| 4zwn-pdb | HEADER HYDROLASE 19-MAY-15 4ZWN
TITLE CRYSTAL STRUCTURE OF A SOLUBLE VARIANT OF THE MONOGLYCERIDE LIPASE
TITLE 2 FROM SACCHAROMYCES CEREVISIAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOGLYCERIDE LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 2-313;
COMPND 5 SYNONYM: MGL,MONOACYLGLYCEROL HYDROLASE,MGH,MONOACYLGLYCEROL LIPASE,
COMPND 6 MAGL,SERINE HYDROLASE YJU3;
COMPND 7 EC: 3.1.1.23;
COMPND 8 ENGINEERED: YES;
COMPND 9 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;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEX HTB
KEYWDS MONOGLYCERIDE LIPASE, MONOACYLGLYCEROL LIPASE, SERINE HYDROLASE,
KEYWDS 2 ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.ASCHAUER,S.RENGACHARI,K.GRUBER,M.OBERER
REVDAT 1 27-APR-16 4ZWN 0
JRNL AUTH P.ASCHAUER,S.RENGACHARI,J.LICHTENEGGER,
JRNL AUTH 2 M.SCHITTMAYER-SCHANTL,N.MAYER,R.BREINBAUER,
JRNL AUTH 3 R.BIRNER-GRUENBERGER,C.C.GRUBER,R.ZIMMERMANN,K.GRUBER,
JRNL AUTH 4 M.OBERER
JRNL TITL THE UNUSUAL SUBSTRATE PREFERENCE OF MONOGYLCERIDE LIPASE
JRNL TITL 2 FROM SACCHAROMYCES CEREVISIAE (YJU3) EXPLAINED BY CRYSTAL
JRNL TITL 3 STRUCTURES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.49 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) : 2.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 49067
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2498
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 45.2776 - 6.5233 0.95 2707 136 0.1487 0.1745
REMARK 3 2 6.5233 - 5.1801 0.99 2687 144 0.1584 0.1782
REMARK 3 3 5.1801 - 4.5260 0.99 2627 156 0.1409 0.1786
REMARK 3 4 4.5260 - 4.1125 0.99 2661 130 0.1437 0.1801
REMARK 3 5 4.1125 - 3.8179 0.99 2591 157 0.1644 0.1836
REMARK 3 6 3.8179 - 3.5929 0.99 2636 139 0.1826 0.2006
REMARK 3 7 3.5929 - 3.4130 0.99 2609 134 0.1979 0.2364
REMARK 3 8 3.4130 - 3.2645 0.99 2613 134 0.2066 0.2480
REMARK 3 9 3.2645 - 3.1389 0.99 2604 137 0.2139 0.2798
REMARK 3 10 3.1389 - 3.0306 0.99 2584 131 0.2186 0.2389
REMARK 3 11 3.0306 - 2.9358 0.99 2591 130 0.2362 0.3097
REMARK 3 12 2.9358 - 2.8519 0.99 2562 139 0.2375 0.2873
REMARK 3 13 2.8519 - 2.7769 0.99 2571 152 0.2412 0.2637
REMARK 3 14 2.7769 - 2.7091 0.99 2589 131 0.2495 0.3178
REMARK 3 15 2.7091 - 2.6475 0.99 2557 139 0.2431 0.2682
REMARK 3 16 2.6475 - 2.5912 0.99 2564 149 0.2533 0.3115
REMARK 3 17 2.5912 - 2.5394 0.98 2587 129 0.2610 0.3231
REMARK 3 18 2.5394 - 2.4915 0.87 2229 131 0.2782 0.3369
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.25
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 : 0.005 10192
REMARK 3 ANGLE : 0.771 13758
REMARK 3 CHIRALITY : 0.040 1415
REMARK 3 PLANARITY : 0.003 1792
REMARK 3 DIHEDRAL : 12.958 3781
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:
REMARK 3 THE AUTHORS PERFORMED MAD EXPERIMENT WITH POTASSIUM TETRA NITRO
REMARK 3 PLATINATE AS HEAVY ATOM COMPLEX USING THE WAVELENGTHS 1.07155(PEAK)
REMARK 3 , 1.07182(INFLECTION) AND 1.06878(REMOTE). THE DATA WAS UPLOADED
REMARK 3 TO THE AUTORICKSHAW SERVER (HTTP://WWW.EMBL-HAMBURG.DE/AUTO-
REMARK 3 RICKSHAW/) AND THEN USED THE BIGGEST FRAGMENT WITH THE BEST E-
REMARK 3 DENSITY FIT OF THE RESULTING MODEL TO DO MOLECULAR REPLACEMENT
REMARK 3 INTO A NATIV DATA SET WITH HIGHER RESOLUTION. AFTER THIS, THE
REMARK 3 MODEL BUILDING PROCESS WAS DONE MANUALLY USING PHENIX.AUTOBUILD.
REMARK 3
REMARK 3 THE DATA IN THE SESSION ARE FOR THE NATIVE DATA SET.
REMARK 3 SO THE PHASING METHOD WAS A MIXTURE OF MR AND MAD.
REMARK 4
REMARK 4 4ZWN 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_1000210013.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-12
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) : 0.9999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.29
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49134
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.490
REMARK 200 RESOLUTION RANGE LOW (A) : 45.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 8.900
REMARK 200 R MERGE (I) : 0.19800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.6
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : 1.49800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: AUTO-RICKSHAW
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
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, SITTING 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 38.59800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.83350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.28300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.83350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.59800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.28300
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 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 ALA A 311
REMARK 465 LYS A 312
REMARK 465 PRO A 313
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 LYS B 312
REMARK 465 PRO B 313
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 309
REMARK 465 GLU C 310
REMARK 465 ALA C 311
REMARK 465 LYS C 312
REMARK 465 PRO C 313
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 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
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASN A 161 NZ LYS D 227 4566 2.17
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 HIS B 281 N - CA - C ANGL. DEV. = 19.9 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 -115.13 50.26
REMARK 500 ILE A 152 -60.33 -109.77
REMARK 500 ILE A 253 -60.71 -99.34
REMARK 500 ARG A 280 -151.83 -124.03
REMARK 500 SER A 285 -47.45 -139.64
REMARK 500 THR A 309 -82.33 -125.86
REMARK 500 THR B 10 -167.13 -106.68
REMARK 500 ASN B 34 40.17 -108.39
REMARK 500 SER B 123 -117.05 50.23
REMARK 500 ARG B 280 -155.65 -109.70
REMARK 500 SER B 285 -54.42 -140.09
REMARK 500 GLU C 38 124.38 -37.43
REMARK 500 SER C 123 -117.19 48.19
REMARK 500 ILE C 152 -60.13 -106.62
REMARK 500 ILE C 253 -62.83 -102.42
REMARK 500 PRO C 277 159.86 -49.50
REMARK 500 ARG C 280 -155.22 -107.48
REMARK 500 SER C 285 -54.38 -140.13
REMARK 500 ASN D 34 -126.75 -156.66
REMARK 500 ASN D 37 12.28 57.41
REMARK 500 SER D 123 -115.43 51.79
REMARK 500 ILE D 152 -60.59 -109.87
REMARK 500 ARG D 280 -156.21 -107.44
REMARK 500 HIS D 281 -73.35 -52.35
REMARK 500 SER D 285 -46.76 -138.13
REMARK 500 THR D 307 11.31 -145.51
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 ASN A 37 GLU A 38 -149.88
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 NO3 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 SO4 C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 401
DBREF 4ZWN A 2 313 UNP P28321 MGLL_YEAST 2 313
DBREF 4ZWN B 2 313 UNP P28321 MGLL_YEAST 2 313
DBREF 4ZWN C 2 313 UNP P28321 MGLL_YEAST 2 313
DBREF 4ZWN D 2 313 UNP P28321 MGLL_YEAST 2 313
SEQADV 4ZWN HIS A -20 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN HIS A -19 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN HIS A -18 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN HIS A -17 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ASP A -16 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN TYR A -15 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ASP A -14 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ILE A -13 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN PRO A -12 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN THR A -11 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN THR A -10 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLU A -9 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ASN A -8 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN LEU A -7 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN TYR A -6 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN PHE A -5 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLN A -4 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLY A -3 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ALA A -2 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN MET A -1 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLY A 0 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN SER A 1 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN SER A 175 UNP P28321 LEU 175 ENGINEERED MUTATION
SEQADV 4ZWN ARG A 264 UNP P28321 GLN 264 ENGINEERED MUTATION
SEQADV 4ZWN HIS B -20 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN HIS B -19 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN HIS B -18 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN HIS B -17 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ASP B -16 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN TYR B -15 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ASP B -14 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ILE B -13 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN PRO B -12 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN THR B -11 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN THR B -10 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLU B -9 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ASN B -8 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN LEU B -7 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN TYR B -6 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN PHE B -5 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLN B -4 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLY B -3 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ALA B -2 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN MET B -1 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLY B 0 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN SER B 1 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN SER B 175 UNP P28321 LEU 175 ENGINEERED MUTATION
SEQADV 4ZWN ARG B 264 UNP P28321 GLN 264 ENGINEERED MUTATION
SEQADV 4ZWN HIS C -20 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN HIS C -19 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN HIS C -18 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN HIS C -17 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ASP C -16 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN TYR C -15 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ASP C -14 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ILE C -13 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN PRO C -12 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN THR C -11 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN THR C -10 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLU C -9 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ASN C -8 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN LEU C -7 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN TYR C -6 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN PHE C -5 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLN C -4 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLY C -3 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ALA C -2 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN MET C -1 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLY C 0 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN SER C 1 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN SER C 175 UNP P28321 LEU 175 ENGINEERED MUTATION
SEQADV 4ZWN ARG C 264 UNP P28321 GLN 264 ENGINEERED MUTATION
SEQADV 4ZWN HIS D -20 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN HIS D -19 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN HIS D -18 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN HIS D -17 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ASP D -16 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN TYR D -15 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ASP D -14 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ILE D -13 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN PRO D -12 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN THR D -11 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN THR D -10 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLU D -9 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ASN D -8 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN LEU D -7 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN TYR D -6 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN PHE D -5 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLN D -4 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLY D -3 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN ALA D -2 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN MET D -1 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN GLY D 0 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN SER D 1 UNP P28321 EXPRESSION TAG
SEQADV 4ZWN SER D 175 UNP P28321 LEU 175 ENGINEERED MUTATION
SEQADV 4ZWN ARG D 264 UNP P28321 GLN 264 ENGINEERED MUTATION
SEQRES 1 A 334 HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR GLU ASN
SEQRES 2 A 334 LEU TYR PHE GLN GLY ALA MET GLY SER ALA PRO TYR PRO
SEQRES 3 A 334 TYR LYS VAL GLN THR THR VAL PRO GLU LEU GLN TYR GLU
SEQRES 4 A 334 ASN PHE ASP GLY ALA LYS PHE GLY TYR MET PHE TRP PRO
SEQRES 5 A 334 VAL GLN ASN GLY THR ASN GLU VAL ARG GLY ARG VAL LEU
SEQRES 6 A 334 LEU ILE HIS GLY PHE GLY GLU TYR THR LYS ILE GLN PHE
SEQRES 7 A 334 ARG LEU MET ASP HIS LEU SER LEU ASN GLY TYR GLU SER
SEQRES 8 A 334 PHE THR PHE ASP GLN ARG GLY ALA GLY VAL THR SER PRO
SEQRES 9 A 334 GLY ARG SER LYS GLY VAL THR ASP GLU TYR HIS VAL PHE
SEQRES 10 A 334 ASN ASP LEU GLU HIS PHE VAL GLU LYS ASN LEU SER GLU
SEQRES 11 A 334 CYS LYS ALA LYS GLY ILE PRO LEU PHE MET TRP GLY HIS
SEQRES 12 A 334 SER MET GLY GLY GLY ILE CYS LEU ASN TYR ALA CYS GLN
SEQRES 13 A 334 GLY LYS HIS LYS ASN GLU ILE SER GLY TYR ILE GLY SER
SEQRES 14 A 334 GLY PRO LEU ILE ILE LEU HIS PRO HIS THR MET TYR ASN
SEQRES 15 A 334 LYS PRO THR GLN ILE ILE ALA PRO LEU LEU ALA LYS PHE
SEQRES 16 A 334 SER PRO ARG VAL ARG ILE ASP THR GLY LEU ASP LEU LYS
SEQRES 17 A 334 GLY ILE THR SER ASP LYS ALA TYR ARG ALA PHE LEU GLY
SEQRES 18 A 334 SER ASP PRO MET SER VAL PRO LEU TYR GLY SER PHE ARG
SEQRES 19 A 334 GLN ILE HIS ASP PHE MET GLN ARG GLY ALA LYS LEU TYR
SEQRES 20 A 334 LYS ASN GLU ASN ASN TYR ILE GLN LYS ASN PHE ALA LYS
SEQRES 21 A 334 ASP LYS PRO VAL ILE ILE MET HIS GLY GLN ASP ASP THR
SEQRES 22 A 334 ILE ASN ASP PRO LYS GLY SER GLU LYS PHE ILE ARG ASP
SEQRES 23 A 334 CYS PRO SER ALA ASP LYS GLU LEU LYS LEU TYR PRO GLY
SEQRES 24 A 334 ALA ARG HIS SER ILE PHE SER LEU GLU THR ASP LYS VAL
SEQRES 25 A 334 PHE ASN THR VAL PHE ASN ASP MET LYS GLN TRP LEU ASP
SEQRES 26 A 334 LYS HIS THR THR THR GLU ALA LYS PRO
SEQRES 1 B 334 HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR GLU ASN
SEQRES 2 B 334 LEU TYR PHE GLN GLY ALA MET GLY SER ALA PRO TYR PRO
SEQRES 3 B 334 TYR LYS VAL GLN THR THR VAL PRO GLU LEU GLN TYR GLU
SEQRES 4 B 334 ASN PHE ASP GLY ALA LYS PHE GLY TYR MET PHE TRP PRO
SEQRES 5 B 334 VAL GLN ASN GLY THR ASN GLU VAL ARG GLY ARG VAL LEU
SEQRES 6 B 334 LEU ILE HIS GLY PHE GLY GLU TYR THR LYS ILE GLN PHE
SEQRES 7 B 334 ARG LEU MET ASP HIS LEU SER LEU ASN GLY TYR GLU SER
SEQRES 8 B 334 PHE THR PHE ASP GLN ARG GLY ALA GLY VAL THR SER PRO
SEQRES 9 B 334 GLY ARG SER LYS GLY VAL THR ASP GLU TYR HIS VAL PHE
SEQRES 10 B 334 ASN ASP LEU GLU HIS PHE VAL GLU LYS ASN LEU SER GLU
SEQRES 11 B 334 CYS LYS ALA LYS GLY ILE PRO LEU PHE MET TRP GLY HIS
SEQRES 12 B 334 SER MET GLY GLY GLY ILE CYS LEU ASN TYR ALA CYS GLN
SEQRES 13 B 334 GLY LYS HIS LYS ASN GLU ILE SER GLY TYR ILE GLY SER
SEQRES 14 B 334 GLY PRO LEU ILE ILE LEU HIS PRO HIS THR MET TYR ASN
SEQRES 15 B 334 LYS PRO THR GLN ILE ILE ALA PRO LEU LEU ALA LYS PHE
SEQRES 16 B 334 SER PRO ARG VAL ARG ILE ASP THR GLY LEU ASP LEU LYS
SEQRES 17 B 334 GLY ILE THR SER ASP LYS ALA TYR ARG ALA PHE LEU GLY
SEQRES 18 B 334 SER ASP PRO MET SER VAL PRO LEU TYR GLY SER PHE ARG
SEQRES 19 B 334 GLN ILE HIS ASP PHE MET GLN ARG GLY ALA LYS LEU TYR
SEQRES 20 B 334 LYS ASN GLU ASN ASN TYR ILE GLN LYS ASN PHE ALA LYS
SEQRES 21 B 334 ASP LYS PRO VAL ILE ILE MET HIS GLY GLN ASP ASP THR
SEQRES 22 B 334 ILE ASN ASP PRO LYS GLY SER GLU LYS PHE ILE ARG ASP
SEQRES 23 B 334 CYS PRO SER ALA ASP LYS GLU LEU LYS LEU TYR PRO GLY
SEQRES 24 B 334 ALA ARG HIS SER ILE PHE SER LEU GLU THR ASP LYS VAL
SEQRES 25 B 334 PHE ASN THR VAL PHE ASN ASP MET LYS GLN TRP LEU ASP
SEQRES 26 B 334 LYS HIS THR THR THR GLU ALA LYS PRO
SEQRES 1 C 334 HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR GLU ASN
SEQRES 2 C 334 LEU TYR PHE GLN GLY ALA MET GLY SER ALA PRO TYR PRO
SEQRES 3 C 334 TYR LYS VAL GLN THR THR VAL PRO GLU LEU GLN TYR GLU
SEQRES 4 C 334 ASN PHE ASP GLY ALA LYS PHE GLY TYR MET PHE TRP PRO
SEQRES 5 C 334 VAL GLN ASN GLY THR ASN GLU VAL ARG GLY ARG VAL LEU
SEQRES 6 C 334 LEU ILE HIS GLY PHE GLY GLU TYR THR LYS ILE GLN PHE
SEQRES 7 C 334 ARG LEU MET ASP HIS LEU SER LEU ASN GLY TYR GLU SER
SEQRES 8 C 334 PHE THR PHE ASP GLN ARG GLY ALA GLY VAL THR SER PRO
SEQRES 9 C 334 GLY ARG SER LYS GLY VAL THR ASP GLU TYR HIS VAL PHE
SEQRES 10 C 334 ASN ASP LEU GLU HIS PHE VAL GLU LYS ASN LEU SER GLU
SEQRES 11 C 334 CYS LYS ALA LYS GLY ILE PRO LEU PHE MET TRP GLY HIS
SEQRES 12 C 334 SER MET GLY GLY GLY ILE CYS LEU ASN TYR ALA CYS GLN
SEQRES 13 C 334 GLY LYS HIS LYS ASN GLU ILE SER GLY TYR ILE GLY SER
SEQRES 14 C 334 GLY PRO LEU ILE ILE LEU HIS PRO HIS THR MET TYR ASN
SEQRES 15 C 334 LYS PRO THR GLN ILE ILE ALA PRO LEU LEU ALA LYS PHE
SEQRES 16 C 334 SER PRO ARG VAL ARG ILE ASP THR GLY LEU ASP LEU LYS
SEQRES 17 C 334 GLY ILE THR SER ASP LYS ALA TYR ARG ALA PHE LEU GLY
SEQRES 18 C 334 SER ASP PRO MET SER VAL PRO LEU TYR GLY SER PHE ARG
SEQRES 19 C 334 GLN ILE HIS ASP PHE MET GLN ARG GLY ALA LYS LEU TYR
SEQRES 20 C 334 LYS ASN GLU ASN ASN TYR ILE GLN LYS ASN PHE ALA LYS
SEQRES 21 C 334 ASP LYS PRO VAL ILE ILE MET HIS GLY GLN ASP ASP THR
SEQRES 22 C 334 ILE ASN ASP PRO LYS GLY SER GLU LYS PHE ILE ARG ASP
SEQRES 23 C 334 CYS PRO SER ALA ASP LYS GLU LEU LYS LEU TYR PRO GLY
SEQRES 24 C 334 ALA ARG HIS SER ILE PHE SER LEU GLU THR ASP LYS VAL
SEQRES 25 C 334 PHE ASN THR VAL PHE ASN ASP MET LYS GLN TRP LEU ASP
SEQRES 26 C 334 LYS HIS THR THR THR GLU ALA LYS PRO
SEQRES 1 D 334 HIS HIS HIS HIS ASP TYR ASP ILE PRO THR THR GLU ASN
SEQRES 2 D 334 LEU TYR PHE GLN GLY ALA MET GLY SER ALA PRO TYR PRO
SEQRES 3 D 334 TYR LYS VAL GLN THR THR VAL PRO GLU LEU GLN TYR GLU
SEQRES 4 D 334 ASN PHE ASP GLY ALA LYS PHE GLY TYR MET PHE TRP PRO
SEQRES 5 D 334 VAL GLN ASN GLY THR ASN GLU VAL ARG GLY ARG VAL LEU
SEQRES 6 D 334 LEU ILE HIS GLY PHE GLY GLU TYR THR LYS ILE GLN PHE
SEQRES 7 D 334 ARG LEU MET ASP HIS LEU SER LEU ASN GLY TYR GLU SER
SEQRES 8 D 334 PHE THR PHE ASP GLN ARG GLY ALA GLY VAL THR SER PRO
SEQRES 9 D 334 GLY ARG SER LYS GLY VAL THR ASP GLU TYR HIS VAL PHE
SEQRES 10 D 334 ASN ASP LEU GLU HIS PHE VAL GLU LYS ASN LEU SER GLU
SEQRES 11 D 334 CYS LYS ALA LYS GLY ILE PRO LEU PHE MET TRP GLY HIS
SEQRES 12 D 334 SER MET GLY GLY GLY ILE CYS LEU ASN TYR ALA CYS GLN
SEQRES 13 D 334 GLY LYS HIS LYS ASN GLU ILE SER GLY TYR ILE GLY SER
SEQRES 14 D 334 GLY PRO LEU ILE ILE LEU HIS PRO HIS THR MET TYR ASN
SEQRES 15 D 334 LYS PRO THR GLN ILE ILE ALA PRO LEU LEU ALA LYS PHE
SEQRES 16 D 334 SER PRO ARG VAL ARG ILE ASP THR GLY LEU ASP LEU LYS
SEQRES 17 D 334 GLY ILE THR SER ASP LYS ALA TYR ARG ALA PHE LEU GLY
SEQRES 18 D 334 SER ASP PRO MET SER VAL PRO LEU TYR GLY SER PHE ARG
SEQRES 19 D 334 GLN ILE HIS ASP PHE MET GLN ARG GLY ALA LYS LEU TYR
SEQRES 20 D 334 LYS ASN GLU ASN ASN TYR ILE GLN LYS ASN PHE ALA LYS
SEQRES 21 D 334 ASP LYS PRO VAL ILE ILE MET HIS GLY GLN ASP ASP THR
SEQRES 22 D 334 ILE ASN ASP PRO LYS GLY SER GLU LYS PHE ILE ARG ASP
SEQRES 23 D 334 CYS PRO SER ALA ASP LYS GLU LEU LYS LEU TYR PRO GLY
SEQRES 24 D 334 ALA ARG HIS SER ILE PHE SER LEU GLU THR ASP LYS VAL
SEQRES 25 D 334 PHE ASN THR VAL PHE ASN ASP MET LYS GLN TRP LEU ASP
SEQRES 26 D 334 LYS HIS THR THR THR GLU ALA LYS PRO
HET NO3 A 401 4
HET SO4 B 401 5
HET SO4 C 401 5
HET NA D 401 1
HETNAM NO3 NITRATE ION
HETNAM SO4 SULFATE ION
HETNAM NA SODIUM ION
FORMUL 5 NO3 N O3 1-
FORMUL 6 SO4 2(O4 S 2-)
FORMUL 8 NA NA 1+
FORMUL 9 HOH *408(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 GLY A 114 1 24
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 ALA B 78 SER B 82 5 5
HELIX 17 AB8 PRO B 83 LYS B 87 5 5
HELIX 18 AB9 ASP B 91 GLY B 114 1 24
HELIX 19 AC1 SER B 123 GLY B 136 1 14
HELIX 20 AC2 HIS B 155 LYS B 162 1 8
HELIX 21 AC3 PRO B 163 LEU B 171 1 9
HELIX 22 AC4 ASP B 185 THR B 190 1 6
HELIX 23 AC5 ASP B 192 ASP B 202 1 11
HELIX 24 AC6 PHE B 212 ASN B 228 1 17
HELIX 25 AC7 ASN B 231 PHE B 237 1 7
HELIX 26 AC8 ASP B 255 CYS B 266 1 12
HELIX 27 AC9 THR B 288 HIS B 306 1 19
HELIX 28 AD1 TYR C 52 ILE C 55 5 4
HELIX 29 AD2 GLN C 56 ASN C 66 1 11
HELIX 30 AD3 PRO C 83 LYS C 87 5 5
HELIX 31 AD4 ASP C 91 GLY C 114 1 24
HELIX 32 AD5 SER C 123 GLY C 136 1 14
HELIX 33 AD6 HIS C 155 LYS C 162 1 8
HELIX 34 AD7 PRO C 163 LEU C 171 1 9
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 TYR D 52 ILE D 55 5 4
HELIX 42 AE6 GLN D 56 ASN D 66 1 11
HELIX 43 AE7 PRO D 83 LYS D 87 5 5
HELIX 44 AE8 ASP D 91 GLY D 114 1 24
HELIX 45 AE9 SER D 123 GLY D 136 1 14
HELIX 46 AF1 HIS D 155 LYS D 162 1 8
HELIX 47 AF2 PRO D 163 GLN D 165 5 3
HELIX 48 AF3 ILE D 166 ALA D 172 1 7
HELIX 49 AF4 ASP D 185 THR D 190 1 6
HELIX 50 AF5 ASP D 192 ASP D 202 1 11
HELIX 51 AF6 PHE D 212 ASN D 228 1 17
HELIX 52 AF7 ASN D 231 PHE D 237 1 7
HELIX 53 AF8 ASP D 255 CYS D 266 1 12
HELIX 54 AF9 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 TYR A 27 N GLN A 16
SHEET 3 AA1 8 TYR A 68 PHE A 73 -1 O THR A 72 N MET A 28
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 PHE A 118 N LEU A 44
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 TYR B 27 N GLN B 16
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 LEU B 44
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 2 ARG B 179 ILE B 180 0
SHEET 2 AA4 2 GLY B 210 SER B 211 -1 O GLY B 210 N ILE B 180
SHEET 1 AA5 8 GLN C 16 ASN C 19 0
SHEET 2 AA5 8 LYS C 24 TRP C 30 -1 O TYR C 27 N GLN C 16
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 LEU C 44
SHEET 6 AA5 8 GLY C 144 SER C 148 1 O SER C 148 N GLY C 121
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 ILE C 180 0
SHEET 2 AA6 2 GLY C 210 SER C 211 -1 O GLY C 210 N ILE C 180
SHEET 1 AA7 8 GLN D 16 PHE D 20 0
SHEET 2 AA7 8 ALA D 23 TRP D 30 -1 O TYR D 27 N GLN D 16
SHEET 3 AA7 8 TYR D 68 PHE D 73 -1 O SER D 70 N TRP D 30
SHEET 4 AA7 8 GLY D 41 ILE D 46 1 N LEU D 45 O PHE D 71
SHEET 5 AA7 8 LEU D 117 HIS D 122 1 O PHE D 118 N LEU D 44
SHEET 6 AA7 8 GLY D 144 SER D 148 1 O SER D 148 N GLY D 121
SHEET 7 AA7 8 VAL D 243 GLY D 248 1 O MET D 246 N GLY D 147
SHEET 8 AA7 8 LYS D 271 TYR D 276 1 O LYS D 274 N ILE D 245
SHEET 1 AA8 2 ARG D 179 ASP D 181 0
SHEET 2 AA8 2 TYR D 209 SER D 211 -1 O GLY D 210 N ILE D 180
CISPEP 1 VAL A 206 PRO A 207 0 -2.99
CISPEP 2 VAL B 206 PRO B 207 0 -0.02
CISPEP 3 VAL C 206 PRO C 207 0 -1.01
CISPEP 4 VAL D 206 PRO D 207 0 -9.33
SITE 1 AC1 1 TYR D 160
SITE 1 AC2 3 LYS B 187 ARG B 196 ARG B 280
SITE 1 AC3 3 LYS C 187 ARG C 196 ARG C 280
SITE 1 AC4 1 ARG D 196
CRYST1 77.196 108.566 167.667 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 0.012954 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009211 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005964 0.00000
TER 2485 GLU A 310
TER 4975 ALA B 311
TER 7444 THR C 308
TER 9913 THR D 308
MASTER 462 0 4 54 40 0 4 610332 4 14 104
END
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