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HEADER HYDROLASE 14-FEB-15 4Y7D
TITLE ALPHA/BETA HYDROLASE FOLD PROTEIN FROM NAKAMURELLA MULTIPARTITA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NAKAMURELLA MULTIPARTITA (STRAIN ATCC 700099 /
SOURCE 3 DSM 44233 / JCM 9543 / Y-104);
SOURCE 4 ORGANISM_TAXID: 479431;
SOURCE 5 STRAIN: ATCC 700099 / DSM 44233 / JCM 9543 / Y-104;
SOURCE 6 GENE: NAMU_0557;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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: PMCSG73
KEYWDS ALPHA/BETA HYDROLASE, STRUCTURAL GENOMICS, APC103603, MIDWEST CENTER
KEYWDS 2 FOR STRUCTURAL GENOMICS, PSI-BIOLOGY, MCSG
EXPDTA X-RAY DIFFRACTION
AUTHOR M.E.CUFF,J.OSIPIUK,J.HOLOWICKI,M.ENDRES,A.JOACHIMIAK,MIDWEST CENTER
AUTHOR 2 FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 25-FEB-15 4Y7D 0
JRNL AUTH M.E.CUFF,J.OSIPIUK,J.HOLOWICKI,M.ENDRES,A.JOACHIMIAK
JRNL TITL ALPHA/BETA HYDROLASE FOLD PROTEIN FROM NAKAMURELLA
JRNL TITL 2 MULTIPARTITA.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.68 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.68
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 69609
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) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3581
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) : 1.68
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4787
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 249
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4267
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 724
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.69000
REMARK 3 B22 (A**2) : 2.99000
REMARK 3 B33 (A**2) : -1.30000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.086
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.088
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.068
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.154
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.975
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.967
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4643 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4442 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6358 ; 1.619 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10227 ; 0.844 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 644 ; 5.574 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 216 ;33.267 ;22.407
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 694 ;13.978 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;16.105 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 705 ; 0.096 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5459 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1102 ; 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): 2382 ; 1.063 ; 1.421
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2381 ; 1.055 ; 1.420
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2993 ; 1.653 ; 2.127
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 11 A 502
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8905 31.8112 69.2672
REMARK 3 T TENSOR
REMARK 3 T11: 0.0956 T22: 0.0420
REMARK 3 T33: 0.0594 T12: -0.0135
REMARK 3 T13: 0.0130 T23: -0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 1.2377 L22: 0.5916
REMARK 3 L33: 1.2884 L12: -0.0897
REMARK 3 L13: -0.2929 L23: -0.1902
REMARK 3 S TENSOR
REMARK 3 S11: 0.0644 S12: -0.1171 S13: 0.0238
REMARK 3 S21: 0.0042 S22: -0.0489 S23: -0.1202
REMARK 3 S31: -0.0832 S32: 0.0657 S33: -0.0155
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 11 B 502
REMARK 3 ORIGIN FOR THE GROUP (A): 34.1380 21.2859 27.2678
REMARK 3 T TENSOR
REMARK 3 T11: 0.0913 T22: 0.0165
REMARK 3 T33: 0.0377 T12: 0.0052
REMARK 3 T13: 0.0009 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.9646 L22: 1.3393
REMARK 3 L33: 1.4337 L12: -0.0633
REMARK 3 L13: 0.3799 L23: -0.8440
REMARK 3 S TENSOR
REMARK 3 S11: -0.0011 S12: 0.1185 S13: 0.0131
REMARK 3 S21: -0.0546 S22: -0.0003 S23: -0.0422
REMARK 3 S31: 0.0410 S32: 0.0555 S33: 0.0014
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 RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4Y7D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000206991.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73782
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.680
REMARK 200 RESOLUTION RANGE LOW (A) : 36.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.68
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.63600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PORPANE -NAOH BUFFER,
REMARK 280 1.2 M DL-MALIC ACID, PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
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 33.70200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.26800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.69700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.26800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.70200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.69700
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
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 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 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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 101.10600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 75.39400
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 63.26800
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 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 GLU A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 ARG A 8
REMARK 465 ASP A 9
REMARK 465 GLU A 10
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 SER B 4
REMARK 465 GLU B 5
REMARK 465 ALA B 6
REMARK 465 SER B 7
REMARK 465 ARG B 8
REMARK 465 ASP B 9
REMARK 465 GLU B 10
REMARK 465 GLY B 299
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 O HOH A 826 O HOH A 957 1.99
REMARK 500 NH1 ARG A 122 O HOH A 922 2.02
REMARK 500 OE2 GLU A 266 O HOH A 601 2.04
REMARK 500 O HOH B 648 O HOH B 680 2.07
REMARK 500 NH2 ARG B 213 O HOH B 951 2.09
REMARK 500 O HOH A 662 O HOH A 954 2.11
REMARK 500 O ARG B 226 O HOH B 601 2.14
REMARK 500 NE2 HIS B 182 O HOH B 602 2.14
REMARK 500 O HOH A 762 O HOH A 957 2.15
REMARK 500 O HOH B 709 O HOH B 885 2.15
REMARK 500 OD2 ASP B 195 O HOH B 603 2.15
REMARK 500 OD2 ASP B 80 O HOH B 604 2.16
REMARK 500 O HOH A 790 O HOH A 888 2.17
REMARK 500 O HOH B 832 O HOH B 961 2.17
REMARK 500 O HOH A 623 O HOH A 625 2.19
REMARK 500 O HOH A 792 O HOH A 911 2.19
REMARK 500 O HOH B 771 O HOH B 949 2.19
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 44 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP B 44 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG B 65 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 153 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ASP B 228 CB - CG - OD1 ANGL. DEV. = 6.3 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 PHE A 69 -122.30 45.81
REMARK 500 PHE A 69 -121.35 44.13
REMARK 500 SER A 104 -124.72 60.13
REMARK 500 ALA A 128 57.69 34.96
REMARK 500 ASP A 228 -72.01 -89.04
REMARK 500 PHE B 69 -122.92 50.88
REMARK 500 SER B 104 -126.21 63.07
REMARK 500 ALA B 128 58.60 37.67
REMARK 500 ASP B 228 -83.84 -86.07
REMARK 500 ASP B 228 -80.85 -88.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 942 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH B 825 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH B 935 DISTANCE = 5.89 ANGSTROMS
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 NA A 502 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 173 O
REMARK 620 2 GLY A 176 O 83.6
REMARK 620 3 HOH A 798 O 83.5 71.5
REMARK 620 4 HOH A 909 O 175.6 100.8 97.1
REMARK 620 5 HOH A 847 O 86.8 170.3 108.1 88.9
REMARK 620 6 HOH A 910 O 86.1 93.7 162.8 94.2 85.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 502 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 173 O
REMARK 620 2 GLY B 176 O 84.6
REMARK 620 3 HOH B 818 O 82.8 72.9
REMARK 620 4 HOH B 874 O 86.5 169.4 100.5
REMARK 620 5 HOH B 937 O 172.9 97.4 104.4 92.1
REMARK 620 6 HOH B 938 O 86.3 90.7 161.1 94.3 86.8
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MCSG-APC103603 RELATED DB: TARGETTRACK
DBREF 4Y7D A 1 299 UNP C8X7A4 C8X7A4_NAKMY 1 299
DBREF 4Y7D B 1 299 UNP C8X7A4 C8X7A4_NAKMY 1 299
SEQADV 4Y7D SER A -2 UNP C8X7A4 EXPRESSION TAG
SEQADV 4Y7D ASN A -1 UNP C8X7A4 EXPRESSION TAG
SEQADV 4Y7D ALA A 0 UNP C8X7A4 EXPRESSION TAG
SEQADV 4Y7D SER B -2 UNP C8X7A4 EXPRESSION TAG
SEQADV 4Y7D ASN B -1 UNP C8X7A4 EXPRESSION TAG
SEQADV 4Y7D ALA B 0 UNP C8X7A4 EXPRESSION TAG
SEQRES 1 A 302 SER ASN ALA MSE ALA THR SER GLU ALA SER ARG ASP GLU
SEQRES 2 A 302 SER VAL GLN THR VAL SER THR ALA ARG GLY GLU VAL ASP
SEQRES 3 A 302 CYS VAL ILE VAL GLY ALA GLY PRO PRO VAL LEU VAL VAL
SEQRES 4 A 302 HIS GLY SER PRO GLY GLY HIS ASP ALA GLY LEU ALA MSE
SEQRES 5 A 302 ALA ARG PHE LEU VAL ALA GLU GLY LEU ARG ALA ILE VAL
SEQRES 6 A 302 VAL ASP ARG PRO GLY TYR PHE GLY THR PRO LEU GLY SER
SEQRES 7 A 302 GLY VAL THR PRO ASP GLU GLN ALA GLU LEU TYR ALA ALA
SEQRES 8 A 302 LEU PHE ASP ALA LEU GLY LEU ALA ALA ALA GLY VAL LEU
SEQRES 9 A 302 CYS TRP SER GLY GLY GLY PRO SER SER TYR ARG LEU ALA
SEQRES 10 A 302 ALA ARG HIS PRO ASP ARG VAL ARG ALA LEU VAL SER VAL
SEQRES 11 A 302 ALA ALA VAL SER HIS ARG TYR HIS PHE ASP GLY GLU LYS
SEQRES 12 A 302 GLY ALA GLU LYS VAL LEU MSE GLY THR GLY LEU GLY ARG
SEQRES 13 A 302 ARG MSE LEU GLN LEU MSE ALA ALA HIS THR PRO GLU LYS
SEQRES 14 A 302 LEU VAL SER ALA THR ILE ALA ALA GLU GLY HIS LEU SER
SEQRES 15 A 302 LYS GLU HIS VAL ALA GLU ARG VAL ALA GLN ILE MSE ALA
SEQRES 16 A 302 ASP PRO ASP LYS GLU ARG PHE THR LEU GLU LEU ALA VAL
SEQRES 17 A 302 SER ALA ASN HIS SER GLY PRO ARG LYS ALA GLY PHE ASP
SEQRES 18 A 302 ASN ASP MSE ASP GLN PHE ALA ARG ILE ASP SER LEU GLU
SEQRES 19 A 302 LEU ASP ARG ILE THR ALA PRO THR LEU VAL VAL SER GLY
SEQRES 20 A 302 THR ALA ASP SER ASP VAL ASP PRO GLU PHE SER ARG PHE
SEQRES 21 A 302 ALA ALA ALA GLN ILE ALA GLY SER GLU LEU VAL HIS LEU
SEQRES 22 A 302 ASP ALA GLY THR HIS LEU ALA PHE TRP VAL HIS PRO ASP
SEQRES 23 A 302 SER GLY PRO VAL ARG ARG ARG ALA ALA GLU LEU LEU ARG
SEQRES 24 A 302 ALA GLY GLY
SEQRES 1 B 302 SER ASN ALA MSE ALA THR SER GLU ALA SER ARG ASP GLU
SEQRES 2 B 302 SER VAL GLN THR VAL SER THR ALA ARG GLY GLU VAL ASP
SEQRES 3 B 302 CYS VAL ILE VAL GLY ALA GLY PRO PRO VAL LEU VAL VAL
SEQRES 4 B 302 HIS GLY SER PRO GLY GLY HIS ASP ALA GLY LEU ALA MSE
SEQRES 5 B 302 ALA ARG PHE LEU VAL ALA GLU GLY LEU ARG ALA ILE VAL
SEQRES 6 B 302 VAL ASP ARG PRO GLY TYR PHE GLY THR PRO LEU GLY SER
SEQRES 7 B 302 GLY VAL THR PRO ASP GLU GLN ALA GLU LEU TYR ALA ALA
SEQRES 8 B 302 LEU PHE ASP ALA LEU GLY LEU ALA ALA ALA GLY VAL LEU
SEQRES 9 B 302 CYS TRP SER GLY GLY GLY PRO SER SER TYR ARG LEU ALA
SEQRES 10 B 302 ALA ARG HIS PRO ASP ARG VAL ARG ALA LEU VAL SER VAL
SEQRES 11 B 302 ALA ALA VAL SER HIS ARG TYR HIS PHE ASP GLY GLU LYS
SEQRES 12 B 302 GLY ALA GLU LYS VAL LEU MSE GLY THR GLY LEU GLY ARG
SEQRES 13 B 302 ARG MSE LEU GLN LEU MSE ALA ALA HIS THR PRO GLU LYS
SEQRES 14 B 302 LEU VAL SER ALA THR ILE ALA ALA GLU GLY HIS LEU SER
SEQRES 15 B 302 LYS GLU HIS VAL ALA GLU ARG VAL ALA GLN ILE MSE ALA
SEQRES 16 B 302 ASP PRO ASP LYS GLU ARG PHE THR LEU GLU LEU ALA VAL
SEQRES 17 B 302 SER ALA ASN HIS SER GLY PRO ARG LYS ALA GLY PHE ASP
SEQRES 18 B 302 ASN ASP MSE ASP GLN PHE ALA ARG ILE ASP SER LEU GLU
SEQRES 19 B 302 LEU ASP ARG ILE THR ALA PRO THR LEU VAL VAL SER GLY
SEQRES 20 B 302 THR ALA ASP SER ASP VAL ASP PRO GLU PHE SER ARG PHE
SEQRES 21 B 302 ALA ALA ALA GLN ILE ALA GLY SER GLU LEU VAL HIS LEU
SEQRES 22 B 302 ASP ALA GLY THR HIS LEU ALA PHE TRP VAL HIS PRO ASP
SEQRES 23 B 302 SER GLY PRO VAL ARG ARG ARG ALA ALA GLU LEU LEU ARG
SEQRES 24 B 302 ALA GLY GLY
MODRES 4Y7D MSE A 49 MET MODIFIED RESIDUE
MODRES 4Y7D MSE A 147 MET MODIFIED RESIDUE
MODRES 4Y7D MSE A 155 MET MODIFIED RESIDUE
MODRES 4Y7D MSE A 159 MET MODIFIED RESIDUE
MODRES 4Y7D MSE A 191 MET MODIFIED RESIDUE
MODRES 4Y7D MSE A 221 MET MODIFIED RESIDUE
MODRES 4Y7D MSE B 49 MET MODIFIED RESIDUE
MODRES 4Y7D MSE B 147 MET MODIFIED RESIDUE
MODRES 4Y7D MSE B 155 MET MODIFIED RESIDUE
MODRES 4Y7D MSE B 159 MET MODIFIED RESIDUE
MODRES 4Y7D MSE B 191 MET MODIFIED RESIDUE
MODRES 4Y7D MSE B 221 MET MODIFIED RESIDUE
HET MSE A 49 8
HET MSE A 147 8
HET MSE A 155 8
HET MSE A 159 8
HET MSE A 191 8
HET MSE A 221 8
HET MSE B 49 8
HET MSE B 147 8
HET MSE B 155 8
HET MSE B 159 8
HET MSE B 191 8
HET MSE B 221 13
HET CL A 501 1
HET NA A 502 1
HET CL B 501 1
HET NA B 502 1
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 3 CL 2(CL 1-)
FORMUL 4 NA 2(NA 1+)
FORMUL 7 HOH *724(H2 O)
HELIX 1 AA1 GLY A 42 GLU A 56 1 15
HELIX 2 AA2 PRO A 72 GLY A 76 5 5
HELIX 3 AA3 THR A 78 LEU A 93 1 16
HELIX 4 AA4 GLY A 106 HIS A 117 1 12
HELIX 5 AA5 LYS A 140 THR A 149 1 10
HELIX 6 AA6 THR A 149 THR A 163 1 15
HELIX 7 AA7 THR A 163 GLU A 175 1 13
HELIX 8 AA8 SER A 179 ALA A 192 1 14
HELIX 9 AA9 ASP A 193 ALA A 207 1 15
HELIX 10 AB1 SER A 210 PRO A 212 5 3
HELIX 11 AB2 ARG A 213 ALA A 225 1 13
HELIX 12 AB3 GLU A 231 ILE A 235 5 5
HELIX 13 AB4 ASP A 251 ILE A 262 1 12
HELIX 14 AB5 LEU A 276 HIS A 281 1 6
HELIX 15 AB6 SER A 284 ALA A 297 1 14
HELIX 16 AB7 GLY B 42 GLU B 56 1 15
HELIX 17 AB8 PRO B 72 GLY B 76 5 5
HELIX 18 AB9 THR B 78 GLY B 94 1 17
HELIX 19 AC1 GLY B 106 HIS B 117 1 12
HELIX 20 AC2 GLY B 141 THR B 149 1 9
HELIX 21 AC3 THR B 149 THR B 163 1 15
HELIX 22 AC4 THR B 163 GLU B 175 1 13
HELIX 23 AC5 SER B 179 ALA B 192 1 14
HELIX 24 AC6 ASP B 193 ALA B 207 1 15
HELIX 25 AC7 SER B 210 PRO B 212 5 3
HELIX 26 AC8 ARG B 213 ALA B 225 1 13
HELIX 27 AC9 GLU B 231 ILE B 235 5 5
HELIX 28 AD1 ASP B 251 ILE B 262 1 12
HELIX 29 AD2 LEU B 276 HIS B 281 1 6
HELIX 30 AD3 SER B 284 GLY B 298 1 15
SHEET 1 AA1 8 GLN A 13 THR A 17 0
SHEET 2 AA1 8 GLY A 20 GLY A 28 -1 O VAL A 22 N VAL A 15
SHEET 3 AA1 8 ARG A 59 VAL A 63 -1 O ALA A 60 N VAL A 27
SHEET 4 AA1 8 PRO A 32 VAL A 36 1 N VAL A 33 O ILE A 61
SHEET 5 AA1 8 ALA A 98 TRP A 103 1 O GLY A 99 N LEU A 34
SHEET 6 AA1 8 VAL A 121 VAL A 127 1 O VAL A 125 N VAL A 100
SHEET 7 AA1 8 THR A 239 GLY A 244 1 O LEU A 240 N SER A 126
SHEET 8 AA1 8 GLU A 266 LEU A 270 1 O GLU A 266 N VAL A 241
SHEET 1 AA2 8 GLN B 13 VAL B 15 0
SHEET 2 AA2 8 VAL B 22 GLY B 28 -1 O VAL B 22 N VAL B 15
SHEET 3 AA2 8 ARG B 59 VAL B 63 -1 O VAL B 62 N VAL B 25
SHEET 4 AA2 8 PRO B 32 VAL B 36 1 N VAL B 33 O ILE B 61
SHEET 5 AA2 8 ALA B 98 TRP B 103 1 O GLY B 99 N LEU B 34
SHEET 6 AA2 8 VAL B 121 VAL B 127 1 O VAL B 127 N CYS B 102
SHEET 7 AA2 8 THR B 239 GLY B 244 1 O LEU B 240 N SER B 126
SHEET 8 AA2 8 GLU B 266 LEU B 270 1 O GLU B 266 N VAL B 241
LINK C ALA A 48 N MSE A 49 1555 1555 1.33
LINK C MSE A 49 N ALA A 50 1555 1555 1.34
LINK C LEU A 146 N MSE A 147 1555 1555 1.34
LINK C MSE A 147 N GLY A 148 1555 1555 1.33
LINK C ARG A 154 N MSE A 155 1555 1555 1.33
LINK C MSE A 155 N LEU A 156 1555 1555 1.33
LINK C LEU A 158 N MSE A 159 1555 1555 1.33
LINK C MSE A 159 N ALA A 160 1555 1555 1.32
LINK O ALA A 173 NA NA A 502 1555 1555 2.33
LINK O GLY A 176 NA NA A 502 1555 1555 2.32
LINK C ILE A 190 N MSE A 191 1555 1555 1.33
LINK C MSE A 191 N ALA A 192 1555 1555 1.34
LINK C ASP A 220 N MSE A 221 1555 1555 1.32
LINK C MSE A 221 N ASP A 222 1555 1555 1.32
LINK C ALA B 48 N MSE B 49 1555 1555 1.33
LINK C MSE B 49 N ALA B 50 1555 1555 1.34
LINK C LEU B 146 N MSE B 147 1555 1555 1.33
LINK C MSE B 147 N GLY B 148 1555 1555 1.33
LINK C ARG B 154 N MSE B 155 1555 1555 1.32
LINK C MSE B 155 N LEU B 156 1555 1555 1.33
LINK C LEU B 158 N MSE B 159 1555 1555 1.33
LINK C MSE B 159 N ALA B 160 1555 1555 1.32
LINK O ALA B 173 NA NA B 502 1555 1555 2.24
LINK O GLY B 176 NA NA B 502 1555 1555 2.38
LINK C ILE B 190 N MSE B 191 1555 1555 1.32
LINK C MSE B 191 N ALA B 192 1555 1555 1.35
LINK C ASP B 220 N MSE B 221 1555 1555 1.32
LINK C MSE B 221 N ASP B 222 1555 1555 1.33
LINK NA NA A 502 O HOH A 798 1555 1555 2.71
LINK NA NA A 502 O HOH A 909 1555 1555 2.44
LINK NA NA A 502 O HOH A 847 1555 1555 2.43
LINK NA NA A 502 O HOH A 910 1555 1555 2.56
LINK NA NA B 502 O HOH B 818 1555 1555 2.92
LINK NA NA B 502 O HOH B 874 1555 1555 2.34
LINK NA NA B 502 O HOH B 937 1555 1555 2.48
LINK NA NA B 502 O HOH B 938 1555 1555 2.39
CISPEP 1 SER A 39 PRO A 40 0 -6.64
CISPEP 2 SER B 39 PRO B 40 0 -9.38
SITE 1 AC1 3 ARG A 186 THR A 274 ALA A 277
SITE 1 AC2 6 ALA A 173 GLY A 176 HOH A 798 HOH A 847
SITE 2 AC2 6 HOH A 909 HOH A 910
SITE 1 AC3 3 ARG B 186 THR B 274 ALA B 277
SITE 1 AC4 6 ALA B 173 GLY B 176 HOH B 818 HOH B 874
SITE 2 AC4 6 HOH B 937 HOH B 938
CRYST1 67.404 75.394 126.536 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 0.014836 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013264 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007903 0.00000
TER 2259 GLY A 299
TER 4513 GLY B 298
MASTER 463 0 16 30 16 0 6 6 4995 2 141 48
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