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HEADER HYDROLASE 05-JUN-17 5XPX
TITLE STRUCTURE ELUCIDATION OF TRUNCATED AMS3 LIPASE FROM AN ANTARCTIC
TITLE 2 PSEUDOMONAS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, E;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SP. A3(2015C);
SOURCE 3 ORGANISM_TAXID: 1680634;
SOURCE 4 STRAIN: 2015C;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.N.Z.R.A.RAHMAN,W.LATIP
REVDAT 1 20-JUN-18 5XPX 0
JRNL AUTH R.N.Z.R.A.RAHMAN,W.LATIP
JRNL TITL STRUCTURE ELUCIDATION OF TRUNCATED AMS3 LIPASE FROM AN
JRNL TITL 2 ANTARCTIC PSEUDOMONAS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 25583
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1391
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) : 2.77
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.84
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1817
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.3180
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.3800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6042
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 20
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.73000
REMARK 3 B22 (A**2) : -1.92000
REMARK 3 B33 (A**2) : -1.81000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.381
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.299
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.282
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.856
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6208 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5488 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8440 ; 1.689 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12671 ; 1.098 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 763 ; 7.306 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 312 ;32.751 ;23.013
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 942 ;19.322 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;18.906 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 883 ; 0.095 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7088 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1415 ; 0.002 ; 0.020
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): 3058 ; 1.671 ; 2.679
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3057 ; 1.630 ; 2.677
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3819 ; 2.766 ; 4.011
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3820 ; 2.767 ; 4.012
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3150 ; 1.592 ; 2.830
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3151 ; 1.592 ; 2.831
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4622 ; 2.704 ; 4.187
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7101 ; 4.510 ;30.835
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7102 ; 4.510 ;30.836
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 : NULL
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 5XPX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1300003609.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27263
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.770
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.82
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 4FDM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES SODIUM PH 7.5, 0.8 M
REMARK 280 POTASSIUM SODIUM TARTRATE TETRAHYDRATE, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293.15K
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 43.37650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.21550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.34650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.21550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.37650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.34650
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E
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 MET A -22
REMARK 465 ALA A -21
REMARK 465 SER A -20
REMARK 465 TRP A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 PRO A -16
REMARK 465 GLN A -15
REMARK 465 PHE A -14
REMARK 465 GLU A -13
REMARK 465 LYS A -12
REMARK 465 GLY A -11
REMARK 465 ALA A -10
REMARK 465 ASP A -9
REMARK 465 ASP A -8
REMARK 465 ASP A -7
REMARK 465 ASP A -6
REMARK 465 LYS A -5
REMARK 465 VAL A -4
REMARK 465 PRO A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 ALA A 1
REMARK 465 SER A 2
REMARK 465 LEU A 3
REMARK 465 PRO A 388
REMARK 465 PRO A 389
REMARK 465 GLY A 390
REMARK 465 PHE A 391
REMARK 465 SER A 392
REMARK 465 SER A 393
REMARK 465 ILE A 394
REMARK 465 SER A 395
REMARK 465 ALA A 396
REMARK 465 HIS A 397
REMARK 465 HIS A 398
REMARK 465 HIS A 399
REMARK 465 HIS A 400
REMARK 465 HIS A 401
REMARK 465 HIS A 402
REMARK 465 HIS A 403
REMARK 465 HIS A 404
REMARK 465 HIS A 405
REMARK 465 HIS A 406
REMARK 465 MET E -22
REMARK 465 ALA E -21
REMARK 465 SER E -20
REMARK 465 TRP E -19
REMARK 465 SER E -18
REMARK 465 HIS E -17
REMARK 465 PRO E -16
REMARK 465 GLN E -15
REMARK 465 PHE E -14
REMARK 465 GLU E -13
REMARK 465 LYS E -12
REMARK 465 GLY E -11
REMARK 465 ALA E -10
REMARK 465 ASP E -9
REMARK 465 ASP E -8
REMARK 465 ASP E -7
REMARK 465 ASP E -6
REMARK 465 LYS E -5
REMARK 465 VAL E -4
REMARK 465 PRO E -3
REMARK 465 ARG E -2
REMARK 465 GLY E -1
REMARK 465 SER E 0
REMARK 465 ALA E 1
REMARK 465 SER E 2
REMARK 465 LEU E 3
REMARK 465 ARG E 4
REMARK 465 ALA E 5
REMARK 465 ASN E 6
REMARK 465 PRO E 388
REMARK 465 PRO E 389
REMARK 465 GLY E 390
REMARK 465 PHE E 391
REMARK 465 SER E 392
REMARK 465 SER E 393
REMARK 465 ILE E 394
REMARK 465 SER E 395
REMARK 465 ALA E 396
REMARK 465 HIS E 397
REMARK 465 HIS E 398
REMARK 465 HIS E 399
REMARK 465 HIS E 400
REMARK 465 HIS E 401
REMARK 465 HIS E 402
REMARK 465 HIS E 403
REMARK 465 HIS E 404
REMARK 465 HIS E 405
REMARK 465 HIS E 406
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 ILE E 107 O VAL E 155 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 ARG A 274 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 LEU A 386 CA - CB - CG ANGL. DEV. = 14.7 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 ALA A 5 19.58 -172.60
REMARK 500 ALA A 52 89.25 -151.50
REMARK 500 SER A 113 -131.33 54.54
REMARK 500 ASP A 175 30.20 -95.49
REMARK 500 VAL A 203 -66.12 74.42
REMARK 500 LEU A 208 39.81 -97.02
REMARK 500 ARG A 271 45.13 -151.98
REMARK 500 ASP A 310 -157.36 -118.92
REMARK 500 ILE A 319 -48.07 -139.35
REMARK 500 ASN A 326 -54.74 -21.42
REMARK 500 LYS A 329 -63.81 -130.03
REMARK 500 ASN A 367 86.91 -156.70
REMARK 500 ALA E 8 121.21 72.47
REMARK 500 GLU E 100 -15.29 -44.30
REMARK 500 SER E 113 -130.41 59.34
REMARK 500 ASN E 141 70.87 52.97
REMARK 500 HIS E 153 59.34 -149.17
REMARK 500 VAL E 155 -73.63 -67.13
REMARK 500 LEU E 156 -62.75 97.57
REMARK 500 ASP E 175 38.52 -99.88
REMARK 500 SER E 201 153.47 -46.32
REMARK 500 VAL E 203 -66.97 68.79
REMARK 500 ASP E 238 50.52 -97.05
REMARK 500 ARG E 271 37.45 -158.70
REMARK 500 ASN E 304 99.81 -171.37
REMARK 500 ILE E 319 -55.71 -132.09
REMARK 500 LYS E 329 -55.44 -140.22
REMARK 500 ASP E 357 165.49 -46.52
REMARK 500 ASN E 367 80.68 -173.35
REMARK 500 SER E 385 45.06 -72.54
REMARK 500 LEU E 386 -48.30 -175.10
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 385 LEU A 386 -149.21
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 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 61 OD1
REMARK 620 2 HIS A 87 NE2 119.1
REMARK 620 3 ASP A 238 OD2 127.7 92.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 286 O
REMARK 620 2 GLU A 360 OE2 72.6
REMARK 620 3 ASP A 365 OD2 108.2 115.2
REMARK 620 4 PRO A 366 O 150.9 82.7 96.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 61 OD1
REMARK 620 2 HIS E 81 NE2 98.8
REMARK 620 3 HIS E 87 NE2 124.5 107.7
REMARK 620 4 ASP E 238 OD2 116.2 105.8 102.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY E 286 O
REMARK 620 2 GLU E 360 OE2 73.4
REMARK 620 3 ASP E 365 OD2 98.1 93.9
REMARK 620 4 PRO E 366 O 142.6 69.2 85.3
REMARK 620 N 1 2 3
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 502
DBREF1 5XPX A 1 388 UNP A0A0K0PTR1_9PSED
DBREF2 5XPX A A0A0K0PTR1 1 388
DBREF1 5XPX E 1 388 UNP A0A0K0PTR1_9PSED
DBREF2 5XPX E A0A0K0PTR1 1 388
SEQADV 5XPX MET A -22 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ALA A -21 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX SER A -20 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX TRP A -19 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX SER A -18 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS A -17 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX PRO A -16 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX GLN A -15 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX PHE A -14 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX GLU A -13 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX LYS A -12 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX GLY A -11 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ALA A -10 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ASP A -9 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ASP A -8 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ASP A -7 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ASP A -6 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX LYS A -5 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX VAL A -4 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX PRO A -3 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ARG A -2 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX GLY A -1 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX SER A 0 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX PRO A 389 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX GLY A 390 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX PHE A 391 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX SER A 392 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX SER A 393 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ILE A 394 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX SER A 395 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ALA A 396 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS A 397 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS A 398 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS A 399 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS A 400 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS A 401 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS A 402 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS A 403 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS A 404 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS A 405 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS A 406 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX MET E -22 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ALA E -21 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX SER E -20 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX TRP E -19 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX SER E -18 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS E -17 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX PRO E -16 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX GLN E -15 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX PHE E -14 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX GLU E -13 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX LYS E -12 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX GLY E -11 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ALA E -10 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ASP E -9 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ASP E -8 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ASP E -7 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ASP E -6 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX LYS E -5 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX VAL E -4 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX PRO E -3 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ARG E -2 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX GLY E -1 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX SER E 0 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX PRO E 389 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX GLY E 390 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX PHE E 391 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX SER E 392 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX SER E 393 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ILE E 394 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX SER E 395 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX ALA E 396 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS E 397 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS E 398 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS E 399 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS E 400 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS E 401 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS E 402 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS E 403 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS E 404 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS E 405 UNP A0A0K0PTR EXPRESSION TAG
SEQADV 5XPX HIS E 406 UNP A0A0K0PTR EXPRESSION TAG
SEQRES 1 A 429 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 A 429 ASP ASP ASP ASP LYS VAL PRO ARG GLY SER ALA SER LEU
SEQRES 3 A 429 ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS GLY PHE
SEQRES 4 A 429 THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE LYS TYR
SEQRES 5 A 429 TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP LEU ASN
SEQRES 6 A 429 ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL GLY PRO
SEQRES 7 A 429 LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA TYR ALA
SEQRES 8 A 429 GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA ALA HIS
SEQRES 9 A 429 ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG THR TYR
SEQRES 10 A 429 PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY ARG ILE
SEQRES 11 A 429 HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR ALA ARG
SEQRES 12 A 429 MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN GLU GLU
SEQRES 13 A 429 ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU SER PRO
SEQRES 14 A 429 LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER VAL THR
SEQRES 15 A 429 THR ILE ALA THR PRO HIS ASP GLY THR THR LEU VAL ASN
SEQRES 16 A 429 MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU GLN LYS
SEQRES 17 A 429 ALA VAL LEU GLU ALA ALA ALA VAL ALA SER ASN VAL PRO
SEQRES 18 A 429 TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP GLN TRP
SEQRES 19 A 429 GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP HIS TYR
SEQRES 20 A 429 PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR SER THR
SEQRES 21 A 429 ASP THR ALA ARG TYR ASP LEU SER VAL SER GLY ALA GLU
SEQRES 22 A 429 LYS LEU ASN GLN TRP VAL GLN ALA SER PRO ASN THR TYR
SEQRES 23 A 429 TYR LEU SER PHE SER THR GLU ARG THR TYR ARG GLY ALA
SEQRES 24 A 429 LEU THR GLY ASN HIS TYR PRO GLU LEU GLY MET ASN ALA
SEQRES 25 A 429 PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY SER TYR
SEQRES 26 A 429 ARG ASN PRO THR LEU GLY ILE ASP ASP ARG TRP LEU GLU
SEQRES 27 A 429 ASN ASP GLY ILE VAL ASN THR VAL SER MET ASN GLY PRO
SEQRES 28 A 429 LYS ARG GLY SER SER ASP ARG ILE VAL PRO TYR ASP GLY
SEQRES 29 A 429 THR LEU LYS LYS GLY VAL TRP ASN ASP MET GLY THR TYR
SEQRES 30 A 429 ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL ASP PRO ASN
SEQRES 31 A 429 PRO SER PHE ASP ILE ARG ALA PHE TYR LEU ARG LEU ALA
SEQRES 32 A 429 GLU GLN LEU ALA SER LEU ARG PRO PRO GLY PHE SER SER
SEQRES 33 A 429 ILE SER ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 E 429 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 E 429 ASP ASP ASP ASP LYS VAL PRO ARG GLY SER ALA SER LEU
SEQRES 3 E 429 ARG ALA ASN ASP ALA PRO ILE VAL LEU LEU HIS GLY PHE
SEQRES 4 E 429 THR GLY TRP GLY ARG GLU GLU MET PHE GLY PHE LYS TYR
SEQRES 5 E 429 TRP GLY GLY VAL ARG GLY ASP ILE GLU GLN TRP LEU ASN
SEQRES 6 E 429 ASP ASN GLY TYR ARG THR TYR THR LEU ALA VAL GLY PRO
SEQRES 7 E 429 LEU SER SER ASN TRP ASP ARG ALA CYS GLU ALA TYR ALA
SEQRES 8 E 429 GLN LEU VAL GLY GLY THR VAL ASP TYR GLY ALA ALA HIS
SEQRES 9 E 429 ALA ALA LYS HIS GLY HIS ALA ARG PHE GLY ARG THR TYR
SEQRES 10 E 429 PRO GLY LEU LEU PRO GLU LEU LYS ARG GLY GLY ARG ILE
SEQRES 11 E 429 HIS ILE ILE ALA HIS SER GLN GLY GLY GLN THR ALA ARG
SEQRES 12 E 429 MET LEU VAL SER LEU LEU GLU ASN GLY SER GLN GLU GLU
SEQRES 13 E 429 ARG GLU TYR ALA LYS ALA HIS ASN VAL SER LEU SER PRO
SEQRES 14 E 429 LEU PHE GLU GLY GLY HIS HIS PHE VAL LEU SER VAL THR
SEQRES 15 E 429 THR ILE ALA THR PRO HIS ASP GLY THR THR LEU VAL ASN
SEQRES 16 E 429 MET VAL ASP PHE THR ASP ARG PHE PHE ASP LEU GLN LYS
SEQRES 17 E 429 ALA VAL LEU GLU ALA ALA ALA VAL ALA SER ASN VAL PRO
SEQRES 18 E 429 TYR THR SER GLN VAL TYR ASP PHE LYS LEU ASP GLN TRP
SEQRES 19 E 429 GLY LEU ARG ARG GLN PRO GLY GLU SER PHE ASP HIS TYR
SEQRES 20 E 429 PHE GLU ARG LEU LYS ARG SER PRO VAL TRP THR SER THR
SEQRES 21 E 429 ASP THR ALA ARG TYR ASP LEU SER VAL SER GLY ALA GLU
SEQRES 22 E 429 LYS LEU ASN GLN TRP VAL GLN ALA SER PRO ASN THR TYR
SEQRES 23 E 429 TYR LEU SER PHE SER THR GLU ARG THR TYR ARG GLY ALA
SEQRES 24 E 429 LEU THR GLY ASN HIS TYR PRO GLU LEU GLY MET ASN ALA
SEQRES 25 E 429 PHE SER ALA VAL VAL CYS ALA PRO PHE LEU GLY SER TYR
SEQRES 26 E 429 ARG ASN PRO THR LEU GLY ILE ASP ASP ARG TRP LEU GLU
SEQRES 27 E 429 ASN ASP GLY ILE VAL ASN THR VAL SER MET ASN GLY PRO
SEQRES 28 E 429 LYS ARG GLY SER SER ASP ARG ILE VAL PRO TYR ASP GLY
SEQRES 29 E 429 THR LEU LYS LYS GLY VAL TRP ASN ASP MET GLY THR TYR
SEQRES 30 E 429 ASN VAL ASP HIS LEU GLU ILE ILE GLY VAL ASP PRO ASN
SEQRES 31 E 429 PRO SER PHE ASP ILE ARG ALA PHE TYR LEU ARG LEU ALA
SEQRES 32 E 429 GLU GLN LEU ALA SER LEU ARG PRO PRO GLY PHE SER SER
SEQRES 33 E 429 ILE SER ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS
HET ZN A 501 1
HET CA A 502 1
HET ZN E 501 1
HET CA E 502 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 CA 2(CA 2+)
FORMUL 7 HOH *20(H2 O)
HELIX 1 AA1 GLU A 23 PHE A 27 5 5
HELIX 2 AA2 GLY A 31 GLY A 35 5 5
HELIX 3 AA3 ASP A 36 ASN A 44 1 9
HELIX 4 AA4 SER A 58 GLY A 72 1 15
HELIX 5 AA5 GLY A 78 GLY A 86 1 9
HELIX 6 AA6 LEU A 98 LYS A 102 5 5
HELIX 7 AA7 GLN A 114 GLY A 129 1 16
HELIX 8 AA8 SER A 130 ASN A 141 1 12
HELIX 9 AA9 SER A 145 GLU A 149 5 5
HELIX 10 AB1 THR A 168 MET A 173 5 6
HELIX 11 AB2 ASP A 175 ALA A 191 1 17
HELIX 12 AB3 SER A 220 ARG A 230 1 11
HELIX 13 AB4 SER A 231 SER A 236 1 6
HELIX 14 AB5 THR A 239 SER A 245 1 7
HELIX 15 AB6 SER A 245 VAL A 256 1 12
HELIX 16 AB7 ASN A 288 CYS A 295 1 8
HELIX 17 AB8 CYS A 295 GLY A 300 1 6
HELIX 18 AB9 ASN A 304 GLY A 308 5 5
HELIX 19 AC1 ASP A 310 LEU A 314 5 5
HELIX 20 AC2 ASN A 321 ASN A 326 5 6
HELIX 21 AC3 ASP A 371 ALA A 384 1 14
HELIX 22 AC4 GLU E 23 PHE E 27 5 5
HELIX 23 AC5 GLY E 31 GLY E 35 5 5
HELIX 24 AC6 ASP E 36 ASN E 44 1 9
HELIX 25 AC7 SER E 58 GLY E 72 1 15
HELIX 26 AC8 GLY E 78 GLY E 86 1 9
HELIX 27 AC9 LEU E 98 LYS E 102 5 5
HELIX 28 AD1 GLN E 114 GLY E 129 1 16
HELIX 29 AD2 SER E 130 ASN E 141 1 12
HELIX 30 AD3 SER E 145 GLU E 149 5 5
HELIX 31 AD4 THR E 168 MET E 173 5 6
HELIX 32 AD5 ASP E 175 ALA E 191 1 17
HELIX 33 AD6 LEU E 208 GLY E 212 5 5
HELIX 34 AD7 SER E 220 ARG E 230 1 11
HELIX 35 AD8 SER E 231 SER E 236 1 6
HELIX 36 AD9 THR E 239 SER E 245 1 7
HELIX 37 AE1 SER E 245 GLN E 254 1 10
HELIX 38 AE2 ASN E 288 CYS E 295 1 8
HELIX 39 AE3 CYS E 295 GLY E 300 1 6
HELIX 40 AE4 ASP E 310 LEU E 314 5 5
HELIX 41 AE5 ASN E 321 ASN E 326 5 6
HELIX 42 AE6 ASP E 371 SER E 385 1 15
SHEET 1 AA1 7 THR A 48 LEU A 51 0
SHEET 2 AA1 7 ILE A 10 LEU A 13 1 N LEU A 12 O LEU A 51
SHEET 3 AA1 7 ILE A 107 HIS A 112 1 O HIS A 108 N VAL A 11
SHEET 4 AA1 7 VAL A 155 ILE A 161 1 O SER A 157 N ILE A 109
SHEET 5 AA1 7 TYR A 263 THR A 269 1 O LEU A 265 N THR A 160
SHEET 6 AA1 7 TRP A 348 TYR A 354 1 O GLY A 352 N SER A 268
SHEET 7 AA1 7 ILE A 336 PRO A 338 1 N VAL A 337 O TRP A 348
SHEET 1 AA2 2 GLY A 73 ASP A 76 0
SHEET 2 AA2 2 PHE A 90 TYR A 94 -1 O GLY A 91 N VAL A 75
SHEET 1 AA3 2 THR A 272 ARG A 274 0
SHEET 2 AA3 2 HIS A 281 PRO A 283 -1 O TYR A 282 N TYR A 273
SHEET 1 AA4 7 THR E 48 THR E 50 0
SHEET 2 AA4 7 ILE E 10 LEU E 13 1 N ILE E 10 O TYR E 49
SHEET 3 AA4 7 ILE E 107 HIS E 112 1 O HIS E 108 N VAL E 11
SHEET 4 AA4 7 LEU E 156 ILE E 161 1 O THR E 159 N ALA E 111
SHEET 5 AA4 7 TYR E 263 GLU E 270 1 O PHE E 267 N THR E 160
SHEET 6 AA4 7 TRP E 348 ASN E 355 1 O ASN E 349 N SER E 266
SHEET 7 AA4 7 ILE E 336 PRO E 338 1 N VAL E 337 O ASP E 350
SHEET 1 AA5 2 GLY E 73 ASP E 76 0
SHEET 2 AA5 2 PHE E 90 TYR E 94 -1 O TYR E 94 N GLY E 73
SHEET 1 AA6 2 THR E 272 ARG E 274 0
SHEET 2 AA6 2 HIS E 281 PRO E 283 -1 O TYR E 282 N TYR E 273
LINK OD1 ASP A 61 ZN ZN A 501 1555 1555 1.97
LINK NE2 HIS A 87 ZN ZN A 501 1555 1555 2.24
LINK OD2 ASP A 238 ZN ZN A 501 1555 1555 1.92
LINK O GLY A 286 CA CA A 502 1555 1555 2.44
LINK OE2 GLU A 360 CA CA A 502 1555 1555 2.73
LINK OD2 ASP A 365 CA CA A 502 1555 1555 2.58
LINK O PRO A 366 CA CA A 502 1555 1555 2.39
LINK OD1 ASP E 61 ZN ZN E 501 1555 1555 2.03
LINK NE2 HIS E 81 ZN ZN E 501 1555 1555 2.09
LINK NE2 HIS E 87 ZN ZN E 501 1555 1555 2.25
LINK OD2 ASP E 238 ZN ZN E 501 1555 1555 1.78
LINK O GLY E 286 CA CA E 502 1555 1555 2.47
LINK OE2 GLU E 360 CA CA E 502 1555 1555 2.75
LINK OD2 ASP E 365 CA CA E 502 1555 1555 2.76
LINK O PRO E 366 CA CA E 502 1555 1555 2.59
SITE 1 AC1 4 ASP A 61 HIS A 81 HIS A 87 ASP A 238
SITE 1 AC2 4 GLY A 286 GLU A 360 ASP A 365 PRO A 366
SITE 1 AC3 4 ASP E 61 HIS E 81 HIS E 87 ASP E 238
SITE 1 AC4 4 GLY E 286 GLU E 360 ASP E 365 PRO E 366
CRYST1 86.753 94.693 126.431 90.00 90.00 90.00 P 21 21 21 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 0.011527 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010560 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007909 0.00000
TER 3034 ARG A 387
TER 6044 ARG E 387
MASTER 481 0 4 42 22 0 4 6 6066 2 19 66
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