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HEADER HYDROLASE 11-AUG-08 3E4D
TITLE STRUCTURAL AND KINETIC STUDY OF AN S-FORMYLGLUTATHIONE
TITLE 2 HYDROLASE FROM AGROBACTERIUM TUMEFACIENS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE D;
COMPND 3 CHAIN: A, B, C, E, D, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AGROBACTERIUM TUMEFACIENS;
SOURCE 3 ORGANISM_TAXID: 176299;
SOURCE 4 GENE: AGR_C_2723, ATU1476;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15TV-LIC
KEYWDS S-FORMYLGLUTATHIONE HYDROLASE, HYDROLASE FOLD FAMILY,
KEYWDS 2 CATALYTIC TRIAD, KINETICS, PROPOSED REACTION MECHANISM
EXPDTA X-RAY DIFFRACTION
AUTHOR K.E.VAN STRAATEN,C.F.GONZALEZ,R.B.VALLADARES,X.XU,
AUTHOR 2 A.V.SAVCHENKO,D.A.R.SANDERS
REVDAT 1 18-AUG-09 3E4D 0
JRNL AUTH K.E.VAN STRAATEN,C.F.GONZALEZ,R.B.VALLADARES,X.XU,
JRNL AUTH 2 A.V.SAVCHENKO,D.A.SANDERS
JRNL TITL THE STRUCTURE OF A PUTATIVE S-FORMYLGLUTATHIONE
JRNL TITL 2 HYDROLASE FROM AGROBACTERIUM TUMEFACIENS
JRNL REF PROTEIN SCI. 2009
JRNL REFN ESSN 1469-896X
JRNL PMID 19653299
JRNL DOI 10.1002/PRO.216
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 106327
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5368
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) : 2.01
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6659
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.1810
REMARK 3 BIN FREE R VALUE SET COUNT : 342
REMARK 3 BIN FREE R VALUE : 0.2180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13226
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.39000
REMARK 3 B22 (A**2) : 0.70000
REMARK 3 B33 (A**2) : -0.99000
REMARK 3 B12 (A**2) : 1.32000
REMARK 3 B13 (A**2) : -0.84000
REMARK 3 B23 (A**2) : -0.15000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.205
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.166
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.117
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.186
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13586 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18424 ; 1.207 ; 1.938
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1664 ; 5.423 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 652 ;32.679 ;23.374
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2150 ;11.296 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 84 ;11.911 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1880 ; 0.089 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10648 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6554 ; 0.184 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 9184 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 885 ; 0.123 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.013 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 55 ; 0.173 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.124 ; 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): 8544 ; 0.556 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13269 ; 0.927 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5904 ; 1.456 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5153 ; 2.216 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 3E4D COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-AUG-08.
REMARK 100 THE RCSB ID CODE IS RCSB048859.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106354
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.010
REMARK 200 RESOLUTION RANGE LOW (A) : 32.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 23.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.28800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MRBUMP
REMARK 200 STARTING MODEL: PDB CODE 1PV1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MGCL2, BIS-TRIS BUFFER,
REMARK 280 PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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, B
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 GLY D 0
REMARK 465 GLY F 0
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 240 CE NZ
REMARK 480 LYS B 228 CD CE NZ
REMARK 480 LYS E 228 CE NZ
REMARK 480 GLU D 22 CG CD OE1 OE2
REMARK 480 LYS D 37 CE NZ
REMARK 480 LYS D 228 CG CD CE NZ
REMARK 480 GLU D 237 CG CD OE1 OE2
REMARK 480 LYS D 240 CG CD CE NZ
REMARK 480 LYS F 25 CD CE NZ
REMARK 480 LYS F 37 CG CD CE NZ
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 THR A 53 -7.59 75.77
REMARK 500 THR A 55 -165.50 -115.64
REMARK 500 ALA A 101 47.90 -148.64
REMARK 500 PHE A 103 22.18 47.27
REMARK 500 GLU A 124 -69.09 -127.31
REMARK 500 ARG A 253 -18.24 75.81
REMARK 500 ASP A 255 -154.54 -111.19
REMARK 500 THR B 53 -7.26 77.40
REMARK 500 THR B 55 -166.90 -113.70
REMARK 500 ALA B 101 46.67 -150.86
REMARK 500 GLU B 124 -63.03 -126.09
REMARK 500 ARG B 253 -20.65 73.42
REMARK 500 ASP B 255 -158.25 -107.87
REMARK 500 THR C 53 -9.75 81.61
REMARK 500 THR C 55 -161.32 -121.52
REMARK 500 ALA C 101 44.24 -148.78
REMARK 500 PHE C 103 18.86 57.04
REMARK 500 GLU C 124 -64.89 -121.57
REMARK 500 ARG C 253 -26.24 75.41
REMARK 500 ASP C 255 -161.53 -111.49
REMARK 500 THR E 53 -5.77 78.00
REMARK 500 THR E 55 -167.70 -126.52
REMARK 500 ASP E 80 -179.72 -66.73
REMARK 500 ALA E 101 49.07 -148.06
REMARK 500 GLU E 124 -58.93 -123.26
REMARK 500 ARG E 253 -16.60 74.78
REMARK 500 ASP E 255 -158.49 -102.74
REMARK 500 THR D 53 -16.92 78.31
REMARK 500 THR D 55 -164.48 -121.29
REMARK 500 ALA D 101 51.11 -143.90
REMARK 500 GLU D 124 -65.04 -120.37
REMARK 500 ARG D 253 -18.63 72.53
REMARK 500 ASP D 255 -162.85 -111.77
REMARK 500 THR F 53 -5.46 75.38
REMARK 500 THR F 55 -161.48 -117.31
REMARK 500 ALA F 101 47.77 -150.14
REMARK 500 PHE F 103 18.54 56.38
REMARK 500 PRO F 213 -76.25 -43.17
REMARK 500 LEU F 230 -67.79 -105.78
REMARK 500 ARG F 253 -22.90 75.82
REMARK 500 ASP F 255 -155.70 -112.61
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 MG A 278 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 91 O
REMARK 620 2 ASN A 94 O 93.3
REMARK 620 3 MSE A 97 O 112.9 87.4
REMARK 620 4 HOH A 368 O 123.3 127.6 107.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 278 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 91 O
REMARK 620 2 ASN B 94 O 84.9
REMARK 620 3 MSE B 97 O 113.0 84.2
REMARK 620 4 HOH B 292 O 128.0 104.8 118.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 278 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 91 O
REMARK 620 2 ASN C 94 O 93.3
REMARK 620 3 MSE C 97 O 124.7 87.8
REMARK 620 4 HOH C 405 O 122.3 110.6 108.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 278 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN E 94 O
REMARK 620 2 MSE E 97 O 91.2
REMARK 620 3 HOH E 358 O 121.3 114.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 278 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 91 O
REMARK 620 2 ASN D 94 O 82.9
REMARK 620 3 MSE D 97 O 113.5 86.8
REMARK 620 4 HOH D 352 O 131.7 102.2 114.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 278 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN F 94 O
REMARK 620 2 MSE F 97 O 83.7
REMARK 620 N 1
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 278
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 279
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 280
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 278
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 279
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 280
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 278
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 278
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 279
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 280
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 278
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 279
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 278
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 279
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 280
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 279
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 280
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 280
DBREF 3E4D A 1 277 UNP A9CJ11 A9CJ11_AGRT5 1 277
DBREF 3E4D B 1 277 UNP A9CJ11 A9CJ11_AGRT5 1 277
DBREF 3E4D C 1 277 UNP A9CJ11 A9CJ11_AGRT5 1 277
DBREF 3E4D E 1 277 UNP A9CJ11 A9CJ11_AGRT5 1 277
DBREF 3E4D D 1 277 UNP A9CJ11 A9CJ11_AGRT5 1 277
DBREF 3E4D F 1 277 UNP A9CJ11 A9CJ11_AGRT5 1 277
SEQADV 3E4D GLY A 0 UNP A9CJ11 EXPRESSION TAG
SEQADV 3E4D GLY B 0 UNP A9CJ11 EXPRESSION TAG
SEQADV 3E4D GLY C 0 UNP A9CJ11 EXPRESSION TAG
SEQADV 3E4D GLY E 0 UNP A9CJ11 EXPRESSION TAG
SEQADV 3E4D GLY D 0 UNP A9CJ11 EXPRESSION TAG
SEQADV 3E4D GLY F 0 UNP A9CJ11 EXPRESSION TAG
SEQRES 1 A 278 GLY MSE ASN ILE ILE SER GLN ASN THR ALA PHE GLY GLY
SEQRES 2 A 278 MSE GLN GLY VAL PHE SER HIS GLN SER GLU THR LEU LYS
SEQRES 3 A 278 SER GLU MSE THR PHE ALA VAL TYR VAL PRO PRO LYS ALA
SEQRES 4 A 278 ILE HIS GLU PRO CYS PRO VAL VAL TRP TYR LEU SER GLY
SEQRES 5 A 278 LEU THR CYS THR HIS ALA ASN VAL MSE GLU LYS GLY GLU
SEQRES 6 A 278 TYR ARG ARG MSE ALA SER GLU LEU GLY LEU VAL VAL VAL
SEQRES 7 A 278 CYS PRO ASP THR SER PRO ARG GLY ASN ASP VAL PRO ASP
SEQRES 8 A 278 GLU LEU THR ASN TRP GLN MSE GLY LYS GLY ALA GLY PHE
SEQRES 9 A 278 TYR LEU ASP ALA THR GLU GLU PRO TRP SER GLU HIS TYR
SEQRES 10 A 278 GLN MSE TYR SER TYR VAL THR GLU GLU LEU PRO ALA LEU
SEQRES 11 A 278 ILE GLY GLN HIS PHE ARG ALA ASP MSE SER ARG GLN SER
SEQRES 12 A 278 ILE PHE GLY HIS SER MSE GLY GLY HIS GLY ALA MSE THR
SEQRES 13 A 278 ILE ALA LEU LYS ASN PRO GLU ARG PHE LYS SER CYS SER
SEQRES 14 A 278 ALA PHE ALA PRO ILE VAL ALA PRO SER SER ALA ASP TRP
SEQRES 15 A 278 SER GLU PRO ALA LEU GLU LYS TYR LEU GLY ALA ASP ARG
SEQRES 16 A 278 ALA ALA TRP ARG ARG TYR ASP ALA CYS SER LEU VAL GLU
SEQRES 17 A 278 ASP GLY ALA ARG PHE PRO GLU PHE LEU ILE ASP GLN GLY
SEQRES 18 A 278 LYS ALA ASP SER PHE LEU GLU LYS GLY LEU ARG PRO TRP
SEQRES 19 A 278 LEU PHE GLU GLU ALA ILE LYS GLY THR ASP ILE GLY LEU
SEQRES 20 A 278 THR LEU ARG MSE HIS ASP ARG TYR ASP HIS SER TYR TYR
SEQRES 21 A 278 PHE ILE SER THR PHE MSE ASP ASP HIS LEU LYS TRP HIS
SEQRES 22 A 278 ALA GLU ARG LEU GLY
SEQRES 1 B 278 GLY MSE ASN ILE ILE SER GLN ASN THR ALA PHE GLY GLY
SEQRES 2 B 278 MSE GLN GLY VAL PHE SER HIS GLN SER GLU THR LEU LYS
SEQRES 3 B 278 SER GLU MSE THR PHE ALA VAL TYR VAL PRO PRO LYS ALA
SEQRES 4 B 278 ILE HIS GLU PRO CYS PRO VAL VAL TRP TYR LEU SER GLY
SEQRES 5 B 278 LEU THR CYS THR HIS ALA ASN VAL MSE GLU LYS GLY GLU
SEQRES 6 B 278 TYR ARG ARG MSE ALA SER GLU LEU GLY LEU VAL VAL VAL
SEQRES 7 B 278 CYS PRO ASP THR SER PRO ARG GLY ASN ASP VAL PRO ASP
SEQRES 8 B 278 GLU LEU THR ASN TRP GLN MSE GLY LYS GLY ALA GLY PHE
SEQRES 9 B 278 TYR LEU ASP ALA THR GLU GLU PRO TRP SER GLU HIS TYR
SEQRES 10 B 278 GLN MSE TYR SER TYR VAL THR GLU GLU LEU PRO ALA LEU
SEQRES 11 B 278 ILE GLY GLN HIS PHE ARG ALA ASP MSE SER ARG GLN SER
SEQRES 12 B 278 ILE PHE GLY HIS SER MSE GLY GLY HIS GLY ALA MSE THR
SEQRES 13 B 278 ILE ALA LEU LYS ASN PRO GLU ARG PHE LYS SER CYS SER
SEQRES 14 B 278 ALA PHE ALA PRO ILE VAL ALA PRO SER SER ALA ASP TRP
SEQRES 15 B 278 SER GLU PRO ALA LEU GLU LYS TYR LEU GLY ALA ASP ARG
SEQRES 16 B 278 ALA ALA TRP ARG ARG TYR ASP ALA CYS SER LEU VAL GLU
SEQRES 17 B 278 ASP GLY ALA ARG PHE PRO GLU PHE LEU ILE ASP GLN GLY
SEQRES 18 B 278 LYS ALA ASP SER PHE LEU GLU LYS GLY LEU ARG PRO TRP
SEQRES 19 B 278 LEU PHE GLU GLU ALA ILE LYS GLY THR ASP ILE GLY LEU
SEQRES 20 B 278 THR LEU ARG MSE HIS ASP ARG TYR ASP HIS SER TYR TYR
SEQRES 21 B 278 PHE ILE SER THR PHE MSE ASP ASP HIS LEU LYS TRP HIS
SEQRES 22 B 278 ALA GLU ARG LEU GLY
SEQRES 1 C 278 GLY MSE ASN ILE ILE SER GLN ASN THR ALA PHE GLY GLY
SEQRES 2 C 278 MSE GLN GLY VAL PHE SER HIS GLN SER GLU THR LEU LYS
SEQRES 3 C 278 SER GLU MSE THR PHE ALA VAL TYR VAL PRO PRO LYS ALA
SEQRES 4 C 278 ILE HIS GLU PRO CYS PRO VAL VAL TRP TYR LEU SER GLY
SEQRES 5 C 278 LEU THR CYS THR HIS ALA ASN VAL MSE GLU LYS GLY GLU
SEQRES 6 C 278 TYR ARG ARG MSE ALA SER GLU LEU GLY LEU VAL VAL VAL
SEQRES 7 C 278 CYS PRO ASP THR SER PRO ARG GLY ASN ASP VAL PRO ASP
SEQRES 8 C 278 GLU LEU THR ASN TRP GLN MSE GLY LYS GLY ALA GLY PHE
SEQRES 9 C 278 TYR LEU ASP ALA THR GLU GLU PRO TRP SER GLU HIS TYR
SEQRES 10 C 278 GLN MSE TYR SER TYR VAL THR GLU GLU LEU PRO ALA LEU
SEQRES 11 C 278 ILE GLY GLN HIS PHE ARG ALA ASP MSE SER ARG GLN SER
SEQRES 12 C 278 ILE PHE GLY HIS SER MSE GLY GLY HIS GLY ALA MSE THR
SEQRES 13 C 278 ILE ALA LEU LYS ASN PRO GLU ARG PHE LYS SER CYS SER
SEQRES 14 C 278 ALA PHE ALA PRO ILE VAL ALA PRO SER SER ALA ASP TRP
SEQRES 15 C 278 SER GLU PRO ALA LEU GLU LYS TYR LEU GLY ALA ASP ARG
SEQRES 16 C 278 ALA ALA TRP ARG ARG TYR ASP ALA CYS SER LEU VAL GLU
SEQRES 17 C 278 ASP GLY ALA ARG PHE PRO GLU PHE LEU ILE ASP GLN GLY
SEQRES 18 C 278 LYS ALA ASP SER PHE LEU GLU LYS GLY LEU ARG PRO TRP
SEQRES 19 C 278 LEU PHE GLU GLU ALA ILE LYS GLY THR ASP ILE GLY LEU
SEQRES 20 C 278 THR LEU ARG MSE HIS ASP ARG TYR ASP HIS SER TYR TYR
SEQRES 21 C 278 PHE ILE SER THR PHE MSE ASP ASP HIS LEU LYS TRP HIS
SEQRES 22 C 278 ALA GLU ARG LEU GLY
SEQRES 1 E 278 GLY MSE ASN ILE ILE SER GLN ASN THR ALA PHE GLY GLY
SEQRES 2 E 278 MSE GLN GLY VAL PHE SER HIS GLN SER GLU THR LEU LYS
SEQRES 3 E 278 SER GLU MSE THR PHE ALA VAL TYR VAL PRO PRO LYS ALA
SEQRES 4 E 278 ILE HIS GLU PRO CYS PRO VAL VAL TRP TYR LEU SER GLY
SEQRES 5 E 278 LEU THR CYS THR HIS ALA ASN VAL MSE GLU LYS GLY GLU
SEQRES 6 E 278 TYR ARG ARG MSE ALA SER GLU LEU GLY LEU VAL VAL VAL
SEQRES 7 E 278 CYS PRO ASP THR SER PRO ARG GLY ASN ASP VAL PRO ASP
SEQRES 8 E 278 GLU LEU THR ASN TRP GLN MSE GLY LYS GLY ALA GLY PHE
SEQRES 9 E 278 TYR LEU ASP ALA THR GLU GLU PRO TRP SER GLU HIS TYR
SEQRES 10 E 278 GLN MSE TYR SER TYR VAL THR GLU GLU LEU PRO ALA LEU
SEQRES 11 E 278 ILE GLY GLN HIS PHE ARG ALA ASP MSE SER ARG GLN SER
SEQRES 12 E 278 ILE PHE GLY HIS SER MSE GLY GLY HIS GLY ALA MSE THR
SEQRES 13 E 278 ILE ALA LEU LYS ASN PRO GLU ARG PHE LYS SER CYS SER
SEQRES 14 E 278 ALA PHE ALA PRO ILE VAL ALA PRO SER SER ALA ASP TRP
SEQRES 15 E 278 SER GLU PRO ALA LEU GLU LYS TYR LEU GLY ALA ASP ARG
SEQRES 16 E 278 ALA ALA TRP ARG ARG TYR ASP ALA CYS SER LEU VAL GLU
SEQRES 17 E 278 ASP GLY ALA ARG PHE PRO GLU PHE LEU ILE ASP GLN GLY
SEQRES 18 E 278 LYS ALA ASP SER PHE LEU GLU LYS GLY LEU ARG PRO TRP
SEQRES 19 E 278 LEU PHE GLU GLU ALA ILE LYS GLY THR ASP ILE GLY LEU
SEQRES 20 E 278 THR LEU ARG MSE HIS ASP ARG TYR ASP HIS SER TYR TYR
SEQRES 21 E 278 PHE ILE SER THR PHE MSE ASP ASP HIS LEU LYS TRP HIS
SEQRES 22 E 278 ALA GLU ARG LEU GLY
SEQRES 1 D 278 GLY MSE ASN ILE ILE SER GLN ASN THR ALA PHE GLY GLY
SEQRES 2 D 278 MSE GLN GLY VAL PHE SER HIS GLN SER GLU THR LEU LYS
SEQRES 3 D 278 SER GLU MSE THR PHE ALA VAL TYR VAL PRO PRO LYS ALA
SEQRES 4 D 278 ILE HIS GLU PRO CYS PRO VAL VAL TRP TYR LEU SER GLY
SEQRES 5 D 278 LEU THR CYS THR HIS ALA ASN VAL MSE GLU LYS GLY GLU
SEQRES 6 D 278 TYR ARG ARG MSE ALA SER GLU LEU GLY LEU VAL VAL VAL
SEQRES 7 D 278 CYS PRO ASP THR SER PRO ARG GLY ASN ASP VAL PRO ASP
SEQRES 8 D 278 GLU LEU THR ASN TRP GLN MSE GLY LYS GLY ALA GLY PHE
SEQRES 9 D 278 TYR LEU ASP ALA THR GLU GLU PRO TRP SER GLU HIS TYR
SEQRES 10 D 278 GLN MSE TYR SER TYR VAL THR GLU GLU LEU PRO ALA LEU
SEQRES 11 D 278 ILE GLY GLN HIS PHE ARG ALA ASP MSE SER ARG GLN SER
SEQRES 12 D 278 ILE PHE GLY HIS SER MSE GLY GLY HIS GLY ALA MSE THR
SEQRES 13 D 278 ILE ALA LEU LYS ASN PRO GLU ARG PHE LYS SER CYS SER
SEQRES 14 D 278 ALA PHE ALA PRO ILE VAL ALA PRO SER SER ALA ASP TRP
SEQRES 15 D 278 SER GLU PRO ALA LEU GLU LYS TYR LEU GLY ALA ASP ARG
SEQRES 16 D 278 ALA ALA TRP ARG ARG TYR ASP ALA CYS SER LEU VAL GLU
SEQRES 17 D 278 ASP GLY ALA ARG PHE PRO GLU PHE LEU ILE ASP GLN GLY
SEQRES 18 D 278 LYS ALA ASP SER PHE LEU GLU LYS GLY LEU ARG PRO TRP
SEQRES 19 D 278 LEU PHE GLU GLU ALA ILE LYS GLY THR ASP ILE GLY LEU
SEQRES 20 D 278 THR LEU ARG MSE HIS ASP ARG TYR ASP HIS SER TYR TYR
SEQRES 21 D 278 PHE ILE SER THR PHE MSE ASP ASP HIS LEU LYS TRP HIS
SEQRES 22 D 278 ALA GLU ARG LEU GLY
SEQRES 1 F 278 GLY MSE ASN ILE ILE SER GLN ASN THR ALA PHE GLY GLY
SEQRES 2 F 278 MSE GLN GLY VAL PHE SER HIS GLN SER GLU THR LEU LYS
SEQRES 3 F 278 SER GLU MSE THR PHE ALA VAL TYR VAL PRO PRO LYS ALA
SEQRES 4 F 278 ILE HIS GLU PRO CYS PRO VAL VAL TRP TYR LEU SER GLY
SEQRES 5 F 278 LEU THR CYS THR HIS ALA ASN VAL MSE GLU LYS GLY GLU
SEQRES 6 F 278 TYR ARG ARG MSE ALA SER GLU LEU GLY LEU VAL VAL VAL
SEQRES 7 F 278 CYS PRO ASP THR SER PRO ARG GLY ASN ASP VAL PRO ASP
SEQRES 8 F 278 GLU LEU THR ASN TRP GLN MSE GLY LYS GLY ALA GLY PHE
SEQRES 9 F 278 TYR LEU ASP ALA THR GLU GLU PRO TRP SER GLU HIS TYR
SEQRES 10 F 278 GLN MSE TYR SER TYR VAL THR GLU GLU LEU PRO ALA LEU
SEQRES 11 F 278 ILE GLY GLN HIS PHE ARG ALA ASP MSE SER ARG GLN SER
SEQRES 12 F 278 ILE PHE GLY HIS SER MSE GLY GLY HIS GLY ALA MSE THR
SEQRES 13 F 278 ILE ALA LEU LYS ASN PRO GLU ARG PHE LYS SER CYS SER
SEQRES 14 F 278 ALA PHE ALA PRO ILE VAL ALA PRO SER SER ALA ASP TRP
SEQRES 15 F 278 SER GLU PRO ALA LEU GLU LYS TYR LEU GLY ALA ASP ARG
SEQRES 16 F 278 ALA ALA TRP ARG ARG TYR ASP ALA CYS SER LEU VAL GLU
SEQRES 17 F 278 ASP GLY ALA ARG PHE PRO GLU PHE LEU ILE ASP GLN GLY
SEQRES 18 F 278 LYS ALA ASP SER PHE LEU GLU LYS GLY LEU ARG PRO TRP
SEQRES 19 F 278 LEU PHE GLU GLU ALA ILE LYS GLY THR ASP ILE GLY LEU
SEQRES 20 F 278 THR LEU ARG MSE HIS ASP ARG TYR ASP HIS SER TYR TYR
SEQRES 21 F 278 PHE ILE SER THR PHE MSE ASP ASP HIS LEU LYS TRP HIS
SEQRES 22 F 278 ALA GLU ARG LEU GLY
MODRES 3E4D MSE A 1 MET SELENOMETHIONINE
MODRES 3E4D MSE A 13 MET SELENOMETHIONINE
MODRES 3E4D MSE A 28 MET SELENOMETHIONINE
MODRES 3E4D MSE A 60 MET SELENOMETHIONINE
MODRES 3E4D MSE A 68 MET SELENOMETHIONINE
MODRES 3E4D MSE A 97 MET SELENOMETHIONINE
MODRES 3E4D MSE A 118 MET SELENOMETHIONINE
MODRES 3E4D MSE A 138 MET SELENOMETHIONINE
MODRES 3E4D MSE A 148 MET SELENOMETHIONINE
MODRES 3E4D MSE A 154 MET SELENOMETHIONINE
MODRES 3E4D MSE A 250 MET SELENOMETHIONINE
MODRES 3E4D MSE A 265 MET SELENOMETHIONINE
MODRES 3E4D MSE B 1 MET SELENOMETHIONINE
MODRES 3E4D MSE B 13 MET SELENOMETHIONINE
MODRES 3E4D MSE B 28 MET SELENOMETHIONINE
MODRES 3E4D MSE B 60 MET SELENOMETHIONINE
MODRES 3E4D MSE B 68 MET SELENOMETHIONINE
MODRES 3E4D MSE B 97 MET SELENOMETHIONINE
MODRES 3E4D MSE B 118 MET SELENOMETHIONINE
MODRES 3E4D MSE B 138 MET SELENOMETHIONINE
MODRES 3E4D MSE B 148 MET SELENOMETHIONINE
MODRES 3E4D MSE B 154 MET SELENOMETHIONINE
MODRES 3E4D MSE B 250 MET SELENOMETHIONINE
MODRES 3E4D MSE B 265 MET SELENOMETHIONINE
MODRES 3E4D MSE C 1 MET SELENOMETHIONINE
MODRES 3E4D MSE C 13 MET SELENOMETHIONINE
MODRES 3E4D MSE C 28 MET SELENOMETHIONINE
MODRES 3E4D MSE C 60 MET SELENOMETHIONINE
MODRES 3E4D MSE C 68 MET SELENOMETHIONINE
MODRES 3E4D MSE C 97 MET SELENOMETHIONINE
MODRES 3E4D MSE C 118 MET SELENOMETHIONINE
MODRES 3E4D MSE C 138 MET SELENOMETHIONINE
MODRES 3E4D MSE C 148 MET SELENOMETHIONINE
MODRES 3E4D MSE C 154 MET SELENOMETHIONINE
MODRES 3E4D MSE C 250 MET SELENOMETHIONINE
MODRES 3E4D MSE C 265 MET SELENOMETHIONINE
MODRES 3E4D MSE E 1 MET SELENOMETHIONINE
MODRES 3E4D MSE E 13 MET SELENOMETHIONINE
MODRES 3E4D MSE E 28 MET SELENOMETHIONINE
MODRES 3E4D MSE E 60 MET SELENOMETHIONINE
MODRES 3E4D MSE E 68 MET SELENOMETHIONINE
MODRES 3E4D MSE E 97 MET SELENOMETHIONINE
MODRES 3E4D MSE E 118 MET SELENOMETHIONINE
MODRES 3E4D MSE E 138 MET SELENOMETHIONINE
MODRES 3E4D MSE E 148 MET SELENOMETHIONINE
MODRES 3E4D MSE E 154 MET SELENOMETHIONINE
MODRES 3E4D MSE E 250 MET SELENOMETHIONINE
MODRES 3E4D MSE E 265 MET SELENOMETHIONINE
MODRES 3E4D MSE D 1 MET SELENOMETHIONINE
MODRES 3E4D MSE D 13 MET SELENOMETHIONINE
MODRES 3E4D MSE D 28 MET SELENOMETHIONINE
MODRES 3E4D MSE D 60 MET SELENOMETHIONINE
MODRES 3E4D MSE D 68 MET SELENOMETHIONINE
MODRES 3E4D MSE D 97 MET SELENOMETHIONINE
MODRES 3E4D MSE D 118 MET SELENOMETHIONINE
MODRES 3E4D MSE D 138 MET SELENOMETHIONINE
MODRES 3E4D MSE D 148 MET SELENOMETHIONINE
MODRES 3E4D MSE D 154 MET SELENOMETHIONINE
MODRES 3E4D MSE D 250 MET SELENOMETHIONINE
MODRES 3E4D MSE D 265 MET SELENOMETHIONINE
MODRES 3E4D MSE F 1 MET SELENOMETHIONINE
MODRES 3E4D MSE F 13 MET SELENOMETHIONINE
MODRES 3E4D MSE F 28 MET SELENOMETHIONINE
MODRES 3E4D MSE F 60 MET SELENOMETHIONINE
MODRES 3E4D MSE F 68 MET SELENOMETHIONINE
MODRES 3E4D MSE F 97 MET SELENOMETHIONINE
MODRES 3E4D MSE F 118 MET SELENOMETHIONINE
MODRES 3E4D MSE F 138 MET SELENOMETHIONINE
MODRES 3E4D MSE F 148 MET SELENOMETHIONINE
MODRES 3E4D MSE F 154 MET SELENOMETHIONINE
MODRES 3E4D MSE F 250 MET SELENOMETHIONINE
MODRES 3E4D MSE F 265 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 13 13
HET MSE A 28 8
HET MSE A 60 8
HET MSE A 68 8
HET MSE A 97 8
HET MSE A 118 8
HET MSE A 138 8
HET MSE A 148 8
HET MSE A 154 8
HET MSE A 250 8
HET MSE A 265 8
HET MSE B 1 8
HET MSE B 13 8
HET MSE B 28 8
HET MSE B 60 8
HET MSE B 68 8
HET MSE B 97 8
HET MSE B 118 8
HET MSE B 138 8
HET MSE B 148 8
HET MSE B 154 8
HET MSE B 250 8
HET MSE B 265 8
HET MSE C 1 8
HET MSE C 13 8
HET MSE C 28 8
HET MSE C 60 8
HET MSE C 68 8
HET MSE C 97 8
HET MSE C 118 8
HET MSE C 138 8
HET MSE C 148 8
HET MSE C 154 8
HET MSE C 250 8
HET MSE C 265 8
HET MSE E 1 8
HET MSE E 13 8
HET MSE E 28 8
HET MSE E 60 8
HET MSE E 68 8
HET MSE E 97 8
HET MSE E 118 8
HET MSE E 138 8
HET MSE E 148 8
HET MSE E 154 8
HET MSE E 250 8
HET MSE E 265 8
HET MSE D 1 8
HET MSE D 13 13
HET MSE D 28 8
HET MSE D 60 8
HET MSE D 68 8
HET MSE D 97 8
HET MSE D 118 8
HET MSE D 138 8
HET MSE D 148 8
HET MSE D 154 8
HET MSE D 250 8
HET MSE D 265 8
HET MSE F 1 8
HET MSE F 13 8
HET MSE F 28 8
HET MSE F 60 8
HET MSE F 68 8
HET MSE F 97 8
HET MSE F 118 8
HET MSE F 138 8
HET MSE F 148 8
HET MSE F 154 8
HET MSE F 250 8
HET MSE F 265 8
HET MG A 278 1
HET CL A 279 1
HET CL A 280 1
HET MG B 278 1
HET CL B 279 1
HET CL B 280 1
HET MG C 278 1
HET CL C 279 1
HET CL C 280 1
HET MG E 278 1
HET CL E 279 1
HET CL E 280 1
HET MG D 278 1
HET CL D 279 1
HET CL D 280 1
HET MG F 278 1
HET CL F 279 1
HET CL F 280 1
HETNAM MSE SELENOMETHIONINE
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 72(C5 H11 N O2 SE)
FORMUL 7 MG 6(MG 2+)
FORMUL 8 CL 12(CL 1-)
FORMUL 25 HOH *670(H2 O)
HELIX 1 1 PRO A 35 HIS A 40 5 6
HELIX 2 2 HIS A 56 GLY A 63 1 8
HELIX 3 3 TYR A 65 GLY A 73 1 9
HELIX 4 4 GLN A 117 GLU A 124 1 8
HELIX 5 5 GLU A 124 PHE A 134 1 11
HELIX 6 6 SER A 147 ASN A 160 1 14
HELIX 7 7 ALA A 175 ALA A 179 5 5
HELIX 8 8 SER A 182 GLY A 191 1 10
HELIX 9 9 ASP A 193 TYR A 200 5 8
HELIX 10 10 ASP A 201 ASP A 208 1 8
HELIX 11 11 PHE A 225 LEU A 230 1 6
HELIX 12 12 PRO A 232 LYS A 240 1 9
HELIX 13 13 SER A 257 GLY A 277 1 21
HELIX 14 14 PRO B 35 HIS B 40 5 6
HELIX 15 15 HIS B 56 GLY B 63 1 8
HELIX 16 16 TYR B 65 GLY B 73 1 9
HELIX 17 17 PRO B 111 HIS B 115 5 5
HELIX 18 18 GLN B 117 GLU B 124 1 8
HELIX 19 19 GLU B 124 PHE B 134 1 11
HELIX 20 20 SER B 147 ASN B 160 1 14
HELIX 21 21 ALA B 175 ALA B 179 5 5
HELIX 22 22 SER B 182 GLY B 191 1 10
HELIX 23 23 ASP B 193 TYR B 200 5 8
HELIX 24 24 ASP B 201 ASP B 208 1 8
HELIX 25 25 PHE B 225 LEU B 230 1 6
HELIX 26 26 PRO B 232 ILE B 239 1 8
HELIX 27 27 SER B 257 GLY B 277 1 21
HELIX 28 28 PRO C 36 GLU C 41 1 6
HELIX 29 29 HIS C 56 GLY C 63 1 8
HELIX 30 30 TYR C 65 GLY C 73 1 9
HELIX 31 31 PRO C 111 HIS C 115 5 5
HELIX 32 32 GLN C 117 GLU C 124 1 8
HELIX 33 33 GLU C 124 PHE C 134 1 11
HELIX 34 34 SER C 147 ASN C 160 1 14
HELIX 35 35 SER C 182 GLY C 191 1 10
HELIX 36 36 ASP C 193 TYR C 200 5 8
HELIX 37 37 ASP C 201 ASP C 208 1 8
HELIX 38 38 PHE C 225 LEU C 230 1 6
HELIX 39 39 PRO C 232 ILE C 239 1 8
HELIX 40 40 SER C 257 GLY C 277 1 21
HELIX 41 41 PRO E 35 HIS E 40 5 6
HELIX 42 42 HIS E 56 GLY E 63 1 8
HELIX 43 43 TYR E 65 GLY E 73 1 9
HELIX 44 44 GLN E 117 GLU E 124 1 8
HELIX 45 45 GLU E 124 PHE E 134 1 11
HELIX 46 46 SER E 147 ASN E 160 1 14
HELIX 47 47 PRO E 161 PHE E 164 5 4
HELIX 48 48 SER E 182 GLY E 191 1 10
HELIX 49 49 ASP E 193 TYR E 200 5 8
HELIX 50 50 ASP E 201 ASP E 208 1 8
HELIX 51 51 PHE E 225 LEU E 230 1 6
HELIX 52 52 PRO E 232 ILE E 239 1 8
HELIX 53 53 SER E 257 GLY E 277 1 21
HELIX 54 54 PRO D 35 HIS D 40 5 6
HELIX 55 55 HIS D 56 GLY D 63 1 8
HELIX 56 56 TYR D 65 GLY D 73 1 9
HELIX 57 57 PRO D 111 HIS D 115 5 5
HELIX 58 58 GLN D 117 GLU D 124 1 8
HELIX 59 59 GLU D 124 PHE D 134 1 11
HELIX 60 60 SER D 147 ASN D 160 1 14
HELIX 61 61 ALA D 175 ALA D 179 5 5
HELIX 62 62 SER D 182 GLY D 191 1 10
HELIX 63 63 TRP D 197 TYR D 200 5 4
HELIX 64 64 ASP D 201 ASP D 208 1 8
HELIX 65 65 PHE D 225 LEU D 230 1 6
HELIX 66 66 PRO D 232 ILE D 239 1 8
HELIX 67 67 SER D 257 GLY D 277 1 21
HELIX 68 68 PRO F 35 HIS F 40 5 6
HELIX 69 69 HIS F 56 GLY F 63 1 8
HELIX 70 70 TYR F 65 GLY F 73 1 9
HELIX 71 71 PRO F 111 HIS F 115 5 5
HELIX 72 72 GLN F 117 GLU F 124 1 8
HELIX 73 73 GLU F 124 PHE F 134 1 11
HELIX 74 74 SER F 147 ASN F 160 1 14
HELIX 75 75 SER F 182 GLY F 191 1 10
HELIX 76 76 ALA F 195 TYR F 200 5 6
HELIX 77 77 ASP F 201 ASP F 208 1 8
HELIX 78 78 PHE F 225 LEU F 230 1 6
HELIX 79 79 PRO F 232 ILE F 239 1 8
HELIX 80 80 SER F 257 GLY F 277 1 21
SHEET 1 A 9 ASN A 2 ALA A 9 0
SHEET 2 A 9 GLY A 12 SER A 21 -1 O SER A 18 N ASN A 2
SHEET 3 A 9 SER A 26 VAL A 34 -1 O SER A 26 N SER A 21
SHEET 4 A 9 VAL A 75 CYS A 78 -1 O CYS A 78 N ALA A 31
SHEET 5 A 9 CYS A 43 LEU A 49 1 N VAL A 46 O VAL A 75
SHEET 6 A 9 ALA A 136 HIS A 146 1 O PHE A 144 N TRP A 47
SHEET 7 A 9 CYS A 167 PHE A 170 1 O PHE A 170 N GLY A 145
SHEET 8 A 9 GLU A 214 GLY A 220 1 O ASP A 218 N ALA A 169
SHEET 9 A 9 GLY A 245 HIS A 251 1 O HIS A 251 N GLN A 219
SHEET 1 B 9 ASN B 2 ALA B 9 0
SHEET 2 B 9 GLY B 12 SER B 21 -1 O GLN B 14 N ASN B 7
SHEET 3 B 9 SER B 26 VAL B 34 -1 O SER B 26 N SER B 21
SHEET 4 B 9 VAL B 75 CYS B 78 -1 O CYS B 78 N ALA B 31
SHEET 5 B 9 CYS B 43 LEU B 49 1 N TYR B 48 O VAL B 77
SHEET 6 B 9 ALA B 136 HIS B 146 1 O PHE B 144 N TRP B 47
SHEET 7 B 9 CYS B 167 PHE B 170 1 O PHE B 170 N GLY B 145
SHEET 8 B 9 GLU B 214 GLY B 220 1 O ASP B 218 N ALA B 169
SHEET 9 B 9 GLY B 245 HIS B 251 1 O ARG B 249 N ILE B 217
SHEET 1 C18 GLY C 245 HIS C 251 0
SHEET 2 C18 GLU C 214 GLY C 220 1 N ILE C 217 O THR C 247
SHEET 3 C18 PHE C 164 PHE C 170 1 N ALA C 169 O ASP C 218
SHEET 4 C18 ALA C 136 HIS C 146 1 N GLN C 141 O LYS C 165
SHEET 5 C18 CYS C 43 LEU C 49 1 N CYS C 43 O ASP C 137
SHEET 6 C18 VAL C 75 CYS C 78 1 O VAL C 77 N TYR C 48
SHEET 7 C18 SER C 26 VAL C 34 -1 N TYR C 33 O VAL C 76
SHEET 8 C18 GLY C 12 SER C 21 -1 N SER C 21 O SER C 26
SHEET 9 C18 MSE C 1 ALA C 9 -1 N ASN C 7 O GLN C 14
SHEET 10 C18 MSE E 1 ALA E 9 -1 O ILE E 3 N MSE C 1
SHEET 11 C18 GLY E 12 SER E 21 -1 O SER E 18 N ASN E 2
SHEET 12 C18 SER E 26 VAL E 34 -1 O VAL E 34 N MSE E 13
SHEET 13 C18 VAL E 75 CYS E 78 -1 O CYS E 78 N ALA E 31
SHEET 14 C18 CYS E 43 LEU E 49 1 N VAL E 46 O VAL E 75
SHEET 15 C18 ALA E 136 HIS E 146 1 O ASP E 137 N CYS E 43
SHEET 16 C18 CYS E 167 PHE E 170 1 O PHE E 170 N GLY E 145
SHEET 17 C18 GLU E 214 GLY E 220 1 O ASP E 218 N ALA E 169
SHEET 18 C18 GLY E 245 HIS E 251 1 O HIS E 251 N GLN E 219
SHEET 1 D 6 ASN D 2 ALA D 9 0
SHEET 2 D 6 GLY D 12 SER D 21 -1 O GLN D 14 N ASN D 7
SHEET 3 D 6 SER D 26 VAL D 34 -1 O MSE D 28 N HIS D 19
SHEET 4 D 6 VAL D 75 CYS D 78 -1 O CYS D 78 N ALA D 31
SHEET 5 D 6 CYS D 43 LEU D 49 1 N PRO D 44 O VAL D 75
SHEET 6 D 6 ALA D 136 GLY D 145 1 O PHE D 144 N TRP D 47
SHEET 1 E 3 SER D 168 PHE D 170 0
SHEET 2 E 3 GLU D 214 GLY D 220 1 O ASP D 218 N ALA D 169
SHEET 3 E 3 GLY D 245 HIS D 251 1 O HIS D 251 N GLN D 219
SHEET 1 F 9 ASN F 2 ALA F 9 0
SHEET 2 F 9 GLY F 12 SER F 21 -1 O SER F 18 N ASN F 2
SHEET 3 F 9 SER F 26 VAL F 34 -1 O PHE F 30 N PHE F 17
SHEET 4 F 9 VAL F 75 CYS F 78 -1 O CYS F 78 N ALA F 31
SHEET 5 F 9 CYS F 43 LEU F 49 1 N TYR F 48 O VAL F 77
SHEET 6 F 9 ALA F 136 GLY F 145 1 O PHE F 144 N TRP F 47
SHEET 7 F 9 PHE F 164 PHE F 170 1 O PHE F 170 N GLY F 145
SHEET 8 F 9 GLU F 214 GLY F 220 1 O ASP F 218 N ALA F 169
SHEET 9 F 9 GLY F 245 HIS F 251 1 O THR F 247 N ILE F 217
LINK C GLY A 0 N MSE A 1 1555 1555 1.34
LINK C MSE A 1 N ASN A 2 1555 1555 1.33
LINK C GLY A 12 N MSE A 13 1555 1555 1.33
LINK C MSE A 13 N GLN A 14 1555 1555 1.33
LINK C GLU A 27 N MSE A 28 1555 1555 1.33
LINK C MSE A 28 N THR A 29 1555 1555 1.33
LINK C VAL A 59 N MSE A 60 1555 1555 1.33
LINK C MSE A 60 N GLU A 61 1555 1555 1.33
LINK C ARG A 67 N MSE A 68 1555 1555 1.34
LINK C MSE A 68 N ALA A 69 1555 1555 1.34
LINK C GLN A 96 N MSE A 97 1555 1555 1.33
LINK C MSE A 97 N GLY A 98 1555 1555 1.32
LINK C GLN A 117 N MSE A 118 1555 1555 1.33
LINK C MSE A 118 N TYR A 119 1555 1555 1.33
LINK C ASP A 137 N MSE A 138 1555 1555 1.33
LINK C MSE A 138 N SER A 139 1555 1555 1.34
LINK C SER A 147 N MSE A 148 1555 1555 1.34
LINK C MSE A 148 N GLY A 149 1555 1555 1.33
LINK C ALA A 153 N MSE A 154 1555 1555 1.33
LINK C MSE A 154 N THR A 155 1555 1555 1.33
LINK C ARG A 249 N MSE A 250 1555 1555 1.32
LINK C MSE A 250 N HIS A 251 1555 1555 1.33
LINK C PHE A 264 N MSE A 265 1555 1555 1.33
LINK C MSE A 265 N ASP A 266 1555 1555 1.34
LINK C GLY B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N ASN B 2 1555 1555 1.33
LINK C GLY B 12 N MSE B 13 1555 1555 1.33
LINK C MSE B 13 N GLN B 14 1555 1555 1.33
LINK C GLU B 27 N MSE B 28 1555 1555 1.33
LINK C MSE B 28 N THR B 29 1555 1555 1.33
LINK C VAL B 59 N MSE B 60 1555 1555 1.33
LINK C MSE B 60 N GLU B 61 1555 1555 1.32
LINK C ARG B 67 N MSE B 68 1555 1555 1.33
LINK C MSE B 68 N ALA B 69 1555 1555 1.34
LINK C GLN B 96 N MSE B 97 1555 1555 1.34
LINK C MSE B 97 N GLY B 98 1555 1555 1.33
LINK C GLN B 117 N MSE B 118 1555 1555 1.33
LINK C MSE B 118 N TYR B 119 1555 1555 1.33
LINK C ASP B 137 N MSE B 138 1555 1555 1.33
LINK C MSE B 138 N SER B 139 1555 1555 1.33
LINK C SER B 147 N MSE B 148 1555 1555 1.33
LINK C MSE B 148 N GLY B 149 1555 1555 1.33
LINK C ALA B 153 N MSE B 154 1555 1555 1.33
LINK C MSE B 154 N THR B 155 1555 1555 1.33
LINK C ARG B 249 N MSE B 250 1555 1555 1.34
LINK C MSE B 250 N HIS B 251 1555 1555 1.33
LINK C PHE B 264 N MSE B 265 1555 1555 1.33
LINK C MSE B 265 N ASP B 266 1555 1555 1.34
LINK C GLY C 0 N MSE C 1 1555 1555 1.33
LINK C MSE C 1 N ASN C 2 1555 1555 1.32
LINK C GLY C 12 N MSE C 13 1555 1555 1.33
LINK C MSE C 13 N GLN C 14 1555 1555 1.33
LINK C GLU C 27 N MSE C 28 1555 1555 1.33
LINK C MSE C 28 N THR C 29 1555 1555 1.33
LINK C VAL C 59 N MSE C 60 1555 1555 1.34
LINK C MSE C 60 N GLU C 61 1555 1555 1.33
LINK C ARG C 67 N MSE C 68 1555 1555 1.33
LINK C MSE C 68 N ALA C 69 1555 1555 1.33
LINK C GLN C 96 N MSE C 97 1555 1555 1.34
LINK C MSE C 97 N GLY C 98 1555 1555 1.33
LINK C GLN C 117 N MSE C 118 1555 1555 1.34
LINK C MSE C 118 N TYR C 119 1555 1555 1.34
LINK C ASP C 137 N MSE C 138 1555 1555 1.32
LINK C MSE C 138 N SER C 139 1555 1555 1.34
LINK C SER C 147 N MSE C 148 1555 1555 1.34
LINK C MSE C 148 N GLY C 149 1555 1555 1.33
LINK C ALA C 153 N MSE C 154 1555 1555 1.33
LINK C MSE C 154 N THR C 155 1555 1555 1.33
LINK C ARG C 249 N MSE C 250 1555 1555 1.33
LINK C MSE C 250 N HIS C 251 1555 1555 1.33
LINK C PHE C 264 N MSE C 265 1555 1555 1.33
LINK C MSE C 265 N ASP C 266 1555 1555 1.33
LINK C GLY E 0 N MSE E 1 1555 1555 1.33
LINK C MSE E 1 N ASN E 2 1555 1555 1.33
LINK C GLY E 12 N MSE E 13 1555 1555 1.33
LINK C MSE E 13 N GLN E 14 1555 1555 1.33
LINK C GLU E 27 N MSE E 28 1555 1555 1.33
LINK C MSE E 28 N THR E 29 1555 1555 1.33
LINK C VAL E 59 N MSE E 60 1555 1555 1.33
LINK C MSE E 60 N GLU E 61 1555 1555 1.33
LINK C ARG E 67 N MSE E 68 1555 1555 1.33
LINK C MSE E 68 N ALA E 69 1555 1555 1.34
LINK C GLN E 96 N MSE E 97 1555 1555 1.33
LINK C MSE E 97 N GLY E 98 1555 1555 1.33
LINK C GLN E 117 N MSE E 118 1555 1555 1.33
LINK C MSE E 118 N TYR E 119 1555 1555 1.34
LINK C ASP E 137 N MSE E 138 1555 1555 1.33
LINK C MSE E 138 N SER E 139 1555 1555 1.33
LINK C SER E 147 N MSE E 148 1555 1555 1.35
LINK C MSE E 148 N GLY E 149 1555 1555 1.33
LINK C ALA E 153 N MSE E 154 1555 1555 1.33
LINK C MSE E 154 N THR E 155 1555 1555 1.34
LINK C ARG E 249 N MSE E 250 1555 1555 1.33
LINK C MSE E 250 N HIS E 251 1555 1555 1.33
LINK C PHE E 264 N MSE E 265 1555 1555 1.33
LINK C MSE E 265 N ASP E 266 1555 1555 1.33
LINK C MSE D 1 N ASN D 2 1555 1555 1.33
LINK C GLY D 12 N MSE D 13 1555 1555 1.33
LINK C MSE D 13 N GLN D 14 1555 1555 1.33
LINK C GLU D 27 N MSE D 28 1555 1555 1.33
LINK C MSE D 28 N THR D 29 1555 1555 1.33
LINK C VAL D 59 N MSE D 60 1555 1555 1.33
LINK C MSE D 60 N GLU D 61 1555 1555 1.33
LINK C ARG D 67 N MSE D 68 1555 1555 1.33
LINK C MSE D 68 N ALA D 69 1555 1555 1.34
LINK C GLN D 96 N MSE D 97 1555 1555 1.33
LINK C MSE D 97 N GLY D 98 1555 1555 1.33
LINK C GLN D 117 N MSE D 118 1555 1555 1.33
LINK C MSE D 118 N TYR D 119 1555 1555 1.33
LINK C ASP D 137 N MSE D 138 1555 1555 1.33
LINK C MSE D 138 N SER D 139 1555 1555 1.33
LINK C SER D 147 N MSE D 148 1555 1555 1.34
LINK C MSE D 148 N GLY D 149 1555 1555 1.33
LINK C ALA D 153 N MSE D 154 1555 1555 1.33
LINK C MSE D 154 N THR D 155 1555 1555 1.33
LINK C ARG D 249 N MSE D 250 1555 1555 1.33
LINK C MSE D 250 N HIS D 251 1555 1555 1.33
LINK C PHE D 264 N MSE D 265 1555 1555 1.33
LINK C MSE D 265 N ASP D 266 1555 1555 1.34
LINK C MSE F 1 N ASN F 2 1555 1555 1.33
LINK C GLY F 12 N MSE F 13 1555 1555 1.32
LINK C MSE F 13 N GLN F 14 1555 1555 1.33
LINK C GLU F 27 N MSE F 28 1555 1555 1.33
LINK C MSE F 28 N THR F 29 1555 1555 1.33
LINK C VAL F 59 N MSE F 60 1555 1555 1.34
LINK C MSE F 60 N GLU F 61 1555 1555 1.33
LINK C ARG F 67 N MSE F 68 1555 1555 1.33
LINK C MSE F 68 N ALA F 69 1555 1555 1.33
LINK C GLN F 96 N MSE F 97 1555 1555 1.34
LINK C MSE F 97 N GLY F 98 1555 1555 1.33
LINK C GLN F 117 N MSE F 118 1555 1555 1.34
LINK C MSE F 118 N TYR F 119 1555 1555 1.33
LINK C ASP F 137 N MSE F 138 1555 1555 1.33
LINK C MSE F 138 N SER F 139 1555 1555 1.34
LINK C SER F 147 N MSE F 148 1555 1555 1.33
LINK C MSE F 148 N GLY F 149 1555 1555 1.33
LINK C ALA F 153 N MSE F 154 1555 1555 1.33
LINK C MSE F 154 N THR F 155 1555 1555 1.33
LINK C ARG F 249 N MSE F 250 1555 1555 1.33
LINK C MSE F 250 N HIS F 251 1555 1555 1.33
LINK C PHE F 264 N MSE F 265 1555 1555 1.34
LINK C MSE F 265 N ASP F 266 1555 1555 1.33
LINK O GLU A 91 MG MG A 278 1555 1555 2.31
LINK O ASN A 94 MG MG A 278 1555 1555 2.23
LINK O MSE A 97 MG MG A 278 1555 1555 2.10
LINK O GLU B 91 MG MG B 278 1555 1555 2.42
LINK O ASN B 94 MG MG B 278 1555 1555 2.31
LINK O MSE B 97 MG MG B 278 1555 1555 2.19
LINK O GLU C 91 MG MG C 278 1555 1555 2.23
LINK O ASN C 94 MG MG C 278 1555 1555 2.18
LINK O MSE C 97 MG MG C 278 1555 1555 2.23
LINK O ASN E 94 MG MG E 278 1555 1555 2.20
LINK O MSE E 97 MG MG E 278 1555 1555 2.11
LINK O GLU D 91 MG MG D 278 1555 1555 2.33
LINK O ASN D 94 MG MG D 278 1555 1555 2.14
LINK O MSE D 97 MG MG D 278 1555 1555 2.18
LINK O ASN F 94 MG MG F 278 1555 1555 2.33
LINK O MSE F 97 MG MG F 278 1555 1555 2.19
LINK MG MG A 278 O HOH A 368 1555 1555 2.20
LINK MG MG B 278 O HOH B 292 1555 1555 1.98
LINK MG MG C 278 O HOH C 405 1555 1555 2.44
LINK MG MG E 278 O HOH E 358 1555 1555 2.50
LINK MG MG D 278 O HOH D 352 1555 1555 2.37
CISPEP 1 GLU A 110 PRO A 111 0 -1.34
CISPEP 2 GLU B 110 PRO B 111 0 -2.96
CISPEP 3 GLU C 110 PRO C 111 0 -4.14
CISPEP 4 GLU E 110 PRO E 111 0 3.84
CISPEP 5 GLU D 110 PRO D 111 0 -1.49
CISPEP 6 GLU F 110 PRO F 111 0 -4.80
SITE 1 AC1 4 ASP A 90 GLU A 91 ASN A 94 HOH A 368
SITE 1 AC2 2 LEU A 52 SER A 147
SITE 1 AC3 3 SER A 224 ASP A 255 HIS A 256
SITE 1 AC4 4 ASP B 90 GLU B 91 ASN B 94 HOH B 292
SITE 1 AC5 3 LEU B 52 SER B 147 HOH B 304
SITE 1 AC6 4 SER B 224 ASP B 255 HIS B 256 HOH B 281
SITE 1 AC7 4 ASP C 90 GLU C 91 ASN C 94 HOH C 405
SITE 1 AC8 4 ASP E 90 GLU E 91 ASN E 94 HOH E 358
SITE 1 AC9 3 LEU E 52 SER E 147 HOH E 316
SITE 1 BC1 2 SER E 224 HIS E 256
SITE 1 BC2 4 ASP D 90 GLU D 91 ASN D 94 HOH D 352
SITE 1 BC3 3 LEU D 52 SER D 147 HOH D 354
SITE 1 BC4 3 ASP F 90 GLU F 91 ASN F 94
SITE 1 BC5 3 LEU F 52 SER F 147 HOH F 330
SITE 1 BC6 3 SER F 224 ASP F 255 HIS F 256
SITE 1 BC7 2 LEU C 52 SER C 147
SITE 1 BC8 4 SER C 224 ASP C 255 HIS C 256 HOH C 282
SITE 1 BC9 4 SER D 224 ASP D 255 HIS D 256 HOH D 355
CRYST1 68.433 68.949 95.648 92.41 99.79 98.47 P 1 6
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 0.014613 0.002177 0.002678 0.00000
SCALE2 0.000000 0.014664 0.001012 0.00000
SCALE3 0.000000 0.000000 0.010635 0.00000
TER 2210 GLY A 277
TER 4415 GLY B 277
TER 6620 GLY C 277
TER 8825 GLY E 277
TER 11031 GLY D 277
TER 13232 GLY F 277
MASTER 426 0 90 80 54 0 18 613914 6 749 132
END |