HEADER HYDROLASE 02-SEP-15 5AMY
TITLE CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME PROCESSED WITH
TITLE 2 THE CRYSTALDIRECT AUTOMATED MOUNTING AND CRYO-COOLING
TITLE 3 TECHNOLOGY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSOZYME C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C, ALLERGEN GAL D IV, GAL D 4;
COMPND 5 EC: 3.2.1.17
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 4 ORGANISM_COMMON: CHICKEN;
SOURCE 5 ORGANISM_TAXID: 9031
KEYWDS HYDROLASE, AUTOMATED CRYSTAL HARVESTING, AUTOMATED CRYO-COOLING,
KEYWDS 2 CRYSTALDIRECT
EXPDTA X-RAY DIFFRACTION
AUTHOR U.ZANDER,G.HOFFMANN,I.CORNACIU,F.CIPRIANI,J.A.MARQUEZ
REVDAT 1 05-OCT-16 5AMY 0
JRNL AUTH U.ZANDER,G.HOFFMANN,I.CORNACIU,J.-P.MARQUETTE,G.PAPP,
JRNL AUTH 2 C.LANDRET,G.SEROUL,J.SINOIR,M.ROEWER,F.FELISAZ,
JRNL AUTH 3 S.RODRIGUEZ-PUENTE,V.MARIAULE,P.MURPHY,M.MATHIEU,F.CIPRIANI,
JRNL AUTH 4 J.A.MARQUEZ
JRNL TITL AUTOMATED HARVESTING AND PROCESSING OF PROTEIN CRYSTALS
JRNL TITL 2 THROUGH LASER PHOTOABLATION.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0123
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,
REMARK 3 STEINER,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) : 27.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.45
REMARK 3 NUMBER OF REFLECTIONS : 10403
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) : 0.17431
REMARK 3 R VALUE (WORKING SET) : 0.17201
REMARK 3 FREE R VALUE : 0.21979
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.8
REMARK 3 FREE R VALUE TEST SET COUNT : 525
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) : 1.800
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.847
REMARK 3 REFLECTION IN BIN (WORKING SET) : 726
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.88
REMARK 3 BIN R VALUE (WORKING SET) : 0.228
REMARK 3 BIN FREE R VALUE SET COUNT : 41
REMARK 3 BIN FREE R VALUE : 0.282
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1001
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 114
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.920
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00
REMARK 3 B22 (A**2) : 0.00
REMARK 3 B33 (A**2) : 0.00
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.137
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.132
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.099
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.230
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1025 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 940 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1389 ; 1.748 ; 1.903
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2140 ; 1.131 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 128 ; 6.297 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 50 ;38.260 ;23.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 166 ;15.156 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;24.246 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 144 ; 0.122 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1206 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 271 ; 0.002 ; 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): 514 ; 1.604 ; 1.941
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 514 ; 1.601 ; 1.941
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 642 ; 2.263 ; 2.907
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 510 ; 3.290 ; 2.371
REMARK 3 SIDE-CHAIN ANGLE REFINED 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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. U VALUES, REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5AMY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-SEP-15.
REMARK 100 THE PDBE ID CODE IS EBI-64877.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91787
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH (MX-225)
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10961
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.80
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.5
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.1
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, 1.25 M
REMARK 280 NACL, PH=4.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 18.45400
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 38.90400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.90400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 27.68100
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.90400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 38.90400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 9.22700
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.90400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.90400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 27.68100
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 38.90400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.90400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 9.22700
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 18.45400
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 A2042 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2045 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2066 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2114 LIES ON A SPECIAL POSITION.
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 LEU A 129 O LEU A 129 7554 1.85
REMARK 500 O HOH A 2012 O HOH A 2012 7554 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 ASP A 18 CB - CG - OD1 ANGL. DEV. = 8.9 DEGREES
REMARK 500 ASP A 18 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AMW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE STRAWBERRY PATHOGENESIS-RELATED
REMARK 900 10 (PR-10) FRA A 2 PROTEIN PROCESSED WITH THE
REMARK 900 CRYSTALDIRECT AUTOMATED MOUNTING AND CRYO-COOLING
REMARK 900 TECHNOLOGY
REMARK 900 RELATED ID: 5AMX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PROTEINASE K PROCESSED WITH THE
REMARK 900 CRYSTALDIRECT AUTOMATED MOUNTING AND CRYO-COOLING
REMARK 900 TECHNOLOGY
REMARK 900 RELATED ID: 5AMZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THAUMATIN PROCESSED WITH THE
REMARK 900 CRYSTALDIRECT AUTOMATED MOUNTING AND CRYO-COOLING
REMARK 900 TECHNOLOGY
REMARK 900 RELATED ID: 5AN2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN (TTR) PROCESSED
REMARK 900 WITH THE CRYSTALDIRECT AUTOMATED MOUNTING AND CRYO-
REMARK 900 COOLING TECHNOLOGY
REMARK 900 RELATED ID: 5AN4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN 8-OXOGUANINE GLYCOSYLASE
REMARK 900 (OGG1) PROCESSED WITH THE CRYSTALDIRECT AUTOMATED
REMARK 900 MOUNTING AND CRYO-COOLING TECHNOLOGY
REMARK 900 RELATED ID: 5AND RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CDK2 IN COMPLEX WITH 2-IMIDAZOL-
REMARK 900 1-YL-1H-BENZIMIDAZOLE PROCESSED WITH THE CRYSTALDIRECT
REMARK 900 AUTOMATED MOUNTING AND CRYO-COOLING TECHNOLOGY
REMARK 900 RELATED ID: 5ANE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CDK2 IN COMPLEX WITH 6-METHOXY-
REMARK 900 7H-PURINE PROCESSED WITH THE CRYSTALDIRECT AUTOMATED
REMARK 900 MOUNTING AND CRYO-COOLING TECHNOLOGY
REMARK 900 RELATED ID: 5ANG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CDK2 IN COMPLEX WITH 7-HYDROXY-
REMARK 900 4-(MORPHOLINOMETHYL)CHROMEN-2-ONE PROCESSED WITH THE
REMARK 900 CRYSTALDIRECT AUTOMATED MOUNTING AND CRYO-COOLING
REMARK 900 TECHNOLOGY
REMARK 900 RELATED ID: 5ANI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CDK2 IN COMPLEX WITH 6-CHLORO-
REMARK 900 7H-PURINE PROCESSED WITH THE CRYSTALDIRECT AUTOMATED
REMARK 900 MOUNTING AND CRYO-COOLING TECHNOLOGY
REMARK 900 RELATED ID: 5ANJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CDK2 IN COMPLEX WITH N-(9H-
REMARK 900 PURIN-6-YL)THIOPHENE-2-CARBOXAMIDE PROCESSED WITH THE
REMARK 900 CRYSTALDIRECT AUTOMATED MOUNTING AND CRYO-COOLING
REMARK 900 TECHNOLOGY
REMARK 900 RELATED ID: 5ANK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CDK2 IN COMPLEX WITH 2,4,6-
REMARK 900 TRIOXO-1-PHENYL-HEXAHYDROPYRIMIDINE-5-CARBOXAMIDE
REMARK 900 PROCESSED WITH THE CRYSTALDIRECT AUTOMATED MOUNTING AND
REMARK 900 CRYO-COOLING TECHNOLOGY
REMARK 900 RELATED ID: 5ANL RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VPS34 IN COMPLEX WITH (2S)-8-((
REMARK 900 3R)-3-METHYLMORPHOLIN-4-YL)-1-(3-METHYL-2-OXO-
REMARK 900 BUTYL)-2-(TRIFLUOROMETHYL)-3,4-DIHYDRO-2H-PYRIMIDO(1,
REMARK 900 2-A)PYRIMIDIN-6- ONE, PROCESSED WITH THE CRYSTALDIRECT
REMARK 900 AUTOMATED MOUNTING AND CRYO-COOLING TECHNOLOGY
REMARK 900 RELATED ID: 5ANO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CDK2 PROCESSED WITH THE
REMARK 900 CRYSTALDIRECT AUTOMATED MOUNTING AND CRYO-COOLING
REMARK 900 TECHNOLOGY
DBREF 5AMY A 1 129 UNP P00698 LYSC_CHICK 19 147
SEQRES 1 A 129 LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS
SEQRES 2 A 129 ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY
SEQRES 3 A 129 ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN
SEQRES 4 A 129 THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP
SEQRES 5 A 129 TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN
SEQRES 6 A 129 ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE
SEQRES 7 A 129 PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER
SEQRES 8 A 129 VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY
SEQRES 9 A 129 MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY
SEQRES 10 A 129 THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU
FORMUL 2 HOH *114(H2 O)
HELIX 1 1 GLY A 4 HIS A 15 1 12
HELIX 2 2 SER A 24 ASN A 37 1 14
HELIX 3 3 CYS A 80 SER A 85 5 6
HELIX 4 4 ILE A 88 SER A 100 1 13
HELIX 5 5 ASN A 103 ALA A 107 5 5
HELIX 6 6 TRP A 108 CYS A 115 1 8
HELIX 7 7 ASP A 119 ARG A 125 5 7
SHEET 1 AA 3 THR A 43 ARG A 45 0
SHEET 2 AA 3 THR A 51 TYR A 53 -1 O ASP A 52 N ASN A 44
SHEET 3 AA 3 ILE A 58 ASN A 59 -1 O ILE A 58 N TYR A 53
SSBOND 1 CYS A 6 CYS A 127 1555 1555 1.99
SSBOND 2 CYS A 30 CYS A 115 1555 1555 2.07
SSBOND 3 CYS A 64 CYS A 80 1555 1555 2.08
SSBOND 4 CYS A 76 CYS A 94 1555 1555 2.08
CRYST1 77.808 77.808 36.908 90.00 90.00 90.00 P 43 21 2 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 0.012852 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012852 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027094 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
