1.9950 - 1.9657 1.00 3144 141 0.1786 0.2224
REMARK 3 24 1.9657 - 1.9380 1.00 3094 160 0.1775 0.2405
REMARK 3 25 1.9380 - 1.9118 1.00 3102 164 0.1780 0.1995
REMARK 3 26 1.9118 - 1.8870 1.00 3100 159 0.1788 0.2211
REMARK 3 27 1.8870 - 1.8634 1.00 3114 171 0.1877 0.2464
REMARK 3 28 1.8634 - 1.8409 1.00 3078 167 0.1923 0.2407
REMARK 3 29 1.8409 - 1.8195 1.00 3130 167 0.1902 0.2153
REMARK 3 30 1.8195 - 1.7991 0.99 3009 151 0.2014 0.2277
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.167
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.684
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.08
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.94
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 : 0.012 6563
REMARK 3 ANGLE : 1.127 8881
REMARK 3 CHIRALITY : 0.076 937
REMARK 3 PLANARITY : 0.008 1159
REMARK 3 DIHEDRAL : 14.258 3881
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 7X0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-FEB-22.
REMARK 100 THE DEPOSITION ID IS D_1300027808.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0082
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 105892
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.799
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 35.2900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 2YIJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.02M CALCIUM CHLORIDE, 0.1M SODIUM
REMARK 280 ACETATE, 30% MPD, 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 47.67150
REMARK 290 SMTRY3 2 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: 2800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 GLY A 0
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 ARG A 3
REMARK 465 LYS A 4
REMARK 465 LYS A 5
REMARK 465 LYS A 6
REMARK 465 GLU A 7
REMARK 465 GLU A 8
REMARK 465 GLU A 9
REMARK 465 GLU A 10
REMARK 465 GLU A 11
REMARK 465 LYS A 12
REMARK 465 LEU A 13
REMARK 465 ARG A 120
REMARK 465 GLU A 121
REMARK 465 PRO A 159
REMARK 465 LEU A 160
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 ARG B 3
REMARK 465 LYS B 4
REMARK 465 LYS B 5
REMARK 465 LYS B 6
REMARK 465 GLU B 7
REMARK 465 GLU B 8
REMARK 465 GLU B 9
REMARK 465 GLU B 10
REMARK 465 GLU B 11
REMARK 465 LYS B 12
REMARK 465 LEU B 13
REMARK 465 ILE B 14
REMARK 465 VAL B 15
REMARK 465 THR B 16
REMARK 465 ARG B 120
REMARK 465 GLU B 121
REMARK 465 PRO B 159
REMARK 465 LEU B 160
REMARK 465 GLU B 161
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 NH2 ARG A 24 OE2 GLU A 227 2.03
REMARK 500 O SER B 119 NZ LYS B 125 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 154 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 154 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP B 413 CB - CG - OD1 ANGL. DEV. = 7.2 DEGREES
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 GLU A 87 -56.92 -120.67
REMARK 500 THR A 93 56.03 -92.60
REMARK 500 GLU A 126 -6.19 -140.65
REMARK 500 SER A 236 -122.50 63.54
REMARK 500 VAL A 407 75.44 -114.74
REMARK 500 GLU B 87 -57.15 -120.30
REMARK 500 THR B 93 55.84 -90.50
REMARK 500 GLU B 126 -2.68 -140.45
REMARK 500 GLU B 167 85.76 -66.64
REMARK 500 SER B 236 -121.69 62.26
REMARK 500 VAL B 407 73.81 -113.05
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7X0C A 1 419 UNP O49523 DSEL_ARATH 1 419
DBREF 7X0C B 1 419 UNP O49523 DSEL_ARATH 1 419
SEQADV 7X0C GLY A 0 UNP O49523 EXPRESSION TAG
SEQADV 7X0C GLY B 0 UNP O49523 EXPRESSION TAG
SEQRES 1 A 420 GLY MET LYS ARG LYS LYS LYS GLU GLU GLU GLU GLU LYS
SEQRES 2 A 420 LEU ILE VAL THR ARG GLU PHE ALA LYS ARG TRP ARG ASP
SEQRES 3 A 420 LEU SER GLY GLN ASN HIS TRP LYS GLY MET LEU GLN PRO
SEQRES 4 A 420 LEU ASP GLN ASP LEU ARG GLU TYR ILE ILE HIS TYR GLY
SEQRES 5 A 420 GLU MET ALA GLN ALA GLY TYR ASP THR PHE ASN ILE ASN
SEQRES 6 A 420 THR GLU SER GLN PHE ALA GLY ALA SER ILE TYR SER ARG
SEQRES 7 A 420 LYS ASP PHE PHE ALA LYS VAL GLY LEU GLU ILE ALA HIS
SEQRES 8 A 420 PRO TYR THR LYS TYR LYS VAL THR LYS PHE ILE TYR ALA
SEQRES 9 A 420 THR SER ASP ILE HIS VAL PRO GLU SER PHE LEU LEU PHE
SEQRES 10 A 420 PRO ILE SER ARG GLU GLY TRP SER LYS GLU SER ASN TRP
SEQRES 11 A 420 MET GLY TYR VAL ALA VAL THR ASP ASP GLN GLY THR ALA
SEQRES 12 A 420 LEU LEU GLY ARG ARG ASP ILE VAL VAL SER TRP ARG GLY
SEQRES 13 A 420 SER VAL GLN PRO LEU GLU TRP VAL GLU ASP PHE GLU PHE
SEQRES 14 A 420 GLY LEU VAL ASN ALA ILE LYS ILE PHE GLY GLU ARG ASN
SEQRES 15 A 420 ASP GLN VAL GLN ILE HIS GLN GLY TRP TYR SER ILE TYR
SEQRES 16 A 420 MET SER GLN ASP GLU ARG SER PRO PHE THR LYS THR ASN
SEQRES 17 A 420 ALA ARG ASP GLN VAL LEU ARG GLU VAL GLY ARG LEU LEU
SEQRES 18 A 420 GLU LYS TYR LYS ASP GLU GLU VAL SER ILE THR ILE CYS
SEQRES 19 A 420 GLY HIS SER LEU GLY ALA ALA LEU ALA THR LEU SER ALA
SEQRES 20 A 420 THR ASP ILE VAL ALA ASN GLY TYR ASN ARG PRO LYS SER
SEQRES 21 A 420 ARG PRO ASP LYS SER CYS PRO VAL THR ALA PHE VAL PHE
SEQRES 22 A 420 ALA SER PRO ARG VAL GLY ASP SER ASP PHE ARG LYS LEU
SEQRES 23 A 420 PHE SER GLY LEU GLU ASP ILE ARG VAL LEU ARG THR ARG
SEQRES 24 A 420 ASN LEU PRO ASP VAL ILE PRO ILE TYR PRO PRO ILE GLY
SEQRES 25 A 420 TYR SER GLU VAL GLY ASP GLU PHE PRO ILE ASP THR ARG
SEQRES 26 A 420 LYS SER PRO TYR MET LYS SER PRO GLY ASN LEU ALA THR
SEQRES 27 A 420 PHE HIS CYS LEU GLU GLY TYR LEU HIS GLY VAL ALA GLY
SEQRES 28 A 420 THR GLN GLY THR ASN LYS ALA ASP LEU PHE ARG LEU ASP
SEQRES 29 A 420 VAL GLU ARG ALA ILE GLY LEU VAL ASN LYS SER VAL ASP
SEQRES 30 A 420 GLY LEU LYS ASP GLU CYS MET VAL PRO GLY LYS TRP ARG
SEQRES 31 A 420 VAL LEU LYS ASN LYS GLY MET ALA GLN GLN ASP ASP GLY
SEQRES 32 A 420 SER TRP GLU LEU VAL ASP HIS GLU ILE ASP ASP ASN GLU
SEQRES 33 A 420 ASP LEU ASP PHE
SEQRES 1 B 420 GLY MET LYS ARG LYS LYS LYS GLU GLU GLU GLU GLU LYS
SEQRES 2 B 420 LEU ILE VAL THR ARG GLU PHE ALA LYS ARG TRP ARG ASP
SEQRES 3 B 420 LEU SER GLY GLN ASN HIS TRP LYS GLY MET LEU GLN PRO
SEQRES 4 B 420 LEU ASP GLN ASP LEU ARG GLU TYR ILE ILE HIS TYR GLY
SEQRES 5 B 420 GLU MET ALA GLN ALA GLY TYR ASP THR PHE ASN ILE ASN
SEQRES 6 B 420 THR GLU SER GLN PHE ALA GLY ALA SER ILE TYR SER ARG
SEQRES 7 B 420 LYS ASP PHE PHE ALA LYS VAL GLY LEU GLU ILE ALA HIS
SEQRES 8 B 420 PRO TYR THR LYS TYR LYS VAL THR LYS PHE ILE TYR ALA
SEQRES 9 B 420 THR SER ASP ILE HIS VAL PRO GLU SER PHE LEU LEU PHE
SEQRES 10 B 420 PRO ILE SER ARG GLU GLY TRP SER LYS GLU SER ASN TRP
SEQRES 11 B 420 MET GLY TYR VAL ALA VAL THR ASP ASP GLN GLY THR ALA
SEQRES 12 B 420 LEU LEU GLY ARG ARG ASP ILE VAL VAL SER TRP ARG GLY
SEQRES 13 B 420 SER VAL GLN PRO LEU GLU TRP VAL GLU ASP PHE GLU PHE
SEQRES 14 B 420 GLY LEU VAL ASN ALA ILE LYS ILE PHE GLY GLU ARG ASN
SEQRES 15 B 420 ASP GLN VAL GLN ILE HIS GLN GLY TRP TYR SER ILE TYR
SEQRES 16 B 420 MET SER GLN ASP GLU ARG SER PRO PHE THR LYS THR ASN
SEQRES 17 B 420 ALA ARG ASP GLN VAL LEU ARG GLU VAL GLY ARG LEU LEU
SEQRES 18 B 420 GLU LYS TYR LYS ASP GLU GLU VAL SER ILE THR ILE CYS
SEQRES 19 B 420 GLY HIS SER LEU GLY ALA ALA LEU ALA THR LEU SER ALA
SEQRES 20 B 420 THR ASP ILE VAL ALA ASN GLY TYR ASN ARG PRO LYS SER
SEQRES 21 B 420 ARG PRO ASP LYS SER CYS PRO VAL THR ALA PHE VAL PHE
SEQRES 22 B 420 ALA SER PRO ARG VAL GLY ASP SER ASP PHE ARG LYS LEU
SEQRES 23 B 420 PHE SER GLY LEU GLU ASP ILE ARG VAL LEU ARG THR ARG
SEQRES 24 B 420 ASN LEU PRO ASP VAL ILE PRO ILE TYR PRO PRO ILE GLY
SEQRES 25 B 420 TYR SER GLU VAL GLY ASP GLU PHE PRO ILE ASP THR ARG
SEQRES 26 B 420 LYS SER PRO TYR MET LYS SER PRO GLY ASN LEU ALA THR
SEQRES 27 B 420 PHE HIS CYS LEU GLU GLY TYR LEU HIS GLY VAL ALA GLY
SEQRES 28 B 420 THR GLN GLY THR ASN LYS ALA ASP LEU PHE ARG LEU ASP
SEQRES 29 B 420 VAL GLU ARG ALA ILE GLY LEU VAL ASN LYS SER VAL ASP
SEQRES 30 B 420 GLY LEU LYS ASP GLU CYS MET VAL PRO GLY LYS TRP ARG
SEQRES 31 B 420 VAL LEU LYS ASN LYS GLY MET ALA GLN GLN ASP ASP GLY
SEQRES 32 B 420 SER TRP GLU LEU VAL ASP HIS GLU ILE ASP ASP ASN GLU
SEQRES 33 B 420 ASP LEU ASP PHE
FORMUL 3 HOH *423(H2 O)
HELIX 1 AA1 ARG A 17 SER A 27 1 11
HELIX 2 AA2 ASP A 40 PHE A 61 1 22
HELIX 3 AA3 ASP A 79 VAL A 84 1 6
HELIX 4 AA4 ASP A 137 GLY A 145 1 9
HELIX 5 AA5 TRP A 162 GLU A 167 5 6
HELIX 6 AA6 ALA A 173 GLY A 178 1 6
HELIX 7 AA7 GLU A 179 ASP A 182 5 4
HELIX 8 AA8 GLN A 188 SER A 196 1 9
HELIX 9 AA9 ASN A 207 TYR A 223 1 17
HELIX 10 AB1 SER A 236 ASN A 252 1 17
HELIX 11 AB2 ASP A 279 GLY A 288 1 10
HELIX 12 AB3 VAL A 303 TYR A 307 5 5
HELIX 13 AB4 ASP A 322 SER A 326 5 5
HELIX 14 AB5 ASN A 334 CYS A 340 1 7
HELIX 15 AB6 CYS A 340 THR A 351 1 12
HELIX 16 AB7 ALA A 367 SER A 374 5 8
HELIX 17 AB8 LYS A 379 MET A 383 5 5
HELIX 18 AB9 LEU A 391 LYS A 394 5 4
HELIX 19 AC1 GLU B 18 SER B 27 1 10
HELIX 20 AC2 ASP B 40 PHE B 61 1 22
HELIX 21 AC3 ASP B 79 VAL B 84 1 6
HELIX 22 AC4 ASP B 137 GLY B 145 1 9
HELIX 23 AC5 TRP B 162 GLU B 167 5 6
HELIX 24 AC6 ALA B 173 GLY B 178 1 6
HELIX 25 AC7 GLU B 179 ASP B 182 5 4
HELIX 26 AC8 GLN B 188 SER B 196 1 9
HELIX 27 AC9 ASN B 207 TYR B 223 1 17
HELIX 28 AD1 SER B 236 ASN B 252 1 17
HELIX 29 AD2 ASP B 279 GLY B 288 1 10
HELIX 30 AD3 VAL B 303 TYR B 307 5 5
HELIX 31 AD4 ASP B 322 SER B 326 5 5
HELIX 32 AD5 ASN B 334 CYS B 340 1 7
HELIX 33 AD6 CYS B 340 THR B 351 1 12
HELIX 34 AD7 ALA B 367 SER B 374 5 8
HELIX 35 AD8 LYS B 379 MET B 383 5 5
HELIX 36 AD9 LEU B 391 LYS B 394 5 4
SHEET 1 AA1 7 TYR A 95 ALA A 103 0
SHEET 2 AA1 7 ASN A 128 THR A 136 -1 O MET A 130 N ILE A 101
SHEET 3 AA1 7 ARG A 147 TRP A 153 -1 O SER A 152 N TYR A 132
SHEET 4 AA1 7 VAL A 228 HIS A 235 1 O SER A 229 N ILE A 149
SHEET 5 AA1 7 VAL A 267 PHE A 272 1 O THR A 268 N ILE A 230
SHEET 6 AA1 7 ILE A 292 ASN A 299 1 O THR A 297 N VAL A 271
SHEET 7 AA1 7 ASP A 317 ILE A 321 1 O ASP A 317 N ARG A 296
SHEET 1 AA2 2 LEU A 170 ASN A 172 0
SHEET 2 AA2 2 GLN A 185 HIS A 187 -1 O ILE A 186 N VAL A 171
SHEET 1 AA3 2 MET A 396 GLN A 398 0
SHEET 2 AA3 2 TRP A 404 LEU A 406 -1 O GLU A 405 N ALA A 397
SHEET 1 AA4 7 TYR B 95 ALA B 103 0
SHEET 2 AA4 7 ASN B 128 THR B 136 -1 O MET B 130 N ILE B 101
SHEET 3 AA4 7 ARG B 147 TRP B 153 -1 O SER B 152 N TYR B 132
SHEET 4 AA4 7 VAL B 228 HIS B 235 1 O THR B 231 N ILE B 149
SHEET 5 AA4 7 VAL B 267 PHE B 272 1 O THR B 268 N ILE B 230
SHEET 6 AA4 7 ILE B 292 ASN B 299 1 O THR B 297 N VAL B 271
SHEET 7 AA4 7 ASP B 317 ILE B 321 1 O ASP B 317 N ARG B 296
SHEET 1 AA5 2 LEU B 170 ASN B 172 0
SHEET 2 AA5 2 GLN B 185 HIS B 187 -1 O ILE B 186 N VAL B 171
SHEET 1 AA6 2 MET B 396 GLN B 398 0
SHEET 2 AA6 2 TRP B 404 LEU B 406 -1 O GLU B 405 N ALA B 397
CISPEP 1 GLN A 37 PRO A 38 0 -2.31
CISPEP 2 TYR A 307 PRO A 308 0 -6.40
CISPEP 3 SER A 331 PRO A 332 0 -5.18
CISPEP 4 GLN B 37 PRO B 38 0 -2.06
CISPEP 5 TYR B 307 PRO B 308 0 -3.68
CISPEP 6 SER B 331 PRO B 332 0 -1.19
CRYST1 73.977 95.343 79.278 90.00 105.14 90.00 P 1 21 1 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 0.013518 0.000000 0.003658 0.00000
SCALE2 0.000000 0.010488 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013068 0.00000
TER 3221 PHE A 419
TER 6411 PHE B 419
MASTER 320 0 0 36 22 0 0 6 6832 2 0 66
END |