HEADER BLOOD CLOTTING 16-APR-12 4AQB
TITLE MBL-FICOLIN ASSOCIATED PROTEIN-1, MAP-1 AKA MAP44
CAVEAT 4AQB NAG B 2 HAS WRONG CHIRALITY AT ATOM C1 NAG C 2 HAS WRONG
CAVEAT 2 4AQB CHIRALITY AT ATOM C1 NAG A 650 WRONG CHIRALITY AT C1 NAG A
CAVEAT 3 4AQB 679 WRONG CHIRALITY AT C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MANNAN-BINDING LECTIN SERINE PROTEASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MBL-FICOLIN ASSOCIATED PROTEIN-1, COMPLEMENT FACTOR MASP-3,
COMPND 5 COMPLEMENT-ACTIVATING COMPONENT OF RA-REACTIVE FACTOR, MANNOSE-
COMPND 6 BINDING LECTIN-ASSOCIATED SERINE PROTEASE 1, MASP-1, MANNOSE-BINDING
COMPND 7 PROTEIN-ASSOCIATED SERINE PROTEASE, RA-REACTIVE FACTOR SERINE
COMPND 8 PROTEASE P100, RARF, SERINE PROTEASE 5, MANNAN-BINDING LECTIN SERINE
COMPND 9 PROTEASE 1 HEAVY CHAIN;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: PLASMA;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: CHO DG44;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PPCR-SCRIPT AMP
KEYWDS BLOOD CLOTTING, MANNAN-BINDING PROTEIN, COMPLEMENT, FICOLINS, LECTIN
KEYWDS 2 COMPLEMENT PATHWAY, MANNOSE- BINDING LECTIN, MBL/FICOLIN ASSOCIATED
KEYWDS 3 PROTEIN-1, MBL/FICOLIN ASSOCIATED SERINE PROTEASES, MAP1, MAP44
EXPDTA X-RAY DIFFRACTION
AUTHOR M.O.SKJOEDT,P.ROVERSI,T.HUMMELSHOJ,Y.PALARASAH,S.JOHNSON,S.M.LEA,
AUTHOR 2 P.GARRED
REVDAT 4 20-DEC-23 4AQB 1 HETSYN
REVDAT 3 29-JUL-20 4AQB 1 CAVEAT COMPND REMARK HETNAM
REVDAT 3 2 1 LINK SITE ATOM
REVDAT 2 03-OCT-12 4AQB 1 JRNL
REVDAT 1 08-AUG-12 4AQB 0
JRNL AUTH M.O.SKJOEDT,P.ROVERSI,T.HUMMELSHOJ,Y.PALARASAH,A.ROSBJERG,
JRNL AUTH 2 S.JOHNSON,S.M.LEA,P.GARRED
JRNL TITL CRYSTAL STRUCTURE AND FUNCTIONAL CHARACTERIZATION OF THE
JRNL TITL 2 COMPLEMENT REGULATOR MANNOSE-BINDING LECTIN
JRNL TITL 3 (MBL)/FICOLIN-ASSOCIATED PROTEIN-1 (MAP-1).
JRNL REF J.BIOL.CHEM. V. 287 32913 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22854970
JRNL DOI 10.1074/JBC.M112.386680
REMARK 2
REMARK 2 RESOLUTION. 4.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 7843
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) : 0.280
REMARK 3 R VALUE (WORKING SET) : 0.279
REMARK 3 FREE R VALUE : 0.301
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.590
REMARK 3 FREE R VALUE TEST SET COUNT : 360
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 5
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 4.20
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 4.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.80
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1997
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2672
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1908
REMARK 3 BIN R VALUE (WORKING SET) : 0.2675
REMARK 3 BIN FREE R VALUE : 0.2617
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.46
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 89
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2774
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 117
REMARK 3 SOLVENT ATOMS : 5
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 129.9
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 145.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 8.74430
REMARK 3 B22 (A**2) : 8.74430
REMARK 3 B33 (A**2) : -17.48850
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 1.502
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.797
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.819
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.822
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2999 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4073 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1049 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 86 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 422 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2999 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 3 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 410 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : 23 ; 1.000 ; HARMONIC
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3182 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.02
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.21
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.28
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 22-138, 702 AND 649-653)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1981 1.8495 9.9228
REMARK 3 T TENSOR
REMARK 3 T11: -0.2853 T22: 0.2851
REMARK 3 T33: -0.2055 T12: -0.1520
REMARK 3 T13: 0.0375 T23: -0.1520
REMARK 3 L TENSOR
REMARK 3 L11: 5.6274 L22: 6.9268
REMARK 3 L33: 7.7296 L12: -1.4636
REMARK 3 L13: -2.0046 L23: 1.5688
REMARK 3 S TENSOR
REMARK 3 S11: 0.0749 S12: -0.5350 S13: -0.0560
REMARK 3 S21: -0.3367 S22: -0.3183 S23: 0.5442
REMARK 3 S31: -0.0866 S32: -0.5320 S33: 0.2435
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 139-183, 678-681, 701)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6116 1.0105 11.8990
REMARK 3 T TENSOR
REMARK 3 T11: -0.0444 T22: 0.3040
REMARK 3 T33: 0.0605 T12: -0.0984
REMARK 3 T13: -0.0604 T23: 0.1520
REMARK 3 L TENSOR
REMARK 3 L11: 2.6314 L22: 0.0000
REMARK 3 L33: 3.2180 L12: 0.0548
REMARK 3 L13: 2.9104 L23: -1.3430
REMARK 3 S TENSOR
REMARK 3 S11: 0.0587 S12: 0.1971 S13: 0.3789
REMARK 3 S21: 0.5442 S22: -0.0249 S23: -0.2950
REMARK 3 S31: -0.2757 S32: -0.1090 S33: -0.0338
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 184-298, 703)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.3816 5.3099 28.6848
REMARK 3 T TENSOR
REMARK 3 T11: 0.2393 T22: -0.0246
REMARK 3 T33: -0.2653 T12: -0.1520
REMARK 3 T13: -0.1520 T23: 0.0961
REMARK 3 L TENSOR
REMARK 3 L11: 8.3154 L22: 6.1439
REMARK 3 L33: 2.1775 L12: 0.9554
REMARK 3 L13: 1.5638 L23: -2.9065
REMARK 3 S TENSOR
REMARK 3 S11: 0.0052 S12: 0.0443 S13: 0.5442
REMARK 3 S21: -0.0050 S22: 0.0005 S23: -0.0840
REMARK 3 S31: 0.1500 S32: -0.1388 S33: -0.0057
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 299-366)
REMARK 3 ORIGIN FOR THE GROUP (A): 78.8382 10.5071 30.5146
REMARK 3 T TENSOR
REMARK 3 T11: 0.2897 T22: 0.2460
REMARK 3 T33: -0.3039 T12: -0.1488
REMARK 3 T13: -0.1520 T23: -0.1476
REMARK 3 L TENSOR
REMARK 3 L11: 3.6872 L22: 3.4684
REMARK 3 L33: 0.5500 L12: 0.9470
REMARK 3 L13: 1.4068 L23: -0.4727
REMARK 3 S TENSOR
REMARK 3 S11: -0.0354 S12: 0.0541 S13: -0.1982
REMARK 3 S21: -0.3990 S22: 0.1817 S23: 0.2231
REMARK 3 S31: 0.1100 S32: -0.0433 S33: -0.1463
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TLS REFINEMENT AND SECONDARY INITIAL
REMARK 3 COORDINATES FROM MOLECULAR REPLACEMENT. SECONDARY STRUCTURE
REMARK 3 RESTRAINTS TO THE INITIAL COORDINATES FROM MOLECULAR REPLACEMENT.
REMARK 4
REMARK 4 4AQB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1290052057.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97930
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7844
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.200
REMARK 200 RESOLUTION RANGE LOW (A) : 58.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.5
REMARK 200 DATA REDUNDANCY : 3.640
REMARK 200 R MERGE (I) : 0.28000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
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 ENTRIES 3DEM AND 3GOV
REMARK 200
REMARK 200 REMARK: DATA ANISOTROPICALLY TRUNCATED AND B-SHARPENED WITH A B=
REMARK 200 -5.85 AT THE UCLA SERVER HTTP SERVICES.MBI.UCLA.EDU ANISOSCALE
REMARK 200 ANISOSCALE_XDS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 81.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM ACETATE, 0.1 M SODIUM
REMARK 280 CACODYLATE PH 6.5, 40% W/V PEG 400
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+1/4
REMARK 290 8555 -Y,-X,-Z+3/4
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 121.28500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 181.92750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 60.64250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 121.28500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 60.64250
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 181.92750
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: 5620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 HIS A 20
REMARK 465 THR A 21
REMARK 465 ILE A 367
REMARK 465 ASP A 368
REMARK 465 LEU A 369
REMARK 465 GLU A 370
REMARK 465 SER A 371
REMARK 465 GLU A 372
REMARK 465 LEU A 373
REMARK 465 LYS A 374
REMARK 465 SER A 375
REMARK 465 GLU A 376
REMARK 465 GLN A 377
REMARK 465 VAL A 378
REMARK 465 THR A 379
REMARK 465 GLU A 380
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 GLU A 303 OE1 OE2
REMARK 470 LYS A 358 CD CE NZ
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 OD1 ASN A 26 O PHE A 28 1.99
REMARK 500 NH2 ARG A 146 SG CYS A 157 2.11
REMARK 500 O VAL A 140 O HOH A 2001 2.12
REMARK 500 NH1 ARG A 146 SG CYS A 157 2.18
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 151 C - N - CA ANGL. DEV. = 21.0 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 ASN A 26 -166.70 -174.99
REMARK 500 TYR A 75 -85.56 -84.58
REMARK 500 THR A 82 -167.69 -108.09
REMARK 500 THR A 98 49.42 73.22
REMARK 500 ASP A 121 -167.12 -77.17
REMARK 500 ASN A 124 55.64 -117.52
REMARK 500 GLU A 149 -123.87 -106.39
REMARK 500 GLU A 150 -94.71 -123.74
REMARK 500 LEU A 151 33.76 76.87
REMARK 500 HIS A 155 -85.55 -109.45
REMARK 500 ARG A 179 -52.15 -136.17
REMARK 500 LEU A 189 110.45 -166.55
REMARK 500 ASP A 230 -147.73 59.56
REMARK 500 CYS A 242 68.31 35.10
REMARK 500 TYR A 244 -71.84 -107.74
REMARK 500 PRO A 253 31.38 -93.37
REMARK 500 ASP A 338 -111.63 56.61
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 GLU A 150 LEU A 151 31.67
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 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 68 OE1
REMARK 620 2 GLU A 68 OE2 50.4
REMARK 620 3 ASP A 76 OD1 88.0 137.1
REMARK 620 4 ASP A 76 OD2 93.2 114.4 49.1
REMARK 620 5 ASP A 121 OD1 105.5 128.0 66.5 111.9
REMARK 620 6 SER A 123 O 121.6 76.8 145.2 135.5 86.6
REMARK 620 7 HOH A2002 O 102.9 61.1 133.9 85.3 145.6 61.9
REMARK 620 8 HOH A2003 O 162.5 138.8 78.5 69.6 79.5 75.1 79.3
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 139 OD1
REMARK 620 2 ASP A 139 OD2 47.0
REMARK 620 3 VAL A 140 O 79.1 73.2
REMARK 620 4 GLU A 142 OE1 131.9 141.9 70.2
REMARK 620 5 ASN A 159 OD1 138.6 91.7 87.0 76.5
REMARK 620 6 TYR A 160 O 75.0 75.6 148.1 141.7 100.3
REMARK 620 7 GLY A 163 O 125.6 143.9 142.7 72.8 88.0 69.0
REMARK 620 8 HOH A2001 O 65.1 98.6 53.1 67.0 132.5 127.2 108.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 703 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 235 OE1
REMARK 620 2 ASP A 245 OD1 126.2
REMARK 620 3 ASP A 245 OD2 94.5 52.6
REMARK 620 4 ASP A 282 OD1 121.2 92.3 141.8
REMARK 620 5 SER A 284 O 85.2 146.9 123.0 76.7
REMARK 620 6 HOH A2004 O 89.0 101.5 57.9 128.8 65.0
REMARK 620 7 HOH A2005 O 153.8 75.5 88.5 65.7 71.5 70.6
REMARK 620 N 1 2 3 4 5 6
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 NO SIGNAL PEPTIDE RESIDUES 1-19
REMARK 999 ISOFORM 3 OF MASP-1, AKA MAP-1, AKA MAP44
DBREF 4AQB A 20 380 UNP P48740 MASP1_HUMAN 20 380
SEQRES 1 A 361 HIS THR VAL GLU LEU ASN ASN MET PHE GLY GLN ILE GLN
SEQRES 2 A 361 SER PRO GLY TYR PRO ASP SER TYR PRO SER ASP SER GLU
SEQRES 3 A 361 VAL THR TRP ASN ILE THR VAL PRO ASP GLY PHE ARG ILE
SEQRES 4 A 361 LYS LEU TYR PHE MET HIS PHE ASN LEU GLU SER SER TYR
SEQRES 5 A 361 LEU CYS GLU TYR ASP TYR VAL LYS VAL GLU THR GLU ASP
SEQRES 6 A 361 GLN VAL LEU ALA THR PHE CYS GLY ARG GLU THR THR ASP
SEQRES 7 A 361 THR GLU GLN THR PRO GLY GLN GLU VAL VAL LEU SER PRO
SEQRES 8 A 361 GLY SER PHE MET SER ILE THR PHE ARG SER ASP PHE SER
SEQRES 9 A 361 ASN GLU GLU ARG PHE THR GLY PHE ASP ALA HIS TYR MET
SEQRES 10 A 361 ALA VAL ASP VAL ASP GLU CYS LYS GLU ARG GLU ASP GLU
SEQRES 11 A 361 GLU LEU SER CYS ASP HIS TYR CYS HIS ASN TYR ILE GLY
SEQRES 12 A 361 GLY TYR TYR CYS SER CYS ARG PHE GLY TYR ILE LEU HIS
SEQRES 13 A 361 THR ASP ASN ARG THR CYS ARG VAL GLU CYS SER ASP ASN
SEQRES 14 A 361 LEU PHE THR GLN ARG THR GLY VAL ILE THR SER PRO ASP
SEQRES 15 A 361 PHE PRO ASN PRO TYR PRO LYS SER SER GLU CYS LEU TYR
SEQRES 16 A 361 THR ILE GLU LEU GLU GLU GLY PHE MET VAL ASN LEU GLN
SEQRES 17 A 361 PHE GLU ASP ILE PHE ASP ILE GLU ASP HIS PRO GLU VAL
SEQRES 18 A 361 PRO CYS PRO TYR ASP TYR ILE LYS ILE LYS VAL GLY PRO
SEQRES 19 A 361 LYS VAL LEU GLY PRO PHE CYS GLY GLU LYS ALA PRO GLU
SEQRES 20 A 361 PRO ILE SER THR GLN SER HIS SER VAL LEU ILE LEU PHE
SEQRES 21 A 361 HIS SER ASP ASN SER GLY GLU ASN ARG GLY TRP ARG LEU
SEQRES 22 A 361 SER TYR ARG ALA ALA GLY ASN GLU CYS PRO GLU LEU GLN
SEQRES 23 A 361 PRO PRO VAL HIS GLY LYS ILE GLU PRO SER GLN ALA LYS
SEQRES 24 A 361 TYR PHE PHE LYS ASP GLN VAL LEU VAL SER CYS ASP THR
SEQRES 25 A 361 GLY TYR LYS VAL LEU LYS ASP ASN VAL GLU MET ASP THR
SEQRES 26 A 361 PHE GLN ILE GLU CYS LEU LYS ASP GLY THR TRP SER ASN
SEQRES 27 A 361 LYS ILE PRO THR CYS LYS LYS ASN GLU ILE ASP LEU GLU
SEQRES 28 A 361 SER GLU LEU LYS SER GLU GLN VAL THR GLU
MODRES 4AQB ASN A 49 ASN GLYCOSYLATION SITE
MODRES 4AQB ASN A 178 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET MAN B 4 11
HET MAN B 5 11
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET MAN C 4 11
HET CA A 701 1
HET CA A 702 1
HET CA A 703 1
HET CA A 706 1
HET CA A 707 1
HET CA A 708 1
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM CA CALCIUM ION
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
FORMUL 2 NAG 4(C8 H15 N O6)
FORMUL 2 BMA 2(C6 H12 O6)
FORMUL 2 MAN 3(C6 H12 O6)
FORMUL 4 CA 6(CA 2+)
FORMUL 10 HOH *5(H2 O)
HELIX 1 1 SER A 70 GLU A 74 5 5
HELIX 2 2 ASP A 141 GLU A 145 5 5
HELIX 3 3 GLU A 145 GLU A 149 5 5
SHEET 1 AA 5 GLU A 23 ASN A 25 0
SHEET 2 AA 5 SER A 44 THR A 51 1 O ASN A 49 N LEU A 24
SHEET 3 AA 5 PHE A 113 SER A 120 -1 O MET A 114 N ILE A 50
SHEET 4 AA 5 TYR A 77 GLU A 81 -1 O TYR A 77 N ARG A 119
SHEET 5 AA 5 VAL A 86 PHE A 90 -1 N LEU A 87 O VAL A 80
SHEET 1 AB 4 PHE A 28 GLN A 32 0
SHEET 2 AB 4 GLY A 130 ASP A 139 -1 O ALA A 133 N ILE A 31
SHEET 3 AB 4 PHE A 56 ASN A 66 -1 O ARG A 57 N VAL A 138
SHEET 4 AB 4 VAL A 107 LEU A 108 -1 O VAL A 107 N LEU A 60
SHEET 1 AC 2 TYR A 156 TYR A 160 0
SHEET 2 AC 2 GLY A 163 SER A 167 -1 O GLY A 163 N TYR A 160
SHEET 1 AD 2 ILE A 173 LEU A 174 0
SHEET 2 AD 2 CYS A 181 ARG A 182 -1 O ARG A 182 N ILE A 173
SHEET 1 AE 4 THR A 194 THR A 198 0
SHEET 2 AE 4 ARG A 291 ALA A 297 -1 O LEU A 292 N ILE A 197
SHEET 3 AE 4 MET A 223 PHE A 228 -1 O MET A 223 N ALA A 297
SHEET 4 AE 4 ILE A 268 SER A 269 -1 O ILE A 268 N LEU A 226
SHEET 1 AF 4 GLU A 211 GLU A 217 0
SHEET 2 AF 4 SER A 274 HIS A 280 -1 O VAL A 275 N ILE A 216
SHEET 3 AF 4 TYR A 246 VAL A 251 -1 O TYR A 246 N HIS A 280
SHEET 4 AF 4 LYS A 254 PHE A 259 -1 O LYS A 254 N VAL A 251
SHEET 1 AG 2 GLU A 300 CYS A 301 0
SHEET 2 AG 2 TYR A 319 PHE A 320 -1 O TYR A 319 N CYS A 301
SHEET 1 AH 3 GLY A 310 GLU A 313 0
SHEET 2 AH 3 GLN A 324 CYS A 329 -1 O LEU A 326 N GLU A 313
SHEET 3 AH 3 THR A 344 GLU A 348 -1 O PHE A 345 N VAL A 327
SHEET 1 AI 3 VAL A 340 MET A 342 0
SHEET 2 AI 3 TYR A 333 LYS A 337 -1 O VAL A 335 N MET A 342
SHEET 3 AI 3 THR A 361 LYS A 364 -1 O THR A 361 N LEU A 336
SSBOND 1 CYS A 73 CYS A 91 1555 1555 2.03
SSBOND 2 CYS A 143 CYS A 157 1555 1555 2.03
SSBOND 3 CYS A 153 CYS A 166 1555 1555 2.03
SSBOND 4 CYS A 168 CYS A 181 1555 1555 2.03
SSBOND 5 CYS A 185 CYS A 212 1555 1555 2.03
SSBOND 6 CYS A 242 CYS A 260 1555 1555 2.03
SSBOND 7 CYS A 301 CYS A 349 1555 1555 2.03
SSBOND 8 CYS A 329 CYS A 362 1555 1555 2.03
LINK ND2 ASN A 49 C1 NAG B 1 1555 1555 1.42
LINK ND2 ASN A 178 C1 NAG C 1 1555 1555 1.43
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.42
LINK O3 BMA B 3 C1 MAN B 4 1555 1555 1.43
LINK O6 BMA B 3 C1 MAN B 5 1555 1555 1.41
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.42
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.43
LINK OE1 GLU A 68 CA CA A 702 1555 1555 2.49
LINK OE2 GLU A 68 CA CA A 702 1555 1555 2.66
LINK OD1 ASP A 76 CA CA A 702 1555 1555 2.67
LINK OD2 ASP A 76 CA CA A 702 1555 1555 2.60
LINK OD1 ASP A 121 CA CA A 702 1555 1555 2.37
LINK O SER A 123 CA CA A 702 1555 1555 2.55
LINK OD1 ASP A 139 CA CA A 701 1555 1555 2.66
LINK OD2 ASP A 139 CA CA A 701 1555 1555 2.85
LINK O VAL A 140 CA CA A 701 1555 1555 2.42
LINK OE1 GLU A 142 CA CA A 701 1555 1555 2.72
LINK OD1 ASN A 159 CA CA A 701 1555 1555 2.14
LINK O TYR A 160 CA CA A 701 1555 1555 2.36
LINK O GLY A 163 CA CA A 701 1555 1555 2.56
LINK OE1 GLU A 235 CA CA A 703 1555 1555 2.10
LINK OD1 ASP A 245 CA CA A 703 1555 1555 2.50
LINK OD2 ASP A 245 CA CA A 703 1555 1555 2.45
LINK OD1 ASP A 282 CA CA A 703 1555 1555 2.10
LINK O SER A 284 CA CA A 703 1555 1555 2.50
LINK CA CA A 701 O HOH A2001 1555 1555 2.30
LINK CA CA A 702 O HOH A2002 1555 1555 2.59
LINK CA CA A 702 O HOH A2003 1555 1555 2.65
LINK CA CA A 703 O HOH A2004 1555 1555 2.22
LINK CA CA A 703 O HOH A2005 1555 1555 2.39
CISPEP 1 TYR A 36 PRO A 37 0 3.49
CISPEP 2 PHE A 202 PRO A 203 0 1.92
CISPEP 3 GLY A 257 PRO A 258 0 0.89
CISPEP 4 GLU A 313 PRO A 314 0 -1.11
CRYST1 94.150 94.150 242.570 90.00 90.00 90.00 P 43 2 2 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 0.010621 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010621 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004123 0.00000
(ATOM LINES ARE NOT SHOWN.)
END