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HEADER HYDROLASE 07-JUL-09 3I6Y
TITLE STRUCTURE OF AN ESTERASE FROM THE OIL-DEGRADING BACTERIUM
TITLE 2 OLEISPIRA ANTARCTICA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE APC40077;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OLEISPIRA ANTARCTICA;
SOURCE 3 ORGANISM_TAXID: 188908;
SOURCE 4 GENE: OLEI01171;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIPL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS OLEISPIRA ANTARCTICA, LIPASE, STRUCTURAL GENOMICS, PSI-2,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.U.SINGER,E.EVDOKIMOVA,O.KAGAN,A.M.EDWARDS,A.JOACHIMIAK,
AUTHOR 2 A.SAVCHENKO,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 28-JUL-09 3I6Y 0
JRNL AUTH A.U.SINGER,E.EVDOKIMOVA,O.KAGAN,A.M.EDWARDS,
JRNL AUTH 2 A.SAVCHENKO,A.F.YAKUNIN
JRNL TITL STRUCTURE OF AN ESTERASE FROM THE OIL-DEGRADING
JRNL TITL 2 BACTERIUM OLEISPIRA ANTARCTICA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 57845
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3072
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3436
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.2530
REMARK 3 BIN FREE R VALUE SET COUNT : 174
REMARK 3 BIN FREE R VALUE : 0.3030
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4545
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 515
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.09000
REMARK 3 B33 (A**2) : -0.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.127
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.124
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.071
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.138
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.944
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4715 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6434 ; 1.484 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 602 ; 6.761 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 232 ;36.599 ;24.224
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 718 ;14.165 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;14.390 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 658 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3795 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2559 ; 0.222 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3266 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 432 ; 0.146 ; 0.200
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): 73 ; 0.223 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 34 ; 0.193 ; 0.200
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): 2992 ; 0.891 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4687 ; 1.281 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2004 ; 2.394 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1747 ; 3.430 ; 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 : 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 1 A 279
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0888 19.8940 -37.5048
REMARK 3 T TENSOR
REMARK 3 T11: -0.0031 T22: -0.0032
REMARK 3 T33: -0.0185 T12: 0.0032
REMARK 3 T13: 0.0082 T23: 0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.0950 L22: 0.2864
REMARK 3 L33: 0.1415 L12: 0.0038
REMARK 3 L13: 0.0323 L23: 0.0809
REMARK 3 S TENSOR
REMARK 3 S11: -0.0077 S12: -0.0053 S13: -0.0069
REMARK 3 S21: -0.0431 S22: -0.0120 S23: -0.0003
REMARK 3 S31: -0.0028 S32: -0.0011 S33: 0.0197
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 1 B 279
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7213 35.4365 -5.1982
REMARK 3 T TENSOR
REMARK 3 T11: -0.0191 T22: 0.0049
REMARK 3 T33: -0.0148 T12: -0.0039
REMARK 3 T13: 0.0027 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.0647 L22: 0.3979
REMARK 3 L33: 0.2098 L12: -0.0753
REMARK 3 L13: 0.0017 L23: 0.1696
REMARK 3 S TENSOR
REMARK 3 S11: -0.0086 S12: -0.0089 S13: -0.0049
REMARK 3 S21: 0.0253 S22: -0.0185 S23: 0.0198
REMARK 3 S31: 0.0025 S32: -0.0116 S33: 0.0270
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 4
REMARK 4 3I6Y COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB054041.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61811
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 27.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.3380
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.31300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: PHASER
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1PV1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M DIAMMONIUM HYDROGEN CITRATE,
REMARK 280 20% PEB3350, CRYOPROTECTED IN PARATONE-N OIL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 294K, PH 5.0
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 44.08950
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
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 GLY A 0
REMARK 465 MSE A 1
REMARK 465 GLY B 0
REMARK 465 MSE B 1
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 OE2 GLU B 74 O HOH B 380 2.01
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 THR A 56 -13.03 74.89
REMARK 500 SER A 58 -168.97 -111.94
REMARK 500 ALA A 103 43.55 -150.46
REMARK 500 PHE A 105 13.23 55.13
REMARK 500 ASP A 256 -158.05 -105.16
REMARK 500 THR B 56 -10.62 78.09
REMARK 500 ALA B 103 44.09 -149.51
REMARK 500 PHE B 105 17.64 54.21
REMARK 500 ASP B 256 -153.72 -104.86
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN B 278 ALA B 279 133.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ALA B 279 24.0 L L OUTSIDE RANGE
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 B 418 DISTANCE = 6.49 ANGSTROMS
REMARK 525 HOH B 546 DISTANCE = 6.29 ANGSTROMS
REMARK 525 HOH A 545 DISTANCE = 6.44 ANGSTROMS
REMARK 525 HOH A 547 DISTANCE = 6.43 ANGSTROMS
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 280
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 281
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 282
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 283
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 284
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 280
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 281
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 282
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B 283
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC40077 RELATED DB: TARGETDB
DBREF 3I6Y A 0 279 PDB 3I6Y 3I6Y 0 279
DBREF 3I6Y B 0 279 PDB 3I6Y 3I6Y 0 279
SEQRES 1 A 280 GLY MSE SER ILE GLU ASN LEU SER SER ASN LYS SER PHE
SEQRES 2 A 280 GLY GLY TRP HIS LYS GLN TYR SER HIS VAL SER ASN THR
SEQRES 3 A 280 LEU ASN CYS ALA MSE ARG PHE ALA ILE TYR LEU PRO PRO
SEQRES 4 A 280 GLN ALA SER THR GLY ALA LYS VAL PRO VAL LEU TYR TRP
SEQRES 5 A 280 LEU SER GLY LEU THR CYS SER ASP GLU ASN PHE MSE GLN
SEQRES 6 A 280 LYS ALA GLY ALA GLN ARG LEU ALA ALA GLU LEU GLY ILE
SEQRES 7 A 280 ALA ILE VAL ALA PRO ASP THR SER PRO ARG GLY GLU GLY
SEQRES 8 A 280 VAL ALA ASP ASP GLU GLY TYR ASP LEU GLY GLN GLY ALA
SEQRES 9 A 280 GLY PHE TYR VAL ASN ALA THR GLN ALA PRO TRP ASN ARG
SEQRES 10 A 280 HIS TYR GLN MSE TYR ASP TYR VAL VAL ASN GLU LEU PRO
SEQRES 11 A 280 GLU LEU ILE GLU SER MSE PHE PRO VAL SER ASP LYS ARG
SEQRES 12 A 280 ALA ILE ALA GLY HIS SER MSE GLY GLY HIS GLY ALA LEU
SEQRES 13 A 280 THR ILE ALA LEU ARG ASN PRO GLU ARG TYR GLN SER VAL
SEQRES 14 A 280 SER ALA PHE SER PRO ILE ASN ASN PRO VAL ASN CYS PRO
SEQRES 15 A 280 TRP GLY GLN LYS ALA PHE THR ALA TYR LEU GLY LYS ASP
SEQRES 16 A 280 THR ASP THR TRP ARG GLU TYR ASP ALA SER LEU LEU MSE
SEQRES 17 A 280 ARG ALA ALA LYS GLN TYR VAL PRO ALA LEU VAL ASP GLN
SEQRES 18 A 280 GLY GLU ALA ASP ASN PHE LEU ALA GLU GLN LEU LYS PRO
SEQRES 19 A 280 GLU VAL LEU GLU ALA ALA ALA SER SER ASN ASN TYR PRO
SEQRES 20 A 280 LEU GLU LEU ARG SER HIS GLU GLY TYR ASP HIS SER TYR
SEQRES 21 A 280 TYR PHE ILE ALA SER PHE ILE GLU ASP HIS LEU ARG PHE
SEQRES 22 A 280 HIS SER ASN TYR LEU ASN ALA
SEQRES 1 B 280 GLY MSE SER ILE GLU ASN LEU SER SER ASN LYS SER PHE
SEQRES 2 B 280 GLY GLY TRP HIS LYS GLN TYR SER HIS VAL SER ASN THR
SEQRES 3 B 280 LEU ASN CYS ALA MSE ARG PHE ALA ILE TYR LEU PRO PRO
SEQRES 4 B 280 GLN ALA SER THR GLY ALA LYS VAL PRO VAL LEU TYR TRP
SEQRES 5 B 280 LEU SER GLY LEU THR CYS SER ASP GLU ASN PHE MSE GLN
SEQRES 6 B 280 LYS ALA GLY ALA GLN ARG LEU ALA ALA GLU LEU GLY ILE
SEQRES 7 B 280 ALA ILE VAL ALA PRO ASP THR SER PRO ARG GLY GLU GLY
SEQRES 8 B 280 VAL ALA ASP ASP GLU GLY TYR ASP LEU GLY GLN GLY ALA
SEQRES 9 B 280 GLY PHE TYR VAL ASN ALA THR GLN ALA PRO TRP ASN ARG
SEQRES 10 B 280 HIS TYR GLN MSE TYR ASP TYR VAL VAL ASN GLU LEU PRO
SEQRES 11 B 280 GLU LEU ILE GLU SER MSE PHE PRO VAL SER ASP LYS ARG
SEQRES 12 B 280 ALA ILE ALA GLY HIS SER MSE GLY GLY HIS GLY ALA LEU
SEQRES 13 B 280 THR ILE ALA LEU ARG ASN PRO GLU ARG TYR GLN SER VAL
SEQRES 14 B 280 SER ALA PHE SER PRO ILE ASN ASN PRO VAL ASN CYS PRO
SEQRES 15 B 280 TRP GLY GLN LYS ALA PHE THR ALA TYR LEU GLY LYS ASP
SEQRES 16 B 280 THR ASP THR TRP ARG GLU TYR ASP ALA SER LEU LEU MSE
SEQRES 17 B 280 ARG ALA ALA LYS GLN TYR VAL PRO ALA LEU VAL ASP GLN
SEQRES 18 B 280 GLY GLU ALA ASP ASN PHE LEU ALA GLU GLN LEU LYS PRO
SEQRES 19 B 280 GLU VAL LEU GLU ALA ALA ALA SER SER ASN ASN TYR PRO
SEQRES 20 B 280 LEU GLU LEU ARG SER HIS GLU GLY TYR ASP HIS SER TYR
SEQRES 21 B 280 TYR PHE ILE ALA SER PHE ILE GLU ASP HIS LEU ARG PHE
SEQRES 22 B 280 HIS SER ASN TYR LEU ASN ALA
MODRES 3I6Y MSE A 30 MET SELENOMETHIONINE
MODRES 3I6Y MSE A 63 MET SELENOMETHIONINE
MODRES 3I6Y MSE A 120 MET SELENOMETHIONINE
MODRES 3I6Y MSE A 135 MET SELENOMETHIONINE
MODRES 3I6Y MSE A 149 MET SELENOMETHIONINE
MODRES 3I6Y MSE A 207 MET SELENOMETHIONINE
MODRES 3I6Y MSE B 30 MET SELENOMETHIONINE
MODRES 3I6Y MSE B 63 MET SELENOMETHIONINE
MODRES 3I6Y MSE B 120 MET SELENOMETHIONINE
MODRES 3I6Y MSE B 135 MET SELENOMETHIONINE
MODRES 3I6Y MSE B 149 MET SELENOMETHIONINE
MODRES 3I6Y MSE B 207 MET SELENOMETHIONINE
HET MSE A 30 8
HET MSE A 63 8
HET MSE A 120 8
HET MSE A 135 16
HET MSE A 149 8
HET MSE A 207 8
HET MSE B 30 8
HET MSE B 63 8
HET MSE B 120 8
HET MSE B 135 16
HET MSE B 149 8
HET MSE B 207 8
HET CL A 280 1
HET EDO A 281 4
HET EDO A 282 4
HET EDO A 283 4
HET EDO A 284 4
HET CL B 280 1
HET EDO B 281 4
HET EDO B 282 4
HET PEG B 283 7
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 3 CL 2(CL 1-)
FORMUL 4 EDO 6(C2 H6 O2)
FORMUL 11 PEG C4 H10 O3
FORMUL 12 HOH *508(H2 O)
HELIX 1 1 PRO A 37 THR A 42 5 6
HELIX 2 2 GLU A 60 ALA A 66 1 7
HELIX 3 3 ALA A 68 GLY A 76 1 9
HELIX 4 4 PRO A 113 HIS A 117 5 5
HELIX 5 5 GLN A 119 ASN A 126 1 8
HELIX 6 6 ASN A 126 PHE A 136 1 11
HELIX 7 7 SER A 148 ASN A 161 1 14
HELIX 8 8 ASN A 176 ASN A 179 5 4
HELIX 9 9 CYS A 180 GLY A 192 1 13
HELIX 10 10 ASP A 194 TYR A 201 5 8
HELIX 11 11 ASP A 202 ALA A 210 1 9
HELIX 12 12 PHE A 226 LEU A 231 1 6
HELIX 13 13 LYS A 232 ASN A 243 1 12
HELIX 14 14 SER A 258 ASN A 278 1 21
HELIX 15 15 PRO B 37 THR B 42 5 6
HELIX 16 16 GLU B 60 ALA B 66 1 7
HELIX 17 17 ALA B 68 GLY B 76 1 9
HELIX 18 18 PRO B 113 HIS B 117 5 5
HELIX 19 19 GLN B 119 ASN B 126 1 8
HELIX 20 20 ASN B 126 PHE B 136 1 11
HELIX 21 21 SER B 148 ASN B 161 1 14
HELIX 22 22 ASN B 176 ASN B 179 5 4
HELIX 23 23 CYS B 180 GLY B 192 1 13
HELIX 24 24 ASP B 194 TYR B 201 5 8
HELIX 25 25 ASP B 202 ALA B 210 1 9
HELIX 26 26 PHE B 226 LEU B 231 1 6
HELIX 27 27 LYS B 232 ASN B 243 1 12
HELIX 28 28 SER B 258 ASN B 278 1 21
SHEET 1 A 9 ILE A 3 SER A 11 0
SHEET 2 A 9 GLY A 14 SER A 23 -1 O GLN A 18 N LEU A 6
SHEET 3 A 9 CYS A 28 LEU A 36 -1 O CYS A 28 N SER A 23
SHEET 4 A 9 ALA A 78 PRO A 82 -1 O ILE A 79 N TYR A 35
SHEET 5 A 9 VAL A 46 LEU A 52 1 N LEU A 49 O ALA A 78
SHEET 6 A 9 VAL A 138 HIS A 147 1 O ALA A 143 N TYR A 50
SHEET 7 A 9 VAL A 168 PHE A 171 1 O PHE A 171 N GLY A 146
SHEET 8 A 9 ALA A 216 GLY A 221 1 O ASP A 219 N ALA A 170
SHEET 9 A 9 LEU A 247 HIS A 252 1 O ARG A 250 N VAL A 218
SHEET 1 B 9 ILE B 3 SER B 11 0
SHEET 2 B 9 GLY B 14 SER B 23 -1 O GLN B 18 N LEU B 6
SHEET 3 B 9 CYS B 28 LEU B 36 -1 O PHE B 32 N TYR B 19
SHEET 4 B 9 ALA B 78 PRO B 82 -1 O ALA B 81 N ALA B 33
SHEET 5 B 9 VAL B 46 LEU B 52 1 N LEU B 49 O ALA B 78
SHEET 6 B 9 VAL B 138 HIS B 147 1 O ALA B 143 N TYR B 50
SHEET 7 B 9 VAL B 168 PHE B 171 1 O PHE B 171 N GLY B 146
SHEET 8 B 9 ALA B 216 GLY B 221 1 O ASP B 219 N ALA B 170
SHEET 9 B 9 LEU B 247 HIS B 252 1 O ARG B 250 N VAL B 218
LINK C ALA A 29 N MSE A 30 1555 1555 1.33
LINK C MSE A 30 N ARG A 31 1555 1555 1.33
LINK C PHE A 62 N MSE A 63 1555 1555 1.35
LINK C MSE A 63 N GLN A 64 1555 1555 1.33
LINK C GLN A 119 N MSE A 120 1555 1555 1.33
LINK C MSE A 120 N TYR A 121 1555 1555 1.35
LINK C SER A 134 N AMSE A 135 1555 1555 1.33
LINK C SER A 134 N BMSE A 135 1555 1555 1.33
LINK C AMSE A 135 N PHE A 136 1555 1555 1.32
LINK C BMSE A 135 N PHE A 136 1555 1555 1.33
LINK C SER A 148 N MSE A 149 1555 1555 1.33
LINK C MSE A 149 N GLY A 150 1555 1555 1.33
LINK C LEU A 206 N MSE A 207 1555 1555 1.32
LINK C MSE A 207 N ARG A 208 1555 1555 1.34
LINK C ALA B 29 N MSE B 30 1555 1555 1.33
LINK C MSE B 30 N ARG B 31 1555 1555 1.33
LINK C PHE B 62 N MSE B 63 1555 1555 1.35
LINK C MSE B 63 N GLN B 64 1555 1555 1.33
LINK C GLN B 119 N MSE B 120 1555 1555 1.32
LINK C MSE B 120 N TYR B 121 1555 1555 1.33
LINK C SER B 134 N AMSE B 135 1555 1555 1.34
LINK C SER B 134 N BMSE B 135 1555 1555 1.34
LINK C AMSE B 135 N PHE B 136 1555 1555 1.33
LINK C BMSE B 135 N PHE B 136 1555 1555 1.33
LINK C SER B 148 N MSE B 149 1555 1555 1.33
LINK C MSE B 149 N GLY B 150 1555 1555 1.33
LINK C LEU B 206 N MSE B 207 1555 1555 1.33
LINK C MSE B 207 N ARG B 208 1555 1555 1.33
CISPEP 1 ALA A 112 PRO A 113 0 0.68
CISPEP 2 ALA B 112 PRO B 113 0 -1.63
SITE 1 AC1 4 LEU A 55 SER A 148 MSE A 149 HOH A 299
SITE 1 AC2 6 VAL A 22 SER A 23 ASN A 24 ASN A 27
SITE 2 AC2 6 CYS A 28 HOH A 541
SITE 1 AC3 6 LYS A 65 TYR A 259 TYR A 260 HOH A 336
SITE 2 AC3 6 GLN B 64 HOH B 290
SITE 1 AC4 7 ALA A 223 ASN A 225 ASP A 256 HOH A 313
SITE 2 AC4 7 HOH A 375 HOH A 423 HOH B 358
SITE 1 AC5 4 PRO A 181 LYS A 185 HOH A 432 HOH A 516
SITE 1 AC6 4 LEU B 55 SER B 148 MSE B 149 HOH B 317
SITE 1 AC7 3 LYS B 10 GLY B 13 HOH B 387
SITE 1 AC8 7 SER B 58 ASP B 59 ASP B 83 ARG B 87
SITE 2 AC8 7 HOH B 398 HOH B 450 HOH B 532
SITE 1 AC9 9 MSE A 63 GLN A 64 LYS B 65 TYR B 259
SITE 2 AC9 9 TYR B 260 HOH B 292 HOH B 336 HOH B 407
SITE 3 AC9 9 HOH B 485
CRYST1 44.845 88.179 84.104 90.00 94.75 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 0.022299 0.000000 0.001851 0.00000
SCALE2 0.000000 0.011341 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011931 0.00000
TER 2259 ALA A 279
TER 4547 ALA B 279
MASTER 392 0 21 28 18 0 15 6 5086 2 167 44
END |