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HEADER HYDROLASE 15-NOV-22 8HGV
TITLE CRYSTAL STRUCTURE OF MONOALKYL PHTHALATE HYDROLASE MEHPH
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOETHYLHEXYLPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GORDONIA;
SOURCE 3 ORGANISM_TAXID: 2053;
SOURCE 4 GENE: MEHPH;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.M.ZHANG,Y.J.WANG,Y.B.CHEN
REVDAT 1 15-MAR-23 8HGV 0
JRNL AUTH Y.CHEN,Y.WANG,Y.XU,J.SUN,L.YANG,C.FENG,J.WANG,Y.ZHOU,
JRNL AUTH 2 Z.M.ZHANG,Y.WANG
JRNL TITL MOLECULAR INSIGHTS INTO THE CATALYTIC MECHANISM OF
JRNL TITL 2 PLASTICIZER DEGRADATION BY A MONOALKYL PHTHALATE HYDROLASE.
JRNL REF COMMUN CHEM V. 6 45 2023
JRNL REFN ESSN 2399-3669
JRNL PMID 36859434
JRNL DOI 10.1038/S42004-023-00846-0
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692+SVN
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.75
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.344
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 24809
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.893
REMARK 3 FREE R VALUE TEST SET COUNT : 1214
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 10.0000 - 4.7671 0.99 2766 135 0.1706 0.1772
REMARK 3 2 4.7671 - 3.7913 1.00 2653 143 0.1506 0.2207
REMARK 3 3 3.7913 - 3.3143 1.00 2638 129 0.1903 0.2480
REMARK 3 4 3.3143 - 3.0122 1.00 2607 129 0.2225 0.2370
REMARK 3 5 3.0122 - 2.7969 1.00 2602 136 0.2482 0.3011
REMARK 3 6 2.7969 - 2.6323 1.00 2584 139 0.2522 0.2948
REMARK 3 7 2.6323 - 2.5007 1.00 2585 129 0.2656 0.2964
REMARK 3 8 2.5007 - 2.3920 1.00 2593 137 0.2716 0.3140
REMARK 3 9 2.3920 - 2.3001 1.00 2567 137 0.2896 0.3561
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) : 0.284
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.152
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.09
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 : 0.003 4371
REMARK 3 ANGLE : 0.708 5957
REMARK 3 CHIRALITY : 0.026 669
REMARK 3 PLANARITY : 0.003 774
REMARK 3 DIHEDRAL : 14.071 1506
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6933 56.2087 59.4369
REMARK 3 T TENSOR
REMARK 3 T11: 0.2945 T22: 0.3318
REMARK 3 T33: 0.3427 T12: 0.0255
REMARK 3 T13: 0.0099 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 1.8494 L22: 3.9638
REMARK 3 L33: 3.7363 L12: 0.7844
REMARK 3 L13: 0.5530 L23: 0.3012
REMARK 3 S TENSOR
REMARK 3 S11: -0.0132 S12: 0.0319 S13: 0.0973
REMARK 3 S21: 0.0694 S22: 0.0187 S23: 0.0324
REMARK 3 S31: -0.2233 S32: 0.0647 S33: 0.0099
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4315 42.9417 57.1073
REMARK 3 T TENSOR
REMARK 3 T11: 0.4418 T22: 0.4200
REMARK 3 T33: 0.3795 T12: 0.0469
REMARK 3 T13: 0.0725 T23: 0.0667
REMARK 3 L TENSOR
REMARK 3 L11: 3.7435 L22: 4.3977
REMARK 3 L33: 6.1070 L12: -0.5781
REMARK 3 L13: -1.0480 L23: -0.7552
REMARK 3 S TENSOR
REMARK 3 S11: -0.0459 S12: 0.3535 S13: 0.1145
REMARK 3 S21: -0.4364 S22: -0.0196 S23: 0.0523
REMARK 3 S31: 0.5034 S32: 0.2769 S33: 0.0774
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 165 THROUGH 196 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8911 43.2444 55.3650
REMARK 3 T TENSOR
REMARK 3 T11: 0.5820 T22: 0.6509
REMARK 3 T33: 0.9686 T12: -0.0766
REMARK 3 T13: -0.1182 T23: 0.1482
REMARK 3 L TENSOR
REMARK 3 L11: 2.6670 L22: 4.8153
REMARK 3 L33: 7.9133 L12: -3.3841
REMARK 3 L13: 2.6611 L23: -1.9682
REMARK 3 S TENSOR
REMARK 3 S11: 0.5134 S12: 0.3964 S13: -0.6879
REMARK 3 S21: -0.4820 S22: 0.5525 S23: 1.5293
REMARK 3 S31: 0.0089 S32: 0.1763 S33: -1.1696
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 197 THROUGH 226 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4822 55.9524 47.6181
REMARK 3 T TENSOR
REMARK 3 T11: 0.4163 T22: 0.4154
REMARK 3 T33: 0.3977 T12: -0.0634
REMARK 3 T13: -0.0540 T23: 0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 6.8790 L22: 3.2907
REMARK 3 L33: 9.7357 L12: -1.8155
REMARK 3 L13: -5.4411 L23: 0.7855
REMARK 3 S TENSOR
REMARK 3 S11: 0.2962 S12: 0.1987 S13: 0.3876
REMARK 3 S21: -0.2190 S22: 0.1345 S23: 0.0916
REMARK 3 S31: -0.5737 S32: -0.4594 S33: -0.3476
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 227 THROUGH 297 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.6584 36.3988 57.5242
REMARK 3 T TENSOR
REMARK 3 T11: 0.4401 T22: 0.4416
REMARK 3 T33: 0.3758 T12: 0.1257
REMARK 3 T13: -0.0030 T23: 0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 0.3166 L22: 3.5578
REMARK 3 L33: 3.7829 L12: 0.2403
REMARK 3 L13: -0.0968 L23: -1.8259
REMARK 3 S TENSOR
REMARK 3 S11: 0.1060 S12: 0.0709 S13: -0.1438
REMARK 3 S21: -0.4085 S22: -0.1627 S23: -0.1250
REMARK 3 S31: 0.3562 S32: 0.3225 S33: 0.0614
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 298 THROUGH 311 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9290 41.2505 73.5063
REMARK 3 T TENSOR
REMARK 3 T11: 0.4867 T22: 0.3522
REMARK 3 T33: 0.3892 T12: -0.0469
REMARK 3 T13: 0.0227 T23: 0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 6.4493 L22: 8.5838
REMARK 3 L33: 8.2961 L12: -0.5481
REMARK 3 L13: 0.5159 L23: -0.9806
REMARK 3 S TENSOR
REMARK 3 S11: 0.1206 S12: -0.6055 S13: 0.0389
REMARK 3 S21: 0.9640 S22: 0.0023 S23: 0.5202
REMARK 3 S31: 0.3880 S32: -0.0172 S33: -0.1064
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 24 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3796 16.5072 32.6182
REMARK 3 T TENSOR
REMARK 3 T11: 0.4083 T22: 0.6096
REMARK 3 T33: 0.5240 T12: -0.0526
REMARK 3 T13: 0.0067 T23: 0.1746
REMARK 3 L TENSOR
REMARK 3 L11: 4.6738 L22: 4.2411
REMARK 3 L33: 2.9634 L12: -1.8772
REMARK 3 L13: 0.8711 L23: -1.0299
REMARK 3 S TENSOR
REMARK 3 S11: -0.0541 S12: -0.7751 S13: -0.8395
REMARK 3 S21: 0.4561 S22: 0.2275 S23: 0.4939
REMARK 3 S31: 0.1124 S32: -0.5615 S33: -0.1471
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 165 THROUGH 226 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.8256 8.8746 26.4374
REMARK 3 T TENSOR
REMARK 3 T11: 0.4961 T22: 0.4261
REMARK 3 T33: 0.5309 T12: 0.0263
REMARK 3 T13: 0.0133 T23: 0.0460
REMARK 3 L TENSOR
REMARK 3 L11: 5.7066 L22: 3.9153
REMARK 3 L33: 5.0526 L12: -0.5008
REMARK 3 L13: 1.0101 L23: -0.8022
REMARK 3 S TENSOR
REMARK 3 S11: 0.2143 S12: -0.3445 S13: -0.3149
REMARK 3 S21: 0.0651 S22: -0.3564 S23: -0.1571
REMARK 3 S31: 0.1745 S32: 0.1019 S33: 0.1894
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 227 THROUGH 311 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6414 21.3951 18.2897
REMARK 3 T TENSOR
REMARK 3 T11: 0.4099 T22: 0.3379
REMARK 3 T33: 0.4469 T12: -0.0200
REMARK 3 T13: -0.0720 T23: 0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 2.7554 L22: 4.2698
REMARK 3 L33: 3.3642 L12: -1.6607
REMARK 3 L13: 0.7375 L23: -0.9426
REMARK 3 S TENSOR
REMARK 3 S11: 0.3794 S12: 0.1021 S13: -0.6325
REMARK 3 S21: -0.2555 S22: -0.2042 S23: 0.4845
REMARK 3 S31: 0.4846 S32: -0.1222 S33: -0.1367
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 8HGV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-22.
REMARK 100 THE DEPOSITION ID IS D_1300033595.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-JUL-21
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 : CAMD
REMARK 200 BEAMLINE : GCPCC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 74613
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 106.690
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL PH 7.2, 17% (W/V) PEG
REMARK 280 3350 AND 200 MM CALCIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 289K
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 38.84500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 27.23000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.06000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 27.23000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.84500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.06000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 54.46000
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 THR A 161
REMARK 465 ASP A 162
REMARK 465 GLY A 175
REMARK 465 GLY A 176
REMARK 465 VAL B 159
REMARK 465 GLY B 160
REMARK 465 THR B 161
REMARK 465 ASP B 162
REMARK 465 GLY B 193
REMARK 465 ASP B 194
REMARK 465 LEU B 195
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 MET A 163 CG SD CE
REMARK 470 GLU A 167 CG CD OE1 OE2
REMARK 470 ARG A 168 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 171 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 179 CG CD OE1 OE2
REMARK 470 ASP A 194 CG OD1 OD2
REMARK 470 GLU A 197 CG CD OE1 OE2
REMARK 470 PHE B 24 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN B 33 CG CD OE1 NE2
REMARK 470 ASP B 39 CG OD1 OD2
REMARK 470 ASP B 42 CG OD1 OD2
REMARK 470 GLU B 70 CG CD OE1 OE2
REMARK 470 GLU B 88 CG CD OE1 OE2
REMARK 470 GLU B 96 CG CD OE1 OE2
REMARK 470 LYS B 117 CG CD CE NZ
REMARK 470 MET B 163 CG SD CE
REMARK 470 ASN B 191 CG OD1 ND2
REMARK 470 GLU B 192 CG CD OE1 OE2
REMARK 470 GLU B 197 CG CD OE1 OE2
REMARK 470 GLU B 210 CG CD OE1 OE2
REMARK 470 LYS B 211 CG CD CE NZ
REMARK 470 GLU B 224 CG CD OE1 OE2
REMARK 470 GLU B 225 CG CD OE1 OE2
REMARK 470 GLU B 299 CG CD OE1 OE2
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 OD1 ASN A 287 O HOH A 401 1.86
REMARK 500 O HOH A 444 O HOH A 451 1.88
REMARK 500 NH2 ARG B 126 O HOH B 401 2.02
REMARK 500 O LEU B 311 O HOH B 402 2.09
REMARK 500 N PHE B 24 O HOH B 403 2.14
REMARK 500 OG SER A 125 O HOH A 402 2.15
REMARK 500 O HOH A 447 O HOH A 453 2.19
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 SER A 125 -124.81 56.31
REMARK 500 ASN A 191 59.13 -90.93
REMARK 500 HIS A 226 -54.59 -121.99
REMARK 500 ASP A 244 -91.20 -110.80
REMARK 500 SER B 125 -130.83 53.25
REMARK 500 VAL B 190 -53.07 -120.46
REMARK 500 ASP B 244 -94.43 -103.88
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8HGV A 24 311 UNP Q2MHH5 Q2MHH5_9ACTN 24 311
DBREF 8HGV B 24 311 UNP Q2MHH5 Q2MHH5_9ACTN 24 311
SEQRES 1 A 288 PHE HIS THR VAL ASP VAL LYS GLY VAL GLN THR ARG TYR
SEQRES 2 A 288 PHE ASP ASP GLY GLN ASP LYS ASP PRO ILE LEU LEU ILE
SEQRES 3 A 288 HIS GLY GLY HIS PHE GLY PHE PHE ILE PRO VAL GLY ILE
SEQRES 4 A 288 GLU SER TRP GLY ASN VAL LEU GLU ASP PHE GLY GLU TYR
SEQRES 5 A 288 GLY ARG VAL LEU ALA VAL ASP LYS LEU GLY GLN GLY GLU
SEQRES 6 A 288 THR GLY LEU PRO LEU ASN ASP GLU ASP TRP THR VAL ASP
SEQRES 7 A 288 ALA VAL ALA GLU HIS VAL ALA ASN PHE ALA THR GLN LEU
SEQRES 8 A 288 GLY LEU LYS ASN LEU THR LEU VAL GLY HIS SER ARG GLY
SEQRES 9 A 288 GLY MET THR ALA VAL LEU LEU ALA LEU LYS TYR PRO GLU
SEQRES 10 A 288 MET VAL LYS LYS LEU VAL ILE ILE SER SER ALA THR ALA
SEQRES 11 A 288 ALA PRO ALA PRO PRO VAL GLY THR ASP MET ASP PHE TYR
SEQRES 12 A 288 GLU ARG VAL GLU ARG THR ALA PRO GLY GLY SER ALA GLU
SEQRES 13 A 288 LEU ILE ARG HIS TYR HIS ALA ALA GLN ALA VAL ASN GLU
SEQRES 14 A 288 GLY ASP LEU PRO GLU ASP TYR ILE GLY ILE ALA THR LYS
SEQRES 15 A 288 TRP LEU GLU SER GLU LYS GLN LEU ASP ALA VAL ALA GLY
SEQRES 16 A 288 TYR ALA ARG ASN ALA GLU GLU HIS TRP LEU PRO SER LEU
SEQRES 17 A 288 SER GLU GLY ARG ARG TRP VAL GLN GLU ARG LEU ALA ASP
SEQRES 18 A 288 ALA GLY ILE PRO VAL PRO THR LEU VAL VAL TRP GLY VAL
SEQRES 19 A 288 ASN ASP ARG SER ALA PRO VAL SER MET GLY LYS GLY LEU
SEQRES 20 A 288 PHE ASP LEU ILE ALA ALA ASN THR LEU ASP SER SER LEU
SEQRES 21 A 288 TYR LEU ILE ASN ASN ALA GLY HIS HIS VAL PHE SER ASP
SEQRES 22 A 288 GLN ARG GLU LYS PHE ASN ALA ALA VAL GLY ALA PHE ILE
SEQRES 23 A 288 SER LEU
SEQRES 1 B 288 PHE HIS THR VAL ASP VAL LYS GLY VAL GLN THR ARG TYR
SEQRES 2 B 288 PHE ASP ASP GLY GLN ASP LYS ASP PRO ILE LEU LEU ILE
SEQRES 3 B 288 HIS GLY GLY HIS PHE GLY PHE PHE ILE PRO VAL GLY ILE
SEQRES 4 B 288 GLU SER TRP GLY ASN VAL LEU GLU ASP PHE GLY GLU TYR
SEQRES 5 B 288 GLY ARG VAL LEU ALA VAL ASP LYS LEU GLY GLN GLY GLU
SEQRES 6 B 288 THR GLY LEU PRO LEU ASN ASP GLU ASP TRP THR VAL ASP
SEQRES 7 B 288 ALA VAL ALA GLU HIS VAL ALA ASN PHE ALA THR GLN LEU
SEQRES 8 B 288 GLY LEU LYS ASN LEU THR LEU VAL GLY HIS SER ARG GLY
SEQRES 9 B 288 GLY MET THR ALA VAL LEU LEU ALA LEU LYS TYR PRO GLU
SEQRES 10 B 288 MET VAL LYS LYS LEU VAL ILE ILE SER SER ALA THR ALA
SEQRES 11 B 288 ALA PRO ALA PRO PRO VAL GLY THR ASP MET ASP PHE TYR
SEQRES 12 B 288 GLU ARG VAL GLU ARG THR ALA PRO GLY GLY SER ALA GLU
SEQRES 13 B 288 LEU ILE ARG HIS TYR HIS ALA ALA GLN ALA VAL ASN GLU
SEQRES 14 B 288 GLY ASP LEU PRO GLU ASP TYR ILE GLY ILE ALA THR LYS
SEQRES 15 B 288 TRP LEU GLU SER GLU LYS GLN LEU ASP ALA VAL ALA GLY
SEQRES 16 B 288 TYR ALA ARG ASN ALA GLU GLU HIS TRP LEU PRO SER LEU
SEQRES 17 B 288 SER GLU GLY ARG ARG TRP VAL GLN GLU ARG LEU ALA ASP
SEQRES 18 B 288 ALA GLY ILE PRO VAL PRO THR LEU VAL VAL TRP GLY VAL
SEQRES 19 B 288 ASN ASP ARG SER ALA PRO VAL SER MET GLY LYS GLY LEU
SEQRES 20 B 288 PHE ASP LEU ILE ALA ALA ASN THR LEU ASP SER SER LEU
SEQRES 21 B 288 TYR LEU ILE ASN ASN ALA GLY HIS HIS VAL PHE SER ASP
SEQRES 22 B 288 GLN ARG GLU LYS PHE ASN ALA ALA VAL GLY ALA PHE ILE
SEQRES 23 B 288 SER LEU
FORMUL 3 HOH *73(H2 O)
HELIX 1 AA1 GLY A 61 GLY A 66 5 6
HELIX 2 AA2 ASN A 67 PHE A 72 1 6
HELIX 3 AA3 GLY A 73 TYR A 75 5 3
HELIX 4 AA4 ASN A 94 TRP A 98 5 5
HELIX 5 AA5 THR A 99 LEU A 114 1 16
HELIX 6 AA6 SER A 125 TYR A 138 1 14
HELIX 7 AA7 ASP A 164 THR A 172 1 9
HELIX 8 AA8 ALA A 178 ALA A 189 1 12
HELIX 9 AA9 PRO A 196 GLU A 208 1 13
HELIX 10 AB1 SER A 209 ALA A 223 1 15
HELIX 11 AB2 HIS A 226 ALA A 243 1 18
HELIX 12 AB3 PRO A 263 ALA A 276 1 14
HELIX 13 AB4 HIS A 292 GLN A 297 1 6
HELIX 14 AB5 GLN A 297 LEU A 311 1 15
HELIX 15 AB6 GLY B 61 GLY B 66 5 6
HELIX 16 AB7 ASN B 67 PHE B 72 1 6
HELIX 17 AB8 GLY B 73 TYR B 75 5 3
HELIX 18 AB9 ASN B 94 TRP B 98 5 5
HELIX 19 AC1 THR B 99 GLY B 115 1 17
HELIX 20 AC2 SER B 125 TYR B 138 1 14
HELIX 21 AC3 ASP B 164 THR B 172 1 9
HELIX 22 AC4 SER B 177 ALA B 189 1 13
HELIX 23 AC5 GLU B 197 GLU B 208 1 12
HELIX 24 AC6 SER B 209 ALA B 223 1 15
HELIX 25 AC7 HIS B 226 ALA B 243 1 18
HELIX 26 AC8 PRO B 263 ALA B 276 1 14
HELIX 27 AC9 HIS B 292 GLN B 297 1 6
HELIX 28 AD1 GLN B 297 SER B 310 1 14
SHEET 1 AA1 8 HIS A 25 VAL A 29 0
SHEET 2 AA1 8 VAL A 32 ASP A 38 -1 O VAL A 32 N VAL A 29
SHEET 3 AA1 8 ARG A 77 VAL A 81 -1 O ALA A 80 N PHE A 37
SHEET 4 AA1 8 PRO A 45 ILE A 49 1 N ILE A 46 O LEU A 79
SHEET 5 AA1 8 LEU A 119 HIS A 124 1 O VAL A 122 N ILE A 49
SHEET 6 AA1 8 VAL A 142 ILE A 148 1 O ILE A 148 N GLY A 123
SHEET 7 AA1 8 THR A 251 GLY A 256 1 O VAL A 254 N ILE A 147
SHEET 8 AA1 8 SER A 281 ILE A 286 1 O TYR A 284 N VAL A 253
SHEET 1 AA2 8 HIS B 25 ASP B 28 0
SHEET 2 AA2 8 GLN B 33 ASP B 38 -1 O THR B 34 N VAL B 27
SHEET 3 AA2 8 ARG B 77 VAL B 81 -1 O ALA B 80 N PHE B 37
SHEET 4 AA2 8 PRO B 45 ILE B 49 1 N ILE B 46 O LEU B 79
SHEET 5 AA2 8 LEU B 119 HIS B 124 1 O VAL B 122 N ILE B 49
SHEET 6 AA2 8 VAL B 142 ILE B 148 1 O ILE B 148 N GLY B 123
SHEET 7 AA2 8 THR B 251 GLY B 256 1 O LEU B 252 N ILE B 147
SHEET 8 AA2 8 SER B 281 ILE B 286 1 O ILE B 286 N TRP B 255
CISPEP 1 ASP A 39 GLY A 40 0 -10.34
CISPEP 2 ASP B 39 GLY B 40 0 -6.94
CISPEP 3 GLY B 175 GLY B 176 0 4.71
CISPEP 4 GLY B 176 SER B 177 0 4.26
CRYST1 77.690 128.120 54.460 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 0.012872 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007805 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018362 0.00000
TER 2165 LEU A 311
TER 4270 LEU B 311
MASTER 428 0 0 28 16 0 0 6 4341 2 0 46
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