HEADER SUGAR BINDING PROTEIN 08-SEP-14 4R9T
TITLE L-FICOLIN COMPLEXED TO SULPHATES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FICOLIN-2;
COMPND 3 CHAIN: B, A, C;
COMPND 4 FRAGMENT: SUGAR BINDING DOMAIN (UNP RESIDUES 97-313);
COMPND 5 SYNONYM: 37 KDA ELASTIN-BINDING PROTEIN, COLLAGEN/FIBRINOGEN DOMAIN-
COMPND 6 CONTAINING PROTEIN 2, EBP-37, FICOLIN-B, FICOLIN-BETA, HUCOLIN, L-
COMPND 7 FICOLIN, SERUM LECTIN P35;
COMPND 8 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: FCN2, FCNL;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469
KEYWDS FIBRINOGEN-LIKE DOMAIN, INNATE IMMUNITY, PATTERN RECOGNITION PROTEIN,
KEYWDS 2 LECTIN, IMMUNOLOGY, LECTIN-LIKE, SUGAR BINDING PROTEIN, PLASMA,
KEYWDS 3 EXTRACELLULAR
EXPDTA X-RAY DIFFRACTION
AUTHOR E.LAFFLY,M.LACROIX,L.MARTIN,E.VASSAL-STERMANN,N.THIELENS,C.GABORIAUD
REVDAT 4 29-JUL-20 4R9T 1 COMPND REMARK SEQADV HETNAM
REVDAT 4 2 1 LINK SITE ATOM
REVDAT 3 14-JAN-15 4R9T 1 JRNL
REVDAT 2 17-DEC-14 4R9T 1 JRNL
REVDAT 1 05-NOV-14 4R9T 0
JRNL AUTH E.LAFFLY,M.LACROIX,L.MARTIN,E.VASSAL-STERMANN,N.M.THIELENS,
JRNL AUTH 2 C.GABORIAUD
JRNL TITL HUMAN FICOLIN-2 RECOGNITION VERSATILITY EXTENDED: AN UPDATE
JRNL TITL 2 ON THE BINDING OF FICOLIN-2 TO SULFATED/PHOSPHATED
JRNL TITL 3 CARBOHYDRATES.
JRNL REF FEBS LETT. V. 588 4694 2014
JRNL REFN ISSN 0014-5793
JRNL PMID 25447524
JRNL DOI 10.1016/J.FEBSLET.2014.10.042
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 34600
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1821
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) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2528
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 133
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5195
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 59
REMARK 3 SOLVENT ATOMS : 61
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.11000
REMARK 3 B12 (A**2) : -0.03000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.272
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.135
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.069
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5425 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4767 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7345 ; 1.668 ; 1.921
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10886 ; 1.306 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 650 ; 7.169 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 290 ;29.976 ;23.759
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 822 ;15.489 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;20.120 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 735 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6332 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1439 ; 0.006 ; 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): 2612 ; 2.809 ; 2.395
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2608 ; 2.785 ; 2.393
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3245 ; 4.357 ; 3.568
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3246 ; 4.250 ; 3.724
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2813 ; 3.417 ; 2.711
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2789 ; 3.421 ; 2.831
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4060 ; 5.444 ; 4.117
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6052 ; 7.750 ;20.282
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6044 ; 7.753 ;20.279
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 3
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 B 72 287 A 72 287 11873 0.12 0.05
REMARK 3 2 B 75 287 C 75 287 12221 0.09 0.05
REMARK 3 3 A 75 287 C 75 287 12025 0.11 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 71 B 288
REMARK 3 RESIDUE RANGE : B 301 B 306
REMARK 3 ORIGIN FOR THE GROUP (A): -39.8630 21.1660 -17.9240
REMARK 3 T TENSOR
REMARK 3 T11: 0.1705 T22: 0.1778
REMARK 3 T33: 0.0383 T12: -0.0662
REMARK 3 T13: -0.0463 T23: 0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 0.2815 L22: 0.6704
REMARK 3 L33: 0.4904 L12: 0.1697
REMARK 3 L13: 0.0703 L23: 0.0303
REMARK 3 S TENSOR
REMARK 3 S11: 0.0301 S12: 0.0005 S13: -0.0612
REMARK 3 S21: -0.0024 S22: 0.0812 S23: -0.0618
REMARK 3 S31: 0.1485 S32: -0.0034 S33: -0.1113
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 72 A 288
REMARK 3 RESIDUE RANGE : A 302 A 302
REMARK 3 ORIGIN FOR THE GROUP (A): -49.8410 16.1260 -17.4690
REMARK 3 T TENSOR
REMARK 3 T11: 0.2580 T22: 0.3308
REMARK 3 T33: 0.2351 T12: 0.0384
REMARK 3 T13: -0.1298 T23: -0.1115
REMARK 3 L TENSOR
REMARK 3 L11: 0.7539 L22: 9.6659
REMARK 3 L33: 1.6617 L12: -2.3236
REMARK 3 L13: -1.0995 L23: 3.0766
REMARK 3 S TENSOR
REMARK 3 S11: 0.0732 S12: 0.2553 S13: 0.1109
REMARK 3 S21: 0.3802 S22: -0.0739 S23: -1.0351
REMARK 3 S31: -0.0834 S32: -0.4302 S33: 0.0007
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 75 C 288
REMARK 3 RESIDUE RANGE : C 301 C 303
REMARK 3 ORIGIN FOR THE GROUP (A): -40.1610 10.6900 -14.3390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1643 T22: 0.1386
REMARK 3 T33: 0.0869 T12: -0.0253
REMARK 3 T13: -0.0062 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 0.2693 L22: 0.7413
REMARK 3 L33: 1.1733 L12: -0.0168
REMARK 3 L13: -0.0894 L23: -0.6953
REMARK 3 S TENSOR
REMARK 3 S11: 0.0045 S12: 0.0682 S13: -0.0011
REMARK 3 S21: -0.1109 S22: 0.0911 S23: 0.2079
REMARK 3 S31: 0.0979 S32: -0.0781 S33: -0.0956
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4R9T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000087079.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97240
REMARK 200 MONOCHROMATOR : SI
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 : 36406
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 48.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 5.7 MG/ML IN 145 MM
REMARK 280 NACL, 50 MM TRIETHANOLAMINE-HCL, PH 7.4. RESERVOIR SOLUTION
REMARK 280 COMPOSED OF 15% (W/V) PEG 8000, 200 MM CA ACETATE AND 0.1 M
REMARK 280 HEPES. LIGAND SOAKING. CRYOPROTECTION WAS ACHIEVED BY ADDING PEG
REMARK 280 400 TO THE DROP JUST BEFORE FLASH-COOLING THE CRYSTAL IN LIQUID
REMARK 280 NITROGEN, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K, PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 94.12667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 47.06333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 47.06333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 94.12667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, C, D
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ASN A 71
REMARK 465 ASN C 71
REMARK 465 PRO C 72
REMARK 465 CYS C 73
REMARK 465 LEU C 74
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 LYS B 81 CD CE NZ
REMARK 480 ARG A 256 O
REMARK 480 ARG C 78 CD NE CZ NH1 NH2
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 ASP A 189 O ALA A 191 2.02
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 B 132 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 132 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG B 144 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 144 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ASP B 224 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG C 78 CG - CD - NE ANGL. DEV. = 14.6 DEGREES
REMARK 500 ARG C 132 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG C 144 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG C 253 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG C 253 NE - CZ - NH2 ANGL. DEV. = -4.6 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 VAL B 124 -22.39 -147.35
REMARK 500 ASP B 125 -3.28 -156.28
REMARK 500 LYS B 243 -95.39 -110.64
REMARK 500 ASN B 244 50.67 -141.32
REMARK 500 CYS B 245 -52.76 -121.06
REMARK 500 ASN B 249 57.28 -155.58
REMARK 500 ARG B 256 75.68 67.02
REMARK 500 ASP A 100 82.34 24.86
REMARK 500 CYS A 101 42.36 -151.21
REMARK 500 ASP A 111 -65.40 -105.12
REMARK 500 VAL A 124 -22.85 -147.40
REMARK 500 ASP A 125 -3.35 -156.93
REMARK 500 GLN A 161 -172.19 95.40
REMARK 500 THR A 163 67.92 66.43
REMARK 500 GLU A 192 0.08 90.04
REMARK 500 LYS A 243 -96.27 -112.67
REMARK 500 ASN A 244 49.93 -93.32
REMARK 500 CYS A 245 -110.14 64.70
REMARK 500 ASN A 249 57.02 -153.00
REMARK 500 ARG A 256 77.14 67.04
REMARK 500 ASP C 111 -61.19 -106.54
REMARK 500 VAL C 124 -22.05 -145.23
REMARK 500 ASP C 125 -0.84 -159.18
REMARK 500 LEU C 210 -30.03 -130.77
REMARK 500 LYS C 243 -96.90 -107.30
REMARK 500 ASN C 249 56.01 -157.28
REMARK 500 ARG C 256 77.14 69.38
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 ALA A 160 GLN A 161 -147.40
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 B 304 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 224 OD2
REMARK 620 2 ASP B 224 OD1 52.8
REMARK 620 3 ASP B 226 OD1 117.6 76.1
REMARK 620 4 ASN B 228 O 153.5 153.7 83.6
REMARK 620 5 GLY B 230 O 80.2 117.4 97.5 81.4
REMARK 620 6 HOH B 422 O 116.1 80.6 82.7 80.3 161.6
REMARK 620 7 HOH B 424 O 78.1 113.5 163.5 83.0 90.0 85.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 224 OD2
REMARK 620 2 ASP A 224 OD1 54.6
REMARK 620 3 ASP A 226 OD1 115.5 76.2
REMARK 620 4 ASN A 228 O 150.2 153.7 80.7
REMARK 620 5 GLY A 230 O 76.8 114.0 90.6 78.3
REMARK 620 6 HOH A 407 O 96.1 72.4 106.8 102.9 162.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 224 OD2
REMARK 620 2 ASP C 224 OD1 54.3
REMARK 620 3 ASP C 226 OD1 120.2 78.6
REMARK 620 4 ASN C 228 O 154.6 150.8 80.4
REMARK 620 5 GLY C 230 O 82.2 120.6 95.0 81.2
REMARK 620 6 HOH C 409 O 113.4 78.4 86.5 80.3 160.9
REMARK 620 7 HOH C 412 O 84.5 119.0 155.2 76.5 90.4 80.7
REMARK 620 N 1 2 3 4 5 6
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2J0G RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO N-ACETYL-MANNOSAMINE
REMARK 900 RELATED ID: 2J0H RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO ACETYL-CHOLINE
REMARK 900 RELATED ID: 2J0Y RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO B-1,3-D-GLUCAN
REMARK 900 RELATED ID: 2J3O RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO N-ACETYL-D- GLUCOSAMIN
REMARK 900 RELATED ID: 4R9J RELATED DB: PDB
REMARK 900 L-FICOLIN COMPLEXED TO GLUCOSAMINE-6-SULFATE
DBREF 4R9T B 72 288 UNP Q15485 FCN2_HUMAN 97 313
DBREF 4R9T A 72 288 UNP Q15485 FCN2_HUMAN 97 313
DBREF 4R9T C 72 288 UNP Q15485 FCN2_HUMAN 97 313
SEQADV 4R9T ASN B 71 UNP Q15485 EXPRESSION TAG
SEQADV 4R9T ASN A 71 UNP Q15485 EXPRESSION TAG
SEQADV 4R9T ASN C 71 UNP Q15485 EXPRESSION TAG
SEQRES 1 B 218 ASN PRO CYS LEU THR GLY PRO ARG THR CYS LYS ASP LEU
SEQRES 2 B 218 LEU ASP ARG GLY HIS PHE LEU SER GLY TRP HIS THR ILE
SEQRES 3 B 218 TYR LEU PRO ASP CYS ARG PRO LEU THR VAL LEU CYS ASP
SEQRES 4 B 218 MET ASP THR ASP GLY GLY GLY TRP THR VAL PHE GLN ARG
SEQRES 5 B 218 ARG VAL ASP GLY SER VAL ASP PHE TYR ARG ASP TRP ALA
SEQRES 6 B 218 THR TYR LYS GLN GLY PHE GLY SER ARG LEU GLY GLU PHE
SEQRES 7 B 218 TRP LEU GLY ASN ASP ASN ILE HIS ALA LEU THR ALA GLN
SEQRES 8 B 218 GLY THR SER GLU LEU ARG VAL ASP LEU VAL ASP PHE GLU
SEQRES 9 B 218 ASP ASN TYR GLN PHE ALA LYS TYR ARG SER PHE LYS VAL
SEQRES 10 B 218 ALA ASP GLU ALA GLU LYS TYR ASN LEU VAL LEU GLY ALA
SEQRES 11 B 218 PHE VAL GLU GLY SER ALA GLY ASP SER LEU THR PHE HIS
SEQRES 12 B 218 ASN ASN GLN SER PHE SER THR LYS ASP GLN ASP ASN ASP
SEQRES 13 B 218 LEU ASN THR GLY ASN CYS ALA VAL MET PHE GLN GLY ALA
SEQRES 14 B 218 TRP TRP TYR LYS ASN CYS HIS VAL SER ASN LEU ASN GLY
SEQRES 15 B 218 ARG TYR LEU ARG GLY THR HIS GLY SER PHE ALA ASN GLY
SEQRES 16 B 218 ILE ASN TRP LYS SER GLY LYS GLY TYR ASN TYR SER TYR
SEQRES 17 B 218 LYS VAL SER GLU MET LYS VAL ARG PRO ALA
SEQRES 1 A 218 ASN PRO CYS LEU THR GLY PRO ARG THR CYS LYS ASP LEU
SEQRES 2 A 218 LEU ASP ARG GLY HIS PHE LEU SER GLY TRP HIS THR ILE
SEQRES 3 A 218 TYR LEU PRO ASP CYS ARG PRO LEU THR VAL LEU CYS ASP
SEQRES 4 A 218 MET ASP THR ASP GLY GLY GLY TRP THR VAL PHE GLN ARG
SEQRES 5 A 218 ARG VAL ASP GLY SER VAL ASP PHE TYR ARG ASP TRP ALA
SEQRES 6 A 218 THR TYR LYS GLN GLY PHE GLY SER ARG LEU GLY GLU PHE
SEQRES 7 A 218 TRP LEU GLY ASN ASP ASN ILE HIS ALA LEU THR ALA GLN
SEQRES 8 A 218 GLY THR SER GLU LEU ARG VAL ASP LEU VAL ASP PHE GLU
SEQRES 9 A 218 ASP ASN TYR GLN PHE ALA LYS TYR ARG SER PHE LYS VAL
SEQRES 10 A 218 ALA ASP GLU ALA GLU LYS TYR ASN LEU VAL LEU GLY ALA
SEQRES 11 A 218 PHE VAL GLU GLY SER ALA GLY ASP SER LEU THR PHE HIS
SEQRES 12 A 218 ASN ASN GLN SER PHE SER THR LYS ASP GLN ASP ASN ASP
SEQRES 13 A 218 LEU ASN THR GLY ASN CYS ALA VAL MET PHE GLN GLY ALA
SEQRES 14 A 218 TRP TRP TYR LYS ASN CYS HIS VAL SER ASN LEU ASN GLY
SEQRES 15 A 218 ARG TYR LEU ARG GLY THR HIS GLY SER PHE ALA ASN GLY
SEQRES 16 A 218 ILE ASN TRP LYS SER GLY LYS GLY TYR ASN TYR SER TYR
SEQRES 17 A 218 LYS VAL SER GLU MET LYS VAL ARG PRO ALA
SEQRES 1 C 218 ASN PRO CYS LEU THR GLY PRO ARG THR CYS LYS ASP LEU
SEQRES 2 C 218 LEU ASP ARG GLY HIS PHE LEU SER GLY TRP HIS THR ILE
SEQRES 3 C 218 TYR LEU PRO ASP CYS ARG PRO LEU THR VAL LEU CYS ASP
SEQRES 4 C 218 MET ASP THR ASP GLY GLY GLY TRP THR VAL PHE GLN ARG
SEQRES 5 C 218 ARG VAL ASP GLY SER VAL ASP PHE TYR ARG ASP TRP ALA
SEQRES 6 C 218 THR TYR LYS GLN GLY PHE GLY SER ARG LEU GLY GLU PHE
SEQRES 7 C 218 TRP LEU GLY ASN ASP ASN ILE HIS ALA LEU THR ALA GLN
SEQRES 8 C 218 GLY THR SER GLU LEU ARG VAL ASP LEU VAL ASP PHE GLU
SEQRES 9 C 218 ASP ASN TYR GLN PHE ALA LYS TYR ARG SER PHE LYS VAL
SEQRES 10 C 218 ALA ASP GLU ALA GLU LYS TYR ASN LEU VAL LEU GLY ALA
SEQRES 11 C 218 PHE VAL GLU GLY SER ALA GLY ASP SER LEU THR PHE HIS
SEQRES 12 C 218 ASN ASN GLN SER PHE SER THR LYS ASP GLN ASP ASN ASP
SEQRES 13 C 218 LEU ASN THR GLY ASN CYS ALA VAL MET PHE GLN GLY ALA
SEQRES 14 C 218 TRP TRP TYR LYS ASN CYS HIS VAL SER ASN LEU ASN GLY
SEQRES 15 C 218 ARG TYR LEU ARG GLY THR HIS GLY SER PHE ALA ASN GLY
SEQRES 16 C 218 ILE ASN TRP LYS SER GLY LYS GLY TYR ASN TYR SER TYR
SEQRES 17 C 218 LYS VAL SER GLU MET LYS VAL ARG PRO ALA
MODRES 4R9T ASN B 215 ASN GLYCOSYLATION SITE
HET NAG D 1 14
HET NAG D 2 14
HET ACT B 303 4
HET CA B 304 1
HET SO4 B 305 5
HET SO4 B 306 5
HET CA A 301 1
HET SO4 A 302 5
HET ACT C 301 4
HET CA C 302 1
HET SO4 C 303 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM ACT ACETATE ION
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 4 NAG 2(C8 H15 N O6)
FORMUL 5 ACT 2(C2 H3 O2 1-)
FORMUL 6 CA 3(CA 2+)
FORMUL 7 SO4 4(O4 S 2-)
FORMUL 14 HOH *61(H2 O)
HELIX 1 1 ASN B 71 GLY B 76 1 6
HELIX 2 2 THR B 79 ARG B 86 1 8
HELIX 3 3 ASP B 133 GLY B 140 1 8
HELIX 4 4 GLY B 151 ALA B 160 1 10
HELIX 5 5 ASP B 189 LYS B 193 5 5
HELIX 6 6 LEU B 210 ASN B 214 5 5
HELIX 7 7 ASN B 231 PHE B 236 1 6
HELIX 8 8 THR A 79 ARG A 86 1 8
HELIX 9 9 ASP A 111 GLY A 115 5 5
HELIX 10 10 ASP A 133 GLY A 140 1 8
HELIX 11 11 GLY A 151 ALA A 160 1 10
HELIX 12 12 LEU A 210 ASN A 214 5 5
HELIX 13 13 ASN A 231 PHE A 236 1 6
HELIX 14 14 THR C 79 ARG C 86 1 8
HELIX 15 15 ASP C 111 GLY C 115 5 5
HELIX 16 16 ASP C 133 GLY C 140 1 8
HELIX 17 17 GLY C 151 GLN C 161 1 11
HELIX 18 18 ASP C 189 LYS C 193 5 5
HELIX 19 19 LEU C 210 ASN C 214 5 5
HELIX 20 20 ASN C 231 PHE C 236 1 6
SHEET 1 A 5 GLY B 92 TYR B 97 0
SHEET 2 A 5 PRO B 103 ASP B 109 -1 O VAL B 106 N HIS B 94
SHEET 3 A 5 TRP B 117 ARG B 123 -1 O VAL B 119 N LEU B 107
SHEET 4 A 5 PHE B 148 TRP B 149 -1 O PHE B 148 N ARG B 122
SHEET 5 A 5 PHE B 141 GLY B 142 -1 N PHE B 141 O TRP B 149
SHEET 1 B 7 GLY B 92 TYR B 97 0
SHEET 2 B 7 PRO B 103 ASP B 109 -1 O VAL B 106 N HIS B 94
SHEET 3 B 7 TRP B 117 ARG B 123 -1 O VAL B 119 N LEU B 107
SHEET 4 B 7 VAL B 280 PRO B 287 -1 O VAL B 285 N THR B 118
SHEET 5 B 7 SER B 164 VAL B 171 -1 N ARG B 167 O LYS B 284
SHEET 6 B 7 TYR B 177 TYR B 182 -1 O ALA B 180 N VAL B 168
SHEET 7 B 7 PHE B 201 GLU B 203 -1 O VAL B 202 N LYS B 181
SHEET 1 C 2 PHE B 185 VAL B 187 0
SHEET 2 C 2 LEU B 196 LEU B 198 -1 O VAL B 197 N LYS B 186
SHEET 1 D 2 SER B 248 ASN B 249 0
SHEET 2 D 2 ASN B 267 TRP B 268 -1 O ASN B 267 N ASN B 249
SHEET 1 E 2 GLY B 257 THR B 258 0
SHEET 2 E 2 TYR B 276 SER B 277 -1 O SER B 277 N GLY B 257
SHEET 1 F 5 GLY A 92 TYR A 97 0
SHEET 2 F 5 PRO A 103 ASP A 109 -1 O VAL A 106 N HIS A 94
SHEET 3 F 5 TRP A 117 ARG A 123 -1 O VAL A 119 N LEU A 107
SHEET 4 F 5 PHE A 148 TRP A 149 -1 O PHE A 148 N ARG A 122
SHEET 5 F 5 PHE A 141 GLY A 142 -1 N PHE A 141 O TRP A 149
SHEET 1 G 7 GLY A 92 TYR A 97 0
SHEET 2 G 7 PRO A 103 ASP A 109 -1 O VAL A 106 N HIS A 94
SHEET 3 G 7 TRP A 117 ARG A 123 -1 O VAL A 119 N LEU A 107
SHEET 4 G 7 VAL A 280 PRO A 287 -1 O VAL A 285 N THR A 118
SHEET 5 G 7 SER A 164 VAL A 171 -1 N GLU A 165 O ARG A 286
SHEET 6 G 7 TYR A 177 TYR A 182 -1 O GLN A 178 N LEU A 170
SHEET 7 G 7 PHE A 201 GLU A 203 -1 O VAL A 202 N LYS A 181
SHEET 1 H 2 PHE A 185 VAL A 187 0
SHEET 2 H 2 LEU A 196 LEU A 198 -1 O VAL A 197 N LYS A 186
SHEET 1 I 2 SER A 248 ASN A 249 0
SHEET 2 I 2 ASN A 267 TRP A 268 -1 O ASN A 267 N ASN A 249
SHEET 1 J 2 GLY A 257 THR A 258 0
SHEET 2 J 2 TYR A 276 SER A 277 -1 O SER A 277 N GLY A 257
SHEET 1 K 5 GLY C 92 TYR C 97 0
SHEET 2 K 5 PRO C 103 ASP C 109 -1 O VAL C 106 N HIS C 94
SHEET 3 K 5 TRP C 117 ARG C 123 -1 O VAL C 119 N LEU C 107
SHEET 4 K 5 PHE C 148 TRP C 149 -1 O PHE C 148 N ARG C 122
SHEET 5 K 5 PHE C 141 GLY C 142 -1 N PHE C 141 O TRP C 149
SHEET 1 L 7 GLY C 92 TYR C 97 0
SHEET 2 L 7 PRO C 103 ASP C 109 -1 O VAL C 106 N HIS C 94
SHEET 3 L 7 TRP C 117 ARG C 123 -1 O VAL C 119 N LEU C 107
SHEET 4 L 7 VAL C 280 PRO C 287 -1 O VAL C 285 N THR C 118
SHEET 5 L 7 SER C 164 VAL C 171 -1 N ASP C 169 O GLU C 282
SHEET 6 L 7 TYR C 177 TYR C 182 -1 O ALA C 180 N VAL C 168
SHEET 7 L 7 PHE C 201 GLU C 203 -1 O VAL C 202 N LYS C 181
SHEET 1 M 2 PHE C 185 VAL C 187 0
SHEET 2 M 2 LEU C 196 LEU C 198 -1 O VAL C 197 N LYS C 186
SHEET 1 N 2 SER C 248 ASN C 249 0
SHEET 2 N 2 ASN C 267 TRP C 268 -1 O ASN C 267 N ASN C 249
SHEET 1 O 2 GLY C 257 THR C 258 0
SHEET 2 O 2 TYR C 276 SER C 277 -1 O SER C 277 N GLY C 257
SSBOND 1 CYS B 73 CYS B 101 1555 1555 2.07
SSBOND 2 CYS B 80 CYS B 108 1555 1555 2.15
SSBOND 3 CYS B 232 CYS B 245 1555 1555 2.10
SSBOND 4 CYS A 80 CYS A 108 1555 1555 2.10
SSBOND 5 CYS A 232 CYS A 245 1555 1555 2.06
SSBOND 6 CYS C 80 CYS C 108 1555 1555 2.10
SSBOND 7 CYS C 232 CYS C 245 1555 1555 2.07
LINK ND2 ASN B 215 C1 NAG D 1 1555 1555 1.43
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.43
LINK OD2 ASP B 224 CA CA B 304 1555 1555 2.34
LINK OD1 ASP B 224 CA CA B 304 1555 1555 2.42
LINK OD1 ASP B 226 CA CA B 304 1555 1555 2.28
LINK O ASN B 228 CA CA B 304 1555 1555 2.36
LINK O GLY B 230 CA CA B 304 1555 1555 2.29
LINK CA CA B 304 O HOH B 422 1555 1555 2.40
LINK CA CA B 304 O HOH B 424 1555 1555 2.33
LINK OD2 ASP A 224 CA CA A 301 1555 1555 2.32
LINK OD1 ASP A 224 CA CA A 301 1555 1555 2.35
LINK OD1 ASP A 226 CA CA A 301 1555 1555 2.33
LINK O ASN A 228 CA CA A 301 1555 1555 2.34
LINK O GLY A 230 CA CA A 301 1555 1555 2.36
LINK CA CA A 301 O HOH A 407 1555 1555 2.35
LINK OD2 ASP C 224 CA CA C 302 1555 1555 2.33
LINK OD1 ASP C 224 CA CA C 302 1555 1555 2.39
LINK OD1 ASP C 226 CA CA C 302 1555 1555 2.31
LINK O ASN C 228 CA CA C 302 1555 1555 2.37
LINK O GLY C 230 CA CA C 302 1555 1555 2.30
LINK CA CA C 302 O HOH C 409 1555 1555 2.34
LINK CA CA C 302 O HOH C 412 1555 1555 2.30
CISPEP 1 ASN B 244 CYS B 245 0 9.20
CISPEP 2 ASP A 100 CYS A 101 0 -3.56
CISPEP 3 GLN A 161 GLY A 162 0 17.58
CISPEP 4 ASN C 244 CYS C 245 0 1.64
CRYST1 96.110 96.110 141.190 90.00 90.00 120.00 P 32 2 1 18
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 0.010405 0.006007 0.000000 0.00000
SCALE2 0.000000 0.012014 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007083 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
