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HEADER HYDROLASE 24-JUN-15 5A62
TITLE HYDROLYTIC POTENTIAL OF THE AMMONIA-OXIDIZING THAUMARCHAEON
TITLE 2 NITROSOSPHAERA GARGENIS - CRYSTAL STRUCTURE AND ACTIVITY
TITLE 3 PROFILES OF CARBOXYLESTERASES LINKED TO THEIR METABOLIC
TITLE 4 FUNCTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE ALPHA/BETA HYDROLASE FOLD PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CANDIDATUS NITROSOSPHAERA GARGENSIS;
SOURCE 3 ORGANISM_TAXID: 497727;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: ROSETTA-GAMI 2;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET21A
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.CHOW,H.KALJUNEN,E.NITTINGER,E.SPIECK,M.RAREY,J.MUELLER-DIECKMANN,
AUTHOR 2 W.R.STREIT
REVDAT 1 06-JUL-16 5A62 0
JRNL AUTH J.CHOW,H.KALJUNEN,E.NITTINGER,E.SPIECK,M.RAREY,
JRNL AUTH 2 J.MUELLER-DIECKMANN,W.R.STREIT
JRNL TITL HYDROLYTIC POTENTIAL OF THE AMMONIA-OXIDIZING THAUMARCHAEON
JRNL TITL 2 NITROSOSPHAERA GARGENIS - CRYSTAL STRUCTURE AND ACTIVITY
JRNL TITL 3 PROFILES OF CARBOXYLESTERASES LINKED TO THEIR METABOLIC
JRNL TITL 4 FUNCTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.15
REMARK 3 NUMBER OF REFLECTIONS : 40671
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) : 0.14269
REMARK 3 R VALUE (WORKING SET) : 0.14159
REMARK 3 FREE R VALUE : 0.16309
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 2156
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) : 1.500
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.539
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3034
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.167
REMARK 3 BIN FREE R VALUE SET COUNT : 151
REMARK 3 BIN FREE R VALUE : 0.211
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2218
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.613
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.10
REMARK 3 B22 (A**2) : 0.10
REMARK 3 B33 (A**2) : -0.16
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.07
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.061
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.061
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.037
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.958
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2278 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2232 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3092 ; 1.978 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5152 ; 0.916 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 296 ; 5.412 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 101 ;31.878 ;23.465
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 419 ;12.025 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;16.531 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 350 ; 0.121 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2562 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 520 ; 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): 1119 ; 1.613 ; 1.405
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1117 ; 1.593 ; 1.401
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1405 ; 2.490 ; 2.103
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1157 ; 2.715 ; 1.727
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.
REMARK 3 RESIDUES 1 AND 274-277 ARE DISORDERED.
REMARK 4
REMARK 4 5A62 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUN-15.
REMARK 100 THE PDBE ID CODE IS EBI-64124.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III
REMARK 200 BEAMLINE : P14 (MX2)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL (SI111,
REMARK 200 SI311)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42828
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.50
REMARK 200 RESOLUTION RANGE LOW (A) : 51.20
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.3
REMARK 200 R MERGE (I) : 0.03
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.4
REMARK 200 R MERGE FOR SHELL (I) : 0.17
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 21.20
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 1A88
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.2
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM ACETATE, 20%
REMARK 280 PEG 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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 3555 X+1/2,Y+1/2,Z+1/2
REMARK 290 4555 -X+1/2,Y,-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 32.73050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 15.11957
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.73050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 41.00860
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 15.11957
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 41.00860
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.5 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 50.94700
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 A2107 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 MET A 1
REMARK 465 LYS A 274
REMARK 465 PRO A 275
REMARK 465 VAL A 276
REMARK 465 GLY A 277
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CE1 TYR A 15 O HOH A 2020 1.26
REMARK 500 CE2 TYR A 15 O HOH A 2020 1.49
REMARK 500 CZ TYR A 15 O HOH A 2020 0.14
REMARK 500 OH TYR A 15 O HOH A 2020 1.41
REMARK 500 OD1A ASP A 40 O HOH A 2040 1.89
REMARK 500 OD1A ASP A 40 O HOH A 2037 1.80
REMARK 500 OD2A ASP A 40 O HOH A 2038 2.11
REMARK 500 OD2A ASP A 40 O HOH A 2040 2.04
REMARK 500 NH2 ARG A 83 O HOH A 2011 1.61
REMARK 500 CD2 HIS A 87 O HOH A 2086 2.05
REMARK 500 OG SER A 159 O HOH A 2139 2.15
REMARK 500 CG PHE A 224 O HOH A 2099 1.55
REMARK 500 CD1 PHE A 224 O HOH A 2099 1.84
REMARK 500 CD2 PHE A 224 O HOH A 2099 1.20
REMARK 500 CE1 PHE A 224 O HOH A 2099 1.86
REMARK 500 CE2 PHE A 224 O HOH A 2099 1.21
REMARK 500 CZ PHE A 224 O HOH A 2099 1.58
REMARK 500 CA TYR A 259 O HOH A 2205 1.73
REMARK 500 C TYR A 259 O HOH A 2205 1.29
REMARK 500 O TYR A 259 O HOH A 2205 1.56
REMARK 500 CB TYR A 259 O HOH A 2205 1.86
REMARK 500 O HOH A 2043 O HOH A 2106 2.18
REMARK 500 O HOH A 2074 O HOH A 2078 2.11
REMARK 500 O HOH A 2106 O HOH A 2109 1.57
REMARK 500 O HOH A 2156 O HOH A 2157 0.80
REMARK 500
REMARK 500 REMARK: NULL
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 NH2B ARG A 139 OD1 ASP A 165 2555 1.94
REMARK 500 NH2B ARG A 139 O SER A 159 2555 2.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 186 CD GLU A 186 OE1 0.100
REMARK 500 GLU A 186 CG GLU A 186 CD 0.101
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 59 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 83 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP A 174 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 GLU A 186 CG - CD - OE1 ANGL. DEV. = 13.6 DEGREES
REMARK 500 ARG A 226 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 226 NE - CZ - NH2 ANGL. DEV. = -4.1 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 10 11.87 59.55
REMARK 500 ASN A 35 -175.44 -173.67
REMARK 500 HIS A 62 -111.92 57.24
REMARK 500 SER A 99 -118.12 58.31
REMARK 500 ASP A 247 -164.13 -128.49
REMARK 500 TRP A 249 39.86 -88.71
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 ACT A 484
DBREF 5A62 A 1 277 UNP K0IM51 K0IM51_NITGG 1 277
SEQRES 1 A 277 MET PRO PHE LEU SER SER PRO SER ASN SER VAL SER THR
SEQRES 2 A 277 TYR TYR GLU ASP HIS GLY ASP ALA ARG SER TYR PRO LEU
SEQRES 3 A 277 VAL LEU ILE HIS PRO ILE GLY GLY ASN ILE LEU ILE TRP
SEQRES 4 A 277 ASP TYR GLU ILE GLN LEU LEU LEU LYS SER GLY PHE ARG
SEQRES 5 A 277 VAL ILE ALA TYR GLU LEU ARG GLY HIS HIS ARG THR ASN
SEQRES 6 A 277 MET GLY LYS THR GLY ALA TYR THR MET GLN ASP LEU ILE
SEQRES 7 A 277 ASP ASP LEU ARG ARG LEU LEU GLU HIS LEU ASN ILE GLY
SEQRES 8 A 277 LYS CYS THR ILE ILE GLY HIS SER ILE GLY GLY ILE ILE
SEQRES 9 A 277 SER SER MET TYR ALA ALA GLN HIS PRO GLY LYS VAL ASP
SEQRES 10 A 277 ALA ILE ILE MET ILE ASN GLY SER PRO LYS LYS PHE GLN
SEQRES 11 A 277 GLU LYS ASP LEU GLU LYS HIS PHE ARG THR ARG GLU VAL
SEQRES 12 A 277 ALA ILE THR GLN GLY MET LYS ALA LEU ALA GLU HIS LYS
SEQRES 13 A 277 LEU VAL SER LEU ASP GLU ALA ARG ASP LEU PHE ALA ASP
SEQRES 14 A 277 LYS ARG HIS ALA ASP PHE PHE ARG GLU VAL PHE THR LYS
SEQRES 15 A 277 THR SER VAL GLU GLY PHE VAL ALA ALA THR VAL ALA LEU
SEQRES 16 A 277 TYR THR ILE PRO GLY ASN VAL VAL GLN GLY LEU ARG ALA
SEQRES 17 A 277 SER GLY CYS LYS VAL PHE ALA ILE VAL GLY SER ASP ASP
SEQRES 18 A 277 ASP VAL PHE MET ARG LEU ILE LYS GLU THR LYS GLU GLU
SEQRES 19 A 277 ILE PRO GLU MET GLU LEU ARG VAL LEU GLN GLY SER ASP
SEQRES 20 A 277 HIS TRP VAL VAL ILE GLU LYS PRO LYS GLU MET TYR ASP
SEQRES 21 A 277 ILE LEU MET GLY PHE LEU ALA ILE VAL THR LYS ASP VAL
SEQRES 22 A 277 LYS PRO VAL GLY
HET ACT A 484 4
HETNAM ACT ACETATE ION
FORMUL 2 ACT C2 H3 O2 1-
FORMUL 3 HOH *209(H2 O)
HELIX 1 1 ASN A 35 ILE A 38 5 4
HELIX 2 2 TRP A 39 SER A 49 1 11
HELIX 3 3 THR A 73 LEU A 88 1 16
HELIX 4 4 SER A 99 HIS A 112 1 14
HELIX 5 5 GLN A 130 GLU A 135 1 6
HELIX 6 6 GLU A 135 GLY A 148 1 14
HELIX 7 7 GLY A 148 VAL A 158 1 11
HELIX 8 8 ASP A 169 THR A 181 1 13
HELIX 9 9 SER A 184 LEU A 195 1 12
HELIX 10 10 TYR A 196 ILE A 198 5 3
HELIX 11 11 ASN A 201 GLY A 210 1 10
HELIX 12 12 ASP A 221 ILE A 235 1 15
HELIX 13 13 TRP A 249 LYS A 254 1 6
HELIX 14 14 PRO A 255 VAL A 273 1 19
SHEET 1 AA 8 PHE A 3 SER A 5 0
SHEET 2 AA 8 SER A 12 HIS A 18 -1 O THR A 13 N LEU A 4
SHEET 3 AA 8 ARG A 52 TYR A 56 -1 O VAL A 53 N HIS A 18
SHEET 4 AA 8 PRO A 25 ILE A 29 1 O LEU A 26 N ILE A 54
SHEET 5 AA 8 CYS A 93 HIS A 98 1 O THR A 94 N VAL A 27
SHEET 6 AA 8 VAL A 116 ILE A 122 1 N ASP A 117 O CYS A 93
SHEET 7 AA 8 LYS A 212 GLY A 218 1 O LYS A 212 N ILE A 119
SHEET 8 AA 8 GLU A 239 LEU A 243 1 O GLU A 239 N ALA A 215
SITE 1 AC1 5 ILE A 32 SER A 99 ILE A 100 HOH A2034
SITE 2 AC1 5 HOH A2125
CRYST1 50.947 65.461 84.591 90.00 104.17 90.00 I 1 2 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 0.019628 0.000000 0.004956 0.00000
SCALE2 0.000000 0.015276 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012193 0.00000
TER 2219 VAL A 273
MASTER 385 0 1 14 8 0 2 6 2431 1 4 22
END |