HEADER TRANSFERASE 12-DEC-07 2ZEH
TITLE CRYSTAL STRUCTURE OF THE HUMAN GLUTAMINYL CYCLASE MUTANT E201Q AT 1.8
TITLE 2 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUTAMINYL-PEPTIDE CYCLOTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 33-361;
COMPND 5 SYNONYM: QC, GLUTAMINYL-TRNA CYCLOTRANSFERASE, GLUTAMINYL CYCLASE,
COMPND 6 GLUTAMYL CYCLASE;
COMPND 7 EC: 2.3.2.5;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: BONE MARROW;
SOURCE 6 GENE: QPCT;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS HYDROGEN BOND NETWORK, GLUTAMINYL CYCLASE, PYROGLUTAMATE, SITE-
KEYWDS 2 DIRECTED MUTAGENESIS, PROTON TRANSFER, ACYLTRANSFERASE,
KEYWDS 3 GLYCOPROTEIN, METAL-BINDING, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.F.HUANG,Y.R.WANG,E.C.CHANG,T.L.CHOU,A.H.WANG
REVDAT 5 01-NOV-23 2ZEH 1 REMARK
REVDAT 4 10-NOV-21 2ZEH 1 SEQADV LINK
REVDAT 3 13-JUL-11 2ZEH 1 VERSN
REVDAT 2 24-FEB-09 2ZEH 1 VERSN
REVDAT 1 22-APR-08 2ZEH 0
JRNL AUTH K.F.HUANG,Y.R.WANG,E.C.CHANG,T.L.CHOU,A.H.WANG
JRNL TITL A CONSERVED HYDROGEN-BOND NETWORK IN THE CATALYTIC CENTRE OF
JRNL TITL 2 ANIMAL GLUTAMINYL CYCLASES IS CRITICAL FOR CATALYSIS.
JRNL REF BIOCHEM.J. V. 411 181 2008
JRNL REFN ISSN 0264-6021
JRNL PMID 18072935
JRNL DOI 10.1042/BJ20071073
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 77523
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 SET) : 0.181
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3907
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2070
REMARK 3 BIN FREE R VALUE : 0.2330
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 374
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5220
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 867
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.70
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.019
REMARK 3 BOND ANGLES (DEGREES) : 1.810
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZEH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-DEC-07.
REMARK 100 THE DEPOSITION ID IS D_1000027869.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL12B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83140
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.49900
REMARK 200 R SYM FOR SHELL (I) : 0.49900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 2AFM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2%-4% DIOXANE, 1.6-1.8M AMMONIUM
REMARK 280 SULFATE, 100MM MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 59.52550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 34.36706
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 110.88400
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 59.52550
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 34.36706
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 110.88400
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 59.52550
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 34.36706
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 110.88400
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 59.52550
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 34.36706
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 110.88400
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 59.52550
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 34.36706
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 110.88400
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 59.52550
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 34.36706
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 110.88400
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 68.73413
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 221.76800
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 68.73413
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 221.76800
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 68.73413
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 221.76800
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 68.73413
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 221.76800
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 68.73413
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 221.76800
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 68.73413
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 221.76800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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,PQS
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,PQS
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -430.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 523 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 697 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 903 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1087 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1123 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1136 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1191 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 769 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 969 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B1154 LIES ON A SPECIAL POSITION.
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 THR A 183
REMARK 465 VAL A 184
REMARK 465 SER A 185
REMARK 465 ASP A 186
REMARK 465 SER A 187
REMARK 465 LYS A 188
REMARK 465 THR B 183
REMARK 465 VAL B 184
REMARK 465 SER B 185
REMARK 465 ASP B 186
REMARK 465 SER B 187
REMARK 465 LYS B 188
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ALA A 131
REMARK 475 ALA B 131
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 O HOH B 1092 O HOH B 1092 11445 0.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 312 NE - CZ - NH1 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 77 45.23 -147.31
REMARK 500 LEU A 205 -120.78 -110.66
REMARK 500 SER A 212 164.26 161.60
REMARK 500 TYR A 297 133.00 -176.51
REMARK 500 ARG B 77 49.62 -143.99
REMARK 500 ALA B 100 154.14 -49.00
REMARK 500 LEU B 205 -40.23 -132.59
REMARK 500 SER B 212 159.54 157.92
REMARK 500 ASN B 296 71.27 -69.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 145 0.07 SIDE CHAIN
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 391 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 159 OD2
REMARK 620 2 GLU A 202 OE2 105.8
REMARK 620 3 HIS A 330 NE2 100.8 115.2
REMARK 620 4 HOH A 401 O 118.6 100.1 116.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 392 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 159 OD2
REMARK 620 2 GLU B 202 OE2 106.9
REMARK 620 3 HIS B 330 NE2 103.1 121.4
REMARK 620 4 HOH B 402 O 115.5 100.0 110.5
REMARK 620 N 1 2 3
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AFM RELATED DB: PDB
REMARK 900 THE WILD-TYPE HUMAN GLUTAMINYL CYCLASE
REMARK 900 RELATED ID: 2ZED RELATED DB: PDB
REMARK 900 RELATED ID: 2ZEE RELATED DB: PDB
REMARK 900 RELATED ID: 2ZEF RELATED DB: PDB
REMARK 900 RELATED ID: 2ZEG RELATED DB: PDB
REMARK 900 RELATED ID: 2ZEL RELATED DB: PDB
REMARK 900 RELATED ID: 2ZEM RELATED DB: PDB
REMARK 900 RELATED ID: 2ZEN RELATED DB: PDB
REMARK 900 RELATED ID: 2ZEO RELATED DB: PDB
REMARK 900 RELATED ID: 2ZEP RELATED DB: PDB
DBREF 2ZEH A 33 361 UNP Q16769 QPCT_HUMAN 33 361
DBREF 2ZEH B 33 361 UNP Q16769 QPCT_HUMAN 33 361
SEQADV 2ZEH GLN A 201 UNP Q16769 GLU 201 ENGINEERED MUTATION
SEQADV 2ZEH GLN B 201 UNP Q16769 GLU 201 ENGINEERED MUTATION
SEQRES 1 A 329 ALA SER ALA TRP PRO GLU GLU LYS ASN TYR HIS GLN PRO
SEQRES 2 A 329 ALA ILE LEU ASN SER SER ALA LEU ARG GLN ILE ALA GLU
SEQRES 3 A 329 GLY THR SER ILE SER GLU MET TRP GLN ASN ASP LEU GLN
SEQRES 4 A 329 PRO LEU LEU ILE GLU ARG TYR PRO GLY SER PRO GLY SER
SEQRES 5 A 329 TYR ALA ALA ARG GLN HIS ILE MET GLN ARG ILE GLN ARG
SEQRES 6 A 329 LEU GLN ALA ASP TRP VAL LEU GLU ILE ASP THR PHE LEU
SEQRES 7 A 329 SER GLN THR PRO TYR GLY TYR ARG SER PHE SER ASN ILE
SEQRES 8 A 329 ILE SER THR LEU ASN PRO THR ALA LYS ARG HIS LEU VAL
SEQRES 9 A 329 LEU ALA CYS HIS TYR ASP SER LYS TYR PHE SER HIS TRP
SEQRES 10 A 329 ASN ASN ARG VAL PHE VAL GLY ALA THR ASP SER ALA VAL
SEQRES 11 A 329 PRO CYS ALA MET MET LEU GLU LEU ALA ARG ALA LEU ASP
SEQRES 12 A 329 LYS LYS LEU LEU SER LEU LYS THR VAL SER ASP SER LYS
SEQRES 13 A 329 PRO ASP LEU SER LEU GLN LEU ILE PHE PHE ASP GLY GLN
SEQRES 14 A 329 GLU ALA PHE LEU HIS TRP SER PRO GLN ASP SER LEU TYR
SEQRES 15 A 329 GLY SER ARG HIS LEU ALA ALA LYS MET ALA SER THR PRO
SEQRES 16 A 329 HIS PRO PRO GLY ALA ARG GLY THR SER GLN LEU HIS GLY
SEQRES 17 A 329 MET ASP LEU LEU VAL LEU LEU ASP LEU ILE GLY ALA PRO
SEQRES 18 A 329 ASN PRO THR PHE PRO ASN PHE PHE PRO ASN SER ALA ARG
SEQRES 19 A 329 TRP PHE GLU ARG LEU GLN ALA ILE GLU HIS GLU LEU HIS
SEQRES 20 A 329 GLU LEU GLY LEU LEU LYS ASP HIS SER LEU GLU GLY ARG
SEQRES 21 A 329 TYR PHE GLN ASN TYR SER TYR GLY GLY VAL ILE GLN ASP
SEQRES 22 A 329 ASP HIS ILE PRO PHE LEU ARG ARG GLY VAL PRO VAL LEU
SEQRES 23 A 329 HIS LEU ILE PRO SER PRO PHE PRO GLU VAL TRP HIS THR
SEQRES 24 A 329 MET ASP ASP ASN GLU GLU ASN LEU ASP GLU SER THR ILE
SEQRES 25 A 329 ASP ASN LEU ASN LYS ILE LEU GLN VAL PHE VAL LEU GLU
SEQRES 26 A 329 TYR LEU HIS LEU
SEQRES 1 B 329 ALA SER ALA TRP PRO GLU GLU LYS ASN TYR HIS GLN PRO
SEQRES 2 B 329 ALA ILE LEU ASN SER SER ALA LEU ARG GLN ILE ALA GLU
SEQRES 3 B 329 GLY THR SER ILE SER GLU MET TRP GLN ASN ASP LEU GLN
SEQRES 4 B 329 PRO LEU LEU ILE GLU ARG TYR PRO GLY SER PRO GLY SER
SEQRES 5 B 329 TYR ALA ALA ARG GLN HIS ILE MET GLN ARG ILE GLN ARG
SEQRES 6 B 329 LEU GLN ALA ASP TRP VAL LEU GLU ILE ASP THR PHE LEU
SEQRES 7 B 329 SER GLN THR PRO TYR GLY TYR ARG SER PHE SER ASN ILE
SEQRES 8 B 329 ILE SER THR LEU ASN PRO THR ALA LYS ARG HIS LEU VAL
SEQRES 9 B 329 LEU ALA CYS HIS TYR ASP SER LYS TYR PHE SER HIS TRP
SEQRES 10 B 329 ASN ASN ARG VAL PHE VAL GLY ALA THR ASP SER ALA VAL
SEQRES 11 B 329 PRO CYS ALA MET MET LEU GLU LEU ALA ARG ALA LEU ASP
SEQRES 12 B 329 LYS LYS LEU LEU SER LEU LYS THR VAL SER ASP SER LYS
SEQRES 13 B 329 PRO ASP LEU SER LEU GLN LEU ILE PHE PHE ASP GLY GLN
SEQRES 14 B 329 GLU ALA PHE LEU HIS TRP SER PRO GLN ASP SER LEU TYR
SEQRES 15 B 329 GLY SER ARG HIS LEU ALA ALA LYS MET ALA SER THR PRO
SEQRES 16 B 329 HIS PRO PRO GLY ALA ARG GLY THR SER GLN LEU HIS GLY
SEQRES 17 B 329 MET ASP LEU LEU VAL LEU LEU ASP LEU ILE GLY ALA PRO
SEQRES 18 B 329 ASN PRO THR PHE PRO ASN PHE PHE PRO ASN SER ALA ARG
SEQRES 19 B 329 TRP PHE GLU ARG LEU GLN ALA ILE GLU HIS GLU LEU HIS
SEQRES 20 B 329 GLU LEU GLY LEU LEU LYS ASP HIS SER LEU GLU GLY ARG
SEQRES 21 B 329 TYR PHE GLN ASN TYR SER TYR GLY GLY VAL ILE GLN ASP
SEQRES 22 B 329 ASP HIS ILE PRO PHE LEU ARG ARG GLY VAL PRO VAL LEU
SEQRES 23 B 329 HIS LEU ILE PRO SER PRO PHE PRO GLU VAL TRP HIS THR
SEQRES 24 B 329 MET ASP ASP ASN GLU GLU ASN LEU ASP GLU SER THR ILE
SEQRES 25 B 329 ASP ASN LEU ASN LYS ILE LEU GLN VAL PHE VAL LEU GLU
SEQRES 26 B 329 TYR LEU HIS LEU
HET ZN A 391 1
HET SO4 A 395 5
HET ZN B 392 1
HET SO4 B 396 5
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 7 HOH *867(H2 O)
HELIX 1 1 ALA A 35 PRO A 37 5 3
HELIX 2 2 GLU A 38 HIS A 43 1 6
HELIX 3 3 ASN A 49 THR A 60 1 12
HELIX 4 4 SER A 61 ASP A 69 1 9
HELIX 5 5 LEU A 70 LEU A 74 5 5
HELIX 6 6 SER A 81 ARG A 97 1 17
HELIX 7 7 SER A 160 LEU A 174 1 15
HELIX 8 8 LEU A 174 SER A 180 1 7
HELIX 9 9 LEU A 213 SER A 225 1 13
HELIX 10 10 PHE A 261 ASN A 263 5 3
HELIX 11 11 SER A 264 LEU A 281 1 18
HELIX 12 12 HIS A 307 ARG A 312 1 6
HELIX 13 13 ASP A 340 HIS A 360 1 21
HELIX 14 14 ALA B 35 PRO B 37 5 3
HELIX 15 15 GLU B 38 HIS B 43 1 6
HELIX 16 16 ASN B 49 THR B 60 1 12
HELIX 17 17 SER B 61 ASP B 69 1 9
HELIX 18 18 LEU B 70 LEU B 74 5 5
HELIX 19 19 SER B 81 ARG B 97 1 17
HELIX 20 20 HIS B 148 ARG B 152 5 5
HELIX 21 21 SER B 160 LEU B 174 1 15
HELIX 22 22 LEU B 174 SER B 180 1 7
HELIX 23 23 LEU B 213 SER B 225 1 13
HELIX 24 24 PHE B 261 ASN B 263 5 3
HELIX 25 25 SER B 264 LEU B 281 1 18
HELIX 26 26 SER B 288 ARG B 292 5 5
HELIX 27 27 HIS B 307 ARG B 312 1 6
HELIX 28 28 ASP B 340 HIS B 360 1 21
SHEET 1 A 6 VAL A 103 SER A 111 0
SHEET 2 A 6 ARG A 118 THR A 126 -1 O ILE A 124 N GLU A 105
SHEET 3 A 6 LEU A 191 PHE A 198 -1 O LEU A 195 N SER A 125
SHEET 4 A 6 ARG A 133 HIS A 140 1 N CYS A 139 O PHE A 198
SHEET 5 A 6 MET A 241 LEU A 247 1 O VAL A 245 N VAL A 136
SHEET 6 A 6 VAL A 317 LEU A 320 1 O LEU A 318 N LEU A 244
SHEET 1 B 6 VAL B 103 THR B 113 0
SHEET 2 B 6 GLY B 116 THR B 126 -1 O ILE B 124 N GLU B 105
SHEET 3 B 6 LEU B 191 PHE B 198 -1 O PHE B 197 N ILE B 123
SHEET 4 B 6 ARG B 133 HIS B 140 1 N CYS B 139 O PHE B 198
SHEET 5 B 6 MET B 241 LEU B 247 1 O VAL B 245 N VAL B 136
SHEET 6 B 6 VAL B 317 LEU B 320 1 O LEU B 318 N LEU B 244
SHEET 1 C 2 PHE B 257 ASN B 259 0
SHEET 2 C 2 PHE B 294 SER B 298 1 O TYR B 297 N ASN B 259
LINK OD2 ASP A 159 ZN ZN A 391 1555 1555 1.96
LINK OE2 GLU A 202 ZN ZN A 391 1555 1555 1.96
LINK NE2 HIS A 330 ZN ZN A 391 1555 1555 2.12
LINK ZN ZN A 391 O HOH A 401 1555 1555 1.99
LINK OD2 ASP B 159 ZN ZN B 392 1555 1555 2.01
LINK OE2 GLU B 202 ZN ZN B 392 1555 1555 1.95
LINK NE2 HIS B 330 ZN ZN B 392 1555 1555 1.97
LINK ZN ZN B 392 O HOH B 402 1555 1555 2.15
CISPEP 1 ASP A 159 SER A 160 0 -3.31
CISPEP 2 HIS A 228 PRO A 229 0 -0.55
CISPEP 3 SER A 323 PRO A 324 0 0.74
CISPEP 4 ASP B 159 SER B 160 0 1.55
CISPEP 5 HIS B 228 PRO B 229 0 -0.59
CISPEP 6 SER B 323 PRO B 324 0 0.42
CRYST1 119.051 119.051 332.652 90.00 90.00 120.00 H 3 2 36
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 0.008400 0.004850 0.000000 0.00000
SCALE2 0.000000 0.009699 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003006 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
