HEADER HYDROLASE 15-OCT-16 5TO0
TITLE HTRA2 S276C MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE PROTEASE HTRA2, MITOCHONDRIAL;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HIGH TEMPERATURE REQUIREMENT PROTEIN A2,HTRA2,OMI STRESS-
COMPND 5 REGULATED ENDOPROTEASE,SERINE PROTEASE 25,SERINE PROTEINASE OMI;
COMPND 6 EC: 3.4.21.108;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HTRA2, OMI, PRSS25;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SERINE PROTEASE, PARKINSON DISEASE, MITOCHONDRIA, PDZ DYNAMICS,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MERSKI,P.J.BARBOSA PEREIRA,S.MACEDO-RIBEIRO
REVDAT 2 17-JAN-24 5TO0 1 REMARK
REVDAT 1 25-OCT-17 5TO0 0
JRNL AUTH M.MERSKI,C.MOREIRA,R.M.ABREU,M.J.RAMOS,P.A.FERNANDES,
JRNL AUTH 2 L.M.MARTINS,P.J.B.PEREIRA,S.MACEDO-RIBEIRO
JRNL TITL MOLECULAR MOTION REGULATES THE ACTIVITY OF THE MITOCHONDRIAL
JRNL TITL 2 SERINE PROTEASE HTRA2.
JRNL REF CELL DEATH DIS V. 8 E3119 2017
JRNL REFN ISSN 2041-4889
JRNL PMID 29022916
JRNL DOI 10.1038/CDDIS.2017.487
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10_2155: ???)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 26268
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.158
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1333
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 15.1725 - 4.0715 0.95 2495 121 0.1117 0.1555
REMARK 3 2 4.0715 - 3.2421 0.95 2483 137 0.1323 0.1692
REMARK 3 3 3.2421 - 2.8353 0.95 2495 140 0.1656 0.1847
REMARK 3 4 2.8353 - 2.5774 0.94 2450 150 0.1805 0.1960
REMARK 3 5 2.5774 - 2.3934 0.94 2442 157 0.1878 0.2009
REMARK 3 6 2.3934 - 2.2528 0.94 2520 146 0.1943 0.2200
REMARK 3 7 2.2528 - 2.1403 0.95 2488 124 0.1960 0.2114
REMARK 3 8 2.1403 - 2.0474 0.95 2491 114 0.2110 0.2515
REMARK 3 9 2.0474 - 1.9687 0.95 2501 138 0.2073 0.2264
REMARK 3 10 1.9687 - 1.9009 0.96 2500 105 0.2298 0.2549
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.570
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.010 2202
REMARK 3 ANGLE : 0.921 3001
REMARK 3 CHIRALITY : 0.061 365
REMARK 3 PLANARITY : 0.005 391
REMARK 3 DIHEDRAL : 14.367 1336
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5TO0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000223603.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26268
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 63.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.400
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 8.40
REMARK 200 R MERGE FOR SHELL (I) : 0.51200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.400
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: 1LCY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.0, 1 M LICL, AND 15-20%
REMARK 280 (W/V) PEG-6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.91200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 24.19790
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.48800
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 41.91200
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 24.19790
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 42.48800
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 41.91200
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 24.19790
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.48800
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.39581
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 84.97600
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 48.39581
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 84.97600
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 48.39581
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 84.97600
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 BIOMT1 2 -0.500000 -0.866025 0.000000 41.91200
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 72.59371
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -41.91200
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 72.59371
REMARK 350 BIOMT3 3 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 133
REMARK 465 ALA A 134
REMARK 465 VAL A 135
REMARK 465 PRO A 136
REMARK 465 SER A 137
REMARK 465 PRO A 138
REMARK 465 PRO A 139
REMARK 465 PRO A 140
REMARK 465 ALA A 141
REMARK 465 ARG A 280
REMARK 465 PRO A 281
REMARK 465 ALA A 282
REMARK 465 ARG A 283
REMARK 465 ASP A 284
REMARK 465 LEU A 285
REMARK 465 GLY A 286
REMARK 465 LEU A 287
REMARK 465 PRO A 288
REMARK 465 GLN A 289
REMARK 465 THR A 290
REMARK 465 GLY A 345
REMARK 465 GLU A 346
REMARK 465 LYS A 347
REMARK 465 LYS A 348
REMARK 465 ASN A 349
REMARK 465 SER A 350
REMARK 465 SER A 351
REMARK 465 SER A 352
REMARK 465 GLY A 353
REMARK 465 ILE A 354
REMARK 465 SER A 355
REMARK 465 GLY A 356
REMARK 465 SER A 357
REMARK 465 GLN A 358
REMARK 465 PRO A 382
REMARK 465 SER A 383
REMARK 465 PHE A 384
REMARK 465 PRO A 385
REMARK 465 ASP A 386
REMARK 465 HIS A 461
REMARK 465 HIS A 462
REMARK 465 HIS A 463
REMARK 465 HIS A 464
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 ILE A 179 CG1 CG2 CD1
REMARK 470 ARG A 207 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 226 CG1 CG2
REMARK 470 LEU A 266 CG CD1 CD2
REMARK 470 ASN A 268 CG OD1 ND2
REMARK 470 THR A 269 OG1 CG2
REMARK 470 GLN A 279 CG CD OE1 NE2
REMARK 470 GLU A 340 CG CD OE1 OE2
REMARK 470 ARG A 344 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 381 CG CD OE1 OE2
REMARK 470 TYR A 428 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 445 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 446 CG CD OE1 OE2
REMARK 470 THR A 447 OG1 CG2
REMARK 470 LEU A 448 CG CD1 CD2
REMARK 470 GLU A 458 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 O HOH A 664 O HOH A 670 2.13
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 649 O HOH A 662 2665 2.17
REMARK 500 O HOH A 646 O HOH A 674 2665 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 HIS A 170 75.57 -106.22
REMARK 500 SER A 180 137.91 179.43
REMARK 500 ALA A 201 -131.58 41.40
REMARK 500 ASP A 228 40.48 36.89
REMARK 500 GLN A 267 33.06 -75.84
REMARK 500 ASN A 268 97.70 -62.54
REMARK 500 TYR A 294 152.51 -45.44
REMARK 500 VAL A 325 -60.33 -91.51
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 MES A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5M3N RELATED DB: PDB
REMARK 900 RELATED ID: 5M3O RELATED DB: PDB
REMARK 900 RELATED ID: 5TNZ RELATED DB: PDB
REMARK 900 RELATED ID: 5TNY RELATED DB: PDB
REMARK 900 RELATED ID: 5TO1 RELATED DB: PDB
DBREF 5TO0 A 134 458 UNP O43464 HTRA2_HUMAN 134 458
SEQADV 5TO0 MET A 133 UNP O43464 INITIATING METHIONINE
SEQADV 5TO0 CYS A 276 UNP O43464 SER 276 ENGINEERED MUTATION
SEQADV 5TO0 HIS A 459 UNP O43464 EXPRESSION TAG
SEQADV 5TO0 HIS A 460 UNP O43464 EXPRESSION TAG
SEQADV 5TO0 HIS A 461 UNP O43464 EXPRESSION TAG
SEQADV 5TO0 HIS A 462 UNP O43464 EXPRESSION TAG
SEQADV 5TO0 HIS A 463 UNP O43464 EXPRESSION TAG
SEQADV 5TO0 HIS A 464 UNP O43464 EXPRESSION TAG
SEQRES 1 A 332 MET ALA VAL PRO SER PRO PRO PRO ALA SER PRO ARG SER
SEQRES 2 A 332 GLN TYR ASN PHE ILE ALA ASP VAL VAL GLU LYS THR ALA
SEQRES 3 A 332 PRO ALA VAL VAL TYR ILE GLU ILE LEU ASP ARG HIS PRO
SEQRES 4 A 332 PHE LEU GLY ARG GLU VAL PRO ILE SER ASN GLY SER GLY
SEQRES 5 A 332 PHE VAL VAL ALA ALA ASP GLY LEU ILE VAL THR ASN ALA
SEQRES 6 A 332 HIS VAL VAL ALA ASP ARG ARG ARG VAL ARG VAL ARG LEU
SEQRES 7 A 332 LEU SER GLY ASP THR TYR GLU ALA VAL VAL THR ALA VAL
SEQRES 8 A 332 ASP PRO VAL ALA ASP ILE ALA THR LEU ARG ILE GLN THR
SEQRES 9 A 332 LYS GLU PRO LEU PRO THR LEU PRO LEU GLY ARG SER ALA
SEQRES 10 A 332 ASP VAL ARG GLN GLY GLU PHE VAL VAL ALA MET GLY SER
SEQRES 11 A 332 PRO PHE ALA LEU GLN ASN THR ILE THR SER GLY ILE VAL
SEQRES 12 A 332 CYS SER ALA GLN ARG PRO ALA ARG ASP LEU GLY LEU PRO
SEQRES 13 A 332 GLN THR ASN VAL GLU TYR ILE GLN THR ASP ALA ALA ILE
SEQRES 14 A 332 ASP PHE GLY ASN SER GLY GLY PRO LEU VAL ASN LEU ASP
SEQRES 15 A 332 GLY GLU VAL ILE GLY VAL ASN THR MET LYS VAL THR ALA
SEQRES 16 A 332 GLY ILE SER PHE ALA ILE PRO SER ASP ARG LEU ARG GLU
SEQRES 17 A 332 PHE LEU HIS ARG GLY GLU LYS LYS ASN SER SER SER GLY
SEQRES 18 A 332 ILE SER GLY SER GLN ARG ARG TYR ILE GLY VAL MET MET
SEQRES 19 A 332 LEU THR LEU SER PRO SER ILE LEU ALA GLU LEU GLN LEU
SEQRES 20 A 332 ARG GLU PRO SER PHE PRO ASP VAL GLN HIS GLY VAL LEU
SEQRES 21 A 332 ILE HIS LYS VAL ILE LEU GLY SER PRO ALA HIS ARG ALA
SEQRES 22 A 332 GLY LEU ARG PRO GLY ASP VAL ILE LEU ALA ILE GLY GLU
SEQRES 23 A 332 GLN MET VAL GLN ASN ALA GLU ASP VAL TYR GLU ALA VAL
SEQRES 24 A 332 ARG THR GLN SER GLN LEU ALA VAL GLN ILE ARG ARG GLY
SEQRES 25 A 332 ARG GLU THR LEU THR LEU TYR VAL THR PRO GLU VAL THR
SEQRES 26 A 332 GLU HIS HIS HIS HIS HIS HIS
HET MES A 501 12
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 2 MES C6 H13 N O4 S
FORMUL 3 HOH *75(H2 O)
HELIX 1 AA1 SER A 142 TYR A 147 1 6
HELIX 2 AA2 ASN A 148 ALA A 158 1 11
HELIX 3 AA3 ALA A 197 ALA A 201 1 5
HELIX 4 AA4 ARG A 247 VAL A 251 5 5
HELIX 5 AA5 SER A 335 HIS A 343 1 9
HELIX 6 AA6 SER A 370 GLU A 381 1 12
HELIX 7 AA7 SER A 400 GLY A 406 1 7
HELIX 8 AA8 ASN A 423 ARG A 432 1 10
SHEET 1 AA1 7 VAL A 161 HIS A 170 0
SHEET 2 AA1 7 ARG A 175 ALA A 188 -1 O SER A 180 N ILE A 166
SHEET 3 AA1 7 LEU A 192 ASN A 196 -1 O VAL A 194 N PHE A 185
SHEET 4 AA1 7 ILE A 229 ARG A 233 -1 O LEU A 232 N ILE A 193
SHEET 5 AA1 7 THR A 215 ASP A 224 -1 N ASP A 224 O ILE A 229
SHEET 6 AA1 7 ARG A 205 ARG A 209 -1 N VAL A 208 O TYR A 216
SHEET 7 AA1 7 VAL A 161 HIS A 170 -1 N TYR A 163 O ARG A 209
SHEET 1 AA2 6 THR A 271 ILE A 274 0
SHEET 2 AA2 6 PHE A 256 ALA A 259 -1 N ALA A 259 O THR A 271
SHEET 3 AA2 6 PRO A 309 ASN A 312 -1 O VAL A 311 N VAL A 258
SHEET 4 AA2 6 VAL A 317 THR A 326 -1 O GLY A 319 N LEU A 310
SHEET 5 AA2 6 ILE A 329 PRO A 334 -1 O ILE A 329 N VAL A 325
SHEET 6 AA2 6 ILE A 295 THR A 297 -1 N ILE A 295 O ALA A 332
SHEET 1 AA3 2 ARG A 360 TYR A 361 0
SHEET 2 AA3 2 GLU A 455 VAL A 456 -1 O GLU A 455 N TYR A 361
SHEET 1 AA4 5 VAL A 364 THR A 368 0
SHEET 2 AA4 5 VAL A 391 VAL A 396 -1 O HIS A 394 N MET A 365
SHEET 3 AA4 5 VAL A 412 ILE A 416 -1 O ILE A 413 N VAL A 391
SHEET 4 AA4 5 LEU A 437 ARG A 443 -1 O GLN A 440 N ALA A 415
SHEET 5 AA4 5 GLU A 446 VAL A 452 -1 O VAL A 452 N LEU A 437
SITE 1 AC1 11 SER A 145 GLN A 146 TYR A 147 ASN A 148
SITE 2 AC1 11 ASP A 152 ARG A 169 HIS A 170 PRO A 171
SITE 3 AC1 11 PHE A 172 LEU A 173 ARG A 252
CRYST1 83.824 83.824 127.464 90.00 90.00 120.00 H 3 9
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 0.011930 0.006888 0.000000 0.00000
SCALE2 0.000000 0.013775 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007845 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
