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HEADER HYDROLASE 11-SEP-07 2Z8X
TITLE CRYSTAL STRUCTURE OF EXTRACELLULAR LIPASE FROM PSEUDOMONAS
TITLE 2 SP. MIS38
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EXTRACELLULAR LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SP. MIS38;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: MIS38 ISOLATE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: DH5;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PUC18
KEYWDS FAMILY I.3 LIPASE, BETA ROLL, CALCIUM BINDING PROTEIN, RTX
KEYWDS 2 PROTEIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ANGKAWIDJAJA,D.J.YOU,H.MATSUMURA,Y.KOGA,K.TAKANO,S.KANAYA
REVDAT 1 30-OCT-07 2Z8X 0
JRNL AUTH C.ANGKAWIDJAJA,D.J.YOU,H.MATSUMURA,K.KUWAHARA,
JRNL AUTH 2 Y.KOGA,K.TAKANO,S.KANAYA
JRNL TITL CRYSTAL STRUCTURE OF A FAMILY I.3 LIPASE FROM
JRNL TITL 2 PSEUDOMONAS SP. MIS38 IN A CLOSED CONFORMATION
JRNL REF FEBS LETT. V. 581 5060 2007
JRNL REFN ASTM FEBLAL NE ISSN 0014-5793
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 107798
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5707
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.48
REMARK 3 BIN RESOLUTION RANGE LOW : 1.52
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6077
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 313
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 5334
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.067
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.039
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.986
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4648 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6317 ; 1.175 ; 1.938
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 615 ; 5.933 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 210 ;37.850 ;25.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 679 ;10.838 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;16.329 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 696 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3629 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2185 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3185 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 612 ; 0.110 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 47 ; 0.083 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 41 ; 0.164 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.084 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 2 ; 0.086 ; 0.200
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): 3070 ; 0.617 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4766 ; 1.037 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1791 ; 1.654 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1551 ; 2.565 ; 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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 0
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 2Z8X COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB027669.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU JUPITER 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 118663
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : 7.100
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: SIRAS
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 20000, 0.1M MES, 0.2M
REMARK 280 CALCIUM ACETATE, 5MM ZINC ACETATE, PH6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
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,1/2+Y,-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 42.15000
REMARK 290 SMTRY3 2 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 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: MONOMER
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMER
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 MET A 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
REMARK 500 OD1 ASP A 507 O HOH A 1351 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 ZN ZN A 628 ZN ZN A 629 2646 0.20
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 NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 488 CB - CG - OD2 ANGL. DEV. = 7.4 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 LYS A 7 -134.49 47.50
REMARK 500 ASP A 62 107.96 -162.14
REMARK 500 SER A 63 147.63 174.38
REMARK 500 GLN A 64 108.26 10.13
REMARK 500 SER A 207 -123.11 66.40
REMARK 500 ASN A 352 15.39 -140.98
REMARK 500 ARG A 392 -156.13 59.44
REMARK 500 TRP A 462 13.23 57.97
REMARK 500 ASP A 467 -136.05 67.77
REMARK 500 LEU A 512 -156.55 58.37
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 SER A 63 GLN A 64 -129.44
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 628 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 128 OD2
REMARK 620 2 HIS A 132 ND1 116.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 618 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 253 OE2
REMARK 620 2 ASP A 275 OD1 104.6
REMARK 620 3 ASP A 275 OD2 95.3 52.8
REMARK 620 4 ASP A 283 O 89.3 83.4 135.7
REMARK 620 5 ASN A 284 OD1 91.8 155.2 145.3 78.2
REMARK 620 6 HOH A 652 O 178.0 77.0 84.7 92.1 87.1
REMARK 620 7 HOH A 656 O 89.5 128.0 76.6 147.6 69.5 88.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 619 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 278 O
REMARK 620 2 ALA A 281 O 85.0
REMARK 620 3 ASP A 283 OD2 83.1 90.7
REMARK 620 4 ASP A 337 OD1 157.5 77.0 83.7
REMARK 620 5 ASP A 337 OD2 149.9 122.1 107.3 52.2
REMARK 620 6 HOH A 735 O 77.3 162.3 87.3 120.2 75.2
REMARK 620 7 HOH A 702 O 88.0 91.2 170.7 105.6 79.3 88.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 620 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 374 O
REMARK 620 2 SER A 376 O 94.1
REMARK 620 3 ASP A 378 OD2 80.3 84.5
REMARK 620 4 GLY A 391 O 80.8 174.3 92.3
REMARK 620 5 ALA A 393 O 88.9 86.8 165.6 95.4
REMARK 620 6 ASP A 396 OD1 163.2 84.3 82.9 99.9 107.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 621 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 383 O
REMARK 620 2 GLY A 385 O 93.0
REMARK 620 3 ASP A 387 OD2 84.0 77.7
REMARK 620 4 ASP A 400 OD1 88.8 161.3 84.0
REMARK 620 5 ASP A 400 OD2 88.7 146.6 135.5 52.0
REMARK 620 6 GLY A 402 O 95.9 76.2 153.9 122.1 70.4
REMARK 620 7 ASN A 405 OD1 170.6 95.4 93.5 81.9 86.8 90.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 622 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 392 O
REMARK 620 2 GLY A 394 O 111.7
REMARK 620 3 ASP A 396 OD2 83.4 85.8
REMARK 620 4 GLY A 409 O 86.3 161.9 98.9
REMARK 620 5 ALA A 411 O 93.8 81.9 165.4 95.2
REMARK 620 6 ASN A 414 OD1 164.3 82.9 92.3 79.4 93.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 623 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 494 O
REMARK 620 2 GLY A 496 O 90.1
REMARK 620 3 ASP A 498 OD2 80.9 84.9
REMARK 620 4 GLY A 511 O 81.4 170.8 90.4
REMARK 620 5 ASP A 513 O 85.6 82.6 161.6 99.9
REMARK 620 6 ASP A 516 OD1 163.3 83.8 83.1 103.5 108.8
REMARK 620 7 ASP A 516 OD2 144.8 121.6 114.2 67.5 84.0 48.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 624 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU A 512 O
REMARK 620 2 GLY A 514 O 108.2
REMARK 620 3 ASP A 516 OD2 83.7 80.3
REMARK 620 4 GLY A 529 O 79.3 172.2 99.0
REMARK 620 5 ALA A 531 O 83.4 81.4 153.0 101.8
REMARK 620 6 ASP A 534 OD1 160.4 81.9 81.4 90.4 115.2
REMARK 620 7 ASP A 534 OD2 138.1 108.1 122.4 65.6 82.2 46.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 629 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 517 NE2
REMARK 620 2 GLU A 537 OE2 102.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 625 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 521 O
REMARK 620 2 GLY A 523 O 86.0
REMARK 620 3 ASP A 525 OD2 89.9 84.7
REMARK 620 4 SER A 538 O 80.2 165.7 91.5
REMARK 620 5 GLY A 540 O 84.5 87.5 170.7 94.9
REMARK 620 6 ASP A 543 OD1 161.1 75.4 91.9 118.6 91.1
REMARK 620 7 ASP A 543 OD2 145.1 124.3 108.2 70.0 80.5 50.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 626 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 530 O
REMARK 620 2 GLY A 532 O 100.5
REMARK 620 3 ASP A 534 OD2 84.6 83.4
REMARK 620 4 PHE A 551 O 90.2 81.7 163.1
REMARK 620 5 ASP A 554 OD1 170.3 86.9 90.0 97.1
REMARK 620 6 HOH A 669 O 80.2 176.6 93.3 101.7 92.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 627 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 541 O
REMARK 620 2 THR A 560 OG1 154.0
REMARK 620 3 ASN A 562 OD1 89.0 71.2
REMARK 620 4 ASP A 563 OD1 77.8 115.4 84.1
REMARK 620 5 ASP A 563 OD2 124.2 78.5 105.2 51.5
REMARK 620 6 HOH A 714 O 92.6 102.9 166.4 109.4 85.0
REMARK 620 7 HOH A 757 O 81.8 80.3 86.3 157.5 151.0 80.7
REMARK 620 N 1 2 3 4 5 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Z8Z RELATED DB: PDB
DBREF 2Z8X A 1 617 UNP Q9RBY1 Q9RBY1_9PSED 1 617
SEQRES 1 A 617 MET GLY VAL TYR ASP TYR LYS ASN PHE GLY THR ALA ASP
SEQRES 2 A 617 SER LYS ALA LEU PHE SER ASP ALA MET ALA ILE THR LEU
SEQRES 3 A 617 TYR SER TYR HIS ASN LEU ASP ASN GLY PHE ALA ALA GLY
SEQRES 4 A 617 TYR GLN HIS ASN GLY PHE GLY LEU GLY LEU PRO ALA THR
SEQRES 5 A 617 LEU VAL THR ALA LEU LEU GLY GLY THR ASP SER GLN GLY
SEQRES 6 A 617 VAL ILE PRO GLY ILE PRO TRP ASN PRO ASP SER GLU LYS
SEQRES 7 A 617 LEU ALA LEU ASP ALA VAL LYS LYS ALA GLY TRP THR PRO
SEQRES 8 A 617 ILE THR ALA SER GLN LEU GLY TYR ASP GLY LYS THR ASP
SEQRES 9 A 617 ALA ARG GLY THR PHE PHE GLY GLU LYS ALA GLY TYR THR
SEQRES 10 A 617 THR ALA GLN VAL GLU ILE LEU GLY LYS TYR ASP ALA GLN
SEQRES 11 A 617 GLY HIS LEU THR GLU ILE GLY ILE ALA PHE ARG GLY THR
SEQRES 12 A 617 SER GLY PRO ARG GLU ASN LEU ILE LEU ASP SER ILE GLY
SEQRES 13 A 617 ASP VAL ILE ASN ASP LEU LEU ALA ALA PHE GLY PRO LYS
SEQRES 14 A 617 ASP TYR ALA LYS ASN TYR VAL GLY GLU ALA PHE GLY ASN
SEQRES 15 A 617 LEU LEU ASN ASP VAL VAL ALA PHE ALA LYS ALA ASN GLY
SEQRES 16 A 617 LEU SER GLY LYS ASP VAL LEU VAL SER GLY HIS SER LEU
SEQRES 17 A 617 GLY GLY LEU ALA VAL ASN SER MET ALA ASP LEU SER GLY
SEQRES 18 A 617 GLY LYS TRP GLY GLY PHE PHE ALA ASP SER ASN TYR ILE
SEQRES 19 A 617 ALA TYR ALA SER PRO THR GLN SER SER THR ASP LYS VAL
SEQRES 20 A 617 LEU ASN VAL GLY TYR GLU ASN ASP PRO VAL PHE ARG ALA
SEQRES 21 A 617 LEU ASP GLY SER THR PHE THR GLY ALA SER VAL GLY VAL
SEQRES 22 A 617 HIS ASP ALA PRO LYS GLU SER ALA THR ASP ASN ILE VAL
SEQRES 23 A 617 SER PHE ASN ASP HIS TYR ALA SER THR ALA TRP ASN LEU
SEQRES 24 A 617 LEU PRO PHE SER ILE LEU ASN ILE PRO THR TRP ILE SER
SEQRES 25 A 617 HIS LEU PRO THR ALA TYR GLY ASP GLY MET ASN ARG ILE
SEQRES 26 A 617 ILE GLU SER LYS PHE TYR ASP LEU THR SER LYS ASP SER
SEQRES 27 A 617 THR ILE ILE VAL ALA ASN LEU SER ASP PRO ALA ARG ALA
SEQRES 28 A 617 ASN THR TRP VAL GLN ASP LEU ASN ARG ASN ALA GLU THR
SEQRES 29 A 617 HIS LYS GLY SER THR PHE ILE ILE GLY SER ASP SER ASN
SEQRES 30 A 617 ASP LEU ILE GLN GLY GLY SER GLY ASN ASP TYR LEU GLU
SEQRES 31 A 617 GLY ARG ALA GLY ASN ASP THR PHE ARG ASP GLY GLY GLY
SEQRES 32 A 617 TYR ASN VAL ILE LEU GLY GLY ALA GLY ASN ASN THR LEU
SEQRES 33 A 617 ASP LEU GLN LYS SER VAL ASN THR PHE ASP PHE ALA ASN
SEQRES 34 A 617 ASP GLY ALA GLY ASN LEU TYR VAL ARG ASP ALA ASN GLY
SEQRES 35 A 617 GLY ILE SER ILE THR ARG ASP ILE GLY SER ILE VAL THR
SEQRES 36 A 617 LYS GLU PRO GLY PHE LEU TRP GLY LEU PHE LYS ASP ASP
SEQRES 37 A 617 VAL THR HIS SER VAL THR ALA SER GLY LEU LYS VAL GLY
SEQRES 38 A 617 SER ASN VAL THR GLN TYR ASP ALA SER VAL LYS GLY THR
SEQRES 39 A 617 ASN GLY ALA ASP THR LEU LYS ALA HIS ALA GLY GLY ASP
SEQRES 40 A 617 TRP LEU PHE GLY LEU ASP GLY ASN ASP HIS LEU ILE GLY
SEQRES 41 A 617 GLY VAL GLY ASN ASP VAL PHE VAL GLY GLY ALA GLY ASN
SEQRES 42 A 617 ASP LEU MET GLU SER GLY GLY GLY ALA ASP THR PHE LEU
SEQRES 43 A 617 PHE ASN GLY ALA PHE GLY GLN ASP ARG VAL VAL GLY PHE
SEQRES 44 A 617 THR SER ASN ASP LYS LEU VAL PHE LEU GLY VAL GLN GLY
SEQRES 45 A 617 VAL LEU PRO ASN ASP ASP PHE ARG ALA HIS ALA SER MET
SEQRES 46 A 617 VAL GLY GLN ASP THR VAL LEU LYS PHE GLY GLY ASP SER
SEQRES 47 A 617 VAL THR LEU VAL GLY VAL ALA LEU ASN SER LEU SER ALA
SEQRES 48 A 617 ASP GLY ILE VAL ILE ALA
HET CA A 618 1
HET CA A 619 1
HET CA A 620 1
HET CA A 621 1
HET CA A 622 1
HET CA A 623 1
HET CA A 624 1
HET CA A 625 1
HET CA A 626 1
HET CA A 627 1
HET ZN A 628 1
HET ZN A 629 1
HETNAM CA CALCIUM ION
HETNAM ZN ZINC ION
FORMUL 2 CA 10(CA 2+)
FORMUL 12 ZN 2(ZN 2+)
FORMUL 14 HOH *769(H2 O)
HELIX 1 1 GLY A 10 TYR A 29 1 20
HELIX 2 2 ASP A 33 GLY A 44 1 12
HELIX 3 3 PRO A 50 GLY A 60 1 11
HELIX 4 4 ASP A 75 ALA A 87 1 13
HELIX 5 5 THR A 93 GLY A 98 1 6
HELIX 6 6 PRO A 146 LEU A 152 5 7
HELIX 7 7 SER A 154 GLY A 167 1 14
HELIX 8 8 ASP A 170 ASN A 194 1 25
HELIX 9 9 SER A 197 LYS A 199 5 3
HELIX 10 10 SER A 207 SER A 220 1 14
HELIX 11 11 LYS A 223 SER A 231 5 9
HELIX 12 12 ASN A 289 SER A 294 1 6
HELIX 13 13 THR A 295 LEU A 299 5 5
HELIX 14 14 ASN A 306 HIS A 313 5 8
HELIX 15 15 LEU A 314 SER A 328 1 15
HELIX 16 16 PHE A 330 THR A 334 5 5
HELIX 17 17 SER A 346 ALA A 351 1 6
HELIX 18 18 SER A 421 PHE A 425 5 5
HELIX 19 19 TRP A 462 LEU A 464 5 3
HELIX 20 20 ASP A 578 ALA A 581 5 4
HELIX 21 21 ALA A 605 LEU A 609 5 5
HELIX 22 22 SER A 610 ASP A 612 5 3
SHEET 1 A 3 TRP A 89 PRO A 91 0
SHEET 2 A 3 GLN A 120 TYR A 127 -1 O GLY A 125 N THR A 90
SHEET 3 A 3 PHE A 109 PHE A 110 -1 N PHE A 109 O VAL A 121
SHEET 1 B 6 TRP A 89 PRO A 91 0
SHEET 2 B 6 GLN A 120 TYR A 127 -1 O GLY A 125 N THR A 90
SHEET 3 B 6 LEU A 133 ARG A 141 -1 O THR A 134 N LYS A 126
SHEET 4 B 6 VAL A 201 HIS A 206 1 O SER A 204 N ILE A 138
SHEET 5 B 6 ASN A 232 TYR A 236 1 O ASN A 232 N VAL A 203
SHEET 6 B 6 VAL A 247 VAL A 250 1 O VAL A 250 N ALA A 235
SHEET 1 C 8 ILE A 285 PHE A 288 0
SHEET 2 C 8 THR A 339 ALA A 343 1 O VAL A 342 N VAL A 286
SHEET 3 C 8 THR A 369 ILE A 372 1 O PHE A 370 N ILE A 341
SHEET 4 C 8 ASP A 387 GLU A 390 1 O TYR A 388 N ILE A 371
SHEET 5 C 8 ASN A 405 LEU A 408 1 O LEU A 408 N LEU A 389
SHEET 6 C 8 ILE A 444 ARG A 448 1 O ILE A 446 N ASN A 405
SHEET 7 C 8 LEU A 435 ARG A 438 -1 N VAL A 437 O SER A 445
SHEET 8 C 8 ASP A 426 ASN A 429 -1 N ALA A 428 O TYR A 436
SHEET 1 D 7 LEU A 379 GLY A 382 0
SHEET 2 D 7 THR A 397 ASP A 400 1 O ARG A 399 N GLY A 382
SHEET 3 D 7 THR A 415 ASP A 417 1 O ASP A 417 N PHE A 398
SHEET 4 D 7 SER A 452 LEU A 461 1 O VAL A 454 N LEU A 416
SHEET 5 D 7 PHE A 465 THR A 474 -1 O HIS A 471 N ILE A 453
SHEET 6 D 7 GLY A 477 VAL A 480 -1 O LYS A 479 N SER A 472
SHEET 7 D 7 ASN A 483 THR A 485 -1 O THR A 485 N LEU A 478
SHEET 1 E 6 SER A 490 LYS A 492 0
SHEET 2 E 6 TRP A 508 PHE A 510 1 O PHE A 510 N VAL A 491
SHEET 3 E 6 VAL A 526 VAL A 528 1 O VAL A 526 N LEU A 509
SHEET 4 E 6 THR A 544 PHE A 547 1 O THR A 544 N PHE A 527
SHEET 5 E 6 LYS A 564 PHE A 567 1 O VAL A 566 N PHE A 547
SHEET 6 E 6 ILE A 614 ILE A 616 1 O VAL A 615 N LEU A 565
SHEET 1 F 7 THR A 499 LYS A 501 0
SHEET 2 F 7 HIS A 517 ILE A 519 1 O ILE A 519 N LEU A 500
SHEET 3 F 7 LEU A 535 GLU A 537 1 O LEU A 535 N LEU A 518
SHEET 4 F 7 GLN A 553 VAL A 557 1 O VAL A 557 N MET A 536
SHEET 5 F 7 ASP A 597 LEU A 601 1 O THR A 600 N VAL A 556
SHEET 6 F 7 ASP A 589 PHE A 594 -1 N THR A 590 O LEU A 601
SHEET 7 F 7 ALA A 583 VAL A 586 -1 N SER A 584 O VAL A 591
LINK OD2 ASP A 128 ZN ZN A 628 1555 1555 1.92
LINK ND1 HIS A 132 ZN ZN A 628 1555 1555 2.05
LINK OE2 GLU A 253 CA CA A 618 1555 1555 2.25
LINK OD1 ASP A 275 CA CA A 618 1555 1555 2.47
LINK OD2 ASP A 275 CA CA A 618 1555 1555 2.46
LINK O LYS A 278 CA CA A 619 1555 1555 2.43
LINK O ALA A 281 CA CA A 619 1555 1555 2.37
LINK O ASP A 283 CA CA A 618 1555 1555 2.42
LINK OD2 ASP A 283 CA CA A 619 1555 1555 2.33
LINK OD1 ASN A 284 CA CA A 618 1555 1555 2.33
LINK OD1 ASP A 337 CA CA A 619 1555 1555 2.53
LINK OD2 ASP A 337 CA CA A 619 1555 1555 2.46
LINK O SER A 374 CA CA A 620 1555 1555 2.32
LINK O SER A 376 CA CA A 620 1555 1555 2.32
LINK OD2 ASP A 378 CA CA A 620 1555 1555 2.39
LINK O GLY A 383 CA CA A 621 1555 1555 2.38
LINK O GLY A 385 CA CA A 621 1555 1555 2.35
LINK OD2 ASP A 387 CA CA A 621 1555 1555 2.36
LINK O GLY A 391 CA CA A 620 1555 1555 2.29
LINK O ARG A 392 CA CA A 622 1555 1555 2.35
LINK O ALA A 393 CA CA A 620 1555 1555 2.34
LINK O GLY A 394 CA CA A 622 1555 1555 2.33
LINK OD1 ASP A 396 CA CA A 620 1555 1555 2.38
LINK OD2 ASP A 396 CA CA A 622 1555 1555 2.31
LINK OD1 ASP A 400 CA CA A 621 1555 1555 2.53
LINK OD2 ASP A 400 CA CA A 621 1555 1555 2.46
LINK O GLY A 402 CA CA A 621 1555 1555 2.35
LINK OD1 ASN A 405 CA CA A 621 1555 1555 2.41
LINK O GLY A 409 CA CA A 622 1555 1555 2.34
LINK O ALA A 411 CA CA A 622 1555 1555 2.35
LINK OD1 ASN A 414 CA CA A 622 1555 1555 2.42
LINK O THR A 494 CA CA A 623 1555 1555 2.33
LINK O GLY A 496 CA CA A 623 1555 1555 2.32
LINK OD2 ASP A 498 CA CA A 623 1555 1555 2.35
LINK O GLY A 511 CA CA A 623 1555 1555 2.32
LINK O LEU A 512 CA CA A 624 1555 1555 2.40
LINK O ASP A 513 CA CA A 623 1555 1555 2.33
LINK O GLY A 514 CA CA A 624 1555 1555 2.44
LINK OD1 ASP A 516 CA CA A 623 1555 1555 2.41
LINK OD2 ASP A 516 CA CA A 624 1555 1555 2.34
LINK OD2 ASP A 516 CA CA A 623 1555 1555 2.84
LINK NE2 HIS A 517 ZN ZN A 629 1555 1555 2.08
LINK O GLY A 521 CA CA A 625 1555 1555 2.39
LINK O GLY A 523 CA CA A 625 1555 1555 2.46
LINK OD2 ASP A 525 CA CA A 625 1555 1555 2.36
LINK O GLY A 529 CA CA A 624 1555 1555 2.38
LINK O GLY A 530 CA CA A 626 1555 1555 2.34
LINK O ALA A 531 CA CA A 624 1555 1555 2.31
LINK O GLY A 532 CA CA A 626 1555 1555 2.41
LINK OD1 ASP A 534 CA CA A 624 1555 1555 2.35
LINK OD2 ASP A 534 CA CA A 626 1555 1555 2.33
LINK OD2 ASP A 534 CA CA A 624 1555 1555 3.00
LINK OE2 GLU A 537 ZN ZN A 629 1555 1555 1.97
LINK O SER A 538 CA CA A 625 1555 1555 2.49
LINK O GLY A 540 CA CA A 625 1555 1555 2.31
LINK O GLY A 541 CA CA A 627 1555 1555 2.38
LINK OD1 ASP A 543 CA CA A 625 1555 1555 2.55
LINK OD2 ASP A 543 CA CA A 625 1555 1555 2.50
LINK O PHE A 551 CA CA A 626 1555 1555 2.22
LINK OD1 ASP A 554 CA CA A 626 1555 1555 2.44
LINK OG1 THR A 560 CA CA A 627 1555 1555 2.47
LINK OD1 ASN A 562 CA CA A 627 1555 1555 2.33
LINK OD1 ASP A 563 CA CA A 627 1555 1555 2.48
LINK OD2 ASP A 563 CA CA A 627 1555 1555 2.56
LINK CA CA A 618 O HOH A 652 1555 1555 2.43
LINK CA CA A 618 O HOH A 656 1555 1555 2.36
LINK CA CA A 619 O HOH A 735 1555 1555 2.45
LINK CA CA A 619 O HOH A 702 1555 1555 2.38
LINK CA CA A 626 O HOH A 669 1555 1555 2.38
LINK CA CA A 627 O HOH A 714 1555 1555 2.35
LINK CA CA A 627 O HOH A 757 1555 1555 2.37
CISPEP 1 ASP A 62 SER A 63 0 -23.88
CRYST1 49.972 84.300 86.849 90.00 96.32 90.00 P 1 21 1 2
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 0.020011 0.000000 0.002215 0.00000
SCALE2 0.000000 0.011862 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011585 0.00000
TER 4554 ALA A 617
MASTER 454 0 12 22 37 0 0 6 5334 1 91 48
END |