HEADER TRANSFERASE, HYDROLASE 21-MAY-12 4F9U
TITLE STRUCTURE OF GLYCOSYLATED GLUTAMINYL CYCLASE FROM DROSOPHILA
TITLE 2 MELANOGASTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CG32412;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 29-340;
COMPND 5 SYNONYM: GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE, GH11174P;
COMPND 6 EC: 2.3.2.5, 3.4.-.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: QC, CG10487, CG32412, DMEL_CG32412;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: PICHIA PASTORIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: X33;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PPICZALPHAB
KEYWDS ALPHA/BETA HYDROLASE, PGLU FORMATION, PE, ALZHEIMER'S DISEASE,
KEYWDS 2 PYROGLUTAMATE, PGLU-AMYLOID, GLYCOSYLATION, TRANSFERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.KOLENKO,B.KOCH,D.RUIZ-CARILO,M.T.STUBBS
REVDAT 4 13-SEP-23 4F9U 1 HETSYN
REVDAT 3 29-JUL-20 4F9U 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 26-SEP-12 4F9U 1 JRNL
REVDAT 1 29-AUG-12 4F9U 0
JRNL AUTH B.KOCH,P.KOLENKO,M.BUCHHOLZ,D.RUIZ CARRILLO,C.PARTHIER,
JRNL AUTH 2 M.WERMANN,J.U.RAHFELD,G.REUTER,S.SCHILLING,M.T.STUBBS,
JRNL AUTH 3 H.U.DEMUTH
JRNL TITL CRYSTAL STRUCTURES OF GLUTAMINYL CYCLASES (QCS) FROM
JRNL TITL 2 DROSOPHILA MELANOGASTER REVEAL ACTIVE SITE CONSERVATION
JRNL TITL 3 BETWEEN INSECT AND MAMMALIAN QCS.
JRNL REF BIOCHEMISTRY V. 51 7383 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 22897232
JRNL DOI 10.1021/BI300687G
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 90.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 57047
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2896
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4027
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4825
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 163
REMARK 3 SOLVENT ATOMS : 573
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.95000
REMARK 3 B22 (A**2) : -0.61000
REMARK 3 B33 (A**2) : -1.63000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.47000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.124
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.277
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5141 ; 0.012 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 3499 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6991 ; 1.488 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8375 ; 0.956 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 602 ; 5.846 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 265 ;32.284 ;23.396
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 795 ;13.394 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;16.313 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 774 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5680 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1120 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4F9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000072636.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57047
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 90.902
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
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) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.51400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3SI2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG35000, 2 MM PQ50, 0.1 M TRIS,
REMARK 280 PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
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 28.48200
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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, 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 ASN A 29
REMARK 465 ILE A 30
REMARK 465 GLY A 31
REMARK 465 SER A 32
REMARK 465 GLY A 198
REMARK 465 SER A 199
REMARK 465 GLN A 200
REMARK 465 ALA A 201
REMARK 465 GLN A 202
REMARK 465 LEU A 203
REMARK 465 ALA A 204
REMARK 465 TYR A 338
REMARK 465 ARG A 339
REMARK 465 THR A 340
REMARK 465 ASN B 29
REMARK 465 ILE B 30
REMARK 465 GLY B 31
REMARK 465 GLY B 198
REMARK 465 SER B 199
REMARK 465 GLN B 200
REMARK 465 ALA B 201
REMARK 465 GLN B 202
REMARK 465 ARG B 339
REMARK 465 THR B 340
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 312 NE - CZ - NH2 ANGL. DEV. = -3.4 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 ARG A 52 53.64 -149.77
REMARK 500 VAL A 88 -57.15 77.97
REMARK 500 ASN A 102 60.33 71.05
REMARK 500 SER A 132 46.86 -140.81
REMARK 500 LYS A 152 -104.60 -120.82
REMARK 500 ASN A 156 53.01 -90.14
REMARK 500 LYS A 174 -54.54 -127.82
REMARK 500 SER A 181 154.37 170.18
REMARK 500 ASP A 272 -178.49 -171.61
REMARK 500 THR A 330 -75.34 -129.03
REMARK 500 ARG B 52 54.76 -152.87
REMARK 500 VAL B 88 -55.18 72.68
REMARK 500 ASN B 102 63.80 62.98
REMARK 500 LYS B 152 -96.34 -123.05
REMARK 500 ASN B 156 48.44 -86.90
REMARK 500 SER B 181 156.50 176.27
REMARK 500 ASP B 272 -174.43 -170.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 131 OD2
REMARK 620 2 GLU A 171 OE1 106.3
REMARK 620 3 HIS A 297 NE2 98.6 120.0
REMARK 620 4 PBD A 402 NAM 111.7 109.1 110.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 131 OD2
REMARK 620 2 GLU B 171 OE1 107.7
REMARK 620 3 HIS B 297 NE2 106.0 112.8
REMARK 620 4 PBD B 402 NAM 116.1 110.3 104.0
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3SI2 RELATED DB: PDB
REMARK 900 RELATED ID: 4F9V RELATED DB: PDB
REMARK 900 RELATED ID: 4FAI RELATED DB: PDB
REMARK 900 RELATED ID: 4FBE RELATED DB: PDB
DBREF 4F9U A 29 340 UNP Q9VRQ9 Q9VRQ9_DROME 29 340
DBREF 4F9U B 29 340 UNP Q9VRQ9 Q9VRQ9_DROME 29 340
SEQRES 1 A 312 ASN ILE GLY SER GLN TRP ARG ASP ASP GLU VAL HIS PHE
SEQRES 2 A 312 ASN ARG THR LEU ASP SER ILE LEU VAL PRO ARG VAL VAL
SEQRES 3 A 312 GLY SER ARG GLY HIS GLN GLN VAL ARG GLU TYR LEU VAL
SEQRES 4 A 312 GLN SER LEU ASN GLY LEU GLY PHE GLN THR GLU VAL ASP
SEQRES 5 A 312 GLU PHE LYS GLN ARG VAL PRO VAL PHE GLY GLU LEU THR
SEQRES 6 A 312 PHE ALA ASN VAL VAL GLY THR ILE ASN PRO GLN ALA GLN
SEQRES 7 A 312 ASN PHE LEU ALA LEU ALA CYS HIS TYR ASP SER LYS TYR
SEQRES 8 A 312 PHE PRO ASN ASP PRO GLY PHE VAL GLY ALA THR ASP SER
SEQRES 9 A 312 ALA VAL PRO CYS ALA ILE LEU LEU ASN THR ALA LYS THR
SEQRES 10 A 312 LEU GLY ALA TYR LEU GLN LYS GLU PHE ARG ASN ARG SER
SEQRES 11 A 312 ASP VAL GLY LEU MET LEU ILE PHE PHE ASP GLY GLU GLU
SEQRES 12 A 312 ALA PHE LYS GLU TRP THR ASP ALA ASP SER VAL TYR GLY
SEQRES 13 A 312 SER LYS HIS LEU ALA ALA LYS LEU ALA SER LYS ARG SER
SEQRES 14 A 312 GLY SER GLN ALA GLN LEU ALA PRO ARG ASN ILE ASP ARG
SEQRES 15 A 312 ILE GLU VAL LEU VAL LEU LEU ASP LEU ILE GLY ALA ARG
SEQRES 16 A 312 ASN PRO LYS PHE SER SER PHE TYR GLU ASN THR ASP GLY
SEQRES 17 A 312 LEU HIS SER SER LEU VAL GLN ILE GLU LYS SER LEU ARG
SEQRES 18 A 312 THR ALA GLY GLN LEU GLU GLY ASN ASN ASN MET PHE LEU
SEQRES 19 A 312 SER ARG VAL SER GLY GLY LEU VAL ASP ASP ASP HIS ARG
SEQRES 20 A 312 PRO PHE LEU ASP GLU ASN VAL PRO VAL LEU HIS LEU VAL
SEQRES 21 A 312 ALA THR PRO PHE PRO ASP VAL TRP HIS THR PRO ARG ASP
SEQRES 22 A 312 ASN ALA ALA ASN LEU HIS TRP PRO SER ILE ARG ASN PHE
SEQRES 23 A 312 ASN ARG VAL PHE ARG ASN PHE VAL TYR GLN TYR LEU LYS
SEQRES 24 A 312 ARG HIS THR SER PRO VAL ASN LEU ARG PHE TYR ARG THR
SEQRES 1 B 312 ASN ILE GLY SER GLN TRP ARG ASP ASP GLU VAL HIS PHE
SEQRES 2 B 312 ASN ARG THR LEU ASP SER ILE LEU VAL PRO ARG VAL VAL
SEQRES 3 B 312 GLY SER ARG GLY HIS GLN GLN VAL ARG GLU TYR LEU VAL
SEQRES 4 B 312 GLN SER LEU ASN GLY LEU GLY PHE GLN THR GLU VAL ASP
SEQRES 5 B 312 GLU PHE LYS GLN ARG VAL PRO VAL PHE GLY GLU LEU THR
SEQRES 6 B 312 PHE ALA ASN VAL VAL GLY THR ILE ASN PRO GLN ALA GLN
SEQRES 7 B 312 ASN PHE LEU ALA LEU ALA CYS HIS TYR ASP SER LYS TYR
SEQRES 8 B 312 PHE PRO ASN ASP PRO GLY PHE VAL GLY ALA THR ASP SER
SEQRES 9 B 312 ALA VAL PRO CYS ALA ILE LEU LEU ASN THR ALA LYS THR
SEQRES 10 B 312 LEU GLY ALA TYR LEU GLN LYS GLU PHE ARG ASN ARG SER
SEQRES 11 B 312 ASP VAL GLY LEU MET LEU ILE PHE PHE ASP GLY GLU GLU
SEQRES 12 B 312 ALA PHE LYS GLU TRP THR ASP ALA ASP SER VAL TYR GLY
SEQRES 13 B 312 SER LYS HIS LEU ALA ALA LYS LEU ALA SER LYS ARG SER
SEQRES 14 B 312 GLY SER GLN ALA GLN LEU ALA PRO ARG ASN ILE ASP ARG
SEQRES 15 B 312 ILE GLU VAL LEU VAL LEU LEU ASP LEU ILE GLY ALA ARG
SEQRES 16 B 312 ASN PRO LYS PHE SER SER PHE TYR GLU ASN THR ASP GLY
SEQRES 17 B 312 LEU HIS SER SER LEU VAL GLN ILE GLU LYS SER LEU ARG
SEQRES 18 B 312 THR ALA GLY GLN LEU GLU GLY ASN ASN ASN MET PHE LEU
SEQRES 19 B 312 SER ARG VAL SER GLY GLY LEU VAL ASP ASP ASP HIS ARG
SEQRES 20 B 312 PRO PHE LEU ASP GLU ASN VAL PRO VAL LEU HIS LEU VAL
SEQRES 21 B 312 ALA THR PRO PHE PRO ASP VAL TRP HIS THR PRO ARG ASP
SEQRES 22 B 312 ASN ALA ALA ASN LEU HIS TRP PRO SER ILE ARG ASN PHE
SEQRES 23 B 312 ASN ARG VAL PHE ARG ASN PHE VAL TYR GLN TYR LEU LYS
SEQRES 24 B 312 ARG HIS THR SER PRO VAL ASN LEU ARG PHE TYR ARG THR
MODRES 4F9U ASN A 42 ASN GLYCOSYLATION SITE
MODRES 4F9U ASN B 42 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET BMA D 3 11
HET MAN D 4 11
HET MAN D 5 11
HET MAN D 6 11
HET MAN D 7 11
HET ZN A 401 1
HET PBD A 402 22
HET GOL A 405 6
HET ZN B 401 1
HET PBD B 402 22
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM ZN ZINC ION
HETNAM PBD 1-(3,4-DIMETHOXYPHENYL)-3-[3-(1H-IMIDAZOL-1-YL)
HETNAM 2 PBD PROPYL]THIOUREA
HETNAM GOL GLYCEROL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 4 BMA C6 H12 O6
FORMUL 4 MAN 4(C6 H12 O6)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 PBD 2(C15 H20 N4 O2 S)
FORMUL 7 GOL C3 H8 O3
FORMUL 10 HOH *573(H2 O)
HELIX 1 1 ASP A 37 LEU A 49 1 13
HELIX 2 2 SER A 56 LEU A 73 1 18
HELIX 3 3 SER A 132 LEU A 146 1 15
HELIX 4 4 LEU A 146 GLN A 151 1 6
HELIX 5 5 LYS A 152 ASN A 156 5 5
HELIX 6 6 VAL A 182 LYS A 195 1 14
HELIX 7 7 ARG A 206 ASP A 209 5 4
HELIX 8 8 TYR A 231 ASN A 233 5 3
HELIX 9 9 THR A 234 ALA A 251 1 18
HELIX 10 10 HIS A 274 ASP A 279 1 6
HELIX 11 11 ASN A 302 LEU A 306 5 5
HELIX 12 12 HIS A 307 HIS A 329 1 23
HELIX 13 13 ASP B 37 LEU B 49 1 13
HELIX 14 14 SER B 56 LEU B 73 1 18
HELIX 15 15 SER B 132 LEU B 146 1 15
HELIX 16 16 LEU B 146 GLN B 151 1 6
HELIX 17 17 LYS B 152 ASN B 156 5 5
HELIX 18 18 VAL B 182 SER B 194 1 13
HELIX 19 19 ARG B 206 ASP B 209 5 4
HELIX 20 20 TYR B 231 ASN B 233 5 3
HELIX 21 21 THR B 234 ALA B 251 1 18
HELIX 22 22 HIS B 274 ASP B 279 1 6
HELIX 23 23 ASN B 302 LEU B 306 5 5
HELIX 24 24 HIS B 307 ARG B 328 1 22
HELIX 25 25 PRO B 332 ARG B 336 5 5
SHEET 1 A 6 GLN A 76 VAL A 86 0
SHEET 2 A 6 GLY A 90 ILE A 101 -1 O PHE A 94 N PHE A 82
SHEET 3 A 6 VAL A 160 PHE A 167 -1 O PHE A 166 N VAL A 97
SHEET 4 A 6 ASN A 107 HIS A 114 1 N CYS A 113 O PHE A 167
SHEET 5 A 6 ILE A 211 ASP A 218 1 O VAL A 215 N ALA A 110
SHEET 6 A 6 VAL A 284 VAL A 288 1 O LEU A 287 N ASP A 218
SHEET 1 B 2 PHE A 227 SER A 229 0
SHEET 2 B 2 PHE A 261 VAL A 265 1 O ARG A 264 N SER A 229
SHEET 1 C 6 GLN B 76 VAL B 86 0
SHEET 2 C 6 GLY B 90 ILE B 101 -1 O VAL B 98 N GLU B 78
SHEET 3 C 6 VAL B 160 PHE B 167 -1 O PHE B 166 N VAL B 97
SHEET 4 C 6 ASN B 107 HIS B 114 1 N CYS B 113 O PHE B 167
SHEET 5 C 6 ILE B 211 ASP B 218 1 O VAL B 215 N ALA B 110
SHEET 6 C 6 VAL B 284 VAL B 288 1 O LEU B 285 N LEU B 214
SSBOND 1 CYS A 113 CYS A 136 1555 1555 2.15
SSBOND 2 CYS B 113 CYS B 136 1555 1555 2.13
LINK ND2 ASN A 42 C1 NAG C 1 1555 1555 1.43
LINK ND2 ASN B 42 C1 NAG D 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.45
LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44
LINK O6 BMA D 3 C1 MAN D 4 1555 1555 1.44
LINK O6 MAN D 4 C1 MAN D 5 1555 1555 1.44
LINK O3 MAN D 4 C1 MAN D 7 1555 1555 1.45
LINK O2 MAN D 5 C1 MAN D 6 1555 1555 1.44
LINK OD2 ASP A 131 ZN ZN A 401 1555 1555 2.05
LINK OE1 GLU A 171 ZN ZN A 401 1555 1555 1.87
LINK NE2 HIS A 297 ZN ZN A 401 1555 1555 1.91
LINK ZN ZN A 401 NAM PBD A 402 1555 1555 2.09
LINK OD2 ASP B 131 ZN ZN B 401 1555 1555 1.82
LINK OE1 GLU B 171 ZN ZN B 401 1555 1555 2.03
LINK NE2 HIS B 297 ZN ZN B 401 1555 1555 2.10
LINK ZN ZN B 401 NAM PBD B 402 1555 1555 2.09
CISPEP 1 ASP A 131 SER A 132 0 3.48
CISPEP 2 THR A 290 PRO A 291 0 3.56
CISPEP 3 ASP B 131 SER B 132 0 -1.25
CISPEP 4 THR B 290 PRO B 291 0 -1.10
CRYST1 60.665 56.964 95.669 90.00 108.16 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 0.016484 0.000000 0.005408 0.00000
SCALE2 0.000000 0.017555 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011001 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
