HEADER SIGNALING PROTEIN 03-MAR-05 1WZ9
TITLE THE 2.1 A STRUCTURE OF A TUMOUR SUPPRESSING SERPIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MASPIN PRECURSOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PROTEASE INHIBITOR 5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SERPINB5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSETC
KEYWDS MASPIN, SERPIN, TUMOR SUPPRESSOR, SERPINB5, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.H.LAW,J.A.IRVING,A.M.BUCKLE,K.RUZYLA,M.BUZZA,T.A.BASHTANNYK-
AUTHOR 2 PUHALOVICH,T.C.BEDDOE,N.KIM,D.M.WORRALL,S.P.BOTTOMLEY,P.I.BIRD,
AUTHOR 3 J.ROSSJOHN,J.C.WHISSTOCK
REVDAT 4 11-OCT-17 1WZ9 1 REMARK
REVDAT 3 24-FEB-09 1WZ9 1 VERSN
REVDAT 2 21-JUN-05 1WZ9 1 JRNL
REVDAT 1 15-MAR-05 1WZ9 0
JRNL AUTH R.H.LAW,J.A.IRVING,A.M.BUCKLE,K.RUZYLA,M.BUZZA,
JRNL AUTH 2 T.A.BASHTANNYK-PUHALOVICH,T.C.BEDDOE,K.NGUYEN,D.M.WORRALL,
JRNL AUTH 3 S.P.BOTTOMLEY,P.I.BIRD,J.ROSSJOHN,J.C.WHISSTOCK
JRNL TITL THE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE HUMAN TUMOR
JRNL TITL 2 SUPPRESSOR MASPIN REVEALS A NOVEL CONFORMATIONAL SWITCH IN
JRNL TITL 3 THE G-HELIX.
JRNL REF J.BIOL.CHEM. V. 280 22356 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15760906
JRNL DOI 10.1074/JBC.M412043200
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 78.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 139.22
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 40352
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2136
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2908
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 159
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5523
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 201
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.42000
REMARK 3 B22 (A**2) : -0.23000
REMARK 3 B33 (A**2) : -0.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.252
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.201
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.157
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.953
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.932
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5628 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7614 ; 1.152 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 718 ; 5.520 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 226 ;38.427 ;26.150
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 943 ;15.601 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;18.406 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 891 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4134 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2512 ; 0.190 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3840 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 273 ; 0.128 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 27 ; 0.175 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 6 ; 0.135 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3721 ; 1.191 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5815 ; 2.039 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2125 ; 3.340 ; 7.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1799 ; 4.843 ;10.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 1WZ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000024180.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42714
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 78.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 36.80
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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 <I/SIGMA(I)> 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: AMORE
REMARK 200 STARTING MODEL: 1XU8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BISTRIS, 2.9M (NH4)2SO4, PH 8.3,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 27.05750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.61250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.52350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.61250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.05750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.52350
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 GLY A 331
REMARK 465 ASP A 332
REMARK 465 SER A 333
REMARK 465 ILE A 334
REMARK 465 GLU A 335
REMARK 465 VAL A 336
REMARK 465 PRO A 337
REMARK 465 GLY A 338
REMARK 465 ALA A 339
REMARK 465 ARG A 340
REMARK 465 ILE A 341
REMARK 465 LEU A 342
REMARK 465 ASP B 150
REMARK 465 ASN B 151
REMARK 465 GLU B 237
REMARK 465 ASP B 238
REMARK 465 GLU B 239
REMARK 465 SER B 240
REMARK 465 ILE B 334
REMARK 465 GLU B 335
REMARK 465 VAL B 336
REMARK 465 PRO B 337
REMARK 465 GLY B 338
REMARK 465 ALA B 339
REMARK 465 ARG B 340
REMARK 465 ILE B 341
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 LYS A 22 CD CE NZ
REMARK 470 GLU A 61 CG CD OE1 OE2
REMARK 470 LYS A 64 CG CD CE NZ
REMARK 470 LYS A 96 CD CE NZ
REMARK 470 GLU A 103 CD OE1 OE2
REMARK 470 LYS A 109 CD CE NZ
REMARK 470 ARG A 110 CD NE CZ NH1 NH2
REMARK 470 LYS A 114 CD CE NZ
REMARK 470 LYS A 122 CG CD CE NZ
REMARK 470 LYS A 124 CD CE NZ
REMARK 470 LYS A 129 CE NZ
REMARK 470 ASP A 150 CG OD1 OD2
REMARK 470 ASN A 151 CG OD1 ND2
REMARK 470 LYS A 158 CE NZ
REMARK 470 LYS A 174 CD CE NZ
REMARK 470 LYS A 181 CE NZ
REMARK 470 ILE A 212 CG1 CG2 CD1
REMARK 470 LYS A 245 CE NZ
REMARK 470 LYS A 268 CG CD CE NZ
REMARK 470 LYS A 270 CD CE NZ
REMARK 470 LYS A 294 CG CD CE NZ
REMARK 470 ILE A 296 CG1 CG2 CD1
REMARK 470 ASP A 300 CG OD1 OD2
REMARK 470 GLN A 343 CG CD OE1 NE2
REMARK 470 HIS A 344 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 345 CD CE NZ
REMARK 470 LYS A 362 CE NZ
REMARK 470 ARG A 364 CD NE CZ NH1 NH2
REMARK 470 ASP B 2 CG OD1 OD2
REMARK 470 CME B 20 SD CE CZ OH
REMARK 470 GLU B 21 CG CD OE1 OE2
REMARK 470 GLU B 23 OE1 OE2
REMARK 470 ASN B 62 OD1 ND2
REMARK 470 LYS B 64 CG CD CE NZ
REMARK 470 SER B 97 OG
REMARK 470 LEU B 100 CG CD1 CD2
REMARK 470 GLU B 103 CG CD OE1 OE2
REMARK 470 LYS B 109 CG CD CE NZ
REMARK 470 ARG B 110 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 114 CG CD CE NZ
REMARK 470 LYS B 122 CG CD CE NZ
REMARK 470 LYS B 124 CG CD CE NZ
REMARK 470 GLU B 126 CG CD OE1 OE2
REMARK 470 GLU B 127 CG CD OE1 OE2
REMARK 470 GLN B 131 CG CD OE1 NE2
REMARK 470 ASN B 146 CG OD1 ND2
REMARK 470 VAL B 153 CG1 CG2
REMARK 470 GLU B 179 OE1 OE2
REMARK 470 LYS B 181 CG CD CE NZ
REMARK 470 LYS B 189 CG CD CE NZ
REMARK 470 ASP B 210 CG OD1 OD2
REMARK 470 CME B 214 SD CE CZ OH
REMARK 470 LYS B 234 CD CE NZ
REMARK 470 ASP B 235 CG OD1 OD2
REMARK 470 VAL B 236 CG1 CG2
REMARK 470 THR B 241 OG1 CG2
REMARK 470 GLU B 244 CG CD OE1 OE2
REMARK 470 LYS B 248 CG CD CE NZ
REMARK 470 GLU B 253 CD OE1 OE2
REMARK 470 LYS B 268 CG CD CE NZ
REMARK 470 LYS B 270 CG CD CE NZ
REMARK 470 MET B 281 CG SD CE
REMARK 470 LYS B 294 CG CD CE NZ
REMARK 470 GLU B 309 CG CD OE1 OE2
REMARK 470 LYS B 311 CG CD CE NZ
REMARK 470 LYS B 321 CD CE NZ
REMARK 470 CME B 323 SD CE CZ OH
REMARK 470 ASP B 332 CG OD1 OD2
REMARK 470 SER B 333 OG
REMARK 470 LEU B 342 CG CD1 CD2
REMARK 470 GLN B 343 CG CD OE1 NE2
REMARK 470 LYS B 345 CG CD CE NZ
REMARK 470 ARG B 364 CD NE CZ NH1 NH2
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 65 72.26 48.74
REMARK 500 ASN A 99 66.73 39.58
REMARK 500 LYS A 114 -5.93 74.23
REMARK 500 ASP A 120 77.54 -109.31
REMARK 500 LYS A 124 55.54 -140.91
REMARK 500 ASN A 188 -161.45 -167.10
REMARK 500 ASN B 99 72.22 45.15
REMARK 500 LYS B 114 -2.41 70.32
REMARK 500 LYS B 124 60.96 -115.87
REMARK 500 LYS B 294 -62.55 -131.43
REMARK 500 ASP B 332 -149.77 -85.45
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 SO4 A 1001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XU8 RELATED DB: PDB
REMARK 900 THE 2.8 A STRUCTURE OF A TUMOUR SUPRESSING SERPIN
DBREF 1WZ9 A 1 375 UNP P36952 MASP_HUMAN 1 375
DBREF 1WZ9 B 1 375 UNP P36952 MASP_HUMAN 1 375
SEQADV 1WZ9 CME A 20 UNP P36952 CYS 20 MODIFIED RESIDUE
SEQADV 1WZ9 VAL A 66 UNP P36952 ILE 66 SEE REMARK 999
SEQADV 1WZ9 CME A 183 UNP P36952 CYS 183 MODIFIED RESIDUE
SEQADV 1WZ9 CME A 205 UNP P36952 CYS 205 MODIFIED RESIDUE
SEQADV 1WZ9 CME A 214 UNP P36952 CYS 214 MODIFIED RESIDUE
SEQADV 1WZ9 CME A 323 UNP P36952 CYS 323 MODIFIED RESIDUE
SEQADV 1WZ9 CME A 373 UNP P36952 CYS 373 MODIFIED RESIDUE
SEQADV 1WZ9 CME B 20 UNP P36952 CYS 20 MODIFIED RESIDUE
SEQADV 1WZ9 VAL B 66 UNP P36952 ILE 66 SEE REMARK 999
SEQADV 1WZ9 CME B 183 UNP P36952 CYS 183 MODIFIED RESIDUE
SEQADV 1WZ9 CME B 205 UNP P36952 CYS 205 MODIFIED RESIDUE
SEQADV 1WZ9 CME B 214 UNP P36952 CYS 214 MODIFIED RESIDUE
SEQADV 1WZ9 CME B 323 UNP P36952 CYS 323 MODIFIED RESIDUE
SEQADV 1WZ9 CME B 373 UNP P36952 CYS 373 MODIFIED RESIDUE
SEQRES 1 A 375 MET ASP ALA LEU GLN LEU ALA ASN SER ALA PHE ALA VAL
SEQRES 2 A 375 ASP LEU PHE LYS GLN LEU CME GLU LYS GLU PRO LEU GLY
SEQRES 3 A 375 ASN VAL LEU PHE SER PRO ILE CYS LEU SER THR SER LEU
SEQRES 4 A 375 SER LEU ALA GLN VAL GLY ALA LYS GLY ASP THR ALA ASN
SEQRES 5 A 375 GLU ILE GLY GLN VAL LEU HIS PHE GLU ASN VAL LYS ASP
SEQRES 6 A 375 VAL PRO PHE GLY PHE GLN THR VAL THR SER ASP VAL ASN
SEQRES 7 A 375 LYS LEU SER SER PHE TYR SER LEU LYS LEU ILE LYS ARG
SEQRES 8 A 375 LEU TYR VAL ASP LYS SER LEU ASN LEU SER THR GLU PHE
SEQRES 9 A 375 ILE SER SER THR LYS ARG PRO TYR ALA LYS GLU LEU GLU
SEQRES 10 A 375 THR VAL ASP PHE LYS ASP LYS LEU GLU GLU THR LYS GLY
SEQRES 11 A 375 GLN ILE ASN ASN SER ILE LYS ASP LEU THR ASP GLY HIS
SEQRES 12 A 375 PHE GLU ASN ILE LEU ALA ASP ASN SER VAL ASN ASP GLN
SEQRES 13 A 375 THR LYS ILE LEU VAL VAL ASN ALA ALA TYR PHE VAL GLY
SEQRES 14 A 375 LYS TRP MET LYS LYS PHE PRO GLU SER GLU THR LYS GLU
SEQRES 15 A 375 CME PRO PHE ARG LEU ASN LYS THR ASP THR LYS PRO VAL
SEQRES 16 A 375 GLN MET MET ASN MET GLU ALA THR PHE CME MET GLY ASN
SEQRES 17 A 375 ILE ASP SER ILE ASN CME LYS ILE ILE GLU LEU PRO PHE
SEQRES 18 A 375 GLN ASN LYS HIS LEU SER MET PHE ILE LEU LEU PRO LYS
SEQRES 19 A 375 ASP VAL GLU ASP GLU SER THR GLY LEU GLU LYS ILE GLU
SEQRES 20 A 375 LYS GLN LEU ASN SER GLU SER LEU SER GLN TRP THR ASN
SEQRES 21 A 375 PRO SER THR MET ALA ASN ALA LYS VAL LYS LEU SER ILE
SEQRES 22 A 375 PRO LYS PHE LYS VAL GLU LYS MET ILE ASP PRO LYS ALA
SEQRES 23 A 375 CYS LEU GLU ASN LEU GLY LEU LYS HIS ILE PHE SER GLU
SEQRES 24 A 375 ASP THR SER ASP PHE SER GLY MET SER GLU THR LYS GLY
SEQRES 25 A 375 VAL ALA LEU SER ASN VAL ILE HIS LYS VAL CME LEU GLU
SEQRES 26 A 375 ILE THR GLU ASP GLY GLY ASP SER ILE GLU VAL PRO GLY
SEQRES 27 A 375 ALA ARG ILE LEU GLN HIS LYS ASP GLU LEU ASN ALA ASP
SEQRES 28 A 375 HIS PRO PHE ILE TYR ILE ILE ARG HIS ASN LYS THR ARG
SEQRES 29 A 375 ASN ILE ILE PHE PHE GLY LYS PHE CME SER PRO
SEQRES 1 B 375 MET ASP ALA LEU GLN LEU ALA ASN SER ALA PHE ALA VAL
SEQRES 2 B 375 ASP LEU PHE LYS GLN LEU CME GLU LYS GLU PRO LEU GLY
SEQRES 3 B 375 ASN VAL LEU PHE SER PRO ILE CYS LEU SER THR SER LEU
SEQRES 4 B 375 SER LEU ALA GLN VAL GLY ALA LYS GLY ASP THR ALA ASN
SEQRES 5 B 375 GLU ILE GLY GLN VAL LEU HIS PHE GLU ASN VAL LYS ASP
SEQRES 6 B 375 VAL PRO PHE GLY PHE GLN THR VAL THR SER ASP VAL ASN
SEQRES 7 B 375 LYS LEU SER SER PHE TYR SER LEU LYS LEU ILE LYS ARG
SEQRES 8 B 375 LEU TYR VAL ASP LYS SER LEU ASN LEU SER THR GLU PHE
SEQRES 9 B 375 ILE SER SER THR LYS ARG PRO TYR ALA LYS GLU LEU GLU
SEQRES 10 B 375 THR VAL ASP PHE LYS ASP LYS LEU GLU GLU THR LYS GLY
SEQRES 11 B 375 GLN ILE ASN ASN SER ILE LYS ASP LEU THR ASP GLY HIS
SEQRES 12 B 375 PHE GLU ASN ILE LEU ALA ASP ASN SER VAL ASN ASP GLN
SEQRES 13 B 375 THR LYS ILE LEU VAL VAL ASN ALA ALA TYR PHE VAL GLY
SEQRES 14 B 375 LYS TRP MET LYS LYS PHE PRO GLU SER GLU THR LYS GLU
SEQRES 15 B 375 CME PRO PHE ARG LEU ASN LYS THR ASP THR LYS PRO VAL
SEQRES 16 B 375 GLN MET MET ASN MET GLU ALA THR PHE CME MET GLY ASN
SEQRES 17 B 375 ILE ASP SER ILE ASN CME LYS ILE ILE GLU LEU PRO PHE
SEQRES 18 B 375 GLN ASN LYS HIS LEU SER MET PHE ILE LEU LEU PRO LYS
SEQRES 19 B 375 ASP VAL GLU ASP GLU SER THR GLY LEU GLU LYS ILE GLU
SEQRES 20 B 375 LYS GLN LEU ASN SER GLU SER LEU SER GLN TRP THR ASN
SEQRES 21 B 375 PRO SER THR MET ALA ASN ALA LYS VAL LYS LEU SER ILE
SEQRES 22 B 375 PRO LYS PHE LYS VAL GLU LYS MET ILE ASP PRO LYS ALA
SEQRES 23 B 375 CYS LEU GLU ASN LEU GLY LEU LYS HIS ILE PHE SER GLU
SEQRES 24 B 375 ASP THR SER ASP PHE SER GLY MET SER GLU THR LYS GLY
SEQRES 25 B 375 VAL ALA LEU SER ASN VAL ILE HIS LYS VAL CME LEU GLU
SEQRES 26 B 375 ILE THR GLU ASP GLY GLY ASP SER ILE GLU VAL PRO GLY
SEQRES 27 B 375 ALA ARG ILE LEU GLN HIS LYS ASP GLU LEU ASN ALA ASP
SEQRES 28 B 375 HIS PRO PHE ILE TYR ILE ILE ARG HIS ASN LYS THR ARG
SEQRES 29 B 375 ASN ILE ILE PHE PHE GLY LYS PHE CME SER PRO
MODRES 1WZ9 CME A 20 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1WZ9 CME A 183 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1WZ9 CME A 205 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1WZ9 CME A 214 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1WZ9 CME A 323 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1WZ9 CME A 373 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1WZ9 CME B 20 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1WZ9 CME B 183 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1WZ9 CME B 205 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1WZ9 CME B 214 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1WZ9 CME B 323 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
MODRES 1WZ9 CME B 373 CYS S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HET CME A 20 10
HET CME A 183 10
HET CME A 205 10
HET CME A 214 10
HET CME A 323 10
HET CME A 373 10
HET CME B 20 6
HET CME B 183 10
HET CME B 205 10
HET CME B 214 6
HET CME B 323 6
HET CME B 373 10
HET SO4 A1001 5
HETNAM CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE
HETNAM SO4 SULFATE ION
FORMUL 1 CME 12(C5 H11 N O3 S2)
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *201(H2 O)
HELIX 1 1 MET A 1 GLU A 23 1 23
HELIX 2 2 SER A 31 ALA A 46 1 16
HELIX 3 3 LYS A 47 LEU A 58 1 12
HELIX 4 4 ASP A 65 SER A 81 1 17
HELIX 5 5 SER A 97 ASN A 99 5 3
HELIX 6 6 SER A 101 LYS A 109 1 9
HELIX 7 7 LYS A 124 THR A 140 1 17
HELIX 8 8 PRO A 176 THR A 180 5 5
HELIX 9 9 GLN A 222 LYS A 224 5 3
HELIX 10 10 ASP A 238 LEU A 250 1 13
HELIX 11 11 ASN A 251 THR A 259 1 9
HELIX 12 12 ASN A 260 MET A 264 5 5
HELIX 13 13 ASP A 283 GLY A 292 1 10
HELIX 14 14 MET B 1 GLU B 23 1 23
HELIX 15 15 SER B 31 GLY B 45 1 15
HELIX 16 16 LYS B 47 LEU B 58 1 12
HELIX 17 17 HIS B 59 VAL B 63 5 5
HELIX 18 18 ASP B 65 SER B 81 1 17
HELIX 19 19 SER B 97 ASN B 99 5 3
HELIX 20 20 SER B 101 ARG B 110 1 10
HELIX 21 21 LYS B 124 THR B 140 1 17
HELIX 22 22 PRO B 176 THR B 180 5 5
HELIX 23 23 GLN B 222 LYS B 224 5 3
HELIX 24 24 GLY B 242 GLN B 249 1 8
HELIX 25 25 ASN B 251 THR B 259 1 9
HELIX 26 26 ASN B 260 MET B 264 5 5
HELIX 27 27 PRO B 284 GLY B 292 1 9
HELIX 28 28 LYS B 294 SER B 298 5 5
SHEET 1 A 7 LEU A 29 PHE A 30 0
SHEET 2 A 7 ASN A 365 PHE A 372 -1 O PHE A 369 N PHE A 30
SHEET 3 A 7 PHE A 354 HIS A 360 -1 N ILE A 358 O ILE A 367
SHEET 4 A 7 LEU A 226 PRO A 233 -1 N LEU A 231 O ILE A 355
SHEET 5 A 7 CME A 214 PRO A 220 -1 N LEU A 219 O MET A 228
SHEET 6 A 7 THR A 192 ILE A 209 -1 N GLY A 207 O ILE A 216
SHEET 7 A 7 LYS A 181 ARG A 186 -1 N PHE A 185 O LYS A 193
SHEET 1 B 8 LEU A 29 PHE A 30 0
SHEET 2 B 8 ASN A 365 PHE A 372 -1 O PHE A 369 N PHE A 30
SHEET 3 B 8 PHE A 354 HIS A 360 -1 N ILE A 358 O ILE A 367
SHEET 4 B 8 LEU A 226 PRO A 233 -1 N LEU A 231 O ILE A 355
SHEET 5 B 8 CME A 214 PRO A 220 -1 N LEU A 219 O MET A 228
SHEET 6 B 8 THR A 192 ILE A 209 -1 N GLY A 207 O ILE A 216
SHEET 7 B 8 ALA A 265 PRO A 274 -1 O ILE A 273 N MET A 198
SHEET 8 B 8 HIS A 344 ASN A 349 1 O LEU A 348 N SER A 272
SHEET 1 C 5 LEU A 116 VAL A 119 0
SHEET 2 C 5 SER A 85 ASP A 95 1 N LEU A 92 O GLU A 117
SHEET 3 C 5 ILE A 159 VAL A 168 -1 O ALA A 164 N ILE A 89
SHEET 4 C 5 LEU A 315 ILE A 326 1 O ILE A 319 N VAL A 161
SHEET 5 C 5 PHE A 276 ILE A 282 -1 N PHE A 276 O ILE A 326
SHEET 1 D 7 VAL B 28 PHE B 30 0
SHEET 2 D 7 ILE B 366 PHE B 372 -1 O LYS B 371 N VAL B 28
SHEET 3 D 7 PHE B 354 HIS B 360 -1 N PHE B 354 O PHE B 372
SHEET 4 D 7 LEU B 226 PRO B 233 -1 N PHE B 229 O ILE B 357
SHEET 5 D 7 CME B 214 PRO B 220 -1 N LEU B 219 O MET B 228
SHEET 6 D 7 THR B 192 ILE B 209 -1 N CME B 205 O GLU B 218
SHEET 7 D 7 LYS B 181 ARG B 186 -1 N LYS B 181 O MET B 197
SHEET 1 E 8 VAL B 28 PHE B 30 0
SHEET 2 E 8 ILE B 366 PHE B 372 -1 O LYS B 371 N VAL B 28
SHEET 3 E 8 PHE B 354 HIS B 360 -1 N PHE B 354 O PHE B 372
SHEET 4 E 8 LEU B 226 PRO B 233 -1 N PHE B 229 O ILE B 357
SHEET 5 E 8 CME B 214 PRO B 220 -1 N LEU B 219 O MET B 228
SHEET 6 E 8 THR B 192 ILE B 209 -1 N CME B 205 O GLU B 218
SHEET 7 E 8 ALA B 265 PRO B 274 -1 O ILE B 273 N MET B 198
SHEET 8 E 8 LYS B 345 ASN B 349 1 O LEU B 348 N SER B 272
SHEET 1 F 5 LEU B 116 VAL B 119 0
SHEET 2 F 5 SER B 85 ASP B 95 1 N VAL B 94 O GLU B 117
SHEET 3 F 5 ILE B 159 VAL B 168 -1 O ALA B 164 N ILE B 89
SHEET 4 F 5 LEU B 315 ILE B 326 1 O ILE B 319 N VAL B 161
SHEET 5 F 5 PHE B 276 ILE B 282 -1 N PHE B 276 O ILE B 326
LINK C LEU A 19 N CME A 20 1555 1555 1.34
LINK C CME A 20 N GLU A 21 1555 1555 1.33
LINK C GLU A 182 N CME A 183 1555 1555 1.33
LINK C CME A 183 N PRO A 184 1555 1555 1.34
LINK C PHE A 204 N CME A 205 1555 1555 1.33
LINK C CME A 205 N MET A 206 1555 1555 1.33
LINK C ASN A 213 N CME A 214 1555 1555 1.33
LINK C CME A 214 N LYS A 215 1555 1555 1.33
LINK C VAL A 322 N CME A 323 1555 1555 1.33
LINK C CME A 323 N LEU A 324 1555 1555 1.33
LINK C PHE A 372 N CME A 373 1555 1555 1.34
LINK C CME A 373 N SER A 374 1555 1555 1.33
LINK C LEU B 19 N CME B 20 1555 1555 1.33
LINK C CME B 20 N GLU B 21 1555 1555 1.34
LINK C GLU B 182 N CME B 183 1555 1555 1.33
LINK C CME B 183 N PRO B 184 1555 1555 1.35
LINK C PHE B 204 N CME B 205 1555 1555 1.33
LINK C CME B 205 N MET B 206 1555 1555 1.33
LINK C ASN B 213 N CME B 214 1555 1555 1.33
LINK C CME B 214 N LYS B 215 1555 1555 1.33
LINK C VAL B 322 N CME B 323 1555 1555 1.33
LINK C CME B 323 N LEU B 324 1555 1555 1.33
LINK C PHE B 372 N CME B 373 1555 1555 1.33
LINK C CME B 373 N SER B 374 1555 1555 1.33
SITE 1 AC1 6 GLY A 26 ASN A 27 LYS A 280 HOH A1024
SITE 2 AC1 6 GLY B 331 ASP B 332
CRYST1 54.115 95.047 139.225 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 0.018479 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010521 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007183 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
