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HEADER HYDROLASE 03-MAR-11 3QYJ
TITLE CRYSTAL STRUCTURE OF ALR0039, A PUTATIVE ALPHA/BETA HYDROLASE FROM
TITLE 2 NOSTOC SP PCC 7120.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALR0039 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC SP.;
SOURCE 3 ORGANISM_TAXID: 103690;
SOURCE 4 STRAIN: PCC 7120 / UTEX 2576;
SOURCE 5 GENE: ALR0039;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS ALPHA/BETA FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.PETIT,O.KAGAN,A.F.YAKUNIN,SAVCHENKO A.
REVDAT 1 16-MAR-11 3QYJ 0
JRNL AUTH P.PETIT,O.KAGAN,A.F.YAKUNIN,SAVCHENKO A.
JRNL TITL CRYSTAL STRUCTURE OF ALR0039, A PUTATIVE ALPHA/BETA
JRNL TITL 2 HYDROLASE FROM NOSTOC SP PCC 7120.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.78 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.78
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 58321
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.300
REMARK 3 FREE R VALUE TEST SET COUNT : 2021
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) : 1.78
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4196
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.12
REMARK 3 BIN R VALUE (WORKING SET) : 0.2340
REMARK 3 BIN FREE R VALUE SET COUNT : 0
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4694
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 634
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 1.40000
REMARK 3 B33 (A**2) : -1.45000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.16000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.103
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.099
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.060
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.854
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4877 ; 0.025 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3279 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6643 ; 1.840 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7962 ; 1.103 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 591 ; 5.985 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 241 ;33.586 ;23.320
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 790 ;13.452 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;22.956 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 713 ; 0.139 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5444 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1037 ; 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): 2923 ; 1.137 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1164 ; 0.373 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4728 ; 1.932 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1954 ; 3.271 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1909 ; 4.593 ; 4.500
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 : 1.40
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
REMARK 4
REMARK 4 3QYJ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064264.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60343
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.778
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.03700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 42.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.25800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.300
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 1Y37
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
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 44.09800
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, 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: 2150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 35.53046
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 44.09800
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 166.93294
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 CYS B 291
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 ARG B 257 CG ARG B 257 CD -0.160
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 MET A 135 CG - SD - CE ANGL. DEV. = -11.7 DEGREES
REMARK 500 ASP A 140 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG B 16 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 16 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 VAL B 71 CG1 - CB - CG2 ANGL. DEV. = 12.5 DEGREES
REMARK 500 ARG B 80 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 MET B 135 CG - SD - CE ANGL. DEV. = -18.0 DEGREES
REMARK 500 ARG B 196 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG B 212 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP B 249 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 257 NE - CZ - NH2 ANGL. DEV. = -4.6 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 GLN A 36 -167.56 -117.44
REMARK 500 ASP A 104 -123.16 57.12
REMARK 500 ASN A 167 77.76 -165.05
REMARK 500 ASP A 182 89.64 -151.30
REMARK 500 THR A 216 -95.02 -130.83
REMARK 500 ASP A 225 36.01 -140.10
REMARK 500 ALA A 276 59.98 -140.21
REMARK 500 GLN B 36 -166.83 -117.68
REMARK 500 ASP B 104 -125.05 58.62
REMARK 500 ASN B 167 86.23 -161.69
REMARK 500 THR B 216 -93.89 -126.72
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3QYJ A 1 291 UNP Q8Z0Q1 Q8Z0Q1_NOSS1 1 291
DBREF 3QYJ B 1 291 UNP Q8Z0Q1 Q8Z0Q1_NOSS1 1 291
SEQRES 1 A 291 MET PHE THR ASN PHE GLU GLN THR ILE VAL ASP THR THR
SEQRES 2 A 291 GLU ALA ARG ILE ASN LEU VAL LYS ALA GLY HIS GLY ALA
SEQRES 3 A 291 PRO LEU LEU LEU LEU HIS GLY TYR PRO GLN THR HIS VAL
SEQRES 4 A 291 MET TRP HIS LYS ILE ALA PRO LEU LEU ALA ASN ASN PHE
SEQRES 5 A 291 THR VAL VAL ALA THR ASP LEU ARG GLY TYR GLY ASP SER
SEQRES 6 A 291 SER ARG PRO ALA SER VAL PRO HIS HIS ILE ASN TYR SER
SEQRES 7 A 291 LYS ARG VAL MET ALA GLN ASP GLN VAL GLU VAL MET SER
SEQRES 8 A 291 LYS LEU GLY TYR GLU GLN PHE TYR VAL VAL GLY HIS ASP
SEQRES 9 A 291 ARG GLY ALA ARG VAL ALA HIS ARG LEU ALA LEU ASP HIS
SEQRES 10 A 291 PRO HIS ARG VAL LYS LYS LEU ALA LEU LEU ASP ILE ALA
SEQRES 11 A 291 PRO THR HIS LYS MET TYR ARG THR THR ASP GLN GLU PHE
SEQRES 12 A 291 ALA THR ALA TYR TYR HIS TRP PHE PHE LEU ILE GLN PRO
SEQRES 13 A 291 ASP ASN LEU PRO GLU THR LEU ILE GLY ALA ASN PRO GLU
SEQRES 14 A 291 TYR TYR LEU ARG LYS CYS LEU GLU LYS TRP GLY LYS ASP
SEQRES 15 A 291 PHE SER ALA PHE HIS PRO GLN ALA LEU ALA GLU TYR ILE
SEQRES 16 A 291 ARG CYS PHE SER GLN PRO ALA VAL ILE HIS ALA THR CYS
SEQRES 17 A 291 GLU ASP TYR ARG ALA ALA ALA THR ILE ASP LEU GLU HIS
SEQRES 18 A 291 ASP GLU LEU ASP MET LYS GLN LYS ILE SER CYS PRO VAL
SEQRES 19 A 291 LEU VAL LEU TRP GLY GLU LYS GLY ILE ILE GLY ARG LYS
SEQRES 20 A 291 TYR ASP VAL LEU ALA THR TRP ARG GLU ARG ALA ILE ASP
SEQRES 21 A 291 VAL SER GLY GLN SER LEU PRO CYS GLY HIS PHE LEU PRO
SEQRES 22 A 291 GLU GLU ALA PRO GLU GLU THR TYR GLN ALA ILE TYR ASN
SEQRES 23 A 291 PHE LEU THR HIS CYS
SEQRES 1 B 291 MET PHE THR ASN PHE GLU GLN THR ILE VAL ASP THR THR
SEQRES 2 B 291 GLU ALA ARG ILE ASN LEU VAL LYS ALA GLY HIS GLY ALA
SEQRES 3 B 291 PRO LEU LEU LEU LEU HIS GLY TYR PRO GLN THR HIS VAL
SEQRES 4 B 291 MET TRP HIS LYS ILE ALA PRO LEU LEU ALA ASN ASN PHE
SEQRES 5 B 291 THR VAL VAL ALA THR ASP LEU ARG GLY TYR GLY ASP SER
SEQRES 6 B 291 SER ARG PRO ALA SER VAL PRO HIS HIS ILE ASN TYR SER
SEQRES 7 B 291 LYS ARG VAL MET ALA GLN ASP GLN VAL GLU VAL MET SER
SEQRES 8 B 291 LYS LEU GLY TYR GLU GLN PHE TYR VAL VAL GLY HIS ASP
SEQRES 9 B 291 ARG GLY ALA ARG VAL ALA HIS ARG LEU ALA LEU ASP HIS
SEQRES 10 B 291 PRO HIS ARG VAL LYS LYS LEU ALA LEU LEU ASP ILE ALA
SEQRES 11 B 291 PRO THR HIS LYS MET TYR ARG THR THR ASP GLN GLU PHE
SEQRES 12 B 291 ALA THR ALA TYR TYR HIS TRP PHE PHE LEU ILE GLN PRO
SEQRES 13 B 291 ASP ASN LEU PRO GLU THR LEU ILE GLY ALA ASN PRO GLU
SEQRES 14 B 291 TYR TYR LEU ARG LYS CYS LEU GLU LYS TRP GLY LYS ASP
SEQRES 15 B 291 PHE SER ALA PHE HIS PRO GLN ALA LEU ALA GLU TYR ILE
SEQRES 16 B 291 ARG CYS PHE SER GLN PRO ALA VAL ILE HIS ALA THR CYS
SEQRES 17 B 291 GLU ASP TYR ARG ALA ALA ALA THR ILE ASP LEU GLU HIS
SEQRES 18 B 291 ASP GLU LEU ASP MET LYS GLN LYS ILE SER CYS PRO VAL
SEQRES 19 B 291 LEU VAL LEU TRP GLY GLU LYS GLY ILE ILE GLY ARG LYS
SEQRES 20 B 291 TYR ASP VAL LEU ALA THR TRP ARG GLU ARG ALA ILE ASP
SEQRES 21 B 291 VAL SER GLY GLN SER LEU PRO CYS GLY HIS PHE LEU PRO
SEQRES 22 B 291 GLU GLU ALA PRO GLU GLU THR TYR GLN ALA ILE TYR ASN
SEQRES 23 B 291 PHE LEU THR HIS CYS
FORMUL 3 HOH *634(H2 O)
HELIX 1 1 THR A 37 HIS A 42 5 6
HELIX 2 2 ILE A 44 ALA A 49 1 6
HELIX 3 3 VAL A 71 TYR A 77 5 7
HELIX 4 4 SER A 78 LEU A 93 1 16
HELIX 5 5 ASP A 104 HIS A 117 1 14
HELIX 6 6 PRO A 131 THR A 138 1 8
HELIX 7 7 ASP A 140 TYR A 147 1 8
HELIX 8 8 TYR A 148 LEU A 153 1 6
HELIX 9 9 ASN A 158 ALA A 166 1 9
HELIX 10 10 ASN A 167 GLY A 180 1 14
HELIX 11 11 ASP A 182 PHE A 186 5 5
HELIX 12 12 HIS A 187 SER A 199 1 13
HELIX 13 13 GLN A 200 ALA A 215 1 16
HELIX 14 14 THR A 216 LEU A 224 1 9
HELIX 15 15 ILE A 243 TYR A 248 1 6
HELIX 16 16 ASP A 249 GLU A 256 1 8
HELIX 17 17 PHE A 271 ALA A 276 1 6
HELIX 18 18 ALA A 276 HIS A 290 1 15
HELIX 19 19 THR B 37 HIS B 42 5 6
HELIX 20 20 ILE B 44 ALA B 49 1 6
HELIX 21 21 VAL B 71 TYR B 77 5 7
HELIX 22 22 SER B 78 LEU B 93 1 16
HELIX 23 23 ASP B 104 HIS B 117 1 14
HELIX 24 24 PRO B 131 THR B 138 1 8
HELIX 25 25 ASP B 140 TYR B 147 1 8
HELIX 26 26 TYR B 148 LEU B 153 1 6
HELIX 27 27 ASN B 158 ALA B 166 1 9
HELIX 28 28 ASN B 167 GLY B 180 1 14
HELIX 29 29 ASP B 182 PHE B 186 5 5
HELIX 30 30 HIS B 187 SER B 199 1 13
HELIX 31 31 GLN B 200 ALA B 215 1 16
HELIX 32 32 THR B 216 ASP B 225 1 10
HELIX 33 33 ILE B 243 TYR B 248 1 6
HELIX 34 34 ASP B 249 GLU B 256 1 8
HELIX 35 35 PHE B 271 ALA B 276 1 6
HELIX 36 36 ALA B 276 HIS B 290 1 15
SHEET 1 A 8 GLU A 6 ASP A 11 0
SHEET 2 A 8 ARG A 16 ALA A 22 -1 O ILE A 17 N VAL A 10
SHEET 3 A 8 THR A 53 THR A 57 -1 O VAL A 54 N ALA A 22
SHEET 4 A 8 PRO A 27 LEU A 31 1 N LEU A 28 O VAL A 55
SHEET 5 A 8 PHE A 98 HIS A 103 1 O TYR A 99 N LEU A 29
SHEET 6 A 8 VAL A 121 LEU A 127 1 O LEU A 127 N GLY A 102
SHEET 7 A 8 VAL A 234 GLY A 239 1 O LEU A 235 N LEU A 124
SHEET 8 A 8 VAL A 261 LEU A 266 1 O LEU A 266 N TRP A 238
SHEET 1 B 8 GLU B 6 ASP B 11 0
SHEET 2 B 8 ARG B 16 ALA B 22 -1 O ILE B 17 N VAL B 10
SHEET 3 B 8 PHE B 52 THR B 57 -1 O VAL B 54 N ALA B 22
SHEET 4 B 8 ALA B 26 LEU B 31 1 N LEU B 28 O VAL B 55
SHEET 5 B 8 PHE B 98 HIS B 103 1 O TYR B 99 N LEU B 29
SHEET 6 B 8 VAL B 121 LEU B 127 1 O ALA B 125 N VAL B 100
SHEET 7 B 8 VAL B 234 GLY B 239 1 O LEU B 235 N LEU B 126
SHEET 8 B 8 VAL B 261 LEU B 266 1 O LEU B 266 N TRP B 238
CISPEP 1 TYR A 34 PRO A 35 0 -8.13
CISPEP 2 TYR B 34 PRO B 35 0 -5.95
CRYST1 44.542 88.196 83.588 90.00 93.09 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 0.022451 0.000000 0.001213 0.00000
SCALE2 0.000000 0.011338 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011981 0.00000
TER 2378 CYS A 291
TER 4734 HIS B 290
MASTER 326 0 0 36 16 0 0 6 5328 2 0 46
END |