HEADER SIGNALING PROTEIN 25-OCT-04 1XU8
TITLE THE 2.8 A STRUCTURE OF A TUMOUR SUPPRESSING SERPIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MASPIN;
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
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.IRVING,R.H.LAW,K.RUZYLA,T.A.BASHTANNYK-PUHALOVICH,N.KIM,
AUTHOR 2 D.M.WORRALL,J.ROSSJOHN,J.C.WHISSTOCK
REVDAT 3 24-FEB-09 1XU8 1 VERSN
REVDAT 2 21-JUN-05 1XU8 1 JRNL
REVDAT 1 15-MAR-05 1XU8 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,
JRNL AUTH 3 D.M.WORRALL,S.P.BOTTOMLEY,P.I.BIRD,J.ROSSJOHN,
JRNL AUTH 4 J.C.WHISSTOCK
JRNL TITL THE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE HUMAN
JRNL TITL 2 TUMOR SUPPRESSOR MASPIN REVEALS A NOVEL
JRNL TITL 3 CONFORMATIONAL SWITCH IN 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 1
REMARK 2
REMARK 2 RESOLUTION. 2.80 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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 17231
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.286
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 945
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1150
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.26
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.4020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5815
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 123
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.65000
REMARK 3 B22 (A**2) : 1.20000
REMARK 3 B33 (A**2) : -1.85000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.483
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.373
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.851
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.910
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.859
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5927 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7988 ; 1.280 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 734 ; 6.163 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 260 ;39.784 ;26.231
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1129 ;18.733 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;22.227 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 911 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4341 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2740 ; 0.226 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4005 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 251 ; 0.196 ; 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): 103 ; 0.265 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.380 ; 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): 3771 ; 1.071 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5977 ; 1.889 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2361 ; 3.188 ; 7.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2011 ; 5.045 ;10.000
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 4 A 332 1
REMARK 3 1 B 4 B 332 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 2578 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 2578 ; 0.08 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 344 A 375 1
REMARK 3 1 B 344 B 375 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 A (A): 275 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 2 A (A**2): 275 ; 0.09 ; 0.50
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1XU8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-04.
REMARK 100 THE RCSB ID CODE IS RCSB030776.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-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 : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18174
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.32200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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: PDB ENTRY 1OVA CHAIN A
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: AMMONIUM SULFATE, BIS-TRIS, 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 26.77000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.30500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.24000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.30500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.77000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.24000
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 300 REMARK: THE BIOLOGICAL UNIT CONSISTS OF A MONOMER.
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 -4
REMARK 465 GLY A -3
REMARK 465 GLN A -2
REMARK 465 ASN A -1
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 GLN A 343
REMARK 465 MET B -4
REMARK 465 GLY B -3
REMARK 465 GLN B -2
REMARK 465 ASN B -1
REMARK 465 SER B 333
REMARK 465 ILE B 334
REMARK 465 GLU B 335
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 VAL B 336 CG1 CG2
REMARK 470 PRO B 337 CG CD
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 3245 O HOH A 3287 1.91
REMARK 500 O HOH A 3267 O HOH A 3287 2.00
REMARK 500 O HOH B 397 O HOH B 422 2.08
REMARK 500 SG CYS B 183 O HOH B 426 2.14
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 ND2 ASN A 223 OE2 GLU B 239 2554 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 4 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 LEU B 4 CA - CB - CG ANGL. DEV. = 18.8 DEGREES
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 MET A 1 38.76 -85.85
REMARK 500 ASP A 2 37.57 -99.85
REMARK 500 LYS A 64 -125.28 -72.97
REMARK 500 ASP A 65 93.51 -54.92
REMARK 500 SER A 97 -8.07 -58.68
REMARK 500 LEU A 98 60.40 -108.75
REMARK 500 ASN A 99 103.33 -25.86
REMARK 500 LYS A 114 -8.47 65.12
REMARK 500 LEU A 139 -19.37 -48.95
REMARK 500 ASP A 150 28.61 163.54
REMARK 500 SER A 152 78.67 26.61
REMARK 500 ASN A 188 -164.59 -170.56
REMARK 500 LYS A 294 -63.77 -96.43
REMARK 500 ARG A 364 6.50 82.38
REMARK 500 ALA B 3 47.77 -92.82
REMARK 500 LYS B 64 -128.20 -74.47
REMARK 500 ASP B 65 96.07 -55.56
REMARK 500 SER B 97 -9.98 -56.02
REMARK 500 LEU B 98 56.95 -108.77
REMARK 500 ASN B 99 101.43 -21.94
REMARK 500 LYS B 114 -7.25 65.85
REMARK 500 ASP B 120 77.70 -104.42
REMARK 500 ALA B 149 58.45 -91.16
REMARK 500 ASP B 150 23.22 163.15
REMARK 500 SER B 152 74.00 27.31
REMARK 500 ASN B 188 -166.23 -172.79
REMARK 500 LYS B 294 -63.97 -100.35
REMARK 500 ALA B 339 -103.29 -75.58
REMARK 500 ARG B 340 -165.63 -166.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MET A 1 ASP A 2 147.45
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 3243
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3244
DBREF 1XU8 A 1 375 UNP P36952 MASP_HUMAN 1 375
DBREF 1XU8 B 1 375 UNP P36952 MASP_HUMAN 1 375
SEQADV 1XU8 MET A -4 UNP P36952 CLONING ARTIFACT
SEQADV 1XU8 GLY A -3 UNP P36952 CLONING ARTIFACT
SEQADV 1XU8 GLN A -2 UNP P36952 CLONING ARTIFACT
SEQADV 1XU8 ASN A -1 UNP P36952 CLONING ARTIFACT
SEQADV 1XU8 SER A 0 UNP P36952 CLONING ARTIFACT
SEQADV 1XU8 VAL A 66 UNP P36952 ILE 66 SEE REMARK 999
SEQADV 1XU8 MET B -4 UNP P36952 CLONING ARTIFACT
SEQADV 1XU8 GLY B -3 UNP P36952 CLONING ARTIFACT
SEQADV 1XU8 GLN B -2 UNP P36952 CLONING ARTIFACT
SEQADV 1XU8 ASN B -1 UNP P36952 CLONING ARTIFACT
SEQADV 1XU8 SER B 0 UNP P36952 CLONING ARTIFACT
SEQADV 1XU8 VAL B 66 UNP P36952 ILE 66 SEE REMARK 999
SEQRES 1 A 380 MET GLY GLN ASN SER MET ASP ALA LEU GLN LEU ALA ASN
SEQRES 2 A 380 SER ALA PHE ALA VAL ASP LEU PHE LYS GLN LEU CYS GLU
SEQRES 3 A 380 LYS GLU PRO LEU GLY ASN VAL LEU PHE SER PRO ILE CYS
SEQRES 4 A 380 LEU SER THR SER LEU SER LEU ALA GLN VAL GLY ALA LYS
SEQRES 5 A 380 GLY ASP THR ALA ASN GLU ILE GLY GLN VAL LEU HIS PHE
SEQRES 6 A 380 GLU ASN VAL LYS ASP VAL PRO PHE GLY PHE GLN THR VAL
SEQRES 7 A 380 THR SER ASP VAL ASN LYS LEU SER SER PHE TYR SER LEU
SEQRES 8 A 380 LYS LEU ILE LYS ARG LEU TYR VAL ASP LYS SER LEU ASN
SEQRES 9 A 380 LEU SER THR GLU PHE ILE SER SER THR LYS ARG PRO TYR
SEQRES 10 A 380 ALA LYS GLU LEU GLU THR VAL ASP PHE LYS ASP LYS LEU
SEQRES 11 A 380 GLU GLU THR LYS GLY GLN ILE ASN ASN SER ILE LYS ASP
SEQRES 12 A 380 LEU THR ASP GLY HIS PHE GLU ASN ILE LEU ALA ASP ASN
SEQRES 13 A 380 SER VAL ASN ASP GLN THR LYS ILE LEU VAL VAL ASN ALA
SEQRES 14 A 380 ALA TYR PHE VAL GLY LYS TRP MET LYS LYS PHE PRO GLU
SEQRES 15 A 380 SER GLU THR LYS GLU CYS PRO PHE ARG LEU ASN LYS THR
SEQRES 16 A 380 ASP THR LYS PRO VAL GLN MET MET ASN MET GLU ALA THR
SEQRES 17 A 380 PHE CYS MET GLY ASN ILE ASP SER ILE ASN CYS LYS ILE
SEQRES 18 A 380 ILE GLU LEU PRO PHE GLN ASN LYS HIS LEU SER MET PHE
SEQRES 19 A 380 ILE LEU LEU PRO LYS ASP VAL GLU ASP GLU SER THR GLY
SEQRES 20 A 380 LEU GLU LYS ILE GLU LYS GLN LEU ASN SER GLU SER LEU
SEQRES 21 A 380 SER GLN TRP THR ASN PRO SER THR MET ALA ASN ALA LYS
SEQRES 22 A 380 VAL LYS LEU SER ILE PRO LYS PHE LYS VAL GLU LYS MET
SEQRES 23 A 380 ILE ASP PRO LYS ALA CYS LEU GLU ASN LEU GLY LEU LYS
SEQRES 24 A 380 HIS ILE PHE SER GLU ASP THR SER ASP PHE SER GLY MET
SEQRES 25 A 380 SER GLU THR LYS GLY VAL ALA LEU SER ASN VAL ILE HIS
SEQRES 26 A 380 LYS VAL CYS LEU GLU ILE THR GLU ASP GLY GLY ASP SER
SEQRES 27 A 380 ILE GLU VAL PRO GLY ALA ARG ILE LEU GLN HIS LYS ASP
SEQRES 28 A 380 GLU LEU ASN ALA ASP HIS PRO PHE ILE TYR ILE ILE ARG
SEQRES 29 A 380 HIS ASN LYS THR ARG ASN ILE ILE PHE PHE GLY LYS PHE
SEQRES 30 A 380 CYS SER PRO
SEQRES 1 B 380 MET GLY GLN ASN SER MET ASP ALA LEU GLN LEU ALA ASN
SEQRES 2 B 380 SER ALA PHE ALA VAL ASP LEU PHE LYS GLN LEU CYS GLU
SEQRES 3 B 380 LYS GLU PRO LEU GLY ASN VAL LEU PHE SER PRO ILE CYS
SEQRES 4 B 380 LEU SER THR SER LEU SER LEU ALA GLN VAL GLY ALA LYS
SEQRES 5 B 380 GLY ASP THR ALA ASN GLU ILE GLY GLN VAL LEU HIS PHE
SEQRES 6 B 380 GLU ASN VAL LYS ASP VAL PRO PHE GLY PHE GLN THR VAL
SEQRES 7 B 380 THR SER ASP VAL ASN LYS LEU SER SER PHE TYR SER LEU
SEQRES 8 B 380 LYS LEU ILE LYS ARG LEU TYR VAL ASP LYS SER LEU ASN
SEQRES 9 B 380 LEU SER THR GLU PHE ILE SER SER THR LYS ARG PRO TYR
SEQRES 10 B 380 ALA LYS GLU LEU GLU THR VAL ASP PHE LYS ASP LYS LEU
SEQRES 11 B 380 GLU GLU THR LYS GLY GLN ILE ASN ASN SER ILE LYS ASP
SEQRES 12 B 380 LEU THR ASP GLY HIS PHE GLU ASN ILE LEU ALA ASP ASN
SEQRES 13 B 380 SER VAL ASN ASP GLN THR LYS ILE LEU VAL VAL ASN ALA
SEQRES 14 B 380 ALA TYR PHE VAL GLY LYS TRP MET LYS LYS PHE PRO GLU
SEQRES 15 B 380 SER GLU THR LYS GLU CYS PRO PHE ARG LEU ASN LYS THR
SEQRES 16 B 380 ASP THR LYS PRO VAL GLN MET MET ASN MET GLU ALA THR
SEQRES 17 B 380 PHE CYS MET GLY ASN ILE ASP SER ILE ASN CYS LYS ILE
SEQRES 18 B 380 ILE GLU LEU PRO PHE GLN ASN LYS HIS LEU SER MET PHE
SEQRES 19 B 380 ILE LEU LEU PRO LYS ASP VAL GLU ASP GLU SER THR GLY
SEQRES 20 B 380 LEU GLU LYS ILE GLU LYS GLN LEU ASN SER GLU SER LEU
SEQRES 21 B 380 SER GLN TRP THR ASN PRO SER THR MET ALA ASN ALA LYS
SEQRES 22 B 380 VAL LYS LEU SER ILE PRO LYS PHE LYS VAL GLU LYS MET
SEQRES 23 B 380 ILE ASP PRO LYS ALA CYS LEU GLU ASN LEU GLY LEU LYS
SEQRES 24 B 380 HIS ILE PHE SER GLU ASP THR SER ASP PHE SER GLY MET
SEQRES 25 B 380 SER GLU THR LYS GLY VAL ALA LEU SER ASN VAL ILE HIS
SEQRES 26 B 380 LYS VAL CYS LEU GLU ILE THR GLU ASP GLY GLY ASP SER
SEQRES 27 B 380 ILE GLU VAL PRO GLY ALA ARG ILE LEU GLN HIS LYS ASP
SEQRES 28 B 380 GLU LEU ASN ALA ASP HIS PRO PHE ILE TYR ILE ILE ARG
SEQRES 29 B 380 HIS ASN LYS THR ARG ASN ILE ILE PHE PHE GLY LYS PHE
SEQRES 30 B 380 CYS SER PRO
HET SO4 A3243 5
HET SO4 A3244 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 HOH *123(H2 O)
HELIX 1 1 ALA A 3 GLU A 23 1 21
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 101 SER A 107 1 7
HELIX 6 6 LYS A 124 THR A 140 1 17
HELIX 7 7 PRO A 176 THR A 180 5 5
HELIX 8 8 GLN A 222 LYS A 224 5 3
HELIX 9 9 ASP A 238 GLN A 249 1 12
HELIX 10 10 ASN A 251 THR A 259 1 9
HELIX 11 11 PRO A 284 GLY A 292 1 9
HELIX 12 12 LEU B 4 GLU B 23 1 20
HELIX 13 13 SER B 31 ALA B 46 1 16
HELIX 14 14 LYS B 47 LEU B 58 1 12
HELIX 15 15 ASP B 65 SER B 81 1 17
HELIX 16 16 SER B 101 LYS B 109 1 9
HELIX 17 17 LYS B 124 THR B 140 1 17
HELIX 18 18 PRO B 176 THR B 180 5 5
HELIX 19 19 GLN B 222 LYS B 224 5 3
HELIX 20 20 ASP B 238 GLN B 249 1 12
HELIX 21 21 ASN B 251 ASN B 260 1 10
HELIX 22 22 PRO B 284 LEU B 291 1 8
SHEET 1 A 7 LEU A 29 PHE A 30 0
SHEET 2 A 7 ILE A 366 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 PHE A 368
SHEET 4 A 7 LEU A 226 PRO A 233 -1 N PHE A 229 O ILE A 357
SHEET 5 A 7 CYS A 214 PRO A 220 -1 N LYS A 215 O LEU A 232
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 ILE A 366 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 PHE A 368
SHEET 4 B 8 LEU A 226 PRO A 233 -1 N PHE A 229 O ILE A 357
SHEET 5 B 8 CYS A 214 PRO A 220 -1 N LYS A 215 O LEU A 232
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 LYS A 345 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 LEU A 86 ASP A 95 1 N VAL A 94 O VAL A 119
SHEET 3 C 5 ILE A 159 VAL A 168 -1 O LEU A 160 N TYR A 93
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 LYS A 280 O VAL A 322
SHEET 1 D 7 LEU B 29 PHE B 30 0
SHEET 2 D 7 ILE B 366 PHE B 372 -1 O PHE B 369 N PHE B 30
SHEET 3 D 7 PHE B 354 HIS B 360 -1 N TYR B 356 O GLY B 370
SHEET 4 D 7 LEU B 226 PRO B 233 -1 N PHE B 229 O ILE B 357
SHEET 5 D 7 CYS 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 GLY B 207 O ILE B 216
SHEET 7 D 7 LYS B 181 ARG B 186 -1 N PHE B 185 O LYS B 193
SHEET 1 E 8 LEU B 29 PHE B 30 0
SHEET 2 E 8 ILE B 366 PHE B 372 -1 O PHE B 369 N PHE B 30
SHEET 3 E 8 PHE B 354 HIS B 360 -1 N TYR B 356 O GLY B 370
SHEET 4 E 8 LEU B 226 PRO B 233 -1 N PHE B 229 O ILE B 357
SHEET 5 E 8 CYS 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 GLY B 207 O ILE B 216
SHEET 7 E 8 ALA B 265 PRO B 274 -1 O ALA B 265 N MET B 206
SHEET 8 E 8 HIS B 344 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 VAL B 119
SHEET 3 F 5 ILE B 159 VAL B 168 -1 O LEU B 160 N TYR B 93
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 VAL B 278 O LEU B 324
SITE 1 AC1 4 LYS A 109 LYS B 173 ALA B 202 THR B 203
SITE 1 AC2 5 LYS A 129 LEU A 148 ASP A 150 ASN A 151
SITE 2 AC2 5 SER A 152
CRYST1 53.540 100.480 136.610 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 0.018679 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009953 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007320 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
