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HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 11-JUL-08 3DS8
TITLE THE CRYSATL STRUCTURE OF THE GENE LIN2722 PRODUCTS FROM
TITLE 2 LISTERIA INNOCUA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIN2722 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA INNOCUA;
SOURCE 3 ORGANISM_TAXID: 1642;
SOURCE 4 STRAIN: CLIP11262;
SOURCE 5 GENE: LIN2722;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG19
KEYWDS UNKONWN FUNCTION, LIN2722, STRUCTURAL GENOMICS, PSI, MCSG,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.ZHANG,R.WU,L.FREEMAN,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 2 24-FEB-09 3DS8 1 VERSN
REVDAT 1 16-SEP-08 3DS8 0
JRNL AUTH R.ZHANG,R.WU,L.FREEMAN,A.JOACHIMIAK
JRNL TITL THE CRYSATL STRUCTURE OF THE GENE LIN2722 PRODUCTS
JRNL TITL 2 FROM LISTERIA INNOCUA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 29792
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1591
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2057
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.1870
REMARK 3 BIN FREE R VALUE SET COUNT : 106
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1994
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 321
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.02
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14000
REMARK 3 B22 (A**2) : 0.14000
REMARK 3 B33 (A**2) : -0.29000
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): 0.106
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.058
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.532
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2057 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1372 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2789 ; 1.656 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3382 ; 1.008 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 254 ; 6.056 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 93 ;37.294 ;26.022
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 362 ;12.282 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;19.504 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 303 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2264 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 374 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 441 ; 0.224 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1481 ; 0.200 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1005 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 997 ; 0.089 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 285 ; 0.205 ; 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): 29 ; 0.326 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 36 ; 0.298 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.299 ; 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): 1534 ; 1.721 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 512 ; 0.317 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2046 ; 1.693 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 904 ; 3.558 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 743 ; 4.769 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 50
REMARK 3 RESIDUE RANGE : A 51 A 100
REMARK 3 RESIDUE RANGE : A 101 A 150
REMARK 3 RESIDUE RANGE : A 151 A 200
REMARK 3 RESIDUE RANGE : A 201 A 254
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4573 2.6299 55.6975
REMARK 3 T TENSOR
REMARK 3 T11: -0.0296 T22: -0.0524
REMARK 3 T33: -0.0380 T12: -0.0053
REMARK 3 T13: -0.0111 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 0.7002 L22: 0.9344
REMARK 3 L33: 0.9524 L12: -0.1230
REMARK 3 L13: 0.2140 L23: 0.0704
REMARK 3 S TENSOR
REMARK 3 S11: -0.0297 S12: 0.0183 S13: 0.0053
REMARK 3 S21: 0.0184 S22: 0.0090 S23: -0.0261
REMARK 3 S31: -0.0394 S32: 0.0694 S33: 0.0207
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 3DS8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-08.
REMARK 100 THE RCSB ID CODE IS RCSB048422.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
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) : 0.9796
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL3000
REMARK 200 DATA SCALING SOFTWARE : HKL3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29792
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 49.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 17.000
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 31.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 10.70
REMARK 200 R MERGE FOR SHELL (I) : 0.58000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HIKL3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% GLYCEROL, 20.5% PEK4000, 0.065M
REMARK 280 TRIS_NA CITRATE, 0.1M NH4 ACETATE, PH 5.6, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.53750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.60550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.60550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 122.30625
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.60550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.60550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.76875
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.60550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.60550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 122.30625
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.60550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.60550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.76875
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 81.53750
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 300 REMARK: AUTHORS STATE THAT THE PROTEIN DOES NOT COMPLEXATE IN
REMARK 300 SOLUTION
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 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 LYS A 1
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 OE1 GLU A 183 OE1 GLU A 183 8555 1.99
REMARK 500 OD1 ASP A 86 OH TYR A 253 4555 2.06
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 213 CB - CG - OD2 ANGL. DEV. = 6.7 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 102 -116.24 53.89
REMARK 500 ARG A 125 -71.20 -104.44
REMARK 500 ASP A 136 -154.13 57.66
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 SO4 A 255
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 256
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 257
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 258
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 259
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC60765.2 RELATED DB: TARGETDB
DBREF 3DS8 A 1 254 UNP Q927R6 Q927R6_LISIN 38 291
SEQRES 1 A 254 LYS ASP GLN ILE PRO ILE ILE LEU ILE HIS GLY SER GLY
SEQRES 2 A 254 GLY ASN ALA SER SER LEU ASP LYS MSE ALA ASP GLN LEU
SEQRES 3 A 254 MSE ASN GLU TYR ARG SER SER ASN GLU ALA LEU THR MSE
SEQRES 4 A 254 THR VAL ASN SER GLU GLY LYS ILE LYS PHE GLU GLY LYS
SEQRES 5 A 254 LEU THR LYS ASP ALA LYS ARG PRO ILE ILE LYS PHE GLY
SEQRES 6 A 254 PHE GLU GLN ASN GLN ALA THR PRO ASP ASP TRP SER LYS
SEQRES 7 A 254 TRP LEU LYS ILE ALA MSE GLU ASP LEU LYS SER ARG TYR
SEQRES 8 A 254 GLY PHE THR GLN MSE ASP GLY VAL GLY HIS SER ASN GLY
SEQRES 9 A 254 GLY LEU ALA LEU THR TYR TYR ALA GLU ASP TYR ALA GLY
SEQRES 10 A 254 ASP LYS THR VAL PRO THR LEU ARG LYS LEU VAL ALA ILE
SEQRES 11 A 254 GLY SER PRO PHE ASN ASP LEU ASP PRO ASN ASP ASN GLY
SEQRES 12 A 254 MSE ASP LEU SER PHE LYS LYS LEU PRO ASN SER THR PRO
SEQRES 13 A 254 GLN MSE ASP TYR PHE ILE LYS ASN GLN THR GLU VAL SER
SEQRES 14 A 254 PRO ASP LEU GLU VAL LEU ALA ILE ALA GLY GLU LEU SER
SEQRES 15 A 254 GLU ASP ASN PRO THR ASP GLY ILE VAL PRO THR ILE SER
SEQRES 16 A 254 SER LEU ALA THR ARG LEU PHE MSE PRO GLY SER ALA LYS
SEQRES 17 A 254 ALA TYR ILE GLU ASP ILE GLN VAL GLY GLU ASP ALA VAL
SEQRES 18 A 254 HIS GLN THR LEU HIS GLU THR PRO LYS SER ILE GLU LYS
SEQRES 19 A 254 THR TYR TRP PHE LEU GLU LYS PHE LYS THR ASP GLU THR
SEQRES 20 A 254 VAL ILE GLN LEU ASP TYR LYS
MODRES 3DS8 MSE A 22 MET SELENOMETHIONINE
MODRES 3DS8 MSE A 27 MET SELENOMETHIONINE
MODRES 3DS8 MSE A 39 MET SELENOMETHIONINE
MODRES 3DS8 MSE A 84 MET SELENOMETHIONINE
MODRES 3DS8 MSE A 96 MET SELENOMETHIONINE
MODRES 3DS8 MSE A 144 MET SELENOMETHIONINE
MODRES 3DS8 MSE A 158 MET SELENOMETHIONINE
MODRES 3DS8 MSE A 203 MET SELENOMETHIONINE
HET MSE A 22 8
HET MSE A 27 8
HET MSE A 39 8
HET MSE A 84 8
HET MSE A 96 8
HET MSE A 144 8
HET MSE A 158 8
HET MSE A 203 8
HET SO4 A 255 5
HET SO4 A 256 5
HET SO4 A 257 5
HET SO4 A 258 5
HET SO4 A 259 5
HETNAM MSE SELENOMETHIONINE
HETNAM SO4 SULFATE ION
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 SO4 5(O4 S 2-)
FORMUL 7 HOH *321(H2 O)
HELIX 1 1 LEU A 19 GLU A 29 1 11
HELIX 2 2 THR A 72 GLY A 92 1 21
HELIX 3 3 SER A 102 TYR A 115 1 14
HELIX 4 4 ASP A 138 GLY A 143 1 6
HELIX 5 5 THR A 155 ASN A 164 1 10
HELIX 6 6 GLN A 165 VAL A 168 5 4
HELIX 7 7 PRO A 192 LEU A 197 1 6
HELIX 8 8 ALA A 198 PHE A 202 5 5
HELIX 9 9 GLU A 218 GLU A 227 5 10
HELIX 10 10 THR A 228 LYS A 241 1 14
SHEET 1 A 9 LYS A 46 GLU A 50 0
SHEET 2 A 9 ALA A 36 ASN A 42 -1 N THR A 38 O GLU A 50
SHEET 3 A 9 ILE A 61 PHE A 66 1 O LYS A 63 N LEU A 37
SHEET 4 A 9 ILE A 6 ILE A 9 1 N LEU A 8 O ILE A 62
SHEET 5 A 9 GLN A 95 HIS A 101 1 O ASP A 97 N ILE A 7
SHEET 6 A 9 THR A 123 ILE A 130 1 O VAL A 128 N GLY A 100
SHEET 7 A 9 GLU A 173 GLU A 180 1 O GLU A 173 N LEU A 127
SHEET 8 A 9 ALA A 209 VAL A 216 1 O GLN A 215 N ALA A 178
SHEET 9 A 9 VAL A 248 GLN A 250 1 O GLN A 250 N TYR A 210
LINK C LYS A 21 N MSE A 22 1555 1555 1.32
LINK C MSE A 22 N ALA A 23 1555 1555 1.33
LINK C LEU A 26 N MSE A 27 1555 1555 1.35
LINK C MSE A 27 N ASN A 28 1555 1555 1.33
LINK C THR A 38 N MSE A 39 1555 1555 1.33
LINK C MSE A 39 N THR A 40 1555 1555 1.33
LINK C ALA A 83 N MSE A 84 1555 1555 1.32
LINK C MSE A 84 N GLU A 85 1555 1555 1.34
LINK C GLN A 95 N MSE A 96 1555 1555 1.34
LINK C MSE A 96 N ASP A 97 1555 1555 1.31
LINK C GLY A 143 N MSE A 144 1555 1555 1.34
LINK C MSE A 144 N ASP A 145 1555 1555 1.33
LINK C GLN A 157 N MSE A 158 1555 1555 1.34
LINK C MSE A 158 N ASP A 159 1555 1555 1.34
LINK C PHE A 202 N MSE A 203 1555 1555 1.34
LINK C MSE A 203 N PRO A 204 1555 1555 1.34
CISPEP 1 TYR A 253 LYS A 254 0 -3.00
SITE 1 AC1 9 GLY A 11 SER A 12 ASN A 28 ARG A 31
SITE 2 AC1 9 SER A 102 ASN A 103 HIS A 222 HOH A 318
SITE 3 AC1 9 HOH A 426
SITE 1 AC2 10 GLY A 11 SER A 12 GLY A 14 SER A 18
SITE 2 AC2 10 HIS A 101 GLN A 223 HIS A 226 HOH A 307
SITE 3 AC2 10 HOH A 371 HOH A 537
SITE 1 AC3 3 ASN A 34 LYS A 58 HOH A 365
SITE 1 AC4 7 ARG A 31 ILE A 190 GLN A 223 HOH A 328
SITE 2 AC4 7 HOH A 359 HOH A 365 HOH A 405
SITE 1 AC5 8 ARG A 125 LYS A 126 GLU A 173 PHE A 242
SITE 2 AC5 8 LYS A 243 THR A 244 HOH A 275 HOH A 546
CRYST1 63.211 63.211 163.075 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015820 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015820 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006132 0.00000
TER 1995 LYS A 254
MASTER 359 0 13 10 9 0 11 6 2340 1 105 20
END |