HEADER HYDROLASE 02-MAR-16 5IJQ
TITLE CRYSTAL STRUCTURE OF AUTOTAXIN (ENPP2) RE-REFINED
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE FAMILY
COMPND 3 MEMBER 2;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: E-NPP 2,AUTOTAXIN,EXTRACELLULAR LYSOPHOSPHOLIPASE D,LYSOPLD;
COMPND 6 EC: 3.1.4.39;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: ENPP2, ATX, NPPS2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: FLP-IN;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293
KEYWDS HYDROLASE, LYSOPHOSPHATIDYLCHOLINE, SOMATOMEDIN, INFLAMMATION,
KEYWDS 2 METASTASIS, NEUROPATHIC PAIN, VASCULAR DEVELOPMENT, NEURAL
KEYWDS 3 DEVELOPMENT
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HAUSMANN,R.P.JOOSTEN,A.PERRAKIS
REVDAT 5 10-JAN-24 5IJQ 1 HETSYN
REVDAT 4 29-JUL-20 5IJQ 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 13-JUL-16 5IJQ 1 JRNL
REVDAT 2 22-JUN-16 5IJQ 1 JRNL
REVDAT 1 15-JUN-16 5IJQ 0
JRNL AUTH J.HAUSMANN,W.J.KEUNE,A.L.HIPGRAVE EDERVEEN,L.VAN ZEIJL,
JRNL AUTH 2 R.P.JOOSTEN,A.PERRAKIS
JRNL TITL STRUCTURAL SNAPSHOTS OF THE CATALYTIC CYCLE OF THE
JRNL TITL 2 PHOSPHODIESTERASE AUTOTAXIN.
JRNL REF J.STRUCT.BIOL. V. 195 199 2016
JRNL REFN ESSN 1095-8657
JRNL PMID 27268273
JRNL DOI 10.1016/J.JSB.2016.06.002
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.5
REMARK 3 NUMBER OF REFLECTIONS : 45374
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) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2386
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6329
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 120
REMARK 3 SOLVENT ATOMS : 290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.83000
REMARK 3 B22 (A**2) : -0.08000
REMARK 3 B33 (A**2) : -0.83000
REMARK 3 B12 (A**2) : -0.24000
REMARK 3 B13 (A**2) : 0.85000
REMARK 3 B23 (A**2) : -0.27000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.204
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.165
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.627
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5IJQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218914.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.283
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52153
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : 4.800
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.490
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: 2GSN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN BUFFER: 3.5-5.0 MG/ML
REMARK 280 AUTOTAXIN IN 50 MM TRIS PH 8.0 AND 150 MM NACL CRYSTALLIZATION
REMARK 280 CONDITION: 20% PEG 3350, 0.2 M AMMONIUM IODIDE, 0.3 M SODIUM
REMARK 280 THIOCYANATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32310 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 ALA A 36
REMARK 465 GLU A 37
REMARK 465 TRP A 38
REMARK 465 ASP A 39
REMARK 465 GLU A 40
REMARK 465 GLY A 41
REMARK 465 PRO A 42
REMARK 465 PRO A 43
REMARK 465 THR A 44
REMARK 465 VAL A 45
REMARK 465 LEU A 46
REMARK 465 SER A 47
REMARK 465 ASP A 48
REMARK 465 SER A 49
REMARK 465 PRO A 50
REMARK 465 TRP A 51
REMARK 465 THR A 52
REMARK 465 ASN A 53
REMARK 465 THR A 54
REMARK 465 SER A 55
REMARK 465 ASN A 398
REMARK 465 ASN A 399
REMARK 465 SER A 400
REMARK 465 LYS A 401
REMARK 465 LEU A 458
REMARK 465 ASP A 459
REMARK 465 VAL A 460
REMARK 465 TYR A 461
REMARK 465 LYS A 462
REMARK 465 LYS A 463
REMARK 465 PRO A 464
REMARK 465 SER A 465
REMARK 465 GLY A 466
REMARK 465 LYS A 467
REMARK 465 ASP A 570
REMARK 465 LYS A 571
REMARK 465 VAL A 572
REMARK 465 GLU A 573
REMARK 465 PRO A 574
REMARK 465 LYS A 575
REMARK 465 ASN A 576
REMARK 465 SER A 860
REMARK 465 GLU A 861
REMARK 465 ILE A 862
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 OG1 THR A 209 ZN ZN A 907 1.64
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 83 57.34 39.58
REMARK 500 LEU A 94 46.75 -100.09
REMARK 500 GLU A 155 79.83 -115.77
REMARK 500 ARG A 368 64.92 -100.84
REMARK 500 CYS A 413 56.77 39.29
REMARK 500 ALA A 435 -37.28 -145.99
REMARK 500 ARG A 450 -0.61 85.43
REMARK 500 ASP A 477 128.95 -32.16
REMARK 500 THR A 485 -162.59 -128.16
REMARK 500 LEU A 596 78.95 -116.78
REMARK 500 SER A 676 -159.06 -120.71
REMARK 500 TRP A 814 -24.89 -153.27
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 ZN A 907 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 171 OD1
REMARK 620 2 ASP A 358 OD2 93.6
REMARK 620 3 HIS A 359 NE2 100.4 95.2
REMARK 620 4 PO4 A 908 O1 100.3 152.5 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 906 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 311 OD1
REMARK 620 2 ASP A 311 OD2 53.3
REMARK 620 3 HIS A 315 NE2 102.5 86.0
REMARK 620 4 HIS A 474 NE2 96.5 149.8 105.3
REMARK 620 5 PO4 A 908 O2 148.3 114.2 105.6 90.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 933 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 669 O
REMARK 620 2 ASP A 672 O 71.7
REMARK 620 3 MET A 675 O 88.4 76.4
REMARK 620 4 GOL A 939 O2 62.6 128.8 80.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 909 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 739 OD1
REMARK 620 2 ASN A 741 OD1 84.0
REMARK 620 3 ASP A 743 OD1 79.5 80.2
REMARK 620 4 LEU A 745 O 90.0 164.0 84.2
REMARK 620 5 ASP A 747 OD1 100.0 90.9 171.0 104.8
REMARK 620 6 HOH A1142 O 165.3 86.9 87.7 95.8 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 934 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 801 O
REMARK 620 2 SER A 804 O 65.5
REMARK 620 3 SER A 807 OG 74.8 71.4
REMARK 620 4 HOH A1148 O 73.1 138.3 93.8
REMARK 620 5 HOH A1204 O 90.3 83.3 154.2 102.1
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XR9 RELATED DB: PDB
REMARK 900 THE ZN ATOMS WERE REFINED WITH ANISOTROPIC B-FACTORS TO STUDY THEIR
REMARK 900 MOVEMENT. ADDITIONAL MODEL CHANGES WERE INCLUSION OF A PREVIOUSLY
REMARK 900 UNIDENTIFIED 7-ALPHA-OXYSTEROL AND TWO SODIUM IONS.
DBREF 5IJQ A 36 862 UNP Q64610 ENPP2_RAT 36 862
SEQADV 5IJQ ALA A 410 UNP Q64610 ASN 410 ENGINEERED MUTATION
SEQADV 5IJQ PHE A 581 UNP Q64610 LEU 581 CLONING ARTIFACT
SEQADV 5IJQ THR A 591 UNP Q64610 ARG 591 CLONING ARTIFACT
SEQADV 5IJQ ALA A 806 UNP Q64610 ASN 806 ENGINEERED MUTATION
SEQRES 1 A 827 ALA GLU TRP ASP GLU GLY PRO PRO THR VAL LEU SER ASP
SEQRES 2 A 827 SER PRO TRP THR ASN THR SER GLY SER CYS LYS GLY ARG
SEQRES 3 A 827 CYS PHE GLU LEU GLN GLU VAL GLY PRO PRO ASP CYS ARG
SEQRES 4 A 827 CYS ASP ASN LEU CYS LYS SER TYR SER SER CYS CYS HIS
SEQRES 5 A 827 ASP PHE ASP GLU LEU CYS LEU LYS THR ALA ARG GLY TRP
SEQRES 6 A 827 GLU CYS THR LYS ASP ARG CYS GLY GLU VAL ARG ASN GLU
SEQRES 7 A 827 GLU ASN ALA CYS HIS CYS SER GLU ASP CYS LEU SER ARG
SEQRES 8 A 827 GLY ASP CYS CYS THR ASN TYR GLN VAL VAL CYS LYS GLY
SEQRES 9 A 827 GLU SER HIS TRP VAL ASP ASP ASP CYS GLU GLU ILE LYS
SEQRES 10 A 827 VAL PRO GLU CYS PRO ALA GLY PHE VAL ARG PRO PRO LEU
SEQRES 11 A 827 ILE ILE PHE SER VAL ASP GLY PHE ARG ALA SER TYR MET
SEQRES 12 A 827 LYS LYS GLY SER LYS VAL MET PRO ASN ILE GLU LYS LEU
SEQRES 13 A 827 ARG SER CYS GLY THR HIS ALA PRO TYR MET ARG PRO VAL
SEQRES 14 A 827 TYR PRO THR LYS THR PHE PRO ASN LEU TYR THR LEU ALA
SEQRES 15 A 827 THR GLY LEU TYR PRO GLU SER HIS GLY ILE VAL GLY ASN
SEQRES 16 A 827 SER MET TYR ASP PRO VAL PHE ASP ALA SER PHE HIS LEU
SEQRES 17 A 827 ARG GLY ARG GLU LYS PHE ASN HIS ARG TRP TRP GLY GLY
SEQRES 18 A 827 GLN PRO LEU TRP ILE THR ALA THR LYS GLN GLY VAL ARG
SEQRES 19 A 827 ALA GLY THR PHE PHE TRP SER VAL SER ILE PRO HIS GLU
SEQRES 20 A 827 ARG ARG ILE LEU THR ILE LEU GLN TRP LEU SER LEU PRO
SEQRES 21 A 827 ASP ASN GLU ARG PRO SER VAL TYR ALA PHE TYR SER GLU
SEQRES 22 A 827 GLN PRO ASP PHE SER GLY HIS LYS TYR GLY PRO PHE GLY
SEQRES 23 A 827 PRO GLU MET THR ASN PRO LEU ARG GLU ILE ASP LYS THR
SEQRES 24 A 827 VAL GLY GLN LEU MET ASP GLY LEU LYS GLN LEU ARG LEU
SEQRES 25 A 827 HIS ARG CYS VAL ASN VAL ILE PHE VAL GLY ASP HIS GLY
SEQRES 26 A 827 MET GLU ASP VAL THR CYS ASP ARG THR GLU PHE LEU SER
SEQRES 27 A 827 ASN TYR LEU THR ASN VAL ASP ASP ILE THR LEU VAL PRO
SEQRES 28 A 827 GLY THR LEU GLY ARG ILE ARG ALA LYS SER ILE ASN ASN
SEQRES 29 A 827 SER LYS TYR ASP PRO LYS THR ILE ILE ALA ALA LEU THR
SEQRES 30 A 827 CYS LYS LYS PRO ASP GLN HIS PHE LYS PRO TYR MET LYS
SEQRES 31 A 827 GLN HIS LEU PRO LYS ARG LEU HIS TYR ALA ASN ASN ARG
SEQRES 32 A 827 ARG ILE GLU ASP ILE HIS LEU LEU VAL ASP ARG ARG TRP
SEQRES 33 A 827 HIS VAL ALA ARG LYS PRO LEU ASP VAL TYR LYS LYS PRO
SEQRES 34 A 827 SER GLY LYS CYS PHE PHE GLN GLY ASP HIS GLY PHE ASP
SEQRES 35 A 827 ASN LYS VAL ASN SER MET GLN THR VAL PHE VAL GLY TYR
SEQRES 36 A 827 GLY PRO THR PHE LYS TYR ARG THR LYS VAL PRO PRO PHE
SEQRES 37 A 827 GLU ASN ILE GLU LEU TYR ASN VAL MET CYS ASP LEU LEU
SEQRES 38 A 827 GLY LEU LYS PRO ALA PRO ASN ASN GLY THR HIS GLY SER
SEQRES 39 A 827 LEU ASN HIS LEU LEU ARG THR ASN THR PHE ARG PRO THR
SEQRES 40 A 827 MET PRO ASP GLU VAL SER ARG PRO ASN TYR PRO GLY ILE
SEQRES 41 A 827 MET TYR LEU GLN SER GLU PHE ASP LEU GLY CYS THR CYS
SEQRES 42 A 827 ASP ASP LYS VAL GLU PRO LYS ASN LYS LEU GLU GLU PHE
SEQRES 43 A 827 ASN LYS ARG LEU HIS THR LYS GLY SER THR LYS GLU ARG
SEQRES 44 A 827 HIS LEU LEU TYR GLY ARG PRO ALA VAL LEU TYR ARG THR
SEQRES 45 A 827 SER TYR ASP ILE LEU TYR HIS THR ASP PHE GLU SER GLY
SEQRES 46 A 827 TYR SER GLU ILE PHE LEU MET PRO LEU TRP THR SER TYR
SEQRES 47 A 827 THR ILE SER LYS GLN ALA GLU VAL SER SER ILE PRO GLU
SEQRES 48 A 827 HIS LEU THR ASN CYS VAL ARG PRO ASP VAL ARG VAL SER
SEQRES 49 A 827 PRO GLY PHE SER GLN ASN CYS LEU ALA TYR LYS ASN ASP
SEQRES 50 A 827 LYS GLN MET SER TYR GLY PHE LEU PHE PRO PRO TYR LEU
SEQRES 51 A 827 SER SER SER PRO GLU ALA LYS TYR ASP ALA PHE LEU VAL
SEQRES 52 A 827 THR ASN MET VAL PRO MET TYR PRO ALA PHE LYS ARG VAL
SEQRES 53 A 827 TRP ALA TYR PHE GLN ARG VAL LEU VAL LYS LYS TYR ALA
SEQRES 54 A 827 SER GLU ARG ASN GLY VAL ASN VAL ILE SER GLY PRO ILE
SEQRES 55 A 827 PHE ASP TYR ASN TYR ASP GLY LEU ARG ASP THR GLU ASP
SEQRES 56 A 827 GLU ILE LYS GLN TYR VAL GLU GLY SER SER ILE PRO VAL
SEQRES 57 A 827 PRO THR HIS TYR TYR SER ILE ILE THR SER CYS LEU ASP
SEQRES 58 A 827 PHE THR GLN PRO ALA ASP LYS CYS ASP GLY PRO LEU SER
SEQRES 59 A 827 VAL SER SER PHE ILE LEU PRO HIS ARG PRO ASP ASN ASP
SEQRES 60 A 827 GLU SER CYS ALA SER SER GLU ASP GLU SER LYS TRP VAL
SEQRES 61 A 827 GLU GLU LEU MET LYS MET HIS THR ALA ARG VAL ARG ASP
SEQRES 62 A 827 ILE GLU HIS LEU THR GLY LEU ASP PHE TYR ARG LYS THR
SEQRES 63 A 827 SER ARG SER TYR SER GLU ILE LEU THR LEU LYS THR TYR
SEQRES 64 A 827 LEU HIS THR TYR GLU SER GLU ILE
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET 5JK A 901 29
HET SCN A 905 3
HET ZN A 906 1
HET ZN A 907 1
HET PO4 A 908 5
HET CA A 909 1
HET IOD A 910 1
HET IOD A 911 1
HET IOD A 912 2
HET IOD A 913 1
HET IOD A 914 1
HET IOD A 915 1
HET IOD A 916 1
HET IOD A 917 1
HET IOD A 918 1
HET IOD A 919 1
HET IOD A 920 1
HET IOD A 921 1
HET IOD A 922 1
HET IOD A 923 1
HET IOD A 924 1
HET IOD A 925 1
HET IOD A 926 1
HET IOD A 927 1
HET IOD A 928 1
HET IOD A 929 1
HET IOD A 930 1
HET IOD A 931 1
HET IOD A 932 1
HET NA A 933 1
HET NA A 934 1
HET SCN A 935 3
HET SCN A 936 3
HET SCN A 937 3
HET IOD A 938 1
HET GOL A 939 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM 5JK 7ALPHA-HYDROXYCHOLESTEROL
HETNAM SCN THIOCYANATE ION
HETNAM ZN ZINC ION
HETNAM PO4 PHOSPHATE ION
HETNAM CA CALCIUM ION
HETNAM IOD IODIDE ION
HETNAM NA SODIUM ION
HETNAM GOL GLYCEROL
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 5JK (3BETA,7ALPHA,9BETA,14BETA)-CHOLEST-5-ENE-3,7-DIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 2 BMA C6 H12 O6
FORMUL 3 5JK C27 H46 O2
FORMUL 4 SCN 4(C N S 1-)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 PO4 O4 P 3-
FORMUL 8 CA CA 2+
FORMUL 9 IOD 24(I 1-)
FORMUL 32 NA 2(NA 1+)
FORMUL 38 GOL C3 H8 O3
FORMUL 39 HOH *290(H2 O)
HELIX 1 AA1 ASP A 88 CYS A 93 1 6
HELIX 2 AA2 THR A 103 CYS A 107 5 5
HELIX 3 AA3 ASN A 132 LYS A 138 1 7
HELIX 4 AA4 HIS A 142 ASP A 146 5 5
HELIX 5 AA5 ARG A 174 GLY A 181 5 8
HELIX 6 AA6 MET A 185 GLY A 195 1 11
HELIX 7 AA7 LYS A 208 GLY A 219 1 12
HELIX 8 AA8 TYR A 221 GLY A 226 1 6
HELIX 9 AA9 ARG A 246 TRP A 254 5 9
HELIX 10 AB1 PRO A 258 GLN A 266 1 9
HELIX 11 AB2 PRO A 280 SER A 293 1 14
HELIX 12 AB3 ASP A 311 GLY A 318 1 8
HELIX 13 AB4 GLY A 321 GLU A 323 5 3
HELIX 14 AB5 MET A 324 LEU A 345 1 22
HELIX 15 AB6 SER A 373 TYR A 375 5 3
HELIX 16 AB7 ASN A 378 ASP A 380 5 3
HELIX 17 AB8 ASP A 403 LEU A 411 1 9
HELIX 18 AB9 GLN A 426 LEU A 428 5 3
HELIX 19 AC1 PRO A 429 HIS A 433 5 5
HELIX 20 AC2 VAL A 480 GLN A 484 5 5
HELIX 21 AC3 GLU A 507 LEU A 516 1 10
HELIX 22 AC4 LEU A 530 LEU A 534 5 5
HELIX 23 AC5 LEU A 558 PHE A 562 5 5
HELIX 24 AC6 LEU A 578 ASN A 582 1 5
HELIX 25 AC7 SER A 590 LEU A 596 1 7
HELIX 26 AC8 PRO A 645 THR A 649 5 5
HELIX 27 AC9 SER A 659 SER A 663 5 5
HELIX 28 AD1 ASN A 665 ASP A 672 1 8
HELIX 29 AD2 PRO A 682 SER A 686 5 5
HELIX 30 AD3 SER A 688 PHE A 696 1 9
HELIX 31 AD4 LEU A 697 THR A 699 5 3
HELIX 32 AD5 TYR A 705 VAL A 718 1 14
HELIX 33 AD6 VAL A 718 ASN A 728 1 11
HELIX 34 AD7 THR A 748 ILE A 752 5 5
HELIX 35 AD8 PRO A 780 CYS A 784 5 5
HELIX 36 AD9 ASP A 810 LYS A 813 5 4
HELIX 37 AE1 TRP A 814 HIS A 822 1 9
HELIX 38 AE2 ARG A 825 GLY A 834 1 10
HELIX 39 AE3 SER A 844 TYR A 854 1 11
SHEET 1 AA1 6 VAL A 302 PRO A 310 0
SHEET 2 AA1 6 LEU A 165 ASP A 171 1 N ILE A 167 O PHE A 305
SHEET 3 AA1 6 ASN A 352 GLY A 357 1 O ILE A 354 N PHE A 168
SHEET 4 AA1 6 PHE A 487 TYR A 490 -1 O TYR A 490 N VAL A 353
SHEET 5 AA1 6 THR A 196 HIS A 197 -1 N THR A 196 O GLY A 489
SHEET 6 AA1 6 THR A 498 LYS A 499 1 O THR A 498 N HIS A 197
SHEET 1 AA2 2 MET A 201 ARG A 202 0
SHEET 2 AA2 2 PHE A 503 GLU A 504 1 O PHE A 503 N ARG A 202
SHEET 1 AA3 2 MET A 232 ASP A 234 0
SHEET 2 AA3 2 ALA A 239 PHE A 241 -1 O PHE A 241 N MET A 232
SHEET 1 AA4 2 GLU A 362 ASP A 363 0
SHEET 2 AA4 2 GLY A 472 ASP A 473 -1 O ASP A 473 N GLU A 362
SHEET 1 AA5 2 THR A 369 PHE A 371 0
SHEET 2 AA5 2 HIS A 452 ALA A 454 1 O ALA A 454 N GLU A 370
SHEET 1 AA6 4 ILE A 382 VAL A 385 0
SHEET 2 AA6 4 LEU A 389 ALA A 394 -1 O ARG A 393 N THR A 383
SHEET 3 AA6 4 ILE A 443 VAL A 447 -1 O LEU A 445 N GLY A 390
SHEET 4 AA6 4 PHE A 420 MET A 424 -1 N TYR A 423 O HIS A 444
SHEET 1 AA7 2 ALA A 602 VAL A 603 0
SHEET 2 AA7 2 LEU A 835 ASP A 836 -1 O ASP A 836 N ALA A 602
SHEET 1 AA8 7 TYR A 609 TYR A 613 0
SHEET 2 AA8 7 GLU A 618 SER A 622 -1 O TYR A 621 N ASP A 610
SHEET 3 AA8 7 PRO A 628 ILE A 635 -1 O SER A 632 N GLU A 618
SHEET 4 AA8 7 VAL A 730 ILE A 737 -1 O VAL A 732 N TYR A 633
SHEET 5 AA8 7 HIS A 766 CYS A 774 -1 O THR A 772 N ASN A 731
SHEET 6 AA8 7 LEU A 788 PRO A 796 -1 O SER A 791 N ILE A 771
SHEET 7 AA8 7 THR A 823 ALA A 824 -1 O ALA A 824 N SER A 792
SHEET 1 AA9 2 SER A 676 PHE A 679 0
SHEET 2 AA9 2 MET A 701 MET A 704 -1 O VAL A 702 N GLY A 678
SSBOND 1 CYS A 58 CYS A 75 1555 1555 2.04
SSBOND 2 CYS A 62 CYS A 93 1555 1555 2.04
SSBOND 3 CYS A 73 CYS A 86 1555 1555 2.04
SSBOND 4 CYS A 79 CYS A 85 1555 1555 2.06
SSBOND 5 CYS A 102 CYS A 119 1555 1555 2.04
SSBOND 6 CYS A 107 CYS A 137 1555 1555 2.05
SSBOND 7 CYS A 117 CYS A 130 1555 1555 2.04
SSBOND 8 CYS A 123 CYS A 129 1555 1555 2.04
SSBOND 9 CYS A 148 CYS A 194 1555 1555 2.00
SSBOND 10 CYS A 156 CYS A 350 1555 1555 2.05
SSBOND 11 CYS A 366 CYS A 468 1555 1555 2.05
SSBOND 12 CYS A 413 CYS A 805 1555 1555 2.06
SSBOND 13 CYS A 566 CYS A 666 1555 1555 2.04
SSBOND 14 CYS A 774 CYS A 784 1555 1555 2.07
LINK ND2 ASN A 524 C1 NAG B 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 1.43
LINK OD1 ASP A 171 ZN ZN A 907 1555 1555 1.86
LINK OD1 ASP A 311 ZN ZN A 906 1555 1555 2.06
LINK OD2 ASP A 311 ZN ZN A 906 1555 1555 2.65
LINK NE2 HIS A 315 ZN ZN A 906 1555 1555 2.06
LINK OD2 ASP A 358 ZN ZN A 907 1555 1555 2.63
LINK NE2 HIS A 359 ZN ZN A 907 1555 1555 2.07
LINK NE2 HIS A 474 ZN ZN A 906 1555 1555 2.06
LINK O TYR A 669 NA NA A 933 1555 1555 2.69
LINK O ASP A 672 NA NA A 933 1555 1555 2.63
LINK O MET A 675 NA NA A 933 1555 1555 2.58
LINK OD1 ASP A 739 CA CA A 909 1555 1555 2.22
LINK OD1 ASN A 741 CA CA A 909 1555 1555 2.28
LINK OD1 ASP A 743 CA CA A 909 1555 1555 2.38
LINK O LEU A 745 CA CA A 909 1555 1555 2.31
LINK OD1 ASP A 747 CA CA A 909 1555 1555 2.29
LINK O ASN A 801 NA NA A 934 1555 1555 2.97
LINK O SER A 804 NA NA A 934 1555 1555 2.90
LINK OG SER A 807 NA NA A 934 1555 1555 2.41
LINK ZN ZN A 906 O2 PO4 A 908 1555 1555 2.15
LINK ZN ZN A 907 O1 PO4 A 908 1555 1555 2.58
LINK CA CA A 909 O HOH A1142 1555 1555 2.34
LINK NA NA A 933 O2 GOL A 939 1555 1555 2.66
LINK NA NA A 934 O HOH A1148 1555 1555 2.40
LINK NA NA A 934 O HOH A1204 1555 1555 2.30
CISPEP 1 PRO A 70 PRO A 71 0 2.59
CISPEP 2 TYR A 205 PRO A 206 0 -3.88
CISPEP 3 GLN A 309 PRO A 310 0 3.79
CRYST1 53.808 63.289 70.471 98.78 106.22 99.77 P 1 1
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 0.018585 0.003200 0.006224 0.00000
SCALE2 0.000000 0.016033 0.003468 0.00000
SCALE3 0.000000 0.000000 0.015120 0.00000
(ATOM LINES ARE NOT SHOWN.)
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