HEADER SUGAR BINDING PROTEIN 01-APR-14 4P8U
TITLE THE CRYSTAL STRUCTURES OF YKL-39 IN THE ABSENCE OF
TITLE 2 CHITOOLIGOSACCHARIDES WAS SOLVED TO RESOLUTIONS OF 2.4 ANGSTROM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHITINASE-3-LIKE PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CHONDROCYTE PROTEIN 39,YKL-39;
COMPND 5 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: CHI3L2;
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: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A(+)
KEYWDS CHITINASE 3-LIKE PROTEIN 2, HUMAN YKL-39, FAMILY-18 CHITINASE, SUGAR
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.SUGINTA,A.RANOK,R.C.ROBINSON,J.WONGSANTICHON
REVDAT 4 27-DEC-23 4P8U 1 SOURCE KEYWDS JRNL REMARK
REVDAT 3 11-FEB-15 4P8U 1 JRNL
REVDAT 2 17-DEC-14 4P8U 1 JRNL
REVDAT 1 01-OCT-14 4P8U 0
JRNL AUTH A.RANOK,J.WONGSANTICHON,R.C.ROBINSON,W.SUGINTA
JRNL TITL STRUCTURAL AND THERMODYNAMIC INSIGHTS INTO
JRNL TITL 2 CHITOOLIGOSACCHARIDE BINDING TO HUMAN CARTILAGE CHITINASE
JRNL TITL 3 3-LIKE PROTEIN 2 (CHI3L2 OR YKL-39).
JRNL REF J.BIOL.CHEM. V. 290 2617 2015
JRNL REFN ESSN 1083-351X
JRNL PMID 25477513
JRNL DOI 10.1074/JBC.M114.588905
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 13746
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 705
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.47
REMARK 3 REFLECTION IN BIN (WORKING SET) : 961
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.4200
REMARK 3 BIN FREE R VALUE SET COUNT : 56
REMARK 3 BIN FREE R VALUE : 0.3460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2896
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 168
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.21
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.58000
REMARK 3 B22 (A**2) : 0.58000
REMARK 3 B33 (A**2) : -1.16000
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): 0.781
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.282
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.279
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.320
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2990 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2797 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4051 ; 1.390 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6459 ; 0.793 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 364 ; 5.306 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 131 ;37.529 ;24.809
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 506 ;20.032 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;20.379 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 435 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3358 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 695 ; 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): 1459 ; 4.164 ; 6.452
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1458 ; 4.164 ; 6.450
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1822 ; 6.176 ; 9.675
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1823 ; 6.174 ; 9.677
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1531 ; 4.695 ; 6.811
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1531 ; 4.691 ; 6.811
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2230 ; 7.069 ;10.071
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3784 ; 9.617 ;53.862
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3754 ; 9.564 ;53.657
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 : 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 4P8U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-14.
REMARK 100 THE DEPOSITION ID IS D_1000200949.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 105
REMARK 200 PH : 5.3-5.9
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : RH COATED
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13746
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 26.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, LITHIUM SULFATE, BIS TRIS,
REMARK 280 PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 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+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.58950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 35.38200
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.38200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 35.29475
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.38200
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.38200
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 105.88425
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.38200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.38200
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 35.29475
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.38200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.38200
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 105.88425
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 0.00000
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 70.58950
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: MONOMERIC
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 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 HOH A 619 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 ALA A 20
REMARK 465 MET A 21
REMARK 465 ALA A 22
REMARK 465 ASP A 23
REMARK 465 ILE A 24
REMARK 465 GLY A 25
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 SG CYS A 31 SG CYS A 56 1.66
REMARK 500 O HOH A 538 O HOH A 651 1.74
REMARK 500 NH1 ARG A 188 OH TYR A 242 1.88
REMARK 500 O PRO A 43 O HOH A 659 2.01
REMARK 500 O PRO A 376 O HOH A 610 2.10
REMARK 500 O HOH A 535 O HOH A 551 2.12
REMARK 500 N SER A 108 O3 SO4 A 402 2.16
REMARK 500 O GLY A 183 O HOH A 644 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 542 O HOH A 543 6454 1.87
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 PRO A 43 41.95 -102.30
REMARK 500 SER A 143 78.98 -102.68
REMARK 500 ASP A 148 -166.80 61.19
REMARK 500 PRO A 221 -175.85 -69.59
REMARK 500 SER A 228 64.88 -151.60
REMARK 500 ASP A 236 91.16 -64.11
REMARK 500 SER A 241 -2.82 -58.72
REMARK 500 TYR A 243 77.26 -108.22
REMARK 500 SER A 277 -160.29 -106.62
REMARK 500 GLN A 323 64.39 70.94
REMARK 500 TYR A 377 61.84 36.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 595 DISTANCE = 6.36 ANGSTROMS
REMARK 525 HOH A 619 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH A 639 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 641 DISTANCE = 9.96 ANGSTROMS
REMARK 525 HOH A 642 DISTANCE = 7.87 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4P8W RELATED DB: PDB
REMARK 900 RELATED ID: 4P8V RELATED DB: PDB
REMARK 900 RELATED ID: 4P8U RELATED DB: PDB
DBREF 4P8U A 27 390 UNP Q15782 CH3L2_HUMAN 27 390
SEQADV 4P8U ALA A 20 UNP Q15782 EXPRESSION TAG
SEQADV 4P8U MET A 21 UNP Q15782 EXPRESSION TAG
SEQADV 4P8U ALA A 22 UNP Q15782 EXPRESSION TAG
SEQADV 4P8U ASP A 23 UNP Q15782 EXPRESSION TAG
SEQADV 4P8U ILE A 24 UNP Q15782 EXPRESSION TAG
SEQADV 4P8U GLY A 25 UNP Q15782 EXPRESSION TAG
SEQADV 4P8U SER A 26 UNP Q15782 EXPRESSION TAG
SEQADV 4P8U VAL A 182 UNP Q15782 ALA 182 ENGINEERED MUTATION
SEQADV 4P8U TRP A 318 UNP Q15782 ARG 318 ENGINEERED MUTATION
SEQRES 1 A 371 ALA MET ALA ASP ILE GLY SER TYR LYS LEU VAL CYS TYR
SEQRES 2 A 371 PHE THR ASN TRP SER GLN ASP ARG GLN GLU PRO GLY LYS
SEQRES 3 A 371 PHE THR PRO GLU ASN ILE ASP PRO PHE LEU CYS SER HIS
SEQRES 4 A 371 LEU ILE TYR SER PHE ALA SER ILE GLU ASN ASN LYS VAL
SEQRES 5 A 371 ILE ILE LYS ASP LYS SER GLU VAL MET LEU TYR GLN THR
SEQRES 6 A 371 ILE ASN SER LEU LYS THR LYS ASN PRO LYS LEU LYS ILE
SEQRES 7 A 371 LEU LEU SER ILE GLY GLY TYR LEU PHE GLY SER LYS GLY
SEQRES 8 A 371 PHE HIS PRO MET VAL ASP SER SER THR SER ARG LEU GLU
SEQRES 9 A 371 PHE ILE ASN SER ILE ILE LEU PHE LEU ARG ASN HIS ASN
SEQRES 10 A 371 PHE ASP GLY LEU ASP VAL SER TRP ILE TYR PRO ASP GLN
SEQRES 11 A 371 LYS GLU ASN THR HIS PHE THR VAL LEU ILE HIS GLU LEU
SEQRES 12 A 371 ALA GLU ALA PHE GLN LYS ASP PHE THR LYS SER THR LYS
SEQRES 13 A 371 GLU ARG LEU LEU LEU THR VAL GLY VAL SER ALA GLY ARG
SEQRES 14 A 371 GLN MET ILE ASP ASN SER TYR GLN VAL GLU LYS LEU ALA
SEQRES 15 A 371 LYS ASP LEU ASP PHE ILE ASN LEU LEU SER PHE ASP PHE
SEQRES 16 A 371 HIS GLY SER TRP GLU LYS PRO LEU ILE THR GLY HIS ASN
SEQRES 17 A 371 SER PRO LEU SER LYS GLY TRP GLN ASP ARG GLY PRO SER
SEQRES 18 A 371 SER TYR TYR ASN VAL GLU TYR ALA VAL GLY TYR TRP ILE
SEQRES 19 A 371 HIS LYS GLY MET PRO SER GLU LYS VAL VAL MET GLY ILE
SEQRES 20 A 371 PRO THR TYR GLY HIS SER PHE THR LEU ALA SER ALA GLU
SEQRES 21 A 371 THR THR VAL GLY ALA PRO ALA SER GLY PRO GLY ALA ALA
SEQRES 22 A 371 GLY PRO ILE THR GLU SER SER GLY PHE LEU ALA TYR TYR
SEQRES 23 A 371 GLU ILE CYS GLN PHE LEU LYS GLY ALA LYS ILE THR TRP
SEQRES 24 A 371 LEU GLN ASP GLN GLN VAL PRO TYR ALA VAL LYS GLY ASN
SEQRES 25 A 371 GLN TRP VAL GLY TYR ASP ASP VAL LYS SER MET GLU THR
SEQRES 26 A 371 LYS VAL GLN PHE LEU LYS ASN LEU ASN LEU GLY GLY ALA
SEQRES 27 A 371 MET ILE TRP SER ILE ASP MET ASP ASP PHE THR GLY LYS
SEQRES 28 A 371 SER CYS ASN GLN GLY PRO TYR PRO LEU VAL GLN ALA VAL
SEQRES 29 A 371 LYS ARG SER LEU GLY SER LEU
HET SO4 A 401 5
HET SO4 A 402 5
HET PEG A 403 7
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 PEG C4 H10 O3
FORMUL 5 HOH *168(H2 O)
HELIX 1 AA1 THR A 47 ILE A 51 5 5
HELIX 2 AA2 SER A 77 ASN A 92 1 16
HELIX 3 AA3 SER A 108 HIS A 112 5 5
HELIX 4 AA4 PRO A 113 ASP A 116 5 4
HELIX 5 AA5 SER A 117 HIS A 135 1 19
HELIX 6 AA6 PRO A 147 LYS A 172 1 26
HELIX 7 AA7 GLY A 187 TYR A 195 1 9
HELIX 8 AA8 GLN A 196 LEU A 204 1 9
HELIX 9 AA9 PRO A 239 TYR A 243 5 5
HELIX 10 AB1 ASN A 244 LYS A 255 1 12
HELIX 11 AB2 PRO A 258 GLU A 260 5 3
HELIX 12 AB3 TYR A 304 LEU A 311 1 8
HELIX 13 AB4 ASP A 338 LEU A 352 1 15
HELIX 14 AB5 SER A 361 ASP A 365 5 5
HELIX 15 AB6 TYR A 377 SER A 389 1 13
SHEET 1 AA110 LYS A 70 ILE A 72 0
SHEET 2 AA110 HIS A 58 GLU A 67 -1 N SER A 65 O ILE A 72
SHEET 3 AA110 LYS A 96 GLY A 102 1 O LEU A 98 N LEU A 59
SHEET 4 AA110 GLY A 139 SER A 143 1 O ASP A 141 N LEU A 99
SHEET 5 AA110 LEU A 179 VAL A 184 1 O LEU A 179 N LEU A 140
SHEET 6 AA110 PHE A 206 LEU A 209 1 O ASN A 208 N VAL A 182
SHEET 7 AA110 VAL A 262 PRO A 267 1 O VAL A 263 N LEU A 209
SHEET 8 AA110 GLY A 356 TRP A 360 1 O MET A 358 N MET A 264
SHEET 9 AA110 LYS A 28 THR A 34 1 N VAL A 30 O ILE A 359
SHEET 10 AA110 HIS A 58 GLU A 67 1 O HIS A 58 N CYS A 31
SHEET 1 AA2 3 ALA A 286 PRO A 289 0
SHEET 2 AA2 3 TYR A 269 LEU A 275 -1 N THR A 274 O GLY A 288
SHEET 3 AA2 3 LEU A 302 ALA A 303 -1 O LEU A 302 N GLY A 270
SHEET 1 AA3 5 ALA A 286 PRO A 289 0
SHEET 2 AA3 5 TYR A 269 LEU A 275 -1 N THR A 274 O GLY A 288
SHEET 3 AA3 5 GLN A 332 GLY A 335 -1 O TRP A 333 N PHE A 273
SHEET 4 AA3 5 VAL A 324 LYS A 329 -1 N ALA A 327 O VAL A 334
SHEET 5 AA3 5 LYS A 315 LEU A 319 -1 N THR A 317 O TYR A 326
SSBOND 1 CYS A 308 CYS A 372 1555 1555 1.97
CISPEP 1 GLU A 42 PRO A 43 0 -0.29
CISPEP 2 SER A 62 PHE A 63 0 1.93
CISPEP 3 HIS A 112 PRO A 113 0 7.83
CISPEP 4 ILE A 145 TYR A 146 0 -10.31
CISPEP 5 LYS A 220 PRO A 221 0 9.28
CISPEP 6 TRP A 360 SER A 361 0 -8.37
SITE 1 AC1 3 LYS A 175 ARG A 385 HOH A 503
SITE 1 AC2 3 GLY A 107 SER A 108 LYS A 109
SITE 1 AC3 5 ASP A 213 TYR A 269 PHE A 301 TRP A 360
SITE 2 AC3 5 HOH A 660
CRYST1 70.764 70.764 141.179 90.00 90.00 90.00 P 41 21 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 0.014131 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014131 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007083 0.00000
(ATOM LINES ARE NOT SHOWN.)
END