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HEADER HYDROLASE 25-AUG-20 7A6G
TITLE STRUCTURAL CHARACTERIZATION OF L-PROLINE AMIDE HYDROLASE FROM
TITLE 2 PSEUDOMONAS SYRINGAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE PROLINE IMINOPEPTIDASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: ALPHA/BETA HYDROLASE FOLD, HYDROLASE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS SYRINGAE PV. TOMATO;
SOURCE 3 ORGANISM_TAXID: 323;
SOURCE 4 GENE: ALO36_01328;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET22B+
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MARTINEZ-RODRIGUEZ,J.A.GAVIRA
REVDAT 1 06-OCT-21 7A6G 0
JRNL AUTH S.MARTINEZ-RODRIGUEZ,J.A.GAVIRA
JRNL TITL STRUCTURAL CHARACTERIZATION OF L-PROLINE AMIDE HYDROLASE
JRNL TITL 2 FROM PSEUDOMONAS SYRINGAE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 20563
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1089
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 42.7310 - 3.8993 1.00 2602 123 0.1408 0.1801
REMARK 3 2 3.8993 - 3.0952 1.00 2460 123 0.1339 0.2012
REMARK 3 3 3.0952 - 2.7041 1.00 2432 160 0.1579 0.2292
REMARK 3 4 2.7041 - 2.4569 1.00 2404 132 0.1594 0.2421
REMARK 3 5 2.4569 - 2.2808 1.00 2407 133 0.1609 0.2321
REMARK 3 6 2.2808 - 2.1463 1.00 2388 129 0.1749 0.2462
REMARK 3 7 2.1463 - 2.0388 1.00 2396 140 0.2026 0.2867
REMARK 3 8 2.0388 - 1.9501 1.00 2385 149 0.2061 0.2600
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.030
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.67
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 34 )
REMARK 3 ORIGIN FOR THE GROUP (A): -33.3209 -13.6836 10.9010
REMARK 3 T TENSOR
REMARK 3 T11: 0.1245 T22: 0.1257
REMARK 3 T33: 0.1476 T12: 0.0267
REMARK 3 T13: -0.0009 T23: -0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 0.0462 L22: 0.1114
REMARK 3 L33: 0.1559 L12: 0.0063
REMARK 3 L13: 0.0624 L23: -0.0794
REMARK 3 S TENSOR
REMARK 3 S11: 0.1100 S12: -0.1059 S13: -0.1129
REMARK 3 S21: 0.1427 S22: -0.0423 S23: 0.1285
REMARK 3 S31: 0.0727 S32: -0.0234 S33: 0.0133
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 35 THROUGH 141 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.0908 -2.1366 8.0628
REMARK 3 T TENSOR
REMARK 3 T11: 0.0937 T22: 0.0823
REMARK 3 T33: 0.0880 T12: 0.0016
REMARK 3 T13: -0.0000 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.5452 L22: 0.3131
REMARK 3 L33: 0.2134 L12: -0.0783
REMARK 3 L13: -0.2274 L23: -0.1552
REMARK 3 S TENSOR
REMARK 3 S11: -0.0052 S12: 0.0251 S13: 0.0790
REMARK 3 S21: 0.0374 S22: 0.0473 S23: 0.0347
REMARK 3 S31: -0.0644 S32: 0.0220 S33: 0.0002
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 142 THROUGH 189 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2878 10.5368 -16.2947
REMARK 3 T TENSOR
REMARK 3 T11: 0.1775 T22: 0.1109
REMARK 3 T33: 0.1050 T12: 0.0448
REMARK 3 T13: 0.0095 T23: 0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.0762 L22: 0.1583
REMARK 3 L33: 0.1430 L12: -0.0688
REMARK 3 L13: -0.0035 L23: 0.0009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0631 S12: 0.0171 S13: 0.0961
REMARK 3 S21: -0.2352 S22: -0.1456 S23: -0.1137
REMARK 3 S31: -0.1243 S32: 0.0051 S33: -0.0033
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 190 THROUGH 275 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.5913 2.3978 -2.9480
REMARK 3 T TENSOR
REMARK 3 T11: 0.0980 T22: 0.0936
REMARK 3 T33: 0.1087 T12: -0.0022
REMARK 3 T13: 0.0064 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.1220 L22: 0.6503
REMARK 3 L33: 0.5942 L12: -0.1709
REMARK 3 L13: -0.1249 L23: -0.2791
REMARK 3 S TENSOR
REMARK 3 S11: 0.0204 S12: 0.0607 S13: 0.0236
REMARK 3 S21: -0.0685 S22: -0.0069 S23: -0.0482
REMARK 3 S31: -0.0382 S32: 0.0073 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 276 THROUGH 305 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.6144 -12.6317 -1.1143
REMARK 3 T TENSOR
REMARK 3 T11: 0.0819 T22: 0.1117
REMARK 3 T33: 0.0926 T12: 0.0234
REMARK 3 T13: 0.0022 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.1317 L22: 0.0946
REMARK 3 L33: 0.0514 L12: 0.1112
REMARK 3 L13: 0.0333 L23: 0.0359
REMARK 3 S TENSOR
REMARK 3 S11: 0.0288 S12: 0.0744 S13: 0.0147
REMARK 3 S21: -0.0131 S22: -0.0322 S23: -0.0785
REMARK 3 S31: 0.0458 S32: 0.0604 S33: 0.0004
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 7A6G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-AUG-20.
REMARK 100 THE DEPOSITION ID IS D_1292110833.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-FEB-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID30B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.7.4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20614
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 42.731
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.17100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.99600
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: MOLREP
REMARK 200 STARTING MODEL: 3WMR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HR1#28: 0.2 M SODIUM ACETATE
REMARK 280 TRIHYDRATE, 0.1 M SODIUM CACODYLATE TRIHYDRATE PH 6.5, 30% W/V
REMARK 280 POLYETHYLENE GLYCOL 8,000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 24.71400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.50800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.51650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.50800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.71400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.51650
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 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 LYS A 306
REMARK 465 ALA A 307
REMARK 465 LEU A 308
REMARK 465 PRO A 309
REMARK 465 GLY A 310
REMARK 465 VAL A 311
REMARK 465 LYS A 312
REMARK 465 ALA A 313
REMARK 465 ARG A 314
REMARK 465 PHE A 315
REMARK 465 GLY A 316
REMARK 465 ILE A 317
REMARK 465 GLU A 318
REMARK 465 GLY A 319
REMARK 465 ARG A 320
REMARK 465 LEU A 321
REMARK 465 GLU A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 465 HIS A 327
REMARK 465 HIS A 328
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 O HOH A 587 O HOH A 661 2.05
REMARK 500 O HOH A 513 O HOH A 635 2.07
REMARK 500 O3 PO4 A 401 O HOH A 501 2.10
REMARK 500 OD1 ASP A 79 O HOH A 502 2.16
REMARK 500 O HOH A 592 O HOH A 688 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 538 O HOH A 612 4555 2.09
REMARK 500 O HOH A 596 O HOH A 625 2354 2.13
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 ASP A 106 96.31 -161.30
REMARK 500 SER A 113 -118.51 60.79
REMARK 500 ALA A 132 147.19 -172.73
REMARK 500 SER A 279 -110.53 -114.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 401
DBREF1 7A6G A 1 316 UNP A0A0Q0CYJ4_PSEUB
DBREF2 7A6G A A0A0Q0CYJ4 1 316
SEQADV 7A6G ILE A 317 UNP A0A0Q0CYJ EXPRESSION TAG
SEQADV 7A6G GLU A 318 UNP A0A0Q0CYJ EXPRESSION TAG
SEQADV 7A6G GLY A 319 UNP A0A0Q0CYJ EXPRESSION TAG
SEQADV 7A6G ARG A 320 UNP A0A0Q0CYJ EXPRESSION TAG
SEQADV 7A6G LEU A 321 UNP A0A0Q0CYJ EXPRESSION TAG
SEQADV 7A6G GLU A 322 UNP A0A0Q0CYJ EXPRESSION TAG
SEQADV 7A6G HIS A 323 UNP A0A0Q0CYJ EXPRESSION TAG
SEQADV 7A6G HIS A 324 UNP A0A0Q0CYJ EXPRESSION TAG
SEQADV 7A6G HIS A 325 UNP A0A0Q0CYJ EXPRESSION TAG
SEQADV 7A6G HIS A 326 UNP A0A0Q0CYJ EXPRESSION TAG
SEQADV 7A6G HIS A 327 UNP A0A0Q0CYJ EXPRESSION TAG
SEQADV 7A6G HIS A 328 UNP A0A0Q0CYJ EXPRESSION TAG
SEQRES 1 A 328 MET ALA ASP MET ALA ASP MET THR ILE LYS GLU GLY PHE
SEQRES 2 A 328 ALA PRO PHE GLY ASP TYR GLN THR TRP TYR ARG ILE THR
SEQRES 3 A 328 GLY ASP LEU ARG GLY GLY GLY THR PRO LEU VAL ILE LEU
SEQRES 4 A 328 HIS GLY GLY PRO GLY CYS THR HIS ASP TYR VAL ASP SER
SEQRES 5 A 328 PHE LYS ASP ILE ALA ASN THR GLY ARG ALA VAL ILE HIS
SEQRES 6 A 328 TYR ASP GLN LEU GLY ASN GLY LYS SER THR HIS LEU PRO
SEQRES 7 A 328 ASP MET GLY SER GLU PHE TRP THR VAL ASP LEU PHE LEU
SEQRES 8 A 328 SER GLU LEU ASP ASN LEU LEU GLU TYR LEU GLU ILE ALA
SEQRES 9 A 328 ASP ASP TYR ALA LEU LEU GLY GLN SER TRP GLY GLY MET
SEQRES 10 A 328 LEU ALA SER GLU HIS ALA VAL LEU GLN PRO THR GLY LEU
SEQRES 11 A 328 GLN ALA LEU ILE ILE ALA ASN SER PRO ALA ASP MET HIS
SEQRES 12 A 328 THR TRP VAL SER GLU ALA ASN ARG LEU ARG GLU GLU LEU
SEQRES 13 A 328 PRO ASP ASP VAL GLN ALA THR LEU LEU LYS HIS GLU GLU
SEQRES 14 A 328 ALA GLY THR LEU THR ASP PRO ALA TYR LEU THR ALA SER
SEQRES 15 A 328 ARG VAL PHE TYR ASP ARG HIS VAL CYS ARG ILE THR PRO
SEQRES 16 A 328 TRP PRO VAL GLU VAL GLU ARG THR PHE HIS GLN ILE ASP
SEQRES 17 A 328 GLU ASP PRO THR VAL TYR ARG ALA MET ASN GLY PRO THR
SEQRES 18 A 328 GLU PHE HIS VAL ILE GLY THR MET LYS ASP TRP SER ILE
SEQRES 19 A 328 VAL ASP ARG LEU SER ASN ILE ASN VAL PRO THR LEU VAL
SEQRES 20 A 328 ILE SER GLY PHE TYR ASP GLU ALA THR PRO LEU VAL ILE
SEQRES 21 A 328 GLN PRO TYR VAL ASP ASN ILE PRO ASP VAL ARG GLN SER
SEQRES 22 A 328 VAL PHE GLN GLU SER SER HIS MET PRO HIS VAL GLU GLU
SEQRES 23 A 328 ARG MET ALA CYS MET GLY ARG VAL ALA ASP PHE LEU ASP
SEQRES 24 A 328 GLU VAL ALA THR SER GLY LYS ALA LEU PRO GLY VAL LYS
SEQRES 25 A 328 ALA ARG PHE GLY ILE GLU GLY ARG LEU GLU HIS HIS HIS
SEQRES 26 A 328 HIS HIS HIS
HET PO4 A 401 5
HETNAM PO4 PHOSPHATE ION
FORMUL 2 PO4 O4 P 3-
FORMUL 3 HOH *248(H2 O)
HELIX 1 AA1 MET A 4 MET A 7 5 4
HELIX 2 AA2 HIS A 47 GLY A 60 5 14
HELIX 3 AA3 THR A 86 LEU A 101 1 16
HELIX 4 AA4 SER A 113 VAL A 124 1 12
HELIX 5 AA5 ASP A 141 GLU A 154 1 14
HELIX 6 AA6 PRO A 157 GLY A 171 1 15
HELIX 7 AA7 ASP A 175 VAL A 190 1 16
HELIX 8 AA8 PRO A 197 ASP A 210 1 14
HELIX 9 AA9 PRO A 211 ASN A 218 1 8
HELIX 10 AB1 ILE A 234 ILE A 241 5 8
HELIX 11 AB2 THR A 256 ILE A 267 1 12
HELIX 12 AB3 MET A 281 GLU A 286 1 6
HELIX 13 AB4 GLU A 286 ALA A 302 1 17
SHEET 1 AA1 8 ILE A 9 PHE A 16 0
SHEET 2 AA1 8 TYR A 19 THR A 26 -1 O ILE A 25 N LYS A 10
SHEET 3 AA1 8 VAL A 63 TYR A 66 -1 O HIS A 65 N ARG A 24
SHEET 4 AA1 8 LEU A 36 LEU A 39 1 N LEU A 36 O ILE A 64
SHEET 5 AA1 8 TYR A 107 GLN A 112 1 O LEU A 110 N LEU A 39
SHEET 6 AA1 8 LEU A 130 ALA A 136 1 O ALA A 136 N GLY A 111
SHEET 7 AA1 8 THR A 245 GLY A 250 1 O LEU A 246 N ILE A 135
SHEET 8 AA1 8 VAL A 270 PHE A 275 1 O ARG A 271 N VAL A 247
CISPEP 1 GLY A 42 PRO A 43 0 -2.53
CISPEP 2 THR A 194 PRO A 195 0 -1.39
SITE 1 AC1 6 GLY A 42 SER A 113 TRP A 114 TRP A 145
SITE 2 AC1 6 ASN A 218 HOH A 501
CRYST1 49.428 65.033 85.016 90.00 90.00 90.00 P 21 21 21 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 0.020231 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015377 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011762 0.00000
TER 2572 GLY A 305
MASTER 368 0 1 13 8 0 2 6 2636 1 5 26
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