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HEADER HYDROLASE 09-SEP-14 4WDQ
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE LINB32 MUTANT (L177W)
TITLE 2 FROM SPHINGOBIUM JAPONICUM UT26
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,3,4,6-TETRACHLORO-1,4-CYCLOHEXADIENE HYDROLASE,4-TCDN
COMPND 5 CHLOROHYDROLASE;
COMPND 6 EC: 3.8.1.5;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOBIUM JAPONICUM UT26S;
SOURCE 3 ORGANISM_TAXID: 452662;
SOURCE 4 GENE: LINB;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE, PROTEIN ENGINEERING
EXPDTA X-RAY DIFFRACTION
AUTHOR O.DEGTJARIK,P.REZACOVA,R.CHALOUPKOVA,J.DAMBORSKY,I.KUTA-SMATANOVA
REVDAT 1 23-DEC-15 4WDQ 0
JRNL AUTH O.DEGTJARIK,P.REZACOVA,R.CHALOUPKOVA,J.DAMBORSKY,
JRNL AUTH 2 I.KUTA-SMATANOVA
JRNL TITL CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE LINB MUTANT
JRNL TITL 2 (L177W) FROM SPHINGOBIUM JAPONICUM UT26
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0037
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) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 36137
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1802
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) : 1.58
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2404
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.1890
REMARK 3 BIN FREE R VALUE SET COUNT : 125
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2353
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 714
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
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): 0.097
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.064
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.780
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2483 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3389 ; 1.399 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 314 ; 5.993 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 129 ;35.300 ;23.023
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 394 ;11.899 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;18.692 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 349 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1987 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1196 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1658 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 586 ; 0.152 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.016 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 41 ; 0.184 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 142 ; 0.178 ; 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): 1550 ; 0.716 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2424 ; 1.005 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1076 ; 1.762 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 956 ; 2.686 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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
REMARK 4
REMARK 4 4WDQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000203066.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-11
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 : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X13
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8123
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000, HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36500
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.28500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP 6.0
REMARK 200 STARTING MODEL: 1CV2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES; 0.2M MGCL2; 25% PEG3350, PH
REMARK 280 5.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 23.36450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.52750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.24500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.52750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.36450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.24500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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 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 504 O HOH A 930 2.10
REMARK 500 O HOH A 547 O HOH A 646 2.16
REMARK 500 O HOH A 481 O HOH A 662 2.18
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 PRO A 39 45.04 -97.98
REMARK 500 ASP A 108 -133.69 55.36
REMARK 500 HIS A 121 50.39 -142.97
REMARK 500 GLN A 172 -54.12 -120.44
REMARK 500 ALA A 247 -64.82 -148.99
REMARK 500 ALA A 271 -96.80 -100.60
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 A1040 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH A1044 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH A1058 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A1071 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH A1082 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH A1088 DISTANCE = 7.37 ANGSTROMS
REMARK 525 HOH A1089 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A1094 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH A1098 DISTANCE = 7.26 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 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 626 O
REMARK 620 2 HOH A 431 O 91.9
REMARK 620 3 HOH A 451 O 179.5 88.5
REMARK 620 4 HOH A 469 O 86.6 85.4 93.7
REMARK 620 5 HOH A 720 O 89.5 93.4 90.1 175.9
REMARK 620 6 HOH A 495 O 90.2 174.9 89.4 90.1 91.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 302 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 694 O
REMARK 620 2 HOH A 465 O 173.1
REMARK 620 3 HOH A1107 O 88.6 95.4
REMARK 620 4 HOH A1108 O 87.8 86.4 91.8
REMARK 620 5 HOH A 618 O 96.5 89.0 92.7 173.9
REMARK 620 6 HOH A 631 O 86.4 89.8 174.5 90.4 85.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 303 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 483 O
REMARK 620 2 HOH A 420 O 173.0
REMARK 620 3 HOH A 450 O 87.4 87.7
REMARK 620 4 HOH A 539 O 94.3 90.5 87.6
REMARK 620 5 HOH A 628 O 89.9 94.7 176.3 95.2
REMARK 620 6 HOH A 429 O 87.0 87.8 88.1 175.4 89.2
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 MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 305
DBREF 4WDQ A 2 296 UNP P51698 LINB_SPHPI 2 296
SEQADV 4WDQ TRP A 177 UNP P51698 LEU 177 ENGINEERED MUTATION
SEQADV 4WDQ HIS A 297 UNP P51698 EXPRESSION TAG
SEQADV 4WDQ HIS A 298 UNP P51698 EXPRESSION TAG
SEQRES 1 A 297 SER LEU GLY ALA LYS PRO PHE GLY GLU LYS LYS PHE ILE
SEQRES 2 A 297 GLU ILE LYS GLY ARG ARG MET ALA TYR ILE ASP GLU GLY
SEQRES 3 A 297 THR GLY ASP PRO ILE LEU PHE GLN HIS GLY ASN PRO THR
SEQRES 4 A 297 SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS CYS ALA
SEQRES 5 A 297 GLY LEU GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY MET
SEQRES 6 A 297 GLY ASP SER ASP LYS LEU ASP PRO SER GLY PRO GLU ARG
SEQRES 7 A 297 TYR ALA TYR ALA GLU HIS ARG ASP TYR LEU ASP ALA LEU
SEQRES 8 A 297 TRP GLU ALA LEU ASP LEU GLY ASP ARG VAL VAL LEU VAL
SEQRES 9 A 297 VAL HIS ASP TRP GLY SER ALA LEU GLY PHE ASP TRP ALA
SEQRES 10 A 297 ARG ARG HIS ARG GLU ARG VAL GLN GLY ILE ALA TYR MET
SEQRES 11 A 297 GLU ALA ILE ALA MET PRO ILE GLU TRP ALA ASP PHE PRO
SEQRES 12 A 297 GLU GLN ASP ARG ASP LEU PHE GLN ALA PHE ARG SER GLN
SEQRES 13 A 297 ALA GLY GLU GLU LEU VAL LEU GLN ASP ASN VAL PHE VAL
SEQRES 14 A 297 GLU GLN VAL LEU PRO GLY TRP ILE LEU ARG PRO LEU SER
SEQRES 15 A 297 GLU ALA GLU MET ALA ALA TYR ARG GLU PRO PHE LEU ALA
SEQRES 16 A 297 ALA GLY GLU ALA ARG ARG PRO THR LEU SER TRP PRO ARG
SEQRES 17 A 297 GLN ILE PRO ILE ALA GLY THR PRO ALA ASP VAL VAL ALA
SEQRES 18 A 297 ILE ALA ARG ASP TYR ALA GLY TRP LEU SER GLU SER PRO
SEQRES 19 A 297 ILE PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA LEU
SEQRES 20 A 297 THR THR GLY ARG MET ARG ASP PHE CYS ARG THR TRP PRO
SEQRES 21 A 297 ASN GLN THR GLU ILE THR VAL ALA GLY ALA HIS PHE ILE
SEQRES 22 A 297 GLN GLU ASP SER PRO ASP GLU ILE GLY ALA ALA ILE ALA
SEQRES 23 A 297 ALA PHE VAL ARG ARG LEU ARG PRO ALA HIS HIS
HET MG A 301 1
HET MG A 302 1
HET MG A 303 1
HET CL A 304 1
HET CL A 305 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 2 MG 3(MG 2+)
FORMUL 5 CL 2(CL 1-)
FORMUL 7 HOH *714(H2 O)
HELIX 1 AA1 SER A 41 ARG A 46 5 6
HELIX 2 AA2 ILE A 48 ALA A 53 5 6
HELIX 3 AA3 ALA A 81 LEU A 96 1 16
HELIX 4 AA4 ASP A 108 HIS A 121 1 14
HELIX 5 AA5 GLU A 139 PHE A 143 5 5
HELIX 6 AA6 PRO A 144 GLN A 146 5 3
HELIX 7 AA7 ASP A 147 SER A 156 1 10
HELIX 8 AA8 ALA A 158 GLN A 165 1 8
HELIX 9 AA9 ASN A 167 GLN A 172 1 6
HELIX 10 AB1 GLN A 172 TRP A 177 1 6
HELIX 11 AB2 SER A 183 GLU A 192 1 10
HELIX 12 AB3 PRO A 193 LEU A 195 5 3
HELIX 13 AB4 GLY A 198 ALA A 200 5 3
HELIX 14 AB5 ARG A 201 TRP A 207 1 7
HELIX 15 AB6 PRO A 208 ILE A 211 5 4
HELIX 16 AB7 PRO A 217 SER A 232 1 16
HELIX 17 AB8 THR A 250 ARG A 258 1 9
HELIX 18 AB9 PHE A 273 ASP A 277 5 5
HELIX 19 AC1 SER A 278 ARG A 294 1 17
SHEET 1 AA1 8 LYS A 12 ILE A 16 0
SHEET 2 AA1 8 ARG A 19 GLU A 26 -1 O ARG A 19 N ILE A 16
SHEET 3 AA1 8 ARG A 57 CYS A 61 -1 O LEU A 58 N GLU A 26
SHEET 4 AA1 8 PRO A 31 GLN A 35 1 N PHE A 34 O ILE A 59
SHEET 5 AA1 8 VAL A 102 HIS A 107 1 O VAL A 103 N LEU A 33
SHEET 6 AA1 8 VAL A 125 MET A 131 1 O ALA A 129 N LEU A 104
SHEET 7 AA1 8 LYS A 238 PRO A 245 1 O ILE A 241 N TYR A 130
SHEET 8 AA1 8 GLN A 263 GLY A 270 1 O THR A 264 N PHE A 240
LINK MG MG A 301 O HOH A 626 1555 1555 2.13
LINK MG MG A 301 O HOH A 431 1555 1555 2.13
LINK MG MG A 301 O HOH A 451 1555 1555 2.08
LINK MG MG A 301 O HOH A 469 1555 1555 2.06
LINK MG MG A 301 O HOH A 720 1555 1555 2.13
LINK MG MG A 302 O HOH A 694 1555 1555 2.05
LINK MG MG A 302 O HOH A 465 1555 1555 2.07
LINK MG MG A 302 O HOH A1107 1555 1555 2.12
LINK MG MG A 302 O HOH A1108 1555 1555 2.17
LINK MG MG A 303 O HOH A 483 1555 1555 2.04
LINK MG MG A 303 O HOH A 420 1555 1555 2.17
LINK MG MG A 303 O HOH A 450 1555 1555 2.05
LINK MG MG A 303 O HOH A 539 1555 1555 1.97
LINK MG MG A 303 O HOH A 628 1555 1555 2.12
LINK MG MG A 301 O HOH A 495 1555 4445 2.11
LINK MG MG A 302 O HOH A 618 1555 3444 2.14
LINK MG MG A 302 O HOH A 631 1555 3444 2.13
LINK MG MG A 303 O HOH A 429 1555 1655 2.06
CISPEP 1 ASN A 38 PRO A 39 0 -13.27
CISPEP 2 ASP A 73 PRO A 74 0 13.86
CISPEP 3 THR A 216 PRO A 217 0 -3.24
CISPEP 4 GLU A 244 PRO A 245 0 3.22
CISPEP 5 GLU A 244 PRO A 245 0 3.26
SITE 1 AC1 6 HOH A 431 HOH A 451 HOH A 469 HOH A 495
SITE 2 AC1 6 HOH A 626 HOH A 720
SITE 1 AC2 6 HOH A 465 HOH A 618 HOH A 631 HOH A 694
SITE 2 AC2 6 HOH A1107 HOH A1108
SITE 1 AC3 6 HOH A 420 HOH A 429 HOH A 450 HOH A 483
SITE 2 AC3 6 HOH A 539 HOH A 628
SITE 1 AC4 5 ASN A 38 TRP A 109 PHE A 169 TRP A 207
SITE 2 AC4 5 PRO A 208
SITE 1 AC5 4 THR A 216 ALA A 218 HOH A 508 HOH A 705
CRYST1 46.729 68.490 81.055 90.00 90.00 90.00 P 21 21 21 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 0.021400 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014601 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012337 0.00000
TER 2408 HIS A 298
MASTER 351 0 5 19 8 0 9 6 3072 1 19 23
END |