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HEADER HYDROLASE 27-JUL-20 6ZVV
TITLE X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE HALOTAG7-P174W LABELED
TITLE 2 WITH A CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 GENE: DHAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HALOALKANE DEHALOGENASE, HALO, TAG, HALOTAG7, SELF-LABELING PROTEIN,
KEYWDS 2 FLUOROPHORE, TETRAMETHYLRHODAMINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.TARNAWSKI,M.FREI,J.HIBLOT,K.JOHNSSON
REVDAT 1 04-AUG-21 6ZVV 0
JRNL AUTH M.TARNAWSKI,M.FREI,J.HIBLOT,K.JOHNSSON
JRNL TITL X-RAY STRUCTURE OF THE HALOALKANE DEHALOGENASE
JRNL TITL 2 HALOTAG7-P174W LABELED WITH A
JRNL TITL 3 CHLOROALKANE-TETRAMETHYLRHODAMINE FLUOROPHORE SUBSTRATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 230042
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11503
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 42.2900 - 4.3500 0.97 7568 399 0.1929 0.2056
REMARK 3 2 4.3500 - 3.4500 0.98 7450 393 0.1898 0.2209
REMARK 3 3 3.4500 - 3.0200 0.98 7401 389 0.1986 0.2113
REMARK 3 4 3.0200 - 2.7400 0.98 7391 389 0.2035 0.2239
REMARK 3 5 2.7400 - 2.5400 0.98 7362 388 0.2086 0.2301
REMARK 3 6 2.5400 - 2.3900 0.97 7295 384 0.1991 0.2179
REMARK 3 7 2.3900 - 2.2700 0.98 7338 386 0.1998 0.2225
REMARK 3 8 2.2700 - 2.1700 0.98 7389 388 0.1983 0.2422
REMARK 3 9 2.1700 - 2.0900 0.99 7335 386 0.2004 0.2209
REMARK 3 10 2.0900 - 2.0200 0.98 7366 388 0.1979 0.2150
REMARK 3 11 2.0200 - 1.9600 0.99 7319 385 0.2025 0.2349
REMARK 3 12 1.9600 - 1.9000 0.99 7405 390 0.1996 0.2131
REMARK 3 13 1.9000 - 1.8500 0.99 7409 390 0.1981 0.2248
REMARK 3 14 1.8500 - 1.8000 0.99 7385 389 0.1997 0.2524
REMARK 3 15 1.8000 - 1.7600 0.99 7318 385 0.1969 0.2256
REMARK 3 16 1.7600 - 1.7300 0.99 7422 390 0.1964 0.2271
REMARK 3 17 1.7300 - 1.6900 0.99 7416 391 0.1940 0.2337
REMARK 3 18 1.6900 - 1.6600 0.99 7374 388 0.1943 0.2279
REMARK 3 19 1.6600 - 1.6300 0.99 7383 389 0.1958 0.2438
REMARK 3 20 1.6300 - 1.6000 1.00 7441 391 0.1962 0.2160
REMARK 3 21 1.6000 - 1.5800 1.00 7448 392 0.1975 0.2395
REMARK 3 22 1.5800 - 1.5500 1.00 7380 389 0.2016 0.2456
REMARK 3 23 1.5500 - 1.5300 1.00 7417 390 0.1962 0.2213
REMARK 3 24 1.5300 - 1.5100 1.00 7435 391 0.1951 0.2375
REMARK 3 25 1.5100 - 1.4900 1.00 7454 393 0.2052 0.2478
REMARK 3 26 1.4900 - 1.4700 0.99 7322 385 0.2112 0.2486
REMARK 3 27 1.4700 - 1.4500 0.97 7238 381 0.2228 0.2636
REMARK 3 28 1.4500 - 1.4300 0.92 6783 357 0.2321 0.2753
REMARK 3 29 1.4300 - 1.4200 0.86 6383 336 0.2415 0.2624
REMARK 3 30 1.4200 - 1.4000 0.79 5912 311 0.2471 0.2716
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.154
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.174
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.16
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 9949
REMARK 3 ANGLE : 0.884 13606
REMARK 3 CHIRALITY : 0.081 1413
REMARK 3 PLANARITY : 0.007 1904
REMARK 3 DIHEDRAL : 8.630 4849
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6ZVV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-20.
REMARK 100 THE DEPOSITION ID IS D_1292110334.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000030
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 230075
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
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 (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.160
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.46
REMARK 200 R MERGE FOR SHELL (I) : 0.28900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.180
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6Y7A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 20% (M/V) PEG
REMARK 280 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 26.51500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 GLU B 294
REMARK 465 ILE B 295
REMARK 465 ILE D 295
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 9 56.91 -91.13
REMARK 500 PRO A 42 47.29 -106.30
REMARK 500 THR A 43 -160.42 -101.57
REMARK 500 GLU A 98 -91.14 -106.21
REMARK 500 ASP A 106 -133.06 52.99
REMARK 500 GLU A 130 60.87 39.89
REMARK 500 ARG A 153 35.68 -85.18
REMARK 500 VAL A 245 -69.16 -130.21
REMARK 500 LEU A 271 -101.08 -117.82
REMARK 500 ASP B 31 -168.31 -101.94
REMARK 500 PRO B 42 46.85 -107.27
REMARK 500 THR B 43 -160.73 -101.96
REMARK 500 GLU B 98 -92.78 -107.89
REMARK 500 ASP B 106 -132.42 50.93
REMARK 500 ARG B 153 44.36 -87.46
REMARK 500 VAL B 245 -70.07 -127.78
REMARK 500 LEU B 271 -104.19 -121.47
REMARK 500 PRO C 42 45.43 -109.37
REMARK 500 GLU C 98 -93.99 -106.38
REMARK 500 ASP C 106 -131.23 52.92
REMARK 500 ARG C 153 42.76 -87.34
REMARK 500 ASP C 156 -63.53 -99.77
REMARK 500 VAL C 245 -70.59 -131.27
REMARK 500 LEU C 271 -99.01 -120.03
REMARK 500 PRO D 42 50.58 -107.71
REMARK 500 THR D 43 -160.92 -102.54
REMARK 500 GLU D 98 -93.40 -104.55
REMARK 500 ASP D 106 -132.02 55.93
REMARK 500 ARG D 153 36.59 -90.40
REMARK 500 VAL D 245 -72.68 -130.82
REMARK 500 LEU D 271 -100.90 -120.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 790 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A 791 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A 792 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 793 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH B 756 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B 757 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH B 758 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH B 759 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH C 739 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH C 740 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH C 741 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH C 742 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH C 743 DISTANCE = 6.61 ANGSTROMS
REMARK 525 HOH C 744 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH C 745 DISTANCE = 6.93 ANGSTROMS
REMARK 525 HOH C 746 DISTANCE = 7.20 ANGSTROMS
REMARK 525 HOH C 747 DISTANCE = 7.90 ANGSTROMS
REMARK 525 HOH C 748 DISTANCE = 7.97 ANGSTROMS
REMARK 525 HOH D 672 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH D 673 DISTANCE = 6.09 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 303 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 73 OD2
REMARK 620 2 HOH B 401 O 80.8
REMARK 620 3 HOH B 430 O 70.5 130.4
REMARK 620 4 HOH B 623 O 91.4 142.2 79.3
REMARK 620 5 HOH B 657 O 83.9 66.8 70.6 149.4
REMARK 620 6 HOH B 717 O 163.0 92.2 124.6 84.7 107.7
REMARK 620 7 HOH D 619 O 130.1 111.7 65.2 101.6 60.9 66.9
REMARK 620 N 1 2 3 4 5 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6ZVU RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVX RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVY RELATED DB: PDB
REMARK 900 RELATED ID: 6ZVW RELATED DB: PDB
DBREF 6ZVV A 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 6ZVV B 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 6ZVV C 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
DBREF 6ZVV D 4 293 UNP P0A3G3 DHAA_RHOSO 4 293
SEQADV 6ZVV GLY A 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVV VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 6ZVV THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 6ZVV GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 6ZVV PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 6ZVV MET A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 6ZVV PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 6ZVV THR A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 6ZVV LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 6ZVV VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 6ZVV THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 6ZVV TRP A 174 UNP P0A3G3 PRO 174 ENGINEERED MUTATION
SEQADV 6ZVV MET A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 6ZVV GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 6ZVV ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 6ZVV GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 6ZVV ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 6ZVV LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 6ZVV ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 6ZVV ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 6ZVV LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 6ZVV SER A 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 6ZVV THR A 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 6ZVV GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVV ILE A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVV GLY B 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVV VAL B 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 6ZVV THR B 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 6ZVV GLY B 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 6ZVV PHE B 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 6ZVV MET B 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 6ZVV PHE B 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 6ZVV THR B 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 6ZVV LYS B 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 6ZVV VAL B 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 6ZVV THR B 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 6ZVV TRP B 174 UNP P0A3G3 PRO 174 ENGINEERED MUTATION
SEQADV 6ZVV MET B 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 6ZVV GLY B 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 6ZVV ASN B 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 6ZVV GLU B 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 6ZVV ASP B 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 6ZVV LYS B 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 6ZVV ALA B 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 6ZVV ASN B 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 6ZVV LEU B 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 6ZVV SER B 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 6ZVV THR B 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 6ZVV GLU B 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVV ILE B 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVV GLY C 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVV VAL C 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 6ZVV THR C 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 6ZVV GLY C 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 6ZVV PHE C 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 6ZVV MET C 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 6ZVV PHE C 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 6ZVV THR C 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 6ZVV LYS C 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 6ZVV VAL C 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 6ZVV THR C 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 6ZVV TRP C 174 UNP P0A3G3 PRO 174 ENGINEERED MUTATION
SEQADV 6ZVV MET C 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 6ZVV GLY C 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 6ZVV ASN C 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 6ZVV GLU C 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 6ZVV ASP C 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 6ZVV LYS C 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 6ZVV ALA C 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 6ZVV ASN C 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 6ZVV LEU C 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 6ZVV SER C 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 6ZVV THR C 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 6ZVV GLU C 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVV ILE C 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVV GLY D 3 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVV VAL D 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 6ZVV THR D 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 6ZVV GLY D 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 6ZVV PHE D 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 6ZVV MET D 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 6ZVV PHE D 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 6ZVV THR D 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 6ZVV LYS D 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 6ZVV VAL D 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 6ZVV THR D 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 6ZVV TRP D 174 UNP P0A3G3 PRO 174 ENGINEERED MUTATION
SEQADV 6ZVV MET D 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 6ZVV GLY D 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 6ZVV ASN D 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 6ZVV GLU D 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 6ZVV ASP D 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 6ZVV LYS D 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 6ZVV ALA D 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 6ZVV ASN D 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 6ZVV LEU D 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 6ZVV SER D 291 UNP P0A3G3 PRO 291 ENGINEERED MUTATION
SEQADV 6ZVV THR D 292 UNP P0A3G3 ALA 292 ENGINEERED MUTATION
SEQADV 6ZVV GLU D 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 6ZVV ILE D 295 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 A 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 A 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 A 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 A 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 A 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 A 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 A 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 A 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 A 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 A 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 A 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 A 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 A 293 THR LEU TRP MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 A 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 A 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 A 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 A 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 A 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 A 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 A 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 A 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 A 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 B 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 B 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 B 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 B 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 B 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 B 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 B 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 B 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 B 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 B 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 B 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 B 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 B 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 B 293 THR LEU TRP MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 B 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 B 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 B 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 B 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 B 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 B 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 B 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 B 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 B 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 C 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 C 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 C 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 C 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 C 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 C 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 C 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 C 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 C 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 C 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 C 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 C 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 C 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 C 293 THR LEU TRP MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 C 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 C 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 C 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 C 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 C 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 C 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 C 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 C 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 C 293 TRP LEU SER THR LEU GLU ILE
SEQRES 1 D 293 GLY ILE GLY THR GLY PHE PRO PHE ASP PRO HIS TYR VAL
SEQRES 2 D 293 GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP VAL GLY
SEQRES 3 D 293 PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS GLY ASN
SEQRES 4 D 293 PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE PRO HIS
SEQRES 5 D 293 VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP LEU ILE
SEQRES 6 D 293 GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY TYR PHE
SEQRES 7 D 293 PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE ILE GLU
SEQRES 8 D 293 ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE HIS ASP
SEQRES 9 D 293 TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS ARG ASN
SEQRES 10 D 293 PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU PHE ILE
SEQRES 11 D 293 ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU PHE ALA
SEQRES 12 D 293 ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP VAL GLY
SEQRES 13 D 293 ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE GLU GLY
SEQRES 14 D 293 THR LEU TRP MET GLY VAL VAL ARG PRO LEU THR GLU VAL
SEQRES 15 D 293 GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN PRO VAL
SEQRES 16 D 293 ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU LEU PRO
SEQRES 17 D 293 ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU VAL GLU
SEQRES 18 D 293 GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL PRO LYS
SEQRES 19 D 293 LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE PRO PRO
SEQRES 20 D 293 ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO ASN CYS
SEQRES 21 D 293 LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU LEU GLN
SEQRES 22 D 293 GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE ALA ARG
SEQRES 23 D 293 TRP LEU SER THR LEU GLU ILE
HET OEH A 301 44
HET CL A 302 1
HET GOL A 303 6
HET OEH B 301 44
HET CL B 302 1
HET CA B 303 1
HET OEH C 301 44
HET CL C 302 1
HET GOL D 301 6
HET OEH D 302 44
HET CL D 303 1
HETNAM OEH [9-[2-CARBOXY-5-[2-[2-(6-CHLORANYLHEXOXY)
HETNAM 2 OEH ETHOXY]ETHYLCARBAMOYL]PHENYL]-6-(DIMETHYLAMINO)
HETNAM 3 OEH XANTHEN-3-YLIDENE]-DIMETHYL-AZANIUM
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETNAM CA CALCIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 OEH 4(C35 H43 CL N3 O6 1+)
FORMUL 6 CL 4(CL 1-)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 10 CA CA 2+
FORMUL 16 HOH *1373(H2 O)
HELIX 1 AA1 SER A 44 ARG A 49 5 6
HELIX 2 AA2 ILE A 51 ALA A 56 1 6
HELIX 3 AA3 PHE A 80 LEU A 95 1 16
HELIX 4 AA4 ASP A 106 ASN A 119 1 14
HELIX 5 AA5 THR A 137 TRP A 141 5 5
HELIX 6 AA6 PRO A 142 PHE A 144 5 3
HELIX 7 AA7 ALA A 145 ARG A 153 1 9
HELIX 8 AA8 THR A 155 ILE A 163 1 9
HELIX 9 AA9 ASN A 166 GLY A 171 1 6
HELIX 10 AB1 LEU A 173 VAL A 177 5 5
HELIX 11 AB2 THR A 182 GLU A 191 1 10
HELIX 12 AB3 PRO A 192 LEU A 194 5 3
HELIX 13 AB4 ASN A 195 ASP A 198 5 4
HELIX 14 AB5 ARG A 199 LEU A 209 1 11
HELIX 15 AB6 PRO A 215 SER A 232 1 18
HELIX 16 AB7 PRO A 248 LEU A 259 1 12
HELIX 17 AB8 LEU A 273 ASN A 278 1 6
HELIX 18 AB9 ASN A 278 THR A 292 1 15
HELIX 19 AC1 SER B 44 ARG B 49 5 6
HELIX 20 AC2 ILE B 51 ALA B 56 1 6
HELIX 21 AC3 PHE B 80 LEU B 95 1 16
HELIX 22 AC4 ASP B 106 ASN B 119 1 14
HELIX 23 AC5 THR B 137 TRP B 141 5 5
HELIX 24 AC6 PRO B 142 PHE B 144 5 3
HELIX 25 AC7 ALA B 145 ARG B 153 1 9
HELIX 26 AC8 THR B 155 ILE B 163 1 9
HELIX 27 AC9 ASN B 166 GLY B 171 1 6
HELIX 28 AD1 LEU B 173 VAL B 177 5 5
HELIX 29 AD2 THR B 182 GLU B 191 1 10
HELIX 30 AD3 PRO B 192 LEU B 194 5 3
HELIX 31 AD4 ASN B 195 ASP B 198 5 4
HELIX 32 AD5 ARG B 199 LEU B 209 1 11
HELIX 33 AD6 PRO B 215 SER B 232 1 18
HELIX 34 AD7 PRO B 248 LEU B 259 1 12
HELIX 35 AD8 LEU B 273 ASN B 278 1 6
HELIX 36 AD9 ASN B 278 LEU B 293 1 16
HELIX 37 AE1 SER C 44 ARG C 49 5 6
HELIX 38 AE2 ILE C 51 ALA C 56 1 6
HELIX 39 AE3 PHE C 80 LEU C 95 1 16
HELIX 40 AE4 ASP C 106 ASN C 119 1 14
HELIX 41 AE5 THR C 137 TRP C 141 5 5
HELIX 42 AE6 PRO C 142 ARG C 153 1 12
HELIX 43 AE7 ASP C 156 ILE C 163 1 8
HELIX 44 AE8 ASN C 166 GLY C 171 1 6
HELIX 45 AE9 LEU C 173 VAL C 177 5 5
HELIX 46 AF1 THR C 182 GLU C 191 1 10
HELIX 47 AF2 PRO C 192 LEU C 194 5 3
HELIX 48 AF3 ASN C 195 ASP C 198 5 4
HELIX 49 AF4 ARG C 199 LEU C 209 1 11
HELIX 50 AF5 PRO C 215 SER C 232 1 18
HELIX 51 AF6 PRO C 248 LEU C 259 1 12
HELIX 52 AF7 LEU C 273 ASN C 278 1 6
HELIX 53 AF8 ASN C 278 SER C 291 1 14
HELIX 54 AF9 SER D 44 ARG D 49 5 6
HELIX 55 AG1 ILE D 51 ALA D 56 1 6
HELIX 56 AG2 PHE D 80 LEU D 95 1 16
HELIX 57 AG3 ASP D 106 ASN D 119 1 14
HELIX 58 AG4 THR D 137 TRP D 141 5 5
HELIX 59 AG5 PRO D 142 ARG D 153 1 12
HELIX 60 AG6 THR D 155 ILE D 163 1 9
HELIX 61 AG7 ASN D 166 GLY D 171 1 6
HELIX 62 AG8 LEU D 173 VAL D 177 5 5
HELIX 63 AG9 THR D 182 GLU D 191 1 10
HELIX 64 AH1 PRO D 192 LEU D 194 5 3
HELIX 65 AH2 ASN D 195 ASP D 198 5 4
HELIX 66 AH3 ARG D 199 LEU D 209 1 11
HELIX 67 AH4 PRO D 215 SER D 232 1 18
HELIX 68 AH5 PRO D 248 LEU D 259 1 12
HELIX 69 AH6 LEU D 273 ASN D 278 1 6
HELIX 70 AH7 ASN D 278 THR D 292 1 15
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O MET A 22 N VAL A 15
SHEET 3 AA1 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 AA1 8 VAL A 35 LEU A 38 1 N PHE A 37 O ILE A 62
SHEET 5 AA1 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 AA1 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 AA1 8 LYS A 236 PRO A 243 1 O LEU A 237 N PHE A 128
SHEET 8 AA1 8 CYS A 262 GLY A 270 1 O ILE A 267 N TRP A 240
SHEET 1 AA2 8 HIS B 13 VAL B 17 0
SHEET 2 AA2 8 GLU B 20 VAL B 27 -1 O GLU B 20 N VAL B 17
SHEET 3 AA2 8 CYS B 61 PRO B 64 -1 O CYS B 61 N VAL B 27
SHEET 4 AA2 8 VAL B 35 LEU B 38 1 N PHE B 37 O ILE B 62
SHEET 5 AA2 8 VAL B 100 HIS B 105 1 O VAL B 101 N LEU B 36
SHEET 6 AA2 8 VAL B 123 MET B 129 1 O ALA B 127 N LEU B 102
SHEET 7 AA2 8 LYS B 236 PRO B 243 1 O LEU B 237 N PHE B 128
SHEET 8 AA2 8 CYS B 262 GLY B 270 1 O ILE B 267 N TRP B 240
SHEET 1 AA3 8 HIS C 13 VAL C 17 0
SHEET 2 AA3 8 GLU C 20 VAL C 27 -1 O GLU C 20 N VAL C 17
SHEET 3 AA3 8 CYS C 61 PRO C 64 -1 O CYS C 61 N VAL C 27
SHEET 4 AA3 8 VAL C 35 LEU C 38 1 N VAL C 35 O ILE C 62
SHEET 5 AA3 8 VAL C 100 HIS C 105 1 O VAL C 101 N LEU C 36
SHEET 6 AA3 8 VAL C 123 MET C 129 1 O LYS C 124 N VAL C 100
SHEET 7 AA3 8 LYS C 236 PRO C 243 1 O LEU C 237 N PHE C 128
SHEET 8 AA3 8 CYS C 262 GLY C 270 1 O ILE C 267 N TRP C 240
SHEET 1 AA4 8 HIS D 13 VAL D 17 0
SHEET 2 AA4 8 GLU D 20 VAL D 27 -1 O GLU D 20 N VAL D 17
SHEET 3 AA4 8 CYS D 61 PRO D 64 -1 O CYS D 61 N VAL D 27
SHEET 4 AA4 8 VAL D 35 LEU D 38 1 N PHE D 37 O ILE D 62
SHEET 5 AA4 8 VAL D 100 HIS D 105 1 O VAL D 101 N LEU D 36
SHEET 6 AA4 8 VAL D 123 MET D 129 1 O ALA D 127 N LEU D 102
SHEET 7 AA4 8 LYS D 236 PRO D 243 1 O LEU D 237 N PHE D 128
SHEET 8 AA4 8 CYS D 262 GLY D 270 1 O ILE D 267 N TRP D 240
LINK OD2 ASP A 106 C20 OEH A 301 1555 1555 1.38
LINK OD2 ASP B 106 C20 OEH B 301 1555 1555 1.38
LINK OD2 ASP C 106 C20 OEH C 301 1555 1555 1.38
LINK OD2 ASP D 106 C20 OEH D 302 1555 1555 1.38
LINK OD2 ASP B 73 CA CA B 303 1555 1555 2.48
LINK CA CA B 303 O HOH B 401 1555 1555 2.32
LINK CA CA B 303 O HOH B 430 1555 1555 2.57
LINK CA CA B 303 O HOH B 623 1555 1555 2.33
LINK CA CA B 303 O HOH B 657 1555 1555 2.50
LINK CA CA B 303 O HOH B 717 1555 1555 2.29
LINK CA CA B 303 O HOH D 619 1555 1655 3.05
CISPEP 1 ASN A 41 PRO A 42 0 -0.05
CISPEP 2 GLU A 214 PRO A 215 0 -6.11
CISPEP 3 THR A 242 PRO A 243 0 4.75
CISPEP 4 ASN B 41 PRO B 42 0 2.28
CISPEP 5 GLU B 214 PRO B 215 0 -4.12
CISPEP 6 THR B 242 PRO B 243 0 4.16
CISPEP 7 ASN C 41 PRO C 42 0 2.77
CISPEP 8 GLU C 214 PRO C 215 0 -4.31
CISPEP 9 THR C 242 PRO C 243 0 6.23
CISPEP 10 ASN D 41 PRO D 42 0 -1.96
CISPEP 11 GLU D 214 PRO D 215 0 -3.33
CISPEP 12 THR D 242 PRO D 243 0 4.55
CRYST1 70.260 53.030 163.210 90.00 93.75 90.00 P 1 21 1 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 0.014233 0.000000 0.000932 0.00000
SCALE2 0.000000 0.018857 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006140 0.00000
TER 2358 ILE A 295
TER 4698 LEU B 293
TER 7061 ILE C 295
TER 9431 GLU D 294
MASTER 341 0 11 70 32 0 0 610967 4 200 92
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