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HEADER HYDROLASE 29-MAY-12 4FDM
TITLE CRYSTALLIZATION AND 3D STRUCTURE ELUCIDATION OF THERMOSTABLE L2 LIPASE
TITLE 2 FROM THERMOPHILIC LOCALLY ISOLATED BACILLUS SP. L2.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THERMOSTABLE LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 29-416;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SP. L2;
SOURCE 3 ORGANISM_TAXID: 307644;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PQE-30UA
KEYWDS THERMOSTABLE LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.N.Z.R.A.RAHMAN,F.M.SHARIFF,A.B.SALLEH,M.B.BASRI
REVDAT 1 08-MAY-13 4FDM 0
JRNL AUTH R.N.ABD RAHMAN,F.M.SHARIFF,M.BASRI,A.B.SALLEH
JRNL TITL 3D STRUCTURE ELUCIDATION OF THERMOSTABLE L2 LIPASE FROM
JRNL TITL 2 THERMOPHILIC BACILLUS SP. L2.
JRNL REF INT.J.MOL.SCI. V. 13 9207 2012
JRNL REFN ISSN 1422-0067
JRNL PMID 22942761
JRNL DOI 10.3390/IJMS13079207
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 62046
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3322
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4497
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2400
REMARK 3 BIN FREE R VALUE SET COUNT : 235
REMARK 3 BIN FREE R VALUE : 0.2640
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2982
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 274
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.02000
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): 0.071
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.071
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.044
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.260
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.014 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.451 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; 5.512 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ;32.353 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ;12.913 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ;20.992 ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : 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 4FDM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-12.
REMARK 100 THE RCSB ID CODE IS RCSB072768.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8
REMARK 200 MONOCHROMATOR : ROTATED-INCLINED DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77987
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.3
REMARK 200 DATA REDUNDANCY IN SHELL : 13.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2DSN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 6000, 50MM MES, 50MM NACL,
REMARK 280 COUNTER-DIFFUSION, TEMPERATURE 293.15K, PH 6.5, LIQUID DIFFUSION
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 35.98850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 41.68700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.89200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 41.68700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.98850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.89200
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 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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 ALA A 1
REMARK 465 SER A 2
REMARK 465 LEU A 3
REMARK 465 ARG A 4
REMARK 465 ALA A 5
REMARK 465 ASN A 6
REMARK 465 ASP A 7
REMARK 465 LEU A 386
REMARK 465 LEU A 387
REMARK 465 PRO A 388
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 CB THR A 17 O HOH A 714 1.85
REMARK 500 CG2 THR A 278 O HOH A 695 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 LEU A 277 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 LEU A 307 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 ASP A 357 CB - CG - OD1 ANGL. DEV. = 6.9 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 113 -136.91 58.55
REMARK 500 ASP A 175 46.35 -106.73
REMARK 500 VAL A 203 -61.01 67.57
REMARK 500 ARG A 271 43.51 -147.54
REMARK 500 ASP A 310 -162.56 -116.63
REMARK 500 ILE A 319 -40.18 -135.78
REMARK 500 ASN A 367 89.75 -164.15
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
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: (10X,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 PHE A 154 24.5 L L OUTSIDE RANGE
REMARK 500 THR A 278 17.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
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 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 238 OD2
REMARK 620 2 ASP A 61 OD1 127.8
REMARK 620 3 HIS A 81 NE2 108.1 97.9
REMARK 620 4 HIS A 87 NE2 98.4 117.9 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 286 O
REMARK 620 2 GLU A 360 OE2 81.3
REMARK 620 3 PRO A 366 O 171.6 92.6
REMARK 620 4 HOH A 617 O 88.0 163.9 96.7
REMARK 620 5 ASP A 365 OD2 101.1 106.7 86.1 87.1
REMARK 620 6 HOH A 628 O 87.1 86.0 86.8 81.4 165.7
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 ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 402
DBREF 4FDM A 1 388 UNP Q5I4I3 Q5I4I3_9BACI 29 416
SEQADV 4FDM HIS A -5 UNP Q5I4I3 EXPRESSION TAG
SEQADV 4FDM HIS A -4 UNP Q5I4I3 EXPRESSION TAG
SEQADV 4FDM HIS A -3 UNP Q5I4I3 EXPRESSION TAG
SEQADV 4FDM HIS A -2 UNP Q5I4I3 EXPRESSION TAG
SEQADV 4FDM HIS A -1 UNP Q5I4I3 EXPRESSION TAG
SEQADV 4FDM HIS A 0 UNP Q5I4I3 EXPRESSION TAG
SEQRES 1 A 394 HIS HIS HIS HIS HIS HIS ALA SER LEU ARG ALA ASN ASP
SEQRES 2 A 394 ALA PRO ILE VAL LEU LEU HIS GLY PHE THR GLY TRP GLY
SEQRES 3 A 394 ARG GLU GLU MET PHE GLY PHE LYS TYR TRP GLY GLY VAL
SEQRES 4 A 394 ARG GLY ASP ILE GLU GLN TRP LEU ASN ASP ASN GLY TYR
SEQRES 5 A 394 ARG THR TYR THR LEU ALA VAL GLY PRO LEU SER SER ASN
SEQRES 6 A 394 TRP ASP ARG ALA CYS GLU ALA TYR ALA GLN LEU VAL GLY
SEQRES 7 A 394 GLY THR VAL ASP TYR GLY ALA ALA HIS ALA ALA LYS HIS
SEQRES 8 A 394 GLY HIS ALA ARG PHE GLY ARG THR TYR PRO GLY LEU LEU
SEQRES 9 A 394 PRO GLU LEU LYS ARG GLY GLY ARG ILE HIS ILE ILE ALA
SEQRES 10 A 394 HIS SER GLN GLY GLY GLN THR ALA ARG MET LEU VAL SER
SEQRES 11 A 394 LEU LEU GLU ASN GLY SER GLN GLU GLU ARG GLU TYR ALA
SEQRES 12 A 394 LYS ALA HIS ASN VAL SER LEU SER PRO LEU PHE GLU GLY
SEQRES 13 A 394 GLY HIS HIS PHE VAL LEU SER VAL THR THR ILE ALA THR
SEQRES 14 A 394 PRO HIS ASP GLY THR THR LEU VAL ASN MET VAL ASP PHE
SEQRES 15 A 394 THR ASP ARG PHE PHE ASP LEU GLN LYS ALA VAL LEU GLU
SEQRES 16 A 394 ALA ALA ALA VAL ALA SER ASN VAL PRO TYR THR SER GLN
SEQRES 17 A 394 VAL TYR ASP PHE LYS LEU ASP GLN TRP GLY LEU ARG ARG
SEQRES 18 A 394 GLN PRO GLY GLU SER PHE ASP HIS TYR PHE GLU ARG LEU
SEQRES 19 A 394 LYS ARG SER PRO VAL TRP THR SER THR ASP THR ALA ARG
SEQRES 20 A 394 TYR ASP LEU SER VAL SER GLY ALA GLU LYS LEU ASN GLN
SEQRES 21 A 394 TRP VAL GLN ALA SER PRO ASN THR TYR TYR LEU SER PHE
SEQRES 22 A 394 SER THR GLU ARG THR TYR ARG GLY ALA LEU THR GLY ASN
SEQRES 23 A 394 HIS TYR PRO GLU LEU GLY MET ASN ALA PHE SER ALA VAL
SEQRES 24 A 394 VAL CYS ALA PRO PHE LEU GLY SER TYR ARG ASN PRO THR
SEQRES 25 A 394 LEU GLY ILE ASP ASP ARG TRP LEU GLU ASN ASP GLY ILE
SEQRES 26 A 394 VAL ASN THR VAL SER MET ASN GLY PRO LYS ARG GLY SER
SEQRES 27 A 394 SER ASP ARG ILE VAL PRO TYR ASP GLY THR LEU LYS LYS
SEQRES 28 A 394 GLY VAL TRP ASN ASP MET GLY THR TYR ASN VAL ASP HIS
SEQRES 29 A 394 LEU GLU ILE ILE GLY VAL ASP PRO ASN PRO SER PHE ASP
SEQRES 30 A 394 ILE ARG ALA PHE TYR LEU ARG LEU ALA GLU GLN LEU ALA
SEQRES 31 A 394 SER LEU LEU PRO
HET ZN A 401 1
HET CA A 402 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 2 ZN ZN 2+
FORMUL 3 CA CA 2+
FORMUL 4 HOH *274(H2 O)
HELIX 1 1 GLU A 23 PHE A 27 5 5
HELIX 2 2 GLY A 31 GLY A 35 5 5
HELIX 3 3 ASP A 36 ASN A 44 1 9
HELIX 4 4 SER A 58 GLY A 72 1 15
HELIX 5 5 GLY A 78 GLY A 86 1 9
HELIX 6 6 LEU A 98 ARG A 103 5 6
HELIX 7 7 GLN A 114 GLY A 129 1 16
HELIX 8 8 SER A 130 ASN A 141 1 12
HELIX 9 9 SER A 145 GLU A 149 5 5
HELIX 10 10 THR A 168 MET A 173 5 6
HELIX 11 11 ASP A 175 ALA A 191 1 17
HELIX 12 12 LEU A 208 GLY A 212 5 5
HELIX 13 13 SER A 220 ARG A 230 1 11
HELIX 14 14 SER A 231 SER A 236 1 6
HELIX 15 15 THR A 239 SER A 245 1 7
HELIX 16 16 SER A 245 VAL A 256 1 12
HELIX 17 17 ASN A 288 CYS A 295 1 8
HELIX 18 18 CYS A 295 GLY A 300 1 6
HELIX 19 19 ASN A 304 GLY A 308 5 5
HELIX 20 20 ASP A 310 LEU A 314 5 5
HELIX 21 21 ASN A 321 ASN A 326 5 6
HELIX 22 22 ASP A 371 SER A 385 1 15
SHEET 1 A 7 THR A 48 LEU A 51 0
SHEET 2 A 7 ILE A 10 LEU A 13 1 N LEU A 12 O LEU A 51
SHEET 3 A 7 ILE A 107 HIS A 112 1 O HIS A 108 N VAL A 11
SHEET 4 A 7 VAL A 155 ILE A 161 1 O THR A 159 N ILE A 109
SHEET 5 A 7 TYR A 263 THR A 269 1 O LEU A 265 N THR A 160
SHEET 6 A 7 TRP A 348 TYR A 354 1 O ASN A 349 N TYR A 264
SHEET 7 A 7 ILE A 336 PRO A 338 1 N VAL A 337 O TRP A 348
SHEET 1 B 2 GLY A 73 ASP A 76 0
SHEET 2 B 2 PHE A 90 TYR A 94 -1 O ARG A 92 N VAL A 75
SHEET 1 C 2 THR A 272 ARG A 274 0
SHEET 2 C 2 HIS A 281 PRO A 283 -1 O TYR A 282 N TYR A 273
LINK OD2 ASP A 238 ZN ZN A 401 1555 1555 1.92
LINK OD1 ASP A 61 ZN ZN A 401 1555 1555 1.98
LINK NE2 HIS A 81 ZN ZN A 401 1555 1555 2.02
LINK NE2 HIS A 87 ZN ZN A 401 1555 1555 2.05
LINK O GLY A 286 CA CA A 402 1555 1555 2.26
LINK OE2 GLU A 360 CA CA A 402 1555 1555 2.34
LINK O PRO A 366 CA CA A 402 1555 1555 2.35
LINK CA CA A 402 O HOH A 617 1555 1555 2.40
LINK OD2 ASP A 365 CA CA A 402 1555 1555 2.42
LINK CA CA A 402 O HOH A 628 1555 1555 2.59
SITE 1 AC1 4 ASP A 61 HIS A 81 HIS A 87 ASP A 238
SITE 1 AC2 6 GLY A 286 GLU A 360 ASP A 365 PRO A 366
SITE 2 AC2 6 HOH A 617 HOH A 628
CRYST1 71.977 81.784 83.374 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 0.013893 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012227 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011994 0.00000
TER 2983 SER A 385
MASTER 362 0 2 22 11 0 3 6 3258 1 13 31
END |