HEADER LECTIN 19-DEC-03 1UUH
TITLE HYALURONAN BINDING DOMAIN OF HUMAN CD44
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CD44 ANTIGEN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HYALURONAN BINDING DOMAIN, RESIDUES 20-178;
COMPND 5 SYNONYM: PHAGOCYTIC GLYCOPROTEIN I, PGP-1, HUTCH-I, EXTRACELLULAR
COMPND 6 MATRIX RECEPTOR-III, ECMR-III, GP90 LYMPHOCYTE HOMING/ADHESION
COMPND 7 RECEPTOR, HERMES ANTIGEN, HYALURONATE RECEPTOR, HEPARAN SULFATE
COMPND 8 PROTEOGLYCAN, EPICAN, CDW44;
COMPND 9 ENGINEERED: YES;
COMPND 10 OTHER_DETAILS: FIRST RESIDUE IS IN FACT THE LAST RESIDUE OF THE
COMPND 11 SIGNAL PEPTIDE, AND WOULD NORMALLY BE CLEAVED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: DE3 PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET19B
KEYWDS LECTIN, HYALURONAN, EXTRACELLULAR MATRIX, RECEPTOR, LINK-DOMAIN, C-
KEYWDS 2 TYPE LECTIN, SUGAR-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR P.TERIETE,S.BANERJI,M.NOBLE,C.BLUNDELL,A.WRIGHT,A.PICKFORD,E.LOWE,
AUTHOR 2 D.MAHONEY,M.TAMMI,J.KAHMANN,I.CAMPBELL,A.DAY,D.JACKSON
REVDAT 3 29-MAY-19 1UUH 1 REMARK LINK
REVDAT 2 24-FEB-09 1UUH 1 VERSN
REVDAT 1 04-MAR-04 1UUH 0
JRNL AUTH P.TERIETE,S.BANERJI,M.NOBLE,C.BLUNDELL,A.WRIGHT,A.PICKFORD,
JRNL AUTH 2 E.LOWE,D.MAHONEY,M.TAMMI,J.KAHMANN,I.CAMPBELL,A.DAY,
JRNL AUTH 3 D.JACKSON
JRNL TITL STRUCTURE OF THE REGULATORY HYALURONAN-BINDING DOMAIN IN THE
JRNL TITL 2 INFLAMMATORY LEUKOCYTE HOMING RECEPTOR CD44
JRNL REF MOL.CELL V. 13 483 2004
JRNL REFN ISSN 1097-2765
JRNL PMID 14992719
JRNL DOI 10.1016/S1097-2765(04)00080-2
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.9999
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 16553
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 881
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1200
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1900
REMARK 3 BIN FREE R VALUE SET COUNT : 52
REMARK 3 BIN FREE R VALUE : 0.2390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2334
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 262
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.28000
REMARK 3 B22 (A**2) : 0.47000
REMARK 3 B33 (A**2) : -0.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.261
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.216
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.141
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.483
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2390 ; 0.020 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2068 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3258 ; 1.956 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4818 ; 1.004 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 298 ; 8.415 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 366 ; 0.138 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2700 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 492 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 462 ; 0.240 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2531 ; 0.263 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1416 ; 0.098 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 120 ; 0.216 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 14 ; 0.233 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 63 ; 0.273 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.176 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1496 ; 0.982 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2436 ; 1.769 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 894 ; 2.854 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 822 ; 4.485 ; 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): 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 PLUS 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: NULL
REMARK 4
REMARK 4 1UUH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1290014252.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
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) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17476
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 23.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.820
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2989
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.53
REMARK 200 R MERGE FOR SHELL (I) : 0.18000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.160
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: SOLVE/RESOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING-DROP PROTEIN 13 MG/ML; WELL
REMARK 280 BUFFER 12% PEG 3350, 50MM NACL, 10% GLYCEROL, PH 5.50, VAPOR
REMARK 280 DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 24.44050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.83400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.63300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.83400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.44050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.63300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO A 170
REMARK 465 SER A 171
REMARK 465 ASN A 172
REMARK 465 PRO A 173
REMARK 465 THR A 174
REMARK 465 ASP A 175
REMARK 465 ASP A 176
REMARK 465 ASP A 177
REMARK 465 VAL A 178
REMARK 465 PRO B 170
REMARK 465 SER B 171
REMARK 465 ASN B 172
REMARK 465 PRO B 173
REMARK 465 THR B 174
REMARK 465 ASP B 175
REMARK 465 ASP B 176
REMARK 465 ASP B 177
REMARK 465 VAL B 178
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O SER A 112 O HOH A 2088 2.18
REMARK 500 O SER B 71 O HOH B 2064 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 70 CA - CB - CG ANGL. DEV. = 14.2 DEGREES
REMARK 500 LEU B 70 CA - CB - CG ANGL. DEV. = 14.5 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 SER A 43 18.90 -152.26
REMARK 500 PRO A 125 30.18 -80.21
REMARK 500 TYR A 161 -15.99 -141.50
REMARK 500 SER B 43 12.55 -152.45
REMARK 500 SER B 112 -151.38 -103.37
REMARK 500 TYR B 114 -157.13 -138.13
REMARK 500 GLU B 126 -122.34 -117.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 HYALURONAN BINDING DOMAIN ONLY
DBREF 1UUH A 20 178 UNP P16070 CD44_HUMAN 20 178
DBREF 1UUH B 20 178 UNP P16070 CD44_HUMAN 20 178
SEQRES 1 A 159 ALA GLN ILE ASP LEU ASN ILE THR CYS ARG PHE ALA GLY
SEQRES 2 A 159 VAL PHE HIS VAL GLU LYS ASN GLY ARG TYR SER ILE SER
SEQRES 3 A 159 ARG THR GLU ALA ALA ASP LEU CYS LYS ALA PHE ASN SER
SEQRES 4 A 159 THR LEU PRO THR MSE ALA GLN MSE GLU LYS ALA LEU SER
SEQRES 5 A 159 ILE GLY PHE GLU THR CYS ARG TYR GLY PHE ILE GLU GLY
SEQRES 6 A 159 HIS VAL VAL ILE PRO ARG ILE HIS PRO ASN SER ILE CYS
SEQRES 7 A 159 ALA ALA ASN ASN THR GLY VAL TYR ILE LEU THR SER ASN
SEQRES 8 A 159 THR SER GLN TYR ASP THR TYR CYS PHE ASN ALA SER ALA
SEQRES 9 A 159 PRO PRO GLU GLU ASP CYS THR SER VAL THR ASP LEU PRO
SEQRES 10 A 159 ASN ALA PHE ASP GLY PRO ILE THR ILE THR ILE VAL ASN
SEQRES 11 A 159 ARG ASP GLY THR ARG TYR VAL GLN LYS GLY GLU TYR ARG
SEQRES 12 A 159 THR ASN PRO GLU ASP ILE TYR PRO SER ASN PRO THR ASP
SEQRES 13 A 159 ASP ASP VAL
SEQRES 1 B 159 ALA GLN ILE ASP LEU ASN ILE THR CYS ARG PHE ALA GLY
SEQRES 2 B 159 VAL PHE HIS VAL GLU LYS ASN GLY ARG TYR SER ILE SER
SEQRES 3 B 159 ARG THR GLU ALA ALA ASP LEU CYS LYS ALA PHE ASN SER
SEQRES 4 B 159 THR LEU PRO THR MSE ALA GLN MSE GLU LYS ALA LEU SER
SEQRES 5 B 159 ILE GLY PHE GLU THR CYS ARG TYR GLY PHE ILE GLU GLY
SEQRES 6 B 159 HIS VAL VAL ILE PRO ARG ILE HIS PRO ASN SER ILE CYS
SEQRES 7 B 159 ALA ALA ASN ASN THR GLY VAL TYR ILE LEU THR SER ASN
SEQRES 8 B 159 THR SER GLN TYR ASP THR TYR CYS PHE ASN ALA SER ALA
SEQRES 9 B 159 PRO PRO GLU GLU ASP CYS THR SER VAL THR ASP LEU PRO
SEQRES 10 B 159 ASN ALA PHE ASP GLY PRO ILE THR ILE THR ILE VAL ASN
SEQRES 11 B 159 ARG ASP GLY THR ARG TYR VAL GLN LYS GLY GLU TYR ARG
SEQRES 12 B 159 THR ASN PRO GLU ASP ILE TYR PRO SER ASN PRO THR ASP
SEQRES 13 B 159 ASP ASP VAL
MODRES 1UUH MSE A 63 MET SELENOMETHIONINE
MODRES 1UUH MSE A 66 MET SELENOMETHIONINE
MODRES 1UUH MSE B 63 MET SELENOMETHIONINE
MODRES 1UUH MSE B 66 MET SELENOMETHIONINE
HET MSE A 63 8
HET MSE A 66 8
HET MSE B 63 8
HET MSE B 66 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 3 HOH *262(H2 O)
HELIX 1 1 SER A 45 PHE A 56 1 12
HELIX 2 2 THR A 62 SER A 71 1 10
HELIX 3 3 ALA A 98 ASN A 101 5 4
HELIX 4 4 ASN A 164 TYR A 169 1 6
HELIX 5 5 SER B 45 PHE B 56 1 12
HELIX 6 6 THR B 62 ILE B 72 1 11
HELIX 7 7 ALA B 98 ASN B 101 5 4
HELIX 8 8 ASN B 164 TYR B 169 1 6
SHEET 1 AA 8 GLY A 103 ILE A 106 0
SHEET 2 AA 8 HIS A 85 ARG A 90 -1 O ILE A 88 N TYR A 105
SHEET 3 AA 8 GLY A 80 ILE A 82 -1 O GLY A 80 N VAL A 87
SHEET 4 AA 8 ASP A 115 PHE A 119 1 O ASP A 115 N PHE A 81
SHEET 5 AA 8 VAL A 33 LYS A 38 -1 O PHE A 34 N CYS A 118
SHEET 6 AA 8 GLN A 21 ILE A 26 -1 O ASN A 25 N GLU A 37
SHEET 7 AA 8 PHE A 139 VAL A 148 1 O THR A 144 N ILE A 22
SHEET 8 AA 8 ARG A 154 GLU A 160 -1 O TYR A 155 N ILE A 147
SHEET 1 AB 2 ARG A 29 PHE A 30 0
SHEET 2 AB 2 GLU A 127 ASP A 128 -1 O ASP A 128 N ARG A 29
SHEET 1 BA 8 GLY B 103 ILE B 106 0
SHEET 2 BA 8 HIS B 85 ARG B 90 -1 O ILE B 88 N TYR B 105
SHEET 3 BA 8 GLY B 80 ILE B 82 -1 O GLY B 80 N VAL B 87
SHEET 4 BA 8 ASP B 115 PHE B 119 1 O ASP B 115 N PHE B 81
SHEET 5 BA 8 VAL B 33 LYS B 38 -1 O PHE B 34 N CYS B 118
SHEET 6 BA 8 GLN B 21 ILE B 26 -1 O ASN B 25 N GLU B 37
SHEET 7 BA 8 PHE B 139 VAL B 148 1 O THR B 144 N ILE B 22
SHEET 8 BA 8 ARG B 154 GLU B 160 -1 O TYR B 155 N ILE B 147
SHEET 1 BB 2 ARG B 29 PHE B 30 0
SHEET 2 BB 2 GLU B 127 ASP B 128 -1 O ASP B 128 N ARG B 29
SSBOND 1 CYS A 28 CYS A 129 1555 1555 2.05
SSBOND 2 CYS A 53 CYS A 118 1555 1555 2.06
SSBOND 3 CYS A 77 CYS A 97 1555 1555 2.04
SSBOND 4 CYS B 28 CYS B 129 1555 1555 2.07
SSBOND 5 CYS B 53 CYS B 118 1555 1555 2.07
SSBOND 6 CYS B 77 CYS B 97 1555 1555 2.05
LINK C THR A 62 N MSE A 63 1555 1555 1.33
LINK C MSE A 63 N ALA A 64 1555 1555 1.34
LINK C GLN A 65 N MSE A 66 1555 1555 1.33
LINK C MSE A 66 N GLU A 67 1555 1555 1.33
LINK C THR B 62 N MSE B 63 1555 1555 1.34
LINK C MSE B 63 N ALA B 64 1555 1555 1.34
LINK C GLN B 65 N MSE B 66 1555 1555 1.33
LINK C MSE B 66 N GLU B 67 1555 1555 1.33
CRYST1 48.881 77.266 87.668 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.020458 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012942 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011407 0.00000
MTRIX1 1 -0.747460 -0.617720 -0.244390 -13.39000 1
MTRIX2 1 0.439440 -0.735660 0.515450 -13.60800 1
MTRIX3 1 0.498200 -0.277890 -0.821330 -23.46900 1
(ATOM LINES ARE NOT SHOWN.)
END