HEADER HYDROLASE/DE NOVO PROTEIN 23-JAN-12 4AFS
TITLE HUMAN CHYMASE - FYNOMER COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHYMASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-CHYMASE, MAST CELL PROTEASE I;
COMPND 5 EC: 3.4.21.39;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: FYNOMER;
COMPND 9 CHAIN: C;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 8 ORGANISM_TAXID: 32630;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE-DE NOVO PROTEIN COMPLEX, INHIBITOR, SERINE PROTEASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.SCHLATTER,S.BRACK,D.W.BANNER,S.BATEY,J.BENZ,J.BERTSCHINGER,W.HUBER,
AUTHOR 2 C.JOSEPH,A.RUFER,A.VAN DER KLOOSTERS,M.WEBER,D.GRABULOVSKI,M.HENNIG
REVDAT 2 15-AUG-12 4AFS 1 AUTHOR JRNL
REVDAT 1 11-JUL-12 4AFS 0
JRNL AUTH D.SCHLATTER,S.BRACK,D.W.BANNER,S.BATEY,J.BENZ,
JRNL AUTH 2 J.BERTSCHINGER,W.HUBER,C.JOSEPH,A.RUFER,A.VAN DER KLOOSTER,
JRNL AUTH 3 M.WEBER,D.GRABULOVSKI,M.HENNIG
JRNL TITL GENERATION, CHARACTERIZATION AND STRUCTURAL DATA OF CHYMASE
JRNL TITL 2 BINDING PROTEINS BASED ON THE HUMAN FYN KINASE SH3 DOMAIN.
JRNL REF MABS V. 4 497 2012
JRNL REFN ISSN 1942-0862
JRNL PMID 22653218
JRNL DOI 10.4161/MABS.20452
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0070
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.00
REMARK 3 NUMBER OF REFLECTIONS : 25639
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) : 0.18913
REMARK 3 R VALUE (WORKING SET) : 0.18662
REMARK 3 FREE R VALUE : 0.23796
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 1365
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) : 1.900
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.949
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1754
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.289
REMARK 3 BIN FREE R VALUE SET COUNT : 112
REMARK 3 BIN FREE R VALUE : 0.333
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2261
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 185
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.5
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.28
REMARK 3 B22 (A**2) : 3.51
REMARK 3 B33 (A**2) : -1.22
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.144
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.144
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.110
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.885
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2344 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3186 ; 1.511 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 287 ; 6.133 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 103 ;33.836 ;23.107
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 377 ;12.537 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;16.347 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 341 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1786 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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
REMARK 3 RIDING POSITIONS. HYDROGENS USED BUT NOT OUTPUT
REMARK 4
REMARK 4 4AFS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JAN-12.
REMARK 100 THE PDBE ID CODE IS EBI-51019.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9998
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL (PSI PILATUS 6M)
REMARK 200 DETECTOR MANUFACTURER : DECTRIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35077
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.75
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.43
REMARK 200 R MERGE (I) : 0.07
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.68
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.35
REMARK 200 R MERGE FOR SHELL (I) : 0.67
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.51
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: IN HOUSE STRUCTURE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M
REMARK 280 TRIS PH 8.5, 25 % PEG 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 39.29200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.53600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.29200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.53600
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: 2470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 C -3
REMARK 465 ARG C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 GLY C 1
REMARK 465 VAL C 2
REMARK 465 THR C 3
REMARK 465 GLY C 65
REMARK 465 GLU C 66
REMARK 465 GLN C 67
REMARK 465 LYS C 68
REMARK 465 LEU C 69
REMARK 465 ILE C 70
REMARK 465 SER C 71
REMARK 465 GLU C 72
REMARK 465 GLU C 73
REMARK 465 ASP C 74
REMARK 465 LEU C 75
REMARK 465 HIS C 76
REMARK 465 HIS C 77
REMARK 465 HIS C 78
REMARK 465 HIS C 79
REMARK 465 HIS C 80
REMARK 465 HIS C 81
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 OG SER A 182 O HOH A 2132 2.17
REMARK 500 O4 PO4 A 1228 O HOH A 2092 2.00
REMARK 500 O HOH A 2108 O HOH A 2109 2.00
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 P PO4 A 1228 P PO4 A 1228 2555 1.24
REMARK 500 P PO4 A 1228 O1 PO4 A 1228 2555 1.34
REMARK 500 P PO4 A 1228 O2 PO4 A 1228 2555 2.18
REMARK 500 P PO4 A 1228 O3 PO4 A 1228 2555 1.32
REMARK 500 O1 PO4 A 1228 O2 PO4 A 1228 2555 1.92
REMARK 500 O1 PO4 A 1228 O3 PO4 A 1228 2555 0.67
REMARK 500 O2 PO4 A 1228 O2 PO4 A 1228 2555 2.09
REMARK 500 O3 PO4 A 1228 O4 PO4 A 1228 2555 1.93
REMARK 500 C1 GOL A 1230 C2 GOL A 1230 2555 1.76
REMARK 500 C1 GOL A 1230 C3 GOL A 1230 2555 1.17
REMARK 500 C1 GOL A 1230 O3 GOL A 1230 2555 0.78
REMARK 500 O1 GOL A 1230 C3 GOL A 1230 2555 1.35
REMARK 500 O1 GOL A 1230 O3 GOL A 1230 2555 0.87
REMARK 500 C2 GOL A 1230 C2 GOL A 1230 2555 0.30
REMARK 500 C2 GOL A 1230 O2 GOL A 1230 2555 1.44
REMARK 500 C2 GOL A 1230 C3 GOL A 1230 2555 1.28
REMARK 500 C2 GOL A 1230 O3 GOL A 1230 2555 2.18
REMARK 500 O2 GOL A 1230 O2 GOL A 1230 2555 0.66
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 23 -157.43 -175.71
REMARK 500 HIS A 58 -72.74 -121.47
REMARK 500 SER A 182 128.64 -29.12
REMARK 500 SER A 197 -71.82 -113.55
REMARK 500 GLN A 224 -4.09 -57.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1227 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 10 NE2
REMARK 620 2 HIS C 22 NE2 88.3
REMARK 620 3 HOH A2019 O 118.6 115.5
REMARK 620 4 GLU A 64 OE2 110.4 109.6 112.1
REMARK 620 N 1 2 3
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A1227
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1228
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1231
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KLT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PMSF-TREATED HUMAN CHYMASE AT 1.
REMARK 900 9 ANGSTROMS RESOLUTION
REMARK 900 RELATED ID: 1PJP RELATED DB: PDB
REMARK 900 THE 2.2 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN
REMARK 900 COMPLEX WITH SUCCINYL-ALA-ALA-PRO-PHE-CHLOROMETHYLKETONE
REMARK 900 RELATED ID: 4AFZ RELATED DB: PDB
REMARK 900 HUMAN CHYMASE - FYNOMER COMPLEX
REMARK 900 RELATED ID: 1NN6 RELATED DB: PDB
REMARK 900 HUMAN PRO-CHYMASE
REMARK 900 RELATED ID: 4AFU RELATED DB: PDB
REMARK 900 HUMAN CHYMASE - FYNOMER COMPLEX
REMARK 900 RELATED ID: 1T31 RELATED DB: PDB
REMARK 900 A DUAL INHIBITOR OF THE LEUKOCYTE PROTEASES CATHEPSIN
REMARK 900 G ANDCHYMASE WITH THERAPEUTIC EFFICACY IN ANIMALS MODELS
REMARK 900 OFINFLAMMATION
REMARK 900 RELATED ID: 4AFQ RELATED DB: PDB
REMARK 900 HUMAN CHYMASE - FYNOMER COMPLEX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ARTIFICIAL PROTEIN BASED ON SH3 DOMAIN OF P06241 (83-145)
DBREF 4AFS A 1 226 UNP P23946 CMA1_HUMAN 22 247
DBREF 4AFS C -3 81 PDB 4AFS 4AFS -3 81
SEQRES 1 A 226 ILE ILE GLY GLY THR GLU CYS LYS PRO HIS SER ARG PRO
SEQRES 2 A 226 TYR MET ALA TYR LEU GLU ILE VAL THR SER ASN GLY PRO
SEQRES 3 A 226 SER LYS PHE CYS GLY GLY PHE LEU ILE ARG ARG ASN PHE
SEQRES 4 A 226 VAL LEU THR ALA ALA HIS CYS ALA GLY ARG SER ILE THR
SEQRES 5 A 226 VAL THR LEU GLY ALA HIS ASN ILE THR GLU GLU GLU ASP
SEQRES 6 A 226 THR TRP GLN LYS LEU GLU VAL ILE LYS GLN PHE ARG HIS
SEQRES 7 A 226 PRO LYS TYR ASN THR SER THR LEU HIS HIS ASP ILE MET
SEQRES 8 A 226 LEU LEU LYS LEU LYS GLU LYS ALA SER LEU THR LEU ALA
SEQRES 9 A 226 VAL GLY THR LEU PRO PHE PRO SER GLN PHE ASN PHE VAL
SEQRES 10 A 226 PRO PRO GLY ARG MET CYS ARG VAL ALA GLY TRP GLY ARG
SEQRES 11 A 226 THR GLY VAL LEU LYS PRO GLY SER ASP THR LEU GLN GLU
SEQRES 12 A 226 VAL LYS LEU ARG LEU MET ASP PRO GLN ALA CYS SER HIS
SEQRES 13 A 226 PHE ARG ASP PHE ASP HIS ASN LEU GLN LEU CYS VAL GLY
SEQRES 14 A 226 ASN PRO ARG LYS THR LYS SER ALA PHE LYS GLY ASP SER
SEQRES 15 A 226 GLY GLY PRO LEU LEU CYS ALA GLY VAL ALA GLN GLY ILE
SEQRES 16 A 226 VAL SER TYR GLY ARG SER ASP ALA LYS PRO PRO ALA VAL
SEQRES 17 A 226 PHE THR ARG ILE SER HIS TYR ARG PRO TRP ILE ASN GLN
SEQRES 18 A 226 ILE LEU GLN ALA ASN
SEQRES 1 C 85 MET ARG GLY SER GLY VAL THR LEU PHE VAL ALA LEU TYR
SEQRES 2 C 85 ASP TYR GLN ALA ASP ARG TRP THR ASP LEU SER PHE HIS
SEQRES 3 C 85 LYS GLY GLU LYS PHE GLN ILE LEU ASP ALA SER PRO PRO
SEQRES 4 C 85 GLY ASP TRP TRP GLU ALA ARG SER LEU THR THR GLY GLU
SEQRES 5 C 85 THR GLY TYR ILE PRO SER ASN TYR VAL ALA PRO VAL ASP
SEQRES 6 C 85 SER ILE GLN GLY GLU GLN LYS LEU ILE SER GLU GLU ASP
SEQRES 7 C 85 LEU HIS HIS HIS HIS HIS HIS
HET ZN A1227 1
HET PO4 A1228 5
HET PO4 A1229 5
HET GOL A1230 6
HET PO4 A1231 5
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETNAM ZN ZINC ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 PO4 3(O4 P 3-)
FORMUL 4 GOL C3 H8 O3
FORMUL 5 ZN ZN 2+
FORMUL 6 HOH *185(H2 O)
HELIX 1 1 ALA A 43 ALA A 47 5 5
HELIX 2 2 ASP A 150 SER A 155 5 6
HELIX 3 3 TYR A 215 GLN A 224 1 10
HELIX 4 4 ASP C 61 ILE C 63 5 3
SHEET 1 AA 7 THR A 5 GLU A 6 0
SHEET 2 AA 7 GLN A 142 ARG A 147 -1 O GLU A 143 N THR A 5
SHEET 3 AA 7 MET A 122 GLY A 127 -1 O CYS A 123 N LEU A 146
SHEET 4 AA 7 PRO A 185 CYS A 188 -1 O PRO A 185 N ALA A 126
SHEET 5 AA 7 VAL A 191 TYR A 198 -1 O VAL A 191 N CYS A 188
SHEET 6 AA 7 ALA A 207 ARG A 211 -1 O VAL A 208 N SER A 197
SHEET 7 AA 7 GLN A 165 VAL A 168 -1 O LEU A 166 N PHE A 209
SHEET 1 AB 7 MET A 15 VAL A 21 0
SHEET 2 AB 7 LYS A 28 ARG A 36 -1 O LYS A 28 N ILE A 20
SHEET 3 AB 7 PHE A 39 THR A 42 -1 O PHE A 39 N ILE A 35
SHEET 4 AB 7 MET A 91 LEU A 95 -1 O MET A 91 N THR A 42
SHEET 5 AB 7 GLN A 68 ARG A 77 -1 N ILE A 73 O LYS A 94
SHEET 6 AB 7 SER A 50 LEU A 55 -1 O ILE A 51 N VAL A 72
SHEET 7 AB 7 MET A 15 VAL A 21 -1 O TYR A 17 N THR A 54
SHEET 1 CA 5 THR C 49 PRO C 53 0
SHEET 2 CA 5 TRP C 38 SER C 43 -1 O TRP C 39 N ILE C 52
SHEET 3 CA 5 LYS C 26 ASP C 31 -1 O GLN C 28 N ARG C 42
SHEET 4 CA 5 PHE C 5 ALA C 7 -1 O PHE C 5 N PHE C 27
SHEET 5 CA 5 VAL C 57 PRO C 59 -1 O ALA C 58 N VAL C 6
SSBOND 1 CYS A 30 CYS A 46 1555 1555 2.06
SSBOND 2 CYS A 123 CYS A 188 1555 1555 2.05
SSBOND 3 CYS A 154 CYS A 167 1555 1555 2.05
LINK ZN ZN A1227 NE2 HIS A 10 1555 1555 1.94
LINK ZN ZN A1227 NE2 HIS C 22 1555 4455 2.02
LINK ZN ZN A1227 O HOH A2019 1555 1555 1.96
LINK ZN ZN A1227 OE2 GLU A 64 1555 1555 1.81
CISPEP 1 PRO A 205 PRO A 206 0 4.45
SITE 1 AC1 4 HIS A 10 GLU A 64 HOH A2019 HIS C 22
SITE 1 AC2 6 ARG A 124 ALA A 189 GLY A 190 HOH A2092
SITE 2 AC2 6 HOH A2152 HOH A2153
SITE 1 AC3 8 PHE A 29 HIS A 45 LYS A 179 GLY A 180
SITE 2 AC3 8 SER A 182 HOH A2131 HOH A2154 TRP C 16
SITE 1 AC4 4 ASN A 115 ARG A 121 GLN A 193 HOH A2133
SITE 1 AC5 2 ARG A 124 LYS A 145
CRYST1 78.584 89.072 48.494 90.00 90.00 90.00 P 21 21 2 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 0.012725 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011227 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020621 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
