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HEADER HYDROLASE 20-MAY-15 4ZXF
TITLE CRYSTAL STRUCTURE OF A SOLUBLE VARIANT OF MONOGLYCERIDE LIPASE FROM
TITLE 2 SACCHAROMYCES CEREVISIAE IN COMPLEX WITH A SUBSTRATE ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOGLYCERIDE LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: MGL,MONOACYLGLYCEROL HYDROLASE,MGH,MONOACYLGLYCEROL LIPASE,
COMPND 5 MAGL,SERINE HYDROLASE YJU3;
COMPND 6 EC: 3.1.1.23;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: YJU3, YKL094W, YKL441;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HYDROLASE, MONOGLYCERIDE LIPASE, MONOACYLGLYCEROL LIPASE, COMPLEX,
KEYWDS 2 SUBSTRATE ANALOG
EXPDTA X-RAY DIFFRACTION
AUTHOR P.ASCHAUER,J.LICHTENEGGER,S.RENGACHARI,K.GRUBER,M.OBERER
REVDAT 1 25-MAY-16 4ZXF 0
JRNL AUTH P.ASCHAUER,S.RENGACHARI,J.LICHTENEGGER,M.SCHITTMAYER,
JRNL AUTH 2 K.M.DAS,N.MAYER,R.BREINBAUER,R.BIRNER-GRUENBERGER,
JRNL AUTH 3 C.C.GRUBER,R.ZIMMERMANN,K.GRUBER,M.OBERER
JRNL TITL CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE
JRNL TITL 2 MONOGLYCERIDE LIPASE YJU3P.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1861 462 2016
JRNL REFN ISSN 0006-3002
JRNL PMID 26869448
JRNL DOI 10.1016/J.BBALIP.2016.02.005
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 47713
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2409
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 65.4984 - 6.4264 0.99 2861 139 0.1766 0.2079
REMARK 3 2 6.4264 - 5.1014 0.99 2711 143 0.1781 0.2301
REMARK 3 3 5.1014 - 4.4567 1.00 2704 145 0.1580 0.2182
REMARK 3 4 4.4567 - 4.0493 1.00 2701 128 0.1561 0.2042
REMARK 3 5 4.0493 - 3.7591 1.00 2712 125 0.1765 0.2157
REMARK 3 6 3.7591 - 3.5375 1.00 2683 137 0.1893 0.2317
REMARK 3 7 3.5375 - 3.3603 1.00 2647 144 0.2008 0.2528
REMARK 3 8 3.3603 - 3.2141 1.00 2643 147 0.2112 0.2760
REMARK 3 9 3.2141 - 3.0903 0.99 2630 135 0.2244 0.2923
REMARK 3 10 3.0903 - 2.9837 0.99 2615 161 0.2394 0.3543
REMARK 3 11 2.9837 - 2.8904 1.00 2633 163 0.2438 0.2744
REMARK 3 12 2.8904 - 2.8078 1.00 2628 141 0.2524 0.3284
REMARK 3 13 2.8078 - 2.7339 1.00 2625 154 0.2547 0.3040
REMARK 3 14 2.7339 - 2.6672 1.00 2648 144 0.2778 0.3530
REMARK 3 15 2.6672 - 2.6065 1.00 2613 159 0.2930 0.3518
REMARK 3 16 2.6065 - 2.5511 0.99 2610 127 0.3016 0.3765
REMARK 3 17 2.5511 - 2.5000 0.99 2640 117 0.3137 0.3762
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) : 0.400
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.540
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 43.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.004 10072
REMARK 3 ANGLE : 0.806 13579
REMARK 3 CHIRALITY : 0.040 1389
REMARK 3 PLANARITY : 0.004 1762
REMARK 3 DIHEDRAL : 14.074 3754
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 4ZXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000210042.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97939
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.21
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47793
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 165.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.17900
REMARK 200 FOR THE DATA SET : 6.5000
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) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.84600
REMARK 200 R SYM FOR SHELL (I) : 0.84600
REMARK 200 FOR SHELL : 0.800
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: 4ZWN
REMARK 200
REMARK 200 REMARK: CLUSTERED PLATES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BICINE/TRIZMA BASE PH 8.7, 10%
REMARK 280 W/V PEG 20 000, 20% V/V PEG MME 550 AND 0.03 M SODIUM NITRATE,
REMARK 280 0.03 M DISODIUM HYDROGEN PHOSPHATE, 0.03 M AMMONIUM SULPHATE,
REMARK 280 MICROSEEDING, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
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 38.38000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.72500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.56500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.72500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.38000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.56500
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, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
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: C
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: 4
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: 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 -26
REMARK 465 SER A -25
REMARK 465 TYR A -24
REMARK 465 TYR A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 ASP A -16
REMARK 465 TYR A -15
REMARK 465 ASP A -14
REMARK 465 ILE A -13
REMARK 465 PRO A -12
REMARK 465 THR A -11
REMARK 465 THR A -10
REMARK 465 GLU A -9
REMARK 465 ASN A -8
REMARK 465 LEU A -7
REMARK 465 TYR A -6
REMARK 465 PHE A -5
REMARK 465 GLN A -4
REMARK 465 GLY A -3
REMARK 465 ALA A -2
REMARK 465 MET A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 GLU A 310
REMARK 465 ALA A 311
REMARK 465 LYS A 312
REMARK 465 PRO A 313
REMARK 465 MET B -26
REMARK 465 SER B -25
REMARK 465 TYR B -24
REMARK 465 TYR B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 ASP B -16
REMARK 465 TYR B -15
REMARK 465 ASP B -14
REMARK 465 ILE B -13
REMARK 465 PRO B -12
REMARK 465 THR B -11
REMARK 465 THR B -10
REMARK 465 GLU B -9
REMARK 465 ASN B -8
REMARK 465 LEU B -7
REMARK 465 TYR B -6
REMARK 465 PHE B -5
REMARK 465 GLN B -4
REMARK 465 GLY B -3
REMARK 465 ALA B -2
REMARK 465 MET B -1
REMARK 465 GLY B 0
REMARK 465 THR B 36
REMARK 465 ASN B 37
REMARK 465 GLU B 38
REMARK 465 ALA B 311
REMARK 465 LYS B 312
REMARK 465 PRO B 313
REMARK 465 MET C -26
REMARK 465 SER C -25
REMARK 465 TYR C -24
REMARK 465 TYR C -23
REMARK 465 HIS C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 ASP C -16
REMARK 465 TYR C -15
REMARK 465 ASP C -14
REMARK 465 ILE C -13
REMARK 465 PRO C -12
REMARK 465 THR C -11
REMARK 465 THR C -10
REMARK 465 GLU C -9
REMARK 465 ASN C -8
REMARK 465 LEU C -7
REMARK 465 TYR C -6
REMARK 465 PHE C -5
REMARK 465 GLN C -4
REMARK 465 GLY C -3
REMARK 465 ALA C -2
REMARK 465 MET C -1
REMARK 465 GLY C 0
REMARK 465 THR C 308
REMARK 465 THR C 309
REMARK 465 GLU C 310
REMARK 465 ALA C 311
REMARK 465 LYS C 312
REMARK 465 PRO C 313
REMARK 465 MET D -26
REMARK 465 SER D -25
REMARK 465 TYR D -24
REMARK 465 TYR D -23
REMARK 465 HIS D -22
REMARK 465 HIS D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 ASP D -16
REMARK 465 TYR D -15
REMARK 465 ASP D -14
REMARK 465 ILE D -13
REMARK 465 PRO D -12
REMARK 465 THR D -11
REMARK 465 THR D -10
REMARK 465 GLU D -9
REMARK 465 ASN D -8
REMARK 465 LEU D -7
REMARK 465 TYR D -6
REMARK 465 PHE D -5
REMARK 465 GLN D -4
REMARK 465 GLY D -3
REMARK 465 ALA D -2
REMARK 465 MET D -1
REMARK 465 GLY D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 ASN D 37
REMARK 465 GLU D 38
REMARK 465 VAL D 39
REMARK 465 LEU D 107
REMARK 465 SER D 108
REMARK 465 GLU D 109
REMARK 465 CYS D 110
REMARK 465 LYS D 111
REMARK 465 ALA D 112
REMARK 465 LYS D 113
REMARK 465 GLY D 114
REMARK 465 ILE D 115
REMARK 465 THR D 308
REMARK 465 THR D 309
REMARK 465 GLU D 310
REMARK 465 ALA D 311
REMARK 465 LYS D 312
REMARK 465 PRO D 313
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 OH TYR D 6 OD2 ASP D 61 2.18
REMARK 500 OG1 THR D 11 NE2 GLN D 33 2.19
REMARK 500 OG1 THR D 10 OD1 ASP D 61 2.19
REMARK 500 CB THR D 10 OE1 GLN D 33 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 PRO D 13 C - N - CA ANGL. DEV. = -13.5 DEGREES
REMARK 500 PRO D 13 C - N - CD ANGL. DEV. = 13.9 DEGREES
REMARK 500 GLU D 14 N - CA - C ANGL. DEV. = -17.5 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 SER A 123 -113.30 56.18
REMARK 500 ASP A 240 18.75 59.06
REMARK 500 ARG A 280 -158.01 -109.45
REMARK 500 SER A 285 -48.10 -140.82
REMARK 500 THR A 308 -83.85 -99.79
REMARK 500 THR B 10 -168.08 -101.81
REMARK 500 TYR B 52 -169.65 -167.29
REMARK 500 SER B 123 -117.95 46.90
REMARK 500 HIS B 138 36.46 -98.16
REMARK 500 ASP B 185 76.91 -100.41
REMARK 500 ARG B 280 -159.32 -116.94
REMARK 500 HIS B 281 -70.29 -49.65
REMARK 500 SER B 285 -50.91 -139.16
REMARK 500 TYR C 4 109.96 -59.85
REMARK 500 ASN C 34 24.93 -142.92
REMARK 500 TYR C 52 -168.05 -166.18
REMARK 500 SER C 123 -114.56 52.35
REMARK 500 ASP C 185 78.86 -105.23
REMARK 500 ARG C 280 -155.17 -109.03
REMARK 500 SER C 285 -51.07 -136.99
REMARK 500 TYR D 4 109.68 -54.07
REMARK 500 VAL D 12 -163.44 -77.58
REMARK 500 PRO D 13 -73.09 -109.54
REMARK 500 GLU D 14 151.83 175.94
REMARK 500 LEU D 15 99.52 -165.50
REMARK 500 ASP D 21 -70.13 29.54
REMARK 500 TYR D 52 -160.29 -119.27
REMARK 500 SER D 82 88.49 -161.60
REMARK 500 SER D 123 -120.14 54.07
REMARK 500 LYS D 239 -79.48 -29.24
REMARK 500 ILE D 253 -60.55 -96.68
REMARK 500 ASP D 270 73.23 -116.82
REMARK 500 ARG D 280 -143.33 -119.26
REMARK 500 SER D 285 -61.93 -141.28
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 VAL D 12 PRO D 13 -143.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 4S7 C 500
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4S7 C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 D 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ZWN RELATED DB: PDB
DBREF 4ZXF A 1 313 UNP P28321 MGLL_YEAST 1 313
DBREF 4ZXF B 1 313 UNP P28321 MGLL_YEAST 1 313
DBREF 4ZXF C 1 313 UNP P28321 MGLL_YEAST 1 313
DBREF 4ZXF D 1 313 UNP P28321 MGLL_YEAST 1 313
SEQADV 4ZXF MET A -26 UNP P28321 INITIATING METHIONINE
SEQADV 4ZXF SER A -25 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR A -24 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR A -23 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS A -22 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS A -21 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS A -20 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS A -19 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS A -18 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS A -17 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ASP A -16 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR A -15 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ASP A -14 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ILE A -13 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF PRO A -12 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF THR A -11 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF THR A -10 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLU A -9 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ASN A -8 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF LEU A -7 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR A -6 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF PHE A -5 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLN A -4 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLY A -3 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ALA A -2 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF MET A -1 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLY A 0 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF SER A 175 UNP P28321 LEU 175 ENGINEERED MUTATION
SEQADV 4ZXF ARG A 264 UNP P28321 GLN 264 ENGINEERED MUTATION
SEQADV 4ZXF MET B -26 UNP P28321 INITIATING METHIONINE
SEQADV 4ZXF SER B -25 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR B -24 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR B -23 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS B -22 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS B -21 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS B -20 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS B -19 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS B -18 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS B -17 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ASP B -16 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR B -15 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ASP B -14 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ILE B -13 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF PRO B -12 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF THR B -11 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF THR B -10 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLU B -9 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ASN B -8 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF LEU B -7 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR B -6 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF PHE B -5 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLN B -4 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLY B -3 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ALA B -2 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF MET B -1 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLY B 0 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF SER B 175 UNP P28321 LEU 175 ENGINEERED MUTATION
SEQADV 4ZXF ARG B 264 UNP P28321 GLN 264 ENGINEERED MUTATION
SEQADV 4ZXF MET C -26 UNP P28321 INITIATING METHIONINE
SEQADV 4ZXF SER C -25 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR C -24 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR C -23 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS C -22 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS C -21 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS C -20 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS C -19 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS C -18 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS C -17 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ASP C -16 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR C -15 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ASP C -14 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ILE C -13 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF PRO C -12 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF THR C -11 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF THR C -10 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLU C -9 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ASN C -8 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF LEU C -7 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR C -6 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF PHE C -5 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLN C -4 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLY C -3 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ALA C -2 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF MET C -1 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLY C 0 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF SER C 175 UNP P28321 LEU 175 ENGINEERED MUTATION
SEQADV 4ZXF ARG C 264 UNP P28321 GLN 264 ENGINEERED MUTATION
SEQADV 4ZXF MET D -26 UNP P28321 INITIATING METHIONINE
SEQADV 4ZXF SER D -25 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR D -24 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR D -23 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS D -22 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS D -21 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS D -20 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS D -19 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS D -18 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF HIS D -17 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ASP D -16 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR D -15 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ASP D -14 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ILE D -13 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF PRO D -12 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF THR D -11 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF THR D -10 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLU D -9 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ASN D -8 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF LEU D -7 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF TYR D -6 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF PHE D -5 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLN D -4 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLY D -3 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF ALA D -2 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF MET D -1 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF GLY D 0 UNP P28321 EXPRESSION TAG
SEQADV 4ZXF SER D 175 UNP P28321 LEU 175 ENGINEERED MUTATION
SEQADV 4ZXF ARG D 264 UNP P28321 GLN 264 ENGINEERED MUTATION
SEQRES 1 A 340 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 340 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 A 340 GLY MET ALA PRO TYR PRO TYR LYS VAL GLN THR THR VAL
SEQRES 4 A 340 PRO GLU LEU GLN TYR GLU ASN PHE ASP GLY ALA LYS PHE
SEQRES 5 A 340 GLY TYR MET PHE TRP PRO VAL GLN ASN GLY THR ASN GLU
SEQRES 6 A 340 VAL ARG GLY ARG VAL LEU LEU ILE HIS GLY PHE GLY GLU
SEQRES 7 A 340 TYR THR LYS ILE GLN PHE ARG LEU MET ASP HIS LEU SER
SEQRES 8 A 340 LEU ASN GLY TYR GLU SER PHE THR PHE ASP GLN ARG GLY
SEQRES 9 A 340 ALA GLY VAL THR SER PRO GLY ARG SER LYS GLY VAL THR
SEQRES 10 A 340 ASP GLU TYR HIS VAL PHE ASN ASP LEU GLU HIS PHE VAL
SEQRES 11 A 340 GLU LYS ASN LEU SER GLU CYS LYS ALA LYS GLY ILE PRO
SEQRES 12 A 340 LEU PHE MET TRP GLY HIS SER MET GLY GLY GLY ILE CYS
SEQRES 13 A 340 LEU ASN TYR ALA CYS GLN GLY LYS HIS LYS ASN GLU ILE
SEQRES 14 A 340 SER GLY TYR ILE GLY SER GLY PRO LEU ILE ILE LEU HIS
SEQRES 15 A 340 PRO HIS THR MET TYR ASN LYS PRO THR GLN ILE ILE ALA
SEQRES 16 A 340 PRO LEU LEU ALA LYS PHE SER PRO ARG VAL ARG ILE ASP
SEQRES 17 A 340 THR GLY LEU ASP LEU LYS GLY ILE THR SER ASP LYS ALA
SEQRES 18 A 340 TYR ARG ALA PHE LEU GLY SER ASP PRO MET SER VAL PRO
SEQRES 19 A 340 LEU TYR GLY SER PHE ARG GLN ILE HIS ASP PHE MET GLN
SEQRES 20 A 340 ARG GLY ALA LYS LEU TYR LYS ASN GLU ASN ASN TYR ILE
SEQRES 21 A 340 GLN LYS ASN PHE ALA LYS ASP LYS PRO VAL ILE ILE MET
SEQRES 22 A 340 HIS GLY GLN ASP ASP THR ILE ASN ASP PRO LYS GLY SER
SEQRES 23 A 340 GLU LYS PHE ILE ARG ASP CYS PRO SER ALA ASP LYS GLU
SEQRES 24 A 340 LEU LYS LEU TYR PRO GLY ALA ARG HIS SER ILE PHE SER
SEQRES 25 A 340 LEU GLU THR ASP LYS VAL PHE ASN THR VAL PHE ASN ASP
SEQRES 26 A 340 MET LYS GLN TRP LEU ASP LYS HIS THR THR THR GLU ALA
SEQRES 27 A 340 LYS PRO
SEQRES 1 B 340 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 B 340 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 B 340 GLY MET ALA PRO TYR PRO TYR LYS VAL GLN THR THR VAL
SEQRES 4 B 340 PRO GLU LEU GLN TYR GLU ASN PHE ASP GLY ALA LYS PHE
SEQRES 5 B 340 GLY TYR MET PHE TRP PRO VAL GLN ASN GLY THR ASN GLU
SEQRES 6 B 340 VAL ARG GLY ARG VAL LEU LEU ILE HIS GLY PHE GLY GLU
SEQRES 7 B 340 TYR THR LYS ILE GLN PHE ARG LEU MET ASP HIS LEU SER
SEQRES 8 B 340 LEU ASN GLY TYR GLU SER PHE THR PHE ASP GLN ARG GLY
SEQRES 9 B 340 ALA GLY VAL THR SER PRO GLY ARG SER LYS GLY VAL THR
SEQRES 10 B 340 ASP GLU TYR HIS VAL PHE ASN ASP LEU GLU HIS PHE VAL
SEQRES 11 B 340 GLU LYS ASN LEU SER GLU CYS LYS ALA LYS GLY ILE PRO
SEQRES 12 B 340 LEU PHE MET TRP GLY HIS SER MET GLY GLY GLY ILE CYS
SEQRES 13 B 340 LEU ASN TYR ALA CYS GLN GLY LYS HIS LYS ASN GLU ILE
SEQRES 14 B 340 SER GLY TYR ILE GLY SER GLY PRO LEU ILE ILE LEU HIS
SEQRES 15 B 340 PRO HIS THR MET TYR ASN LYS PRO THR GLN ILE ILE ALA
SEQRES 16 B 340 PRO LEU LEU ALA LYS PHE SER PRO ARG VAL ARG ILE ASP
SEQRES 17 B 340 THR GLY LEU ASP LEU LYS GLY ILE THR SER ASP LYS ALA
SEQRES 18 B 340 TYR ARG ALA PHE LEU GLY SER ASP PRO MET SER VAL PRO
SEQRES 19 B 340 LEU TYR GLY SER PHE ARG GLN ILE HIS ASP PHE MET GLN
SEQRES 20 B 340 ARG GLY ALA LYS LEU TYR LYS ASN GLU ASN ASN TYR ILE
SEQRES 21 B 340 GLN LYS ASN PHE ALA LYS ASP LYS PRO VAL ILE ILE MET
SEQRES 22 B 340 HIS GLY GLN ASP ASP THR ILE ASN ASP PRO LYS GLY SER
SEQRES 23 B 340 GLU LYS PHE ILE ARG ASP CYS PRO SER ALA ASP LYS GLU
SEQRES 24 B 340 LEU LYS LEU TYR PRO GLY ALA ARG HIS SER ILE PHE SER
SEQRES 25 B 340 LEU GLU THR ASP LYS VAL PHE ASN THR VAL PHE ASN ASP
SEQRES 26 B 340 MET LYS GLN TRP LEU ASP LYS HIS THR THR THR GLU ALA
SEQRES 27 B 340 LYS PRO
SEQRES 1 C 340 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 C 340 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 C 340 GLY MET ALA PRO TYR PRO TYR LYS VAL GLN THR THR VAL
SEQRES 4 C 340 PRO GLU LEU GLN TYR GLU ASN PHE ASP GLY ALA LYS PHE
SEQRES 5 C 340 GLY TYR MET PHE TRP PRO VAL GLN ASN GLY THR ASN GLU
SEQRES 6 C 340 VAL ARG GLY ARG VAL LEU LEU ILE HIS GLY PHE GLY GLU
SEQRES 7 C 340 TYR THR LYS ILE GLN PHE ARG LEU MET ASP HIS LEU SER
SEQRES 8 C 340 LEU ASN GLY TYR GLU SER PHE THR PHE ASP GLN ARG GLY
SEQRES 9 C 340 ALA GLY VAL THR SER PRO GLY ARG SER LYS GLY VAL THR
SEQRES 10 C 340 ASP GLU TYR HIS VAL PHE ASN ASP LEU GLU HIS PHE VAL
SEQRES 11 C 340 GLU LYS ASN LEU SER GLU CYS LYS ALA LYS GLY ILE PRO
SEQRES 12 C 340 LEU PHE MET TRP GLY HIS SER MET GLY GLY GLY ILE CYS
SEQRES 13 C 340 LEU ASN TYR ALA CYS GLN GLY LYS HIS LYS ASN GLU ILE
SEQRES 14 C 340 SER GLY TYR ILE GLY SER GLY PRO LEU ILE ILE LEU HIS
SEQRES 15 C 340 PRO HIS THR MET TYR ASN LYS PRO THR GLN ILE ILE ALA
SEQRES 16 C 340 PRO LEU LEU ALA LYS PHE SER PRO ARG VAL ARG ILE ASP
SEQRES 17 C 340 THR GLY LEU ASP LEU LYS GLY ILE THR SER ASP LYS ALA
SEQRES 18 C 340 TYR ARG ALA PHE LEU GLY SER ASP PRO MET SER VAL PRO
SEQRES 19 C 340 LEU TYR GLY SER PHE ARG GLN ILE HIS ASP PHE MET GLN
SEQRES 20 C 340 ARG GLY ALA LYS LEU TYR LYS ASN GLU ASN ASN TYR ILE
SEQRES 21 C 340 GLN LYS ASN PHE ALA LYS ASP LYS PRO VAL ILE ILE MET
SEQRES 22 C 340 HIS GLY GLN ASP ASP THR ILE ASN ASP PRO LYS GLY SER
SEQRES 23 C 340 GLU LYS PHE ILE ARG ASP CYS PRO SER ALA ASP LYS GLU
SEQRES 24 C 340 LEU LYS LEU TYR PRO GLY ALA ARG HIS SER ILE PHE SER
SEQRES 25 C 340 LEU GLU THR ASP LYS VAL PHE ASN THR VAL PHE ASN ASP
SEQRES 26 C 340 MET LYS GLN TRP LEU ASP LYS HIS THR THR THR GLU ALA
SEQRES 27 C 340 LYS PRO
SEQRES 1 D 340 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 D 340 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 D 340 GLY MET ALA PRO TYR PRO TYR LYS VAL GLN THR THR VAL
SEQRES 4 D 340 PRO GLU LEU GLN TYR GLU ASN PHE ASP GLY ALA LYS PHE
SEQRES 5 D 340 GLY TYR MET PHE TRP PRO VAL GLN ASN GLY THR ASN GLU
SEQRES 6 D 340 VAL ARG GLY ARG VAL LEU LEU ILE HIS GLY PHE GLY GLU
SEQRES 7 D 340 TYR THR LYS ILE GLN PHE ARG LEU MET ASP HIS LEU SER
SEQRES 8 D 340 LEU ASN GLY TYR GLU SER PHE THR PHE ASP GLN ARG GLY
SEQRES 9 D 340 ALA GLY VAL THR SER PRO GLY ARG SER LYS GLY VAL THR
SEQRES 10 D 340 ASP GLU TYR HIS VAL PHE ASN ASP LEU GLU HIS PHE VAL
SEQRES 11 D 340 GLU LYS ASN LEU SER GLU CYS LYS ALA LYS GLY ILE PRO
SEQRES 12 D 340 LEU PHE MET TRP GLY HIS SER MET GLY GLY GLY ILE CYS
SEQRES 13 D 340 LEU ASN TYR ALA CYS GLN GLY LYS HIS LYS ASN GLU ILE
SEQRES 14 D 340 SER GLY TYR ILE GLY SER GLY PRO LEU ILE ILE LEU HIS
SEQRES 15 D 340 PRO HIS THR MET TYR ASN LYS PRO THR GLN ILE ILE ALA
SEQRES 16 D 340 PRO LEU LEU ALA LYS PHE SER PRO ARG VAL ARG ILE ASP
SEQRES 17 D 340 THR GLY LEU ASP LEU LYS GLY ILE THR SER ASP LYS ALA
SEQRES 18 D 340 TYR ARG ALA PHE LEU GLY SER ASP PRO MET SER VAL PRO
SEQRES 19 D 340 LEU TYR GLY SER PHE ARG GLN ILE HIS ASP PHE MET GLN
SEQRES 20 D 340 ARG GLY ALA LYS LEU TYR LYS ASN GLU ASN ASN TYR ILE
SEQRES 21 D 340 GLN LYS ASN PHE ALA LYS ASP LYS PRO VAL ILE ILE MET
SEQRES 22 D 340 HIS GLY GLN ASP ASP THR ILE ASN ASP PRO LYS GLY SER
SEQRES 23 D 340 GLU LYS PHE ILE ARG ASP CYS PRO SER ALA ASP LYS GLU
SEQRES 24 D 340 LEU LYS LEU TYR PRO GLY ALA ARG HIS SER ILE PHE SER
SEQRES 25 D 340 LEU GLU THR ASP LYS VAL PHE ASN THR VAL PHE ASN ASP
SEQRES 26 D 340 MET LYS GLN TRP LEU ASP LYS HIS THR THR THR GLU ALA
SEQRES 27 D 340 LYS PRO
HET SO4 A 401 5
HET SO4 B 401 5
HET 4S7 C 500 27
HET NO3 D 401 4
HET NO3 D 402 4
HETNAM SO4 SULFATE ION
HETNAM 4S7 1-{3-[(R)-HYDROXY(OCTADECYLOXY)
HETNAM 2 4S7 PHOSPHORYL]PROPYL}TRIAZA-1,2-DIEN-2-IUM
HETNAM NO3 NITRATE ION
HETSYN 4S7 OCTADECYL HYDROGEN (R)-(3-AZIDOPROPYL)PHOSPHONATE
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 4S7 C21 H45 N3 O3 P 1+
FORMUL 8 NO3 2(N O3 1-)
FORMUL 10 HOH *151(H2 O)
HELIX 1 AA1 TYR A 52 ILE A 55 5 4
HELIX 2 AA2 GLN A 56 ASN A 66 1 11
HELIX 3 AA3 PRO A 83 LYS A 87 5 5
HELIX 4 AA4 ASP A 91 LYS A 113 1 23
HELIX 5 AA5 SER A 123 GLY A 136 1 14
HELIX 6 AA6 HIS A 155 LYS A 162 1 8
HELIX 7 AA7 PRO A 163 LEU A 171 1 9
HELIX 8 AA8 ASP A 185 THR A 190 1 6
HELIX 9 AA9 ASP A 192 ASP A 202 1 11
HELIX 10 AB1 PHE A 212 ASN A 228 1 17
HELIX 11 AB2 ASN A 231 PHE A 237 1 7
HELIX 12 AB3 ASP A 255 CYS A 266 1 12
HELIX 13 AB4 THR A 288 HIS A 306 1 19
HELIX 14 AB5 TYR B 52 ILE B 55 5 4
HELIX 15 AB6 GLN B 56 ASN B 66 1 11
HELIX 16 AB7 PRO B 83 LYS B 87 5 5
HELIX 17 AB8 ASP B 91 CYS B 110 1 20
HELIX 18 AB9 SER B 123 GLY B 136 1 14
HELIX 19 AC1 HIS B 155 LYS B 162 1 8
HELIX 20 AC2 PRO B 163 ALA B 172 1 10
HELIX 21 AC3 ASP B 185 THR B 190 1 6
HELIX 22 AC4 ASP B 192 SER B 201 1 10
HELIX 23 AC5 PHE B 212 ASN B 228 1 17
HELIX 24 AC6 ASN B 231 PHE B 237 1 7
HELIX 25 AC7 ASP B 255 CYS B 266 1 12
HELIX 26 AC8 THR B 288 LYS B 305 1 18
HELIX 27 AC9 TYR C 52 ILE C 55 5 4
HELIX 28 AD1 GLN C 56 ASN C 66 1 11
HELIX 29 AD2 PRO C 83 LYS C 87 5 5
HELIX 30 AD3 ASP C 91 LYS C 113 1 23
HELIX 31 AD4 SER C 123 GLY C 136 1 14
HELIX 32 AD5 HIS C 155 LYS C 162 1 8
HELIX 33 AD6 PRO C 163 GLN C 165 5 3
HELIX 34 AD7 ILE C 166 ALA C 172 1 7
HELIX 35 AD8 ASP C 185 THR C 190 1 6
HELIX 36 AD9 ASP C 192 ASP C 202 1 11
HELIX 37 AE1 PHE C 212 ASN C 228 1 17
HELIX 38 AE2 ASN C 231 PHE C 237 1 7
HELIX 39 AE3 ASP C 255 CYS C 266 1 12
HELIX 40 AE4 THR C 288 HIS C 306 1 19
HELIX 41 AE5 THR D 53 ILE D 55 5 3
HELIX 42 AE6 GLN D 56 ASN D 66 1 11
HELIX 43 AE7 ASP D 91 ASN D 106 1 16
HELIX 44 AE8 SER D 123 GLY D 136 1 14
HELIX 45 AE9 HIS D 155 LYS D 162 1 8
HELIX 46 AF1 PRO D 163 ALA D 172 1 10
HELIX 47 AF2 ASP D 185 THR D 190 1 6
HELIX 48 AF3 ASP D 192 GLY D 200 1 9
HELIX 49 AF4 PHE D 212 ASN D 228 1 17
HELIX 50 AF5 ASN D 231 PHE D 237 1 7
HELIX 51 AF6 ASP D 255 CYS D 266 1 12
HELIX 52 AF7 THR D 288 HIS D 306 1 19
SHEET 1 AA1 8 GLN A 16 PHE A 20 0
SHEET 2 AA1 8 ALA A 23 TRP A 30 -1 O PHE A 25 N GLU A 18
SHEET 3 AA1 8 TYR A 68 PHE A 73 -1 O SER A 70 N TRP A 30
SHEET 4 AA1 8 GLY A 41 ILE A 46 1 N LEU A 45 O PHE A 71
SHEET 5 AA1 8 LEU A 117 HIS A 122 1 O TRP A 120 N ILE A 46
SHEET 6 AA1 8 GLY A 144 SER A 148 1 O SER A 148 N GLY A 121
SHEET 7 AA1 8 VAL A 243 GLY A 248 1 O MET A 246 N GLY A 147
SHEET 8 AA1 8 LYS A 271 TYR A 276 1 O LYS A 274 N ILE A 245
SHEET 1 AA2 2 ARG A 179 ILE A 180 0
SHEET 2 AA2 2 GLY A 210 SER A 211 -1 O GLY A 210 N ILE A 180
SHEET 1 AA3 8 GLN B 16 PHE B 20 0
SHEET 2 AA3 8 ALA B 23 TRP B 30 -1 O PHE B 25 N GLU B 18
SHEET 3 AA3 8 TYR B 68 PHE B 73 -1 O THR B 72 N MET B 28
SHEET 4 AA3 8 GLY B 41 ILE B 46 1 N LEU B 45 O PHE B 71
SHEET 5 AA3 8 LEU B 117 HIS B 122 1 O TRP B 120 N ILE B 46
SHEET 6 AA3 8 GLY B 144 SER B 148 1 O SER B 148 N GLY B 121
SHEET 7 AA3 8 VAL B 243 GLY B 248 1 O MET B 246 N GLY B 147
SHEET 8 AA3 8 LYS B 271 TYR B 276 1 O LYS B 274 N ILE B 245
SHEET 1 AA4 4 LEU B 208 SER B 211 0
SHEET 2 AA4 4 ARG B 179 THR B 182 -1 N ILE B 180 O GLY B 210
SHEET 3 AA4 4 ARG D 179 ASP D 181 -1 O ARG D 179 N ASP B 181
SHEET 4 AA4 4 GLY D 210 SER D 211 -1 O GLY D 210 N ILE D 180
SHEET 1 AA5 8 GLN C 16 ASN C 19 0
SHEET 2 AA5 8 LYS C 24 TRP C 30 -1 O PHE C 25 N GLU C 18
SHEET 3 AA5 8 TYR C 68 PHE C 73 -1 O SER C 70 N TRP C 30
SHEET 4 AA5 8 GLY C 41 ILE C 46 1 N LEU C 45 O PHE C 71
SHEET 5 AA5 8 LEU C 117 HIS C 122 1 O TRP C 120 N ILE C 46
SHEET 6 AA5 8 GLY C 144 SER C 148 1 O ILE C 146 N MET C 119
SHEET 7 AA5 8 VAL C 243 GLY C 248 1 O MET C 246 N GLY C 147
SHEET 8 AA5 8 LYS C 271 TYR C 276 1 O LYS C 274 N ILE C 245
SHEET 1 AA6 2 ARG C 179 ASP C 181 0
SHEET 2 AA6 2 TYR C 209 SER C 211 -1 O GLY C 210 N ILE C 180
SHEET 1 AA7 7 TYR D 27 TRP D 30 0
SHEET 2 AA7 7 TYR D 68 PHE D 73 -1 O SER D 70 N TRP D 30
SHEET 3 AA7 7 GLY D 41 ILE D 46 1 N VAL D 43 O GLU D 69
SHEET 4 AA7 7 LEU D 117 HIS D 122 1 O PHE D 118 N ARG D 42
SHEET 5 AA7 7 GLY D 144 SER D 148 1 O SER D 148 N GLY D 121
SHEET 6 AA7 7 VAL D 243 GLY D 248 1 O MET D 246 N GLY D 147
SHEET 7 AA7 7 LYS D 271 TYR D 276 1 O LYS D 274 N ILE D 245
CISPEP 1 VAL A 206 PRO A 207 0 4.22
CISPEP 2 VAL B 206 PRO B 207 0 1.75
CISPEP 3 VAL C 206 PRO C 207 0 -5.27
CISPEP 4 VAL D 206 PRO D 207 0 1.35
SITE 1 AC1 3 LYS A 187 ARG A 196 ARG A 280
SITE 1 AC2 4 LYS B 187 LYS B 193 ARG B 196 ARG B 280
SITE 1 AC3 14 GLY C 48 PHE C 49 SER C 123 MET C 124
SITE 2 AC3 14 LEU C 151 MET C 159 LYS C 162 GLN C 165
SITE 3 AC3 14 ILE C 166 LEU C 184 LEU C 208 PHE C 218
SITE 4 AC3 14 HIS C 281 MET D 159
SITE 1 AC4 1 PHE A 174
SITE 1 AC5 2 LYS D 193 ARG D 196
CRYST1 76.760 107.130 165.450 90.00 90.00 90.00 P 21 21 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 0.013028 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009334 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006044 0.00000
TER 2470 THR A 309
TER 4933 GLU B 310
TER 7397 THR C 307
TER 9766 THR D 307
MASTER 514 0 5 52 39 0 8 6 9952 4 45 108
END |