HEADER HYDROLASE 22-NOV-10 3POF
TITLE CRYSTAL STRUCTURE OF MASP-1 CUB2 DOMAIN BOUND TO CA2+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MANNAN-BINDING LECTIN SERINE PROTEASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: MASP-1 CUB2 DOMAIN (UNP RESIDUES 188-301);
COMPND 5 SYNONYM: COMPLEMENT FACTOR MASP-3, COMPLEMENT-ACTIVATING COMPONENT OF
COMPND 6 RA-REACTIVE FACTOR, MANNOSE-BINDING LECTIN-ASSOCIATED SERINE PROTEASE
COMPND 7 1, MASP-1, MANNOSE-BINDING PROTEIN-ASSOCIATED SERINE PROTEASE, RA-
COMPND 8 REACTIVE FACTOR SERINE PROTEASE P100, RARF, SERINE PROTEASE 5,
COMPND 9 MANNAN-BINDING LECTIN SERINE PROTEASE 1 HEAVY CHAIN, MANNAN-BINDING
COMPND 10 LECTIN SERINE PROTEASE 1 LIGHT CHAIN;
COMPND 11 EC: 3.4.21.-;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: CRARF, MASP-1, MASP1, MASP3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS CUB DOMAIN, CA2+ BINDING SITE, COMPLEMENT PROTEIN, LECTIN PATHWAY OF
KEYWDS 2 COMPLEMENT, MBL, MBP, FICOLINS, BLOODSTREAM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.GINGRAS,P.C.E.MOODY,R.WALLIS
REVDAT 3 06-SEP-23 3POF 1 REMARK SEQADV LINK
REVDAT 2 30-NOV-11 3POF 1 JRNL
REVDAT 1 24-AUG-11 3POF 0
JRNL AUTH A.R.GINGRAS,U.V.GIRIJA,A.H.KEEBLE,R.PANCHAL,D.A.MITCHELL,
JRNL AUTH 2 P.C.MOODY,R.WALLIS
JRNL TITL STRUCTURAL BASIS OF MANNAN-BINDING LECTIN RECOGNITION BY ITS
JRNL TITL 2 ASSOCIATED SERINE PROTEASE MASP-1: IMPLICATIONS FOR
JRNL TITL 3 COMPLEMENT ACTIVATION.
JRNL REF STRUCTURE V. 19 1635 2011
JRNL REFN ISSN 0969-2126
JRNL PMID 22078562
JRNL DOI 10.1016/J.STR.2011.08.014
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 51198
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) : 0.119
REMARK 3 R VALUE (WORKING SET) : 0.117
REMARK 3 FREE R VALUE : 0.149
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2695
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3754
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1400
REMARK 3 BIN FREE R VALUE SET COUNT : 198
REMARK 3 BIN FREE R VALUE : 0.1900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1817
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 251
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.40
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.048
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.047
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.025
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.466
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2033 ; 0.034 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1429 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2797 ; 2.396 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3495 ; 1.091 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 266 ; 6.474 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 110 ;35.565 ;24.545
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 337 ;13.747 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;23.968 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 281 ; 0.172 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2320 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 418 ; 0.001 ; 0.020
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): 1206 ; 2.966 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 469 ; 1.074 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1992 ; 4.457 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 827 ; 6.020 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 784 ; 8.307 ; 4.500
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): 3462 ; 2.868 ; 3.000
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3POF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062622.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUL-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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : MULTI-LAYER OPTICS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53908
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.920
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 4.92
REMARK 200 R MERGE FOR SHELL (I) : 0.33100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.380
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 3POE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M LITHIUM SULFATE, 100MM TRIS
REMARK 280 BUFFER, PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 279K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
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 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
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 50.23000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.23000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.23000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.23000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.23000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.23000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 50.23000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 50.23000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 50.23000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 50.23000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 50.23000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 50.23000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 50.23000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 50.23000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 50.23000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 50.23000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 50.23000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 50.23000
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 S SO4 A 278 LIES ON A SPECIAL POSITION.
REMARK 375 O3 SO4 A 278 LIES ON A SPECIAL POSITION.
REMARK 375 S SO4 B 2 LIES ON A SPECIAL POSITION.
REMARK 375 O4 SO4 B 2 LIES ON A SPECIAL POSITION.
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 163
REMARK 465 VAL A 164
REMARK 465 MET B 163
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU B 200 CG CD OE1 OE2
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 293 O HOH B 312 5555 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 167 CB SER A 167 OG -0.088
REMARK 500 SER A 265 CB SER A 265 OG -0.106
REMARK 500 GLU A 267 CG GLU A 267 CD 0.101
REMARK 500 GLU A 267 CD GLU A 267 OE2 0.114
REMARK 500 ARG A 276 CB ARG A 276 CG -0.171
REMARK 500 CYS B 166 CB CYS B 166 SG -0.117
REMARK 500 GLU B 210 CG GLU B 210 CD -0.090
REMARK 500 TYR B 225 CG TYR B 225 CD2 -0.078
REMARK 500 GLU B 247 CG GLU B 247 CD 0.107
REMARK 500 SER B 250 CB SER B 250 OG -0.094
REMARK 500 ARG B 276 CB ARG B 276 CG -0.162
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 ARG A 174 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 174 NE - CZ - NH2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP A 211 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 226 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 198 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 GLU B 210 OE1 - CD - OE2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP B 211 CB - CG - OD1 ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU B 273 CA - CB - CG ANGL. DEV. = 14.4 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 CYS A 166 28.89 -160.74
REMARK 500 ASP A 182 -0.48 75.39
REMARK 500 ASP A 211 -154.13 62.67
REMARK 500 ASP A 211 -154.12 62.70
REMARK 500 TYR A 225 -64.25 -107.13
REMARK 500 ASP B 211 -153.43 62.82
REMARK 500 ASP B 211 -153.00 61.61
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 CA A 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 7 O
REMARK 620 2 HOH A 14 O 83.0
REMARK 620 3 GLU A 216 OE1 172.7 93.1
REMARK 620 4 ASP A 226 OD2 91.7 75.1 93.2
REMARK 620 5 ASP A 226 OD1 88.2 124.0 99.0 49.9
REMARK 620 6 ASP A 263 OD1 85.0 158.5 96.8 123.1 73.2
REMARK 620 7 SER A 265 O 82.7 82.7 90.7 157.6 150.7 78.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 1 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 4 O
REMARK 620 2 HOH B 8 O 84.5
REMARK 620 3 GLU B 216 OE1 170.0 87.5
REMARK 620 4 ASP B 226 OD2 90.2 81.1 94.5
REMARK 620 5 ASP B 226 OD1 91.5 126.3 98.1 45.3
REMARK 620 6 ASP B 263 OD1 83.3 162.6 103.1 111.3 66.5
REMARK 620 7 SER B 265 O 82.9 86.9 90.7 166.6 145.8 79.3
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3POB RELATED DB: PDB
REMARK 900 CUB DOMAIN IN COMPLEX WITH MBL PEPTIDE
DBREF 3POF A 164 277 UNP Q8CHN8 MASP1_RAT 188 301
DBREF 3POF B 164 277 UNP Q8CHN8 MASP1_RAT 188 301
SEQADV 3POF MET A 163 UNP Q8CHN8 INITIATING METHIONINE
SEQADV 3POF MET B 163 UNP Q8CHN8 INITIATING METHIONINE
SEQRES 1 A 115 MET VAL GLU CYS SER GLY ASN LEU PHE THR GLN ARG THR
SEQRES 2 A 115 GLY THR ILE THR SER PRO ASP TYR PRO ASN PRO TYR PRO
SEQRES 3 A 115 LYS SER SER GLU CYS SER TYR THR ILE ASP LEU GLU GLU
SEQRES 4 A 115 GLY PHE MET VAL THR LEU GLN PHE GLU ASP ILE PHE ASP
SEQRES 5 A 115 ILE GLU ASP HIS PRO GLU VAL PRO CYS PRO TYR ASP TYR
SEQRES 6 A 115 ILE LYS ILE LYS ALA GLY SER LYS VAL TRP GLY PRO PHE
SEQRES 7 A 115 CYS GLY GLU LYS SER PRO GLU PRO ILE SER THR GLN SER
SEQRES 8 A 115 HIS SER ILE GLN ILE LEU PHE ARG SER ASP ASN SER GLY
SEQRES 9 A 115 GLU ASN ARG GLY TRP ARG LEU SER TYR ARG ALA
SEQRES 1 B 115 MET VAL GLU CYS SER GLY ASN LEU PHE THR GLN ARG THR
SEQRES 2 B 115 GLY THR ILE THR SER PRO ASP TYR PRO ASN PRO TYR PRO
SEQRES 3 B 115 LYS SER SER GLU CYS SER TYR THR ILE ASP LEU GLU GLU
SEQRES 4 B 115 GLY PHE MET VAL THR LEU GLN PHE GLU ASP ILE PHE ASP
SEQRES 5 B 115 ILE GLU ASP HIS PRO GLU VAL PRO CYS PRO TYR ASP TYR
SEQRES 6 B 115 ILE LYS ILE LYS ALA GLY SER LYS VAL TRP GLY PRO PHE
SEQRES 7 B 115 CYS GLY GLU LYS SER PRO GLU PRO ILE SER THR GLN SER
SEQRES 8 B 115 HIS SER ILE GLN ILE LEU PHE ARG SER ASP ASN SER GLY
SEQRES 9 B 115 GLU ASN ARG GLY TRP ARG LEU SER TYR ARG ALA
HET CA A 1 1
HET SO4 A 278 5
HET TRS A 279 8
HET CA B 1 1
HET SO4 B 2 5
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETSYN TRS TRIS BUFFER
FORMUL 3 CA 2(CA 2+)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 5 TRS C4 H12 N O3 1+
FORMUL 8 HOH *251(H2 O)
SHEET 1 A 5 CYS A 166 PHE A 171 0
SHEET 2 A 5 GLU A 192 ASP A 198 1 O THR A 196 N PHE A 171
SHEET 3 A 5 SER A 255 ARG A 261 -1 O ILE A 258 N TYR A 195
SHEET 4 A 5 TYR A 227 ALA A 232 -1 N LYS A 229 O LEU A 259
SHEET 5 A 5 LYS A 235 PHE A 240 -1 O TRP A 237 N ILE A 230
SHEET 1 B 4 THR A 175 THR A 179 0
SHEET 2 B 4 ARG A 272 ARG A 276 -1 O LEU A 273 N ILE A 178
SHEET 3 B 4 THR A 206 PHE A 209 -1 N THR A 206 O ARG A 276
SHEET 4 B 4 ILE A 249 SER A 250 -1 O ILE A 249 N LEU A 207
SHEET 1 C 5 ASN B 169 PHE B 171 0
SHEET 2 C 5 GLU B 192 ASP B 198 1 O THR B 196 N PHE B 171
SHEET 3 C 5 SER B 255 ARG B 261 -1 O PHE B 260 N CYS B 193
SHEET 4 C 5 TYR B 227 ALA B 232 -1 N LYS B 231 O GLN B 257
SHEET 5 C 5 LYS B 235 PHE B 240 -1 O TRP B 237 N ILE B 230
SHEET 1 D 4 THR B 175 THR B 179 0
SHEET 2 D 4 ARG B 272 ARG B 276 -1 O LEU B 273 N ILE B 178
SHEET 3 D 4 THR B 206 PHE B 209 -1 N GLN B 208 O SER B 274
SHEET 4 D 4 ILE B 249 SER B 250 -1 O ILE B 249 N LEU B 207
SSBOND 1 CYS A 166 CYS A 193 1555 1555 2.23
SSBOND 2 CYS A 223 CYS A 241 1555 1555 2.25
SSBOND 3 CYS B 166 CYS B 193 1555 1555 2.65
SSBOND 4 CYS B 223 CYS B 241 1555 1555 2.18
LINK CA CA A 1 O HOH A 7 1555 1555 2.37
LINK CA CA A 1 O HOH A 14 1555 1555 2.49
LINK CA CA A 1 OE1 GLU A 216 1555 1555 2.20
LINK CA CA A 1 OD2 ASP A 226 1555 1555 2.43
LINK CA CA A 1 OD1 ASP A 226 1555 1555 2.68
LINK CA CA A 1 OD1 ASP A 263 1555 1555 2.39
LINK CA CA A 1 O SER A 265 1555 1555 2.32
LINK CA CA B 1 O HOH B 4 1555 1555 2.43
LINK CA CA B 1 O HOH B 8 1555 1555 2.43
LINK CA CA B 1 OE1 GLU B 216 1555 1555 2.25
LINK CA CA B 1 OD2 ASP B 226 1555 1555 2.34
LINK CA CA B 1 OD1 ASP B 226 1555 1555 3.11
LINK CA CA B 1 OD1 ASP B 263 1555 1555 2.36
LINK CA CA B 1 O SER B 265 1555 1555 2.28
CISPEP 1 TYR A 183 PRO A 184 0 3.79
CISPEP 2 GLY A 238 PRO A 239 0 9.07
CISPEP 3 TYR B 183 PRO B 184 0 7.45
CISPEP 4 GLY B 238 PRO B 239 0 4.38
SITE 1 AC1 6 HOH A 7 HOH A 14 GLU A 216 ASP A 226
SITE 2 AC1 6 ASP A 263 SER A 265
SITE 1 AC2 3 HOH A 31 ARG A 269 HOH A 304
SITE 1 AC3 12 HOH A 34 HOH A 161 ASP A 182 TYR A 183
SITE 2 AC3 12 ASN A 185 PHE A 209 GLU A 210 ASP A 211
SITE 3 AC3 12 SER A 245 HOH A 284 HOH A 299 THR B 175
SITE 1 AC4 6 HOH B 4 HOH B 8 GLU B 216 ASP B 226
SITE 2 AC4 6 ASP B 263 SER B 265
SITE 1 AC5 3 HOH B 30 HOH B 62 ARG B 269
CRYST1 100.460 100.460 100.460 90.00 90.00 90.00 P 21 3 24
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 0.009954 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009954 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009954 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
