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HEADER TRANSFERASE 13-JUN-24 9C9F
TITLE CRYSTAL STRUCTURES FLUOROACETATE DEHALOGENASE D4B FROM DELFTIA
TITLE 2 ACIDOVORANS STRAIN D4B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROACETATE DEHALOGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DELFTIA ACIDOVORANS;
SOURCE 3 ORGANISM_TAXID: 80866;
SOURCE 4 STRAIN: D4B;
SOURCE 5 GENE: DACI_4283;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DEHALOGENASE PFAS, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.T.CAPUTO,M.HU,C.SCOTT
REVDAT 1 27-AUG-25 9C9F 0
JRNL AUTH M.HU,A.T.CAPUTO,C.SCOTT
JRNL TITL CRYSTAL STRUCTURES OF TWO FLUOROACETATE DEHALOGENASES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.LIEBSCHNER,P.V.AFONINE,M.L.BAKER,G.BUNKOCZI,V.B.CHEN,
REMARK 1 AUTH 2 T.I.CROLL,B.HINTZE,L.W.HUNG,S.JAIN,A.J.MCCOY,N.W.MORIARTY,
REMARK 1 AUTH 3 R.D.OEFFNER,B.K.POON,M.G.PRISANT,R.J.READ,J.S.RICHARDSON,
REMARK 1 AUTH 4 D.C.RICHARDSON,M.D.SAMMITO,O.V.SOBOLEV,D.H.STOCKWELL,
REMARK 1 AUTH 5 T.C.TERWILLIGER,A.G.URZHUMTSEV,L.L.VIDEAU,C.J.WILLIAMS,
REMARK 1 AUTH 6 P.D.ADAMS
REMARK 1 TITL MACROMOLECULAR STRUCTURE DETERMINATION USING X-RAYS,
REMARK 1 TITL 2 NEUTRONS AND ELECTRONS: RECENT DEVELOPMENTS IN PHENIX
REMARK 1 REF ACTA CRYSTALLOGR., SECT. D: V. 75 861 2019
REMARK 1 REF 2 BIOL. CRYSTALLOGR.
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 31588918
REMARK 1 DOI 10.1107/S2059798319011471
REMARK 2
REMARK 2 RESOLUTION. 1.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.21_5207
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) : 1.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 77162
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.890
REMARK 3 FREE R VALUE TEST SET COUNT : 3777
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 39.4100 - 5.9400 0.98 2738 154 0.1846 0.1803
REMARK 3 2 5.9400 - 4.7200 0.99 2777 122 0.1788 0.1781
REMARK 3 3 4.7200 - 4.1200 0.99 2787 138 0.1584 0.2232
REMARK 3 4 4.1200 - 3.7400 0.99 2790 132 0.1686 0.1623
REMARK 3 5 3.7400 - 3.4800 0.98 2760 137 0.1908 0.2239
REMARK 3 6 3.4800 - 3.2700 0.98 2717 144 0.2075 0.2400
REMARK 3 7 3.2700 - 3.1100 0.98 2708 156 0.2098 0.2499
REMARK 3 8 3.1100 - 2.9700 0.98 2818 117 0.2195 0.2214
REMARK 3 9 2.9700 - 2.8600 0.98 2713 138 0.2254 0.2446
REMARK 3 10 2.8600 - 2.7600 0.98 2776 129 0.2368 0.2952
REMARK 3 11 2.7600 - 2.6700 0.98 2694 149 0.2400 0.2975
REMARK 3 12 2.6700 - 2.6000 0.98 2749 169 0.2479 0.2968
REMARK 3 13 2.6000 - 2.5300 0.98 2701 131 0.2421 0.2688
REMARK 3 14 2.5300 - 2.4700 0.98 2764 170 0.2478 0.2577
REMARK 3 15 2.4700 - 2.4100 0.97 2701 176 0.2446 0.2902
REMARK 3 16 2.4100 - 2.3600 0.97 2697 156 0.2460 0.2663
REMARK 3 17 2.3600 - 2.3100 0.97 2772 125 0.2562 0.2877
REMARK 3 18 2.3100 - 2.2700 0.97 2691 115 0.2648 0.2871
REMARK 3 19 2.2700 - 2.2300 0.97 2738 163 0.2626 0.2888
REMARK 3 20 2.2300 - 2.1900 0.97 2734 145 0.2756 0.3109
REMARK 3 21 2.1900 - 2.1600 0.97 2648 147 0.2936 0.3149
REMARK 3 22 2.1600 - 2.1200 0.97 2763 129 0.3042 0.3259
REMARK 3 23 2.1200 - 2.0900 0.97 2761 117 0.3025 0.3215
REMARK 3 24 2.0900 - 2.0600 0.96 2693 137 0.3115 0.3313
REMARK 3 25 2.0600 - 2.0300 0.96 2671 137 0.3191 0.3533
REMARK 3 26 2.0300 - 2.0100 0.93 2644 130 0.3313 0.3671
REMARK 3 27 2.0100 - 1.9800 0.86 2380 114 0.3267 0.3779
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) : 0.287
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.22
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.11
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 : 0.005 9660
REMARK 3 ANGLE : 0.838 13148
REMARK 3 CHIRALITY : 0.044 1386
REMARK 3 PLANARITY : 0.016 1751
REMARK 3 DIHEDRAL : 14.414 3563
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 : 1
REMARK 3 NCS GROUP : ens_1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "A" and (resid 6 through 52 or
REMARK 3 resid 54 through 298))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "B" and (resid 6 through 52 or
REMARK 3 resid 54 through 298))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "C" and (resid 6 through 52 or
REMARK 3 resid 54 through 298))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: NULL
REMARK 3 SELECTION : (chain "D" and (resid 6 through 52 or
REMARK 3 resid 54 through 298))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 9C9F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-24.
REMARK 100 THE DEPOSITION ID IS D_1000284402.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95374
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JAN 10, 2022
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.9
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77693
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.980
REMARK 200 RESOLUTION RANGE LOW (A) : 82.538
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.18100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 1.31500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.3
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14 MG/ML 25 %(W/V) POLYETHYLENE GLYCOL
REMARK 280 3350, 0.2 M AMMONIUM ACETATE, 0.1 M TRIS-HCL PH 8.5, VAPOR
REMARK 280 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
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 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 HIS A 2
REMARK 465 THR A 3
REMARK 465 ASP A 4
REMARK 465 PRO A 5
REMARK 465 GLY A 300
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 ALA B 299
REMARK 465 GLY B 300
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 HIS C 2
REMARK 465 THR C 3
REMARK 465 ASP C 4
REMARK 465 PRO C 5
REMARK 465 ALA C 299
REMARK 465 GLY C 300
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 HE ARG C 66 OD2 ASP C 91 1.56
REMARK 500 HH TYR D 68 O HOH D 402 1.58
REMARK 500 H ASP D 134 O LEU D 245 1.58
REMARK 500 HE ARG A 66 OD2 ASP A 91 1.60
REMARK 500 HH12 ARG D 260 O HOH D 410 1.60
REMARK 500 NH1 ARG B 14 OE1 GLU B 22 1.93
REMARK 500 O GLY B 29 O HOH B 401 2.02
REMARK 500 OE2 GLU C 248 O HOH C 401 2.02
REMARK 500 O SER C 186 O HOH C 402 2.05
REMARK 500 O HOH D 559 O HOH D 566 2.14
REMARK 500 NH1 ARG A 254 O HOH A 401 2.18
REMARK 500 O HOH C 525 O HOH C 542 2.18
REMARK 500 OD2 ASP C 290 O HOH C 403 2.19
REMARK 500 O ALA B 291 O HOH B 402 2.19
REMARK 500 O HOH C 536 O HOH D 572 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 HH22 ARG C 11 O GLN D 57 1556 1.59
REMARK 500 NE2 GLN A 298 OE1 GLN B 56 1556 2.13
REMARK 500 O HOH B 586 O HOH D 516 1455 2.17
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 PRO A 41 58.35 -99.17
REMARK 500 GLN A 42 -164.08 -121.18
REMARK 500 ASP A 110 -133.38 56.45
REMARK 500 ASP A 173 84.61 -165.03
REMARK 500 PRO B 41 58.25 -98.35
REMARK 500 GLN B 42 -161.87 -122.88
REMARK 500 ASP B 110 -133.50 58.00
REMARK 500 TYR B 153 54.17 -90.00
REMARK 500 ASP B 173 86.51 -164.84
REMARK 500 ARG B 185 -178.60 -172.05
REMARK 500 PRO C 41 58.67 -98.01
REMARK 500 GLN C 42 -164.12 -122.13
REMARK 500 ASP C 110 -133.65 57.83
REMARK 500 TYR C 153 53.91 -90.59
REMARK 500 ASP C 173 85.80 -164.20
REMARK 500 PRO D 41 57.95 -98.31
REMARK 500 GLN D 42 -163.37 -121.72
REMARK 500 ASP D 110 -132.29 58.12
REMARK 500 TYR D 153 54.30 -90.83
REMARK 500 ASP D 173 86.85 -166.09
REMARK 500 ALA D 299 170.11 173.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 11 0.14 SIDE CHAIN
REMARK 500 ARG A 168 0.10 SIDE CHAIN
REMARK 500 ARG A 270 0.11 SIDE CHAIN
REMARK 500 ARG B 168 0.08 SIDE CHAIN
REMARK 500 ARG C 168 0.09 SIDE CHAIN
REMARK 500 ARG D 168 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9C9F A 1 300 UNP A9BLX5 A9BLX5_DELAS 1 300
DBREF 9C9F B 1 300 UNP A9BLX5 A9BLX5_DELAS 1 300
DBREF 9C9F C 1 300 UNP A9BLX5 A9BLX5_DELAS 1 300
DBREF 9C9F D 1 300 UNP A9BLX5 A9BLX5_DELAS 1 300
SEQADV 9C9F MET A -19 UNP A9BLX5 INITIATING METHIONINE
SEQADV 9C9F GLY A -18 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER A -17 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER A -16 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS A -15 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS A -14 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS A -13 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS A -12 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS A -11 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS A -10 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER A -9 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER A -8 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F GLY A -7 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F LEU A -6 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F VAL A -5 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F PRO A -4 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F ARG A -3 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F GLY A -2 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER A -1 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS A 0 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F MET B -19 UNP A9BLX5 INITIATING METHIONINE
SEQADV 9C9F GLY B -18 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER B -17 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER B -16 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS B -15 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS B -14 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS B -13 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS B -12 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS B -11 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS B -10 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER B -9 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER B -8 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F GLY B -7 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F LEU B -6 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F VAL B -5 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F PRO B -4 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F ARG B -3 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F GLY B -2 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER B -1 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS B 0 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F MET C -19 UNP A9BLX5 INITIATING METHIONINE
SEQADV 9C9F GLY C -18 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER C -17 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER C -16 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS C -15 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS C -14 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS C -13 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS C -12 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS C -11 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS C -10 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER C -9 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER C -8 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F GLY C -7 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F LEU C -6 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F VAL C -5 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F PRO C -4 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F ARG C -3 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F GLY C -2 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER C -1 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS C 0 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F MET D -19 UNP A9BLX5 INITIATING METHIONINE
SEQADV 9C9F GLY D -18 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER D -17 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER D -16 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS D -15 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS D -14 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS D -13 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS D -12 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS D -11 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS D -10 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER D -9 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER D -8 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F GLY D -7 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F LEU D -6 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F VAL D -5 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F PRO D -4 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F ARG D -3 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F GLY D -2 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F SER D -1 UNP A9BLX5 EXPRESSION TAG
SEQADV 9C9F HIS D 0 UNP A9BLX5 EXPRESSION TAG
SEQRES 1 A 320 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 320 LEU VAL PRO ARG GLY SER HIS MET HIS THR ASP PRO TRP
SEQRES 3 A 320 MET PRO GLY LEU ARG GLN GLN ARG ILE THR VAL ASP ASP
SEQRES 4 A 320 GLY VAL GLU ILE ASN ALA TRP VAL GLY GLY GLN GLY PRO
SEQRES 5 A 320 ALA LEU LEU LEU VAL HIS GLY HIS PRO GLN THR SER ALA
SEQRES 6 A 320 ILE TRP HIS ARG VAL ALA PRO ARG LEU ALA GLN GLN PHE
SEQRES 7 A 320 THR VAL VAL LEU ALA ASP LEU ARG GLY TYR GLY ASP SER
SEQRES 8 A 320 SER ARG PRO ALA GLY ASP PRO GLU HIS VAL ASN TYR SER
SEQRES 9 A 320 LYS ARG THR MET ALA ARG ASP LEU LEU ARG LEU MET ALA
SEQRES 10 A 320 ARG LEU GLY HIS GLU HIS PHE SER VAL LEU ALA HIS ASP
SEQRES 11 A 320 ARG GLY ALA ARG VAL ALA HIS ARG LEU ALA MET ASP TYR
SEQRES 12 A 320 PRO ALA SER VAL GLN ARG LEU VAL LEU LEU ASP ILE ALA
SEQRES 13 A 320 PRO THR LEU ALA MET TYR GLU GLN THR GLY GLU ALA PHE
SEQRES 14 A 320 ALA ARG ALA TYR TRP HIS TRP PHE PHE LEU ILE GLN PRO
SEQRES 15 A 320 ALA PRO LEU PRO GLU ARG LEU ILE GLU ALA ASP PRO ALA
SEQRES 16 A 320 ALA TYR VAL ARG GLU ILE MET GLY ARG ARG SER ALA GLY
SEQRES 17 A 320 LEU ALA PRO PHE ASP PRO ARG ALA LEU ALA GLU TYR GLN
SEQRES 18 A 320 ARG CYS LEU ALA LEU PRO GLY SER ALA HIS GLY MET CYS
SEQRES 19 A 320 GLU ASP TYR ARG ALA SER ALA GLY ILE ASP LEU ASP HIS
SEQRES 20 A 320 ASP ARG GLU ASP ARG GLN LEU GLY ARG ARG LEU SER MET
SEQRES 21 A 320 PRO LEU LEU VAL LEU TRP GLY GLU GLU GLY VAL VAL HIS
SEQRES 22 A 320 ARG CYS PHE ASP PRO LEU ARG GLU TRP GLN LEU VAL ALA
SEQRES 23 A 320 ASP ASP VAL ARG GLY ARG PRO LEU ALA CYS GLY HIS TYR
SEQRES 24 A 320 ILE ALA GLU GLU ALA PRO ASP ALA LEU LEU ASP ALA ALA
SEQRES 25 A 320 LEU PRO PHE LEU LEU GLN ALA GLY
SEQRES 1 B 320 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 320 LEU VAL PRO ARG GLY SER HIS MET HIS THR ASP PRO TRP
SEQRES 3 B 320 MET PRO GLY LEU ARG GLN GLN ARG ILE THR VAL ASP ASP
SEQRES 4 B 320 GLY VAL GLU ILE ASN ALA TRP VAL GLY GLY GLN GLY PRO
SEQRES 5 B 320 ALA LEU LEU LEU VAL HIS GLY HIS PRO GLN THR SER ALA
SEQRES 6 B 320 ILE TRP HIS ARG VAL ALA PRO ARG LEU ALA GLN GLN PHE
SEQRES 7 B 320 THR VAL VAL LEU ALA ASP LEU ARG GLY TYR GLY ASP SER
SEQRES 8 B 320 SER ARG PRO ALA GLY ASP PRO GLU HIS VAL ASN TYR SER
SEQRES 9 B 320 LYS ARG THR MET ALA ARG ASP LEU LEU ARG LEU MET ALA
SEQRES 10 B 320 ARG LEU GLY HIS GLU HIS PHE SER VAL LEU ALA HIS ASP
SEQRES 11 B 320 ARG GLY ALA ARG VAL ALA HIS ARG LEU ALA MET ASP TYR
SEQRES 12 B 320 PRO ALA SER VAL GLN ARG LEU VAL LEU LEU ASP ILE ALA
SEQRES 13 B 320 PRO THR LEU ALA MET TYR GLU GLN THR GLY GLU ALA PHE
SEQRES 14 B 320 ALA ARG ALA TYR TRP HIS TRP PHE PHE LEU ILE GLN PRO
SEQRES 15 B 320 ALA PRO LEU PRO GLU ARG LEU ILE GLU ALA ASP PRO ALA
SEQRES 16 B 320 ALA TYR VAL ARG GLU ILE MET GLY ARG ARG SER ALA GLY
SEQRES 17 B 320 LEU ALA PRO PHE ASP PRO ARG ALA LEU ALA GLU TYR GLN
SEQRES 18 B 320 ARG CYS LEU ALA LEU PRO GLY SER ALA HIS GLY MET CYS
SEQRES 19 B 320 GLU ASP TYR ARG ALA SER ALA GLY ILE ASP LEU ASP HIS
SEQRES 20 B 320 ASP ARG GLU ASP ARG GLN LEU GLY ARG ARG LEU SER MET
SEQRES 21 B 320 PRO LEU LEU VAL LEU TRP GLY GLU GLU GLY VAL VAL HIS
SEQRES 22 B 320 ARG CYS PHE ASP PRO LEU ARG GLU TRP GLN LEU VAL ALA
SEQRES 23 B 320 ASP ASP VAL ARG GLY ARG PRO LEU ALA CYS GLY HIS TYR
SEQRES 24 B 320 ILE ALA GLU GLU ALA PRO ASP ALA LEU LEU ASP ALA ALA
SEQRES 25 B 320 LEU PRO PHE LEU LEU GLN ALA GLY
SEQRES 1 C 320 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 320 LEU VAL PRO ARG GLY SER HIS MET HIS THR ASP PRO TRP
SEQRES 3 C 320 MET PRO GLY LEU ARG GLN GLN ARG ILE THR VAL ASP ASP
SEQRES 4 C 320 GLY VAL GLU ILE ASN ALA TRP VAL GLY GLY GLN GLY PRO
SEQRES 5 C 320 ALA LEU LEU LEU VAL HIS GLY HIS PRO GLN THR SER ALA
SEQRES 6 C 320 ILE TRP HIS ARG VAL ALA PRO ARG LEU ALA GLN GLN PHE
SEQRES 7 C 320 THR VAL VAL LEU ALA ASP LEU ARG GLY TYR GLY ASP SER
SEQRES 8 C 320 SER ARG PRO ALA GLY ASP PRO GLU HIS VAL ASN TYR SER
SEQRES 9 C 320 LYS ARG THR MET ALA ARG ASP LEU LEU ARG LEU MET ALA
SEQRES 10 C 320 ARG LEU GLY HIS GLU HIS PHE SER VAL LEU ALA HIS ASP
SEQRES 11 C 320 ARG GLY ALA ARG VAL ALA HIS ARG LEU ALA MET ASP TYR
SEQRES 12 C 320 PRO ALA SER VAL GLN ARG LEU VAL LEU LEU ASP ILE ALA
SEQRES 13 C 320 PRO THR LEU ALA MET TYR GLU GLN THR GLY GLU ALA PHE
SEQRES 14 C 320 ALA ARG ALA TYR TRP HIS TRP PHE PHE LEU ILE GLN PRO
SEQRES 15 C 320 ALA PRO LEU PRO GLU ARG LEU ILE GLU ALA ASP PRO ALA
SEQRES 16 C 320 ALA TYR VAL ARG GLU ILE MET GLY ARG ARG SER ALA GLY
SEQRES 17 C 320 LEU ALA PRO PHE ASP PRO ARG ALA LEU ALA GLU TYR GLN
SEQRES 18 C 320 ARG CYS LEU ALA LEU PRO GLY SER ALA HIS GLY MET CYS
SEQRES 19 C 320 GLU ASP TYR ARG ALA SER ALA GLY ILE ASP LEU ASP HIS
SEQRES 20 C 320 ASP ARG GLU ASP ARG GLN LEU GLY ARG ARG LEU SER MET
SEQRES 21 C 320 PRO LEU LEU VAL LEU TRP GLY GLU GLU GLY VAL VAL HIS
SEQRES 22 C 320 ARG CYS PHE ASP PRO LEU ARG GLU TRP GLN LEU VAL ALA
SEQRES 23 C 320 ASP ASP VAL ARG GLY ARG PRO LEU ALA CYS GLY HIS TYR
SEQRES 24 C 320 ILE ALA GLU GLU ALA PRO ASP ALA LEU LEU ASP ALA ALA
SEQRES 25 C 320 LEU PRO PHE LEU LEU GLN ALA GLY
SEQRES 1 D 320 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 320 LEU VAL PRO ARG GLY SER HIS MET HIS THR ASP PRO TRP
SEQRES 3 D 320 MET PRO GLY LEU ARG GLN GLN ARG ILE THR VAL ASP ASP
SEQRES 4 D 320 GLY VAL GLU ILE ASN ALA TRP VAL GLY GLY GLN GLY PRO
SEQRES 5 D 320 ALA LEU LEU LEU VAL HIS GLY HIS PRO GLN THR SER ALA
SEQRES 6 D 320 ILE TRP HIS ARG VAL ALA PRO ARG LEU ALA GLN GLN PHE
SEQRES 7 D 320 THR VAL VAL LEU ALA ASP LEU ARG GLY TYR GLY ASP SER
SEQRES 8 D 320 SER ARG PRO ALA GLY ASP PRO GLU HIS VAL ASN TYR SER
SEQRES 9 D 320 LYS ARG THR MET ALA ARG ASP LEU LEU ARG LEU MET ALA
SEQRES 10 D 320 ARG LEU GLY HIS GLU HIS PHE SER VAL LEU ALA HIS ASP
SEQRES 11 D 320 ARG GLY ALA ARG VAL ALA HIS ARG LEU ALA MET ASP TYR
SEQRES 12 D 320 PRO ALA SER VAL GLN ARG LEU VAL LEU LEU ASP ILE ALA
SEQRES 13 D 320 PRO THR LEU ALA MET TYR GLU GLN THR GLY GLU ALA PHE
SEQRES 14 D 320 ALA ARG ALA TYR TRP HIS TRP PHE PHE LEU ILE GLN PRO
SEQRES 15 D 320 ALA PRO LEU PRO GLU ARG LEU ILE GLU ALA ASP PRO ALA
SEQRES 16 D 320 ALA TYR VAL ARG GLU ILE MET GLY ARG ARG SER ALA GLY
SEQRES 17 D 320 LEU ALA PRO PHE ASP PRO ARG ALA LEU ALA GLU TYR GLN
SEQRES 18 D 320 ARG CYS LEU ALA LEU PRO GLY SER ALA HIS GLY MET CYS
SEQRES 19 D 320 GLU ASP TYR ARG ALA SER ALA GLY ILE ASP LEU ASP HIS
SEQRES 20 D 320 ASP ARG GLU ASP ARG GLN LEU GLY ARG ARG LEU SER MET
SEQRES 21 D 320 PRO LEU LEU VAL LEU TRP GLY GLU GLU GLY VAL VAL HIS
SEQRES 22 D 320 ARG CYS PHE ASP PRO LEU ARG GLU TRP GLN LEU VAL ALA
SEQRES 23 D 320 ASP ASP VAL ARG GLY ARG PRO LEU ALA CYS GLY HIS TYR
SEQRES 24 D 320 ILE ALA GLU GLU ALA PRO ASP ALA LEU LEU ASP ALA ALA
SEQRES 25 D 320 LEU PRO PHE LEU LEU GLN ALA GLY
FORMUL 5 HOH *716(H2 O)
HELIX 1 AA1 THR A 43 HIS A 48 5 6
HELIX 2 AA2 VAL A 50 GLN A 56 1 7
HELIX 3 AA3 SER A 84 LEU A 99 1 16
HELIX 4 AA4 ASP A 110 TYR A 123 1 14
HELIX 5 AA5 PRO A 137 GLN A 144 1 8
HELIX 6 AA6 GLY A 146 TYR A 153 1 8
HELIX 7 AA7 TRP A 154 LEU A 159 1 6
HELIX 8 AA8 PRO A 164 ASP A 173 1 10
HELIX 9 AA9 ASP A 173 ARG A 184 1 12
HELIX 10 AB1 ASP A 193 ALA A 205 1 13
HELIX 11 AB2 GLY A 208 ALA A 221 1 14
HELIX 12 AB3 GLY A 222 GLY A 235 1 14
HELIX 13 AB4 GLY A 250 PHE A 256 1 7
HELIX 14 AB5 ASP A 257 ALA A 266 1 10
HELIX 15 AB6 TYR A 279 ALA A 284 1 6
HELIX 16 AB7 ALA A 284 ALA A 299 1 16
HELIX 17 AB8 THR B 43 ARG B 49 5 7
HELIX 18 AB9 VAL B 50 ALA B 55 1 6
HELIX 19 AC1 SER B 84 LEU B 99 1 16
HELIX 20 AC2 ASP B 110 TYR B 123 1 14
HELIX 21 AC3 PRO B 137 GLN B 144 1 8
HELIX 22 AC4 GLY B 146 TYR B 153 1 8
HELIX 23 AC5 TRP B 154 LEU B 159 1 6
HELIX 24 AC6 PRO B 164 ASP B 173 1 10
HELIX 25 AC7 ASP B 173 ARG B 184 1 12
HELIX 26 AC8 ASP B 193 ALA B 205 1 13
HELIX 27 AC9 GLY B 208 ALA B 221 1 14
HELIX 28 AD1 GLY B 222 LEU B 234 1 13
HELIX 29 AD2 GLY B 250 PHE B 256 1 7
HELIX 30 AD3 ASP B 257 ALA B 266 1 10
HELIX 31 AD4 TYR B 279 ALA B 284 1 6
HELIX 32 AD5 ALA B 284 GLN B 298 1 15
HELIX 33 AD6 THR C 43 ARG C 49 5 7
HELIX 34 AD7 VAL C 50 ALA C 55 1 6
HELIX 35 AD8 SER C 84 LEU C 99 1 16
HELIX 36 AD9 ASP C 110 TYR C 123 1 14
HELIX 37 AE1 PRO C 137 GLN C 144 1 8
HELIX 38 AE2 GLY C 146 TYR C 153 1 8
HELIX 39 AE3 TRP C 154 LEU C 159 1 6
HELIX 40 AE4 PRO C 164 ASP C 173 1 10
HELIX 41 AE5 ASP C 173 ARG C 184 1 12
HELIX 42 AE6 ASP C 193 ALA C 205 1 13
HELIX 43 AE7 GLY C 208 ALA C 221 1 14
HELIX 44 AE8 GLY C 222 GLY C 235 1 14
HELIX 45 AE9 GLY C 250 PHE C 256 1 7
HELIX 46 AF1 ASP C 257 ALA C 266 1 10
HELIX 47 AF2 TYR C 279 ALA C 284 1 6
HELIX 48 AF3 ALA C 284 GLN C 298 1 15
HELIX 49 AF4 THR D 43 ARG D 49 5 7
HELIX 50 AF5 VAL D 50 GLN D 56 1 7
HELIX 51 AF6 SER D 84 LEU D 99 1 16
HELIX 52 AF7 ASP D 110 TYR D 123 1 14
HELIX 53 AF8 PRO D 137 GLN D 144 1 8
HELIX 54 AF9 GLY D 146 TYR D 153 1 8
HELIX 55 AG1 TRP D 154 LEU D 159 1 6
HELIX 56 AG2 PRO D 164 ASP D 173 1 10
HELIX 57 AG3 ASP D 173 ARG D 184 1 12
HELIX 58 AG4 ASP D 193 ALA D 205 1 13
HELIX 59 AG5 GLY D 208 ALA D 221 1 14
HELIX 60 AG6 GLY D 222 LEU D 234 1 13
HELIX 61 AG7 GLY D 250 PHE D 256 1 7
HELIX 62 AG8 ASP D 257 ALA D 266 1 10
HELIX 63 AG9 TYR D 279 ALA D 284 1 6
HELIX 64 AH1 ALA D 284 GLN D 298 1 15
SHEET 1 AA1 8 ARG A 11 ASP A 18 0
SHEET 2 AA1 8 VAL A 21 GLY A 29 -1 O ALA A 25 N GLN A 13
SHEET 3 AA1 8 THR A 59 ALA A 63 -1 O LEU A 62 N TRP A 26
SHEET 4 AA1 8 ALA A 33 VAL A 37 1 N LEU A 36 O VAL A 61
SHEET 5 AA1 8 PHE A 104 HIS A 109 1 O SER A 105 N LEU A 35
SHEET 6 AA1 8 VAL A 127 LEU A 133 1 O GLN A 128 N PHE A 104
SHEET 7 AA1 8 LEU A 242 GLY A 247 1 O LEU A 243 N LEU A 130
SHEET 8 AA1 8 VAL A 269 LEU A 274 1 O LEU A 274 N TRP A 246
SHEET 1 AA2 8 ARG B 11 ASP B 18 0
SHEET 2 AA2 8 VAL B 21 GLY B 29 -1 O ALA B 25 N GLN B 13
SHEET 3 AA2 8 THR B 59 ALA B 63 -1 O LEU B 62 N TRP B 26
SHEET 4 AA2 8 ALA B 33 VAL B 37 1 N LEU B 36 O VAL B 61
SHEET 5 AA2 8 PHE B 104 HIS B 109 1 O SER B 105 N LEU B 35
SHEET 6 AA2 8 VAL B 127 LEU B 133 1 O GLN B 128 N PHE B 104
SHEET 7 AA2 8 LEU B 242 GLY B 247 1 O LEU B 243 N LEU B 130
SHEET 8 AA2 8 VAL B 269 LEU B 274 1 O LEU B 274 N TRP B 246
SHEET 1 AA3 8 ARG C 11 ASP C 18 0
SHEET 2 AA3 8 VAL C 21 GLY C 29 -1 O VAL C 27 N ARG C 11
SHEET 3 AA3 8 THR C 59 ALA C 63 -1 O LEU C 62 N TRP C 26
SHEET 4 AA3 8 ALA C 33 VAL C 37 1 N LEU C 36 O VAL C 61
SHEET 5 AA3 8 PHE C 104 HIS C 109 1 O SER C 105 N LEU C 35
SHEET 6 AA3 8 VAL C 127 LEU C 133 1 O GLN C 128 N PHE C 104
SHEET 7 AA3 8 LEU C 242 GLY C 247 1 O LEU C 243 N LEU C 130
SHEET 8 AA3 8 VAL C 269 LEU C 274 1 O LEU C 274 N TRP C 246
SHEET 1 AA4 8 ARG D 11 ASP D 18 0
SHEET 2 AA4 8 VAL D 21 GLY D 29 -1 O ILE D 23 N ILE D 15
SHEET 3 AA4 8 THR D 59 ALA D 63 -1 O LEU D 62 N TRP D 26
SHEET 4 AA4 8 ALA D 33 VAL D 37 1 N LEU D 36 O VAL D 61
SHEET 5 AA4 8 PHE D 104 HIS D 109 1 O SER D 105 N LEU D 35
SHEET 6 AA4 8 VAL D 127 LEU D 133 1 O LEU D 133 N ALA D 108
SHEET 7 AA4 8 LEU D 242 GLY D 247 1 O LEU D 243 N LEU D 130
SHEET 8 AA4 8 VAL D 269 LEU D 274 1 O LEU D 274 N TRP D 246
CISPEP 1 HIS A 40 PRO A 41 0 -5.39
CISPEP 2 ALA A 163 PRO A 164 0 8.90
CISPEP 3 HIS B 40 PRO B 41 0 -5.46
CISPEP 4 ALA B 163 PRO B 164 0 9.04
CISPEP 5 HIS C 40 PRO C 41 0 -5.70
CISPEP 6 ALA C 163 PRO C 164 0 8.61
CISPEP 7 HIS D 40 PRO D 41 0 -5.65
CISPEP 8 ALA D 163 PRO D 164 0 9.58
CRYST1 42.936 83.778 84.917 101.60 96.03 94.67 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.023290 0.001904 0.002928 0.00000
SCALE2 0.000000 0.011976 0.002591 0.00000
SCALE3 0.000000 0.000000 0.012116 0.00000
MTRIX1 1 -0.980004 -0.198956 0.002986 -0.63242 1
MTRIX2 1 -0.197962 0.976405 0.086277 0.17353 1
MTRIX3 1 -0.020081 0.083960 -0.996267 -0.33828 1
MTRIX1 2 -0.999699 -0.024447 -0.001871 18.11868 1
MTRIX2 2 0.024444 -0.999700 0.001820 37.60664 1
MTRIX3 2 -0.001915 0.001773 0.999997 0.11899 1
MTRIX1 3 0.983917 0.178345 0.009991 18.72350 1
MTRIX2 3 0.178507 -0.979696 -0.091278 37.47259 1
MTRIX3 3 -0.006491 0.091594 -0.995775 -0.30091 1
TER 4601 ALA A 299
TER 9314 GLN B 298
TER 13906 GLN C 298
TER 18606 GLY D 300
MASTER 452 0 0 64 32 0 0 1510109 4 0 100
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