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HEADER HYDROLASE 23-MAR-22 7ZBA
TITLE HALOTAG WITH ME-TRAQ-G LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS HALOTAG, HALOALKANE DEHALOGENASE, SILICON RHODAMINE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HUBNER,P.RIVERA-FUENTES,F.POJER,K.LAU
REVDAT 1 01-FEB-23 7ZBA 0
JRNL AUTH S.HUBNER,G.QUARGNALI,S.THALLMAIR,P.RIVERA-FUENTES
JRNL TITL A LOCALLY ACTIVATABLE SENSOR FOR ROBUST QUANTIFICATION OF
JRNL TITL 2 ORGANELLAR GLUTATHIONE
JRNL REF BIORXIV 2022
JRNL REFN ISSN 2692-8205
JRNL DOI 10.1101/2022.04.01.486692
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.V.AFONINE,R.W.GROSSE-KUNSTLEVE,N.ECHOLS,J.J.HEADD,
REMARK 1 AUTH 2 N.W.MORIARTY,M.MUSTYAKIMOV,T.C.TERWILLIGER,A.URZHUMTSEV,
REMARK 1 AUTH 3 P.H.ZWART,P.D.ADAMS
REMARK 1 TITL TOWARDS AUTOMATED CRYSTALLOGRAPHIC STRUCTURE REFINEMENT WITH
REMARK 1 TITL 2 PHENIX.REFINE.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 68 352 2012
REMARK 1 REFN ESSN 1399-0047
REMARK 1 PMID 22505256
REMARK 1 DOI 10.1107/S0907444912001308
REMARK 1 REFERENCE 2
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 D STRUCT V. 75 861 2019
REMARK 1 REF 2 BIOL
REMARK 1 REFN ISSN 2059-7983
REMARK 1 PMID 31588918
REMARK 1 DOI 10.1107/S2059798319011471
REMARK 2
REMARK 2 RESOLUTION. 1.23 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
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) : 1.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 168606
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.236
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8427
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 44.5600 - 3.8200 1.00 5753 303 0.2339 0.2404
REMARK 3 2 3.8200 - 3.0300 1.00 5505 289 0.2279 0.2614
REMARK 3 3 3.0300 - 2.6500 1.00 5449 287 0.2221 0.2455
REMARK 3 4 2.6500 - 2.4100 1.00 5427 285 0.2183 0.2365
REMARK 3 5 2.4100 - 2.2300 1.00 5389 284 0.2175 0.2199
REMARK 3 6 2.2300 - 2.1000 1.00 5373 283 0.2179 0.2254
REMARK 3 7 2.1000 - 2.0000 1.00 5395 284 0.2227 0.2501
REMARK 3 8 2.0000 - 1.9100 1.00 5347 282 0.2227 0.2342
REMARK 3 9 1.9100 - 1.8400 1.00 5367 282 0.2251 0.2556
REMARK 3 10 1.8400 - 1.7700 1.00 5294 279 0.2297 0.2544
REMARK 3 11 1.7700 - 1.7200 1.00 5363 282 0.2326 0.2609
REMARK 3 12 1.7200 - 1.6700 1.00 5356 283 0.2305 0.2411
REMARK 3 13 1.6700 - 1.6200 1.00 5310 279 0.2339 0.2812
REMARK 3 14 1.6200 - 1.5800 1.00 5326 280 0.2397 0.2554
REMARK 3 15 1.5800 - 1.5500 1.00 5333 279 0.2490 0.2935
REMARK 3 16 1.5500 - 1.5200 1.00 5340 281 0.2482 0.2922
REMARK 3 17 1.5200 - 1.4900 1.00 5270 278 0.2558 0.2845
REMARK 3 18 1.4900 - 1.4600 1.00 5354 282 0.2557 0.2745
REMARK 3 19 1.4600 - 1.4300 1.00 5237 275 0.2530 0.2872
REMARK 3 20 1.4300 - 1.4100 1.00 5336 281 0.2548 0.2604
REMARK 3 21 1.4100 - 1.3800 1.00 5273 278 0.2633 0.2894
REMARK 3 22 1.3800 - 1.3600 1.00 5369 282 0.2721 0.2888
REMARK 3 23 1.3600 - 1.3400 1.00 5249 276 0.2764 0.3277
REMARK 3 24 1.3400 - 1.3200 1.00 5339 281 0.2787 0.3033
REMARK 3 25 1.3200 - 1.3100 1.00 5249 276 0.2846 0.3155
REMARK 3 26 1.3100 - 1.2900 1.00 5321 279 0.2932 0.3215
REMARK 3 27 1.2900 - 1.2700 1.00 5284 279 0.3050 0.3276
REMARK 3 28 1.2700 - 1.2600 1.00 5287 278 0.3166 0.3246
REMARK 3 29 1.2600 - 1.2400 1.00 5289 278 0.3351 0.3562
REMARK 3 30 1.2400 - 1.2300 0.94 4995 262 0.3476 0.3619
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.813
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.23
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 4997
REMARK 3 ANGLE : 0.865 6829
REMARK 3 CHIRALITY : 0.071 708
REMARK 3 PLANARITY : 0.007 885
REMARK 3 DIHEDRAL : 8.532 679
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1134 -19.0094 -20.3627
REMARK 3 T TENSOR
REMARK 3 T11: 0.1109 T22: 0.1286
REMARK 3 T33: 0.1021 T12: 0.0060
REMARK 3 T13: 0.0104 T23: 0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 0.2230 L22: 0.4753
REMARK 3 L33: 0.1681 L12: 0.0695
REMARK 3 L13: -0.0482 L23: 0.1744
REMARK 3 S TENSOR
REMARK 3 S11: 0.0042 S12: 0.0192 S13: 0.0204
REMARK 3 S21: 0.0085 S22: 0.0059 S23: 0.0226
REMARK 3 S31: 0.0148 S32: -0.0450 S33: -0.0086
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 4 through 29 or
REMARK 3 resid 31 through 131 or resid 133 through
REMARK 3 138 or resid 140 through 256 or resid 258
REMARK 3 through 260 or resid 262 through 284 or
REMARK 3 resid 286 through 293 or resid 304
REMARK 3 through 309))
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 4 through 29 or
REMARK 3 resid 31 through 88 or (resid 89 through
REMARK 3 90 and (name N or name CA or name C or
REMARK 3 name O or name CB )) or resid 91 through
REMARK 3 131 or resid 133 through 138 or resid 140
REMARK 3 through 256 or resid 258 through 260 or
REMARK 3 resid 262 through 284 or resid 286
REMARK 3 through 293 or resid 303 through 309))
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7ZBA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAR-22.
REMARK 100 THE DEPOSITION ID IS D_1292121661.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-21
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 : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 325063
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.230
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.30
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 8.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.150
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: 6U32
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% V/V PEG SMEAR MEDIUM, 0.1 M TRIS,
REMARK 280 PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 280K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 22.18150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.82600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.74950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.82600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.18150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.74950
REMARK 290 SMTRY3 4 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: 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 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 1
REMARK 465 ALA A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 294
REMARK 465 ILE A 295
REMARK 465 SER A 296
REMARK 465 GLY A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 294
REMARK 465 ILE B 295
REMARK 465 SER B 296
REMARK 465 GLY B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 89 CG OD1 OD2
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 CG ASP A 106 C31 IL7 A 405 2.17
REMARK 500 OD2 ASP A 106 C30 IL7 A 405 2.17
REMARK 500 OE1 GLU A 224 O HOH A 501 2.17
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 O HOH A 600 O HOH A 701 1455 1.88
REMARK 500 O HOH A 516 O HOH B 684 3454 2.04
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 9 37.64 -90.37
REMARK 500 PRO A 42 49.24 -105.33
REMARK 500 THR A 43 -161.51 -101.98
REMARK 500 GLU A 98 -93.38 -107.40
REMARK 500 ASP A 106 -130.23 54.90
REMARK 500 ASN A 119 53.72 -142.38
REMARK 500 ARG A 153 43.86 -88.45
REMARK 500 ASP A 156 -76.61 -100.40
REMARK 500 VAL A 245 -75.59 -132.42
REMARK 500 LEU A 271 -98.20 -118.39
REMARK 500 PRO B 9 38.24 -88.42
REMARK 500 PRO B 42 48.77 -105.88
REMARK 500 THR B 43 -161.42 -101.87
REMARK 500 GLU B 98 -92.50 -107.51
REMARK 500 ASP B 106 -131.21 54.57
REMARK 500 ASN B 119 52.97 -141.94
REMARK 500 ARG B 153 42.24 -88.91
REMARK 500 ASP B 156 -74.48 -98.26
REMARK 500 VAL B 245 -73.78 -131.89
REMARK 500 LEU B 271 -97.78 -116.96
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 732 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 733 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A 734 DISTANCE = 7.02 ANGSTROMS
REMARK 525 HOH A 735 DISTANCE = 7.24 ANGSTROMS
REMARK 525 HOH B 741 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH B 742 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH B 743 DISTANCE = 6.12 ANGSTROMS
DBREF 7ZBA A 1 290 UNP P0A3G3 DHAA_RHOSO 1 290
DBREF 7ZBA B 1 290 UNP P0A3G3 DHAA_RHOSO 1 290
SEQADV 7ZBA ALA A 2 UNP P0A3G3 SER 2 ENGINEERED MUTATION
SEQADV 7ZBA VAL A 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7ZBA THR A 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7ZBA GLY A 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7ZBA PHE A 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7ZBA MET A 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7ZBA PHE A 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7ZBA THR A 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7ZBA LYS A 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7ZBA VAL A 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7ZBA THR A 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7ZBA MET A 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7ZBA GLY A 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7ZBA ASN A 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7ZBA GLU A 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7ZBA ASP A 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7ZBA LYS A 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7ZBA ALA A 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7ZBA ASN A 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7ZBA LEU A 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7ZBA SER A 291 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA THR A 292 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA LEU A 293 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA GLU A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA ILE A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA SER A 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA GLY A 297 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA HIS A 298 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA HIS A 299 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA HIS A 300 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA HIS A 301 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA HIS A 302 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA HIS A 303 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA ALA B 2 UNP P0A3G3 SER 2 ENGINEERED MUTATION
SEQADV 7ZBA VAL B 47 UNP P0A3G3 LEU 47 ENGINEERED MUTATION
SEQADV 7ZBA THR B 58 UNP P0A3G3 SER 58 ENGINEERED MUTATION
SEQADV 7ZBA GLY B 78 UNP P0A3G3 ASP 78 ENGINEERED MUTATION
SEQADV 7ZBA PHE B 87 UNP P0A3G3 TYR 87 ENGINEERED MUTATION
SEQADV 7ZBA MET B 88 UNP P0A3G3 LEU 88 ENGINEERED MUTATION
SEQADV 7ZBA PHE B 128 UNP P0A3G3 CYS 128 ENGINEERED MUTATION
SEQADV 7ZBA THR B 155 UNP P0A3G3 ALA 155 ENGINEERED MUTATION
SEQADV 7ZBA LYS B 160 UNP P0A3G3 GLU 160 ENGINEERED MUTATION
SEQADV 7ZBA VAL B 167 UNP P0A3G3 ALA 167 ENGINEERED MUTATION
SEQADV 7ZBA THR B 172 UNP P0A3G3 ALA 172 ENGINEERED MUTATION
SEQADV 7ZBA MET B 175 UNP P0A3G3 LYS 175 ENGINEERED MUTATION
SEQADV 7ZBA GLY B 176 UNP P0A3G3 CYS 176 ENGINEERED MUTATION
SEQADV 7ZBA ASN B 195 UNP P0A3G3 LYS 195 ENGINEERED MUTATION
SEQADV 7ZBA GLU B 224 UNP P0A3G3 ALA 224 ENGINEERED MUTATION
SEQADV 7ZBA ASP B 227 UNP P0A3G3 ASN 227 ENGINEERED MUTATION
SEQADV 7ZBA LYS B 257 UNP P0A3G3 GLU 257 ENGINEERED MUTATION
SEQADV 7ZBA ALA B 264 UNP P0A3G3 THR 264 ENGINEERED MUTATION
SEQADV 7ZBA ASN B 272 UNP P0A3G3 HIS 272 ENGINEERED MUTATION
SEQADV 7ZBA LEU B 273 UNP P0A3G3 TYR 273 ENGINEERED MUTATION
SEQADV 7ZBA SER B 291 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA THR B 292 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA LEU B 293 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA GLU B 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA ILE B 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA SER B 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA GLY B 297 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA HIS B 298 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA HIS B 299 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA HIS B 300 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA HIS B 301 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA HIS B 302 UNP P0A3G3 EXPRESSION TAG
SEQADV 7ZBA HIS B 303 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 303 MET ALA GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 303 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 A 303 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 303 GLY ASN PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE
SEQRES 5 A 303 PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 303 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY
SEQRES 7 A 303 TYR PHE PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE
SEQRES 8 A 303 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 303 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 303 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 A 303 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 A 303 PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP
SEQRES 13 A 303 VAL GLY ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE
SEQRES 14 A 303 GLU GLY THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR
SEQRES 15 A 303 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN
SEQRES 16 A 303 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 303 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 A 303 VAL GLU GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 303 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 A 303 PRO PRO ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO
SEQRES 21 A 303 ASN CYS LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU
SEQRES 22 A 303 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 A 303 ALA ARG TRP LEU SER THR LEU GLU ILE SER GLY HIS HIS
SEQRES 24 A 303 HIS HIS HIS HIS
SEQRES 1 B 303 MET ALA GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 B 303 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 B 303 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 B 303 GLY ASN PRO THR SER SER TYR VAL TRP ARG ASN ILE ILE
SEQRES 5 B 303 PRO HIS VAL ALA PRO THR HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 B 303 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU GLY
SEQRES 7 B 303 TYR PHE PHE ASP ASP HIS VAL ARG PHE MET ASP ALA PHE
SEQRES 8 B 303 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 B 303 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 B 303 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU
SEQRES 11 B 303 PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 B 303 PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR THR ASP
SEQRES 13 B 303 VAL GLY ARG LYS LEU ILE ILE ASP GLN ASN VAL PHE ILE
SEQRES 14 B 303 GLU GLY THR LEU PRO MET GLY VAL VAL ARG PRO LEU THR
SEQRES 15 B 303 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU ASN
SEQRES 16 B 303 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 B 303 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 B 303 VAL GLU GLU TYR MET ASP TRP LEU HIS GLN SER PRO VAL
SEQRES 19 B 303 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 B 303 PRO PRO ALA GLU ALA ALA ARG LEU ALA LYS SER LEU PRO
SEQRES 21 B 303 ASN CYS LYS ALA VAL ASP ILE GLY PRO GLY LEU ASN LEU
SEQRES 22 B 303 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 B 303 ALA ARG TRP LEU SER THR LEU GLU ILE SER GLY HIS HIS
SEQRES 24 B 303 HIS HIS HIS HIS
HET GOL A 401 13
HET GOL A 402 11
HET GOL A 403 14
HET GOL A 404 14
HET IL7 A 405 86
HET CL A 406 1
HET IL7 B 401 86
HET GOL B 402 13
HET GOL B 403 14
HET GOL B 404 13
HET GOL B 405 14
HET CL B 406 1
HET GOL B 407 14
HETNAM GOL GLYCEROL
HETNAM IL7 4-(7-AZANYL-5,5-DIMETHYL-3-METHYLIMINO-
HETNAM 2 IL7 BENZO[B][1]BENZOSILIN-10-YL)-N-[2-[2-(6-
HETNAM 3 IL7 CHLORANYLHEXOXY)ETHOXY]ETHYL]-3-METHYL-BENZAMIDE
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN IL7 HALOTAG WITH ME-TRAQ-G LIGAND
FORMUL 3 GOL 9(C3 H8 O3)
FORMUL 7 IL7 2(C34 H44 CL N3 O3 SI)
FORMUL 8 CL 2(CL 1-)
FORMUL 16 HOH *478(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 ASP A 156 ILE A 163 1 8
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 SER A 291 1 14
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 ASP B 156 ILE B 163 1 8
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 SER B 291 1 14
SHEET 1 AA1 8 HIS A 13 VAL A 17 0
SHEET 2 AA1 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
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 VAL A 265 N LEU A 238
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 VAL B 265 N LEU B 238
LINK OD2 ASP A 106 C31 IL7 A 405 1555 1555 1.37
LINK OD2 ASP B 106 C31 IL7 B 401 1555 1555 1.38
CISPEP 1 ASN A 41 PRO A 42 0 -0.30
CISPEP 2 GLU A 214 PRO A 215 0 -7.60
CISPEP 3 THR A 242 PRO A 243 0 3.64
CISPEP 4 ASN B 41 PRO B 42 0 -0.80
CISPEP 5 GLU B 214 PRO B 215 0 -5.04
CISPEP 6 THR B 242 PRO B 243 0 3.12
CRYST1 44.363 81.499 159.652 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.022541 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012270 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006264 0.00000
TER 4653 LEU A 293
TER 9299 LEU B 293
MASTER 414 0 13 36 16 0 0 6 5269 2 292 48
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