HEADER HYDROLASE 15-OCT-07 2RJQ
TITLE CRYSTAL STRUCTURE OF ADAMTS5 WITH INHIBITOR BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADAMTS-5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 262-628;
COMPND 5 SYNONYM: A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN
COMPND 6 MOTIFS 5, ADAM-TS 5, ADAM-TS5, AGGRECANASE-2, ADMP-2, ADAM-TS 11;
COMPND 7 EC: 3.4.24.-;
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: ADAMTS5, ADAMTS11, ADMP2;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: OVARY (CHO) CELLS
KEYWDS METALLOPROTEASE DOMAIN, AGGRECANASE, CLEAVAGE ON PAIR OF BASIC
KEYWDS 2 RESIDUES, EXTRACELLULAR MATRIX, GLYCOPROTEIN, HYDROLASE, METAL-
KEYWDS 3 BINDING, SECRETED, ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.MOSYAK,M.STAHL,W.SOMERS
REVDAT 7 30-AUG-23 2RJQ 1 HETSYN
REVDAT 6 29-JUL-20 2RJQ 1 COMPND REMARK SEQADV HETNAM
REVDAT 6 2 1 LINK SITE ATOM
REVDAT 5 25-OCT-17 2RJQ 1 REMARK
REVDAT 4 13-JUL-11 2RJQ 1 VERSN
REVDAT 3 24-FEB-09 2RJQ 1 VERSN
REVDAT 2 08-JAN-08 2RJQ 1 JRNL
REVDAT 1 11-DEC-07 2RJQ 0
JRNL AUTH L.MOSYAK,K.GEORGIADIS,T.SHANE,K.SVENSON,T.HEBERT,T.MCDONAGH,
JRNL AUTH 2 S.MACKIE,S.OLLAND,L.LIN,X.ZHONG,R.KRIZ,E.L.REIFENBERG,
JRNL AUTH 3 L.A.COLLINS-RACIE,C.CORCORAN,B.FREEMAN,R.ZOLLNER,T.MARVELL,
JRNL AUTH 4 M.VERA,P.E.SUM,E.R.LAVALLIE,M.STAHL,W.SOMERS
JRNL TITL CRYSTAL STRUCTURES OF THE TWO MAJOR AGGRECAN DEGRADING
JRNL TITL 2 ENZYMES, ADAMTS4 AND ADAMTS5.
JRNL REF PROTEIN SCI. V. 17 16 2008
JRNL REFN ISSN 0961-8368
JRNL PMID 18042673
JRNL DOI 10.1110/PS.073287008
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.5
REMARK 3 NUMBER OF REFLECTIONS : 13609
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) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 683
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 434
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 39.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.3390
REMARK 3 BIN FREE R VALUE SET COUNT : 18
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2236
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 81
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.85000
REMARK 3 B22 (A**2) : 3.85000
REMARK 3 B33 (A**2) : -5.78000
REMARK 3 B12 (A**2) : 1.93000
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): 0.533
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.309
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.267
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.759
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
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): 2349 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3186 ; 0.899 ; 1.985
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 291 ; 4.802 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;34.603 ;24.400
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 394 ;14.736 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;15.061 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 361 ; 0.056 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1744 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 979 ; 0.167 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1558 ; 0.290 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 83 ; 0.129 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 12 ; 0.116 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 41 ; 0.150 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.130 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 1 ; 0.039 ; 0.200
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): 1486 ; 0.198 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2321 ; 0.380 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 953 ; 0.549 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 865 ; 1.038 ; 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 264 A 485
REMARK 3 ORIGIN FOR THE GROUP (A): -43.2050 -14.5299 15.0999
REMARK 3 T TENSOR
REMARK 3 T11: 0.0633 T22: -0.2603
REMARK 3 T33: -0.1667 T12: 0.1116
REMARK 3 T13: 0.1140 T23: 0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 6.3094 L22: 5.3404
REMARK 3 L33: 6.3778 L12: -1.3582
REMARK 3 L13: -0.9123 L23: 0.6910
REMARK 3 S TENSOR
REMARK 3 S11: 0.3293 S12: 0.3399 S13: 0.7812
REMARK 3 S21: -0.1339 S22: -0.0200 S23: -0.2070
REMARK 3 S31: -0.7394 S32: -0.2715 S33: -0.3093
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 486 A 555
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1383 -15.9099 8.0791
REMARK 3 T TENSOR
REMARK 3 T11: 0.1431 T22: 0.0178
REMARK 3 T33: 0.4197 T12: -0.0331
REMARK 3 T13: 0.1112 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 11.8705 L22: 3.1423
REMARK 3 L33: 11.0450 L12: -1.4137
REMARK 3 L13: -5.6126 L23: 3.1291
REMARK 3 S TENSOR
REMARK 3 S11: 0.4895 S12: 0.2798 S13: 1.7469
REMARK 3 S21: -0.4582 S22: 0.3132 S23: -0.7536
REMARK 3 S31: -0.9428 S32: 0.6015 S33: -0.8028
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. ALTHOUGH THE AMINO ACID SEQUENCE OF THE CRYSTALLIZED
REMARK 3 PROTEIN ENCOMPASSES THREE DOMAINS: CATALYTIC, DISINTEGRIN-LIKE
REMARK 3 DOMAIN AND THROMBOSPONDIN-LIKE DOMAIN, THE LATTER DOMAIN,
REMARK 3 RESIDUES 557-628, HAS NO SUPPORTING ELECTRON DENSITY.
REMARK 4
REMARK 4 2RJQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-07.
REMARK 100 THE DEPOSITION ID IS D_1000044942.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : SI 220, ROSENBAUM-ROCK DOUBLE
REMARK 200 -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 : 13624
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
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) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29000
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: PDB ENTRY 2RJP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 0.2 M AMMONIUM SULFATE,
REMARK 280 0.1M MES PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 31.16233
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 62.32467
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 62.32467
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 31.16233
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, 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 SER A 262
REMARK 465 ILE A 263
REMARK 465 LYS A 556
REMARK 465 THR A 557
REMARK 465 LYS A 558
REMARK 465 LYS A 559
REMARK 465 LYS A 560
REMARK 465 TYR A 561
REMARK 465 TYR A 562
REMARK 465 SER A 563
REMARK 465 THR A 564
REMARK 465 SER A 565
REMARK 465 SER A 566
REMARK 465 HIS A 567
REMARK 465 GLY A 568
REMARK 465 ASN A 569
REMARK 465 TRP A 570
REMARK 465 GLY A 571
REMARK 465 SER A 572
REMARK 465 TRP A 573
REMARK 465 GLY A 574
REMARK 465 SER A 575
REMARK 465 TRP A 576
REMARK 465 GLY A 577
REMARK 465 GLN A 578
REMARK 465 CYS A 579
REMARK 465 SER A 580
REMARK 465 ARG A 581
REMARK 465 SER A 582
REMARK 465 CYS A 583
REMARK 465 GLY A 584
REMARK 465 GLY A 585
REMARK 465 GLY A 586
REMARK 465 VAL A 587
REMARK 465 GLN A 588
REMARK 465 PHE A 589
REMARK 465 ALA A 590
REMARK 465 TYR A 591
REMARK 465 ARG A 592
REMARK 465 HIS A 593
REMARK 465 CYS A 594
REMARK 465 ASN A 595
REMARK 465 ASN A 596
REMARK 465 PRO A 597
REMARK 465 ALA A 598
REMARK 465 PRO A 599
REMARK 465 ARG A 600
REMARK 465 ASN A 601
REMARK 465 ASN A 602
REMARK 465 GLY A 603
REMARK 465 ARG A 604
REMARK 465 TYR A 605
REMARK 465 CYS A 606
REMARK 465 THR A 607
REMARK 465 GLY A 608
REMARK 465 LYS A 609
REMARK 465 ARG A 610
REMARK 465 ALA A 611
REMARK 465 ILE A 612
REMARK 465 TYR A 613
REMARK 465 ARG A 614
REMARK 465 SER A 615
REMARK 465 CYS A 616
REMARK 465 SER A 617
REMARK 465 LEU A 618
REMARK 465 MET A 619
REMARK 465 PRO A 620
REMARK 465 CYS A 621
REMARK 465 PRO A 622
REMARK 465 PRO A 623
REMARK 465 ASN A 624
REMARK 465 GLY A 625
REMARK 465 LYS A 626
REMARK 465 SER A 627
REMARK 465 PHE A 628
REMARK 465 GLY A 629
REMARK 465 SER A 630
REMARK 465 ALA A 631
REMARK 465 TRP A 632
REMARK 465 SER A 633
REMARK 465 HIS A 634
REMARK 465 PRO A 635
REMARK 465 GLN A 636
REMARK 465 PHE A 637
REMARK 465 GLU A 638
REMARK 465 LYS A 639
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 ARG A 285 47.89 -150.09
REMARK 500 GLN A 350 51.78 -91.13
REMARK 500 ASP A 354 63.58 -104.35
REMARK 500 ARG A 437 -163.94 -126.72
REMARK 500 GLU A 484 45.03 -84.82
REMARK 500 GLN A 524 -115.97 49.97
REMARK 500 GLN A 550 -22.68 67.70
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 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 410 NE2
REMARK 620 2 HIS A 414 NE2 98.5
REMARK 620 3 HIS A 420 NE2 110.5 106.3
REMARK 620 4 BAT A 559 O1 98.8 159.8 77.1
REMARK 620 5 BAT A 559 O2 99.2 85.4 145.6 81.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 5 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 270 OE2
REMARK 620 2 ASP A 360 OD1 87.2
REMARK 620 3 CYS A 471 O 140.1 83.8
REMARK 620 4 ASP A 474 OD1 69.8 157.0 113.9
REMARK 620 5 HOH A 578 O 66.7 98.7 76.4 73.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 6 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 369 OD1
REMARK 620 2 LEU A 370 O 88.7
REMARK 620 3 CYS A 376 O 91.9 91.2
REMARK 620 4 THR A 378 O 172.6 90.6 95.4
REMARK 620 5 GLU A 398 OE1 79.2 94.9 169.1 93.6
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2RJP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADAMTS4 WITH INHIBITOR BOUND
REMARK 900 RELATED ID: 3B2Z RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ADAMTS4 (APO FORM)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT THAT WAS CRYSTALLIZED ENCODES
REMARK 999 RESIDUES 262-628 OF HUMAN ADAMTS-5 PLUS A
REMARK 999 C-TERMINAL STREP-TAG (SEQUENCE: GSAWSHPQFEK).
DBREF 2RJQ A 262 628 UNP Q9UNA0 ATS5_HUMAN 262 628
SEQADV 2RJQ GLY A 629 UNP Q9UNA0 EXPRESSION TAG
SEQADV 2RJQ SER A 630 UNP Q9UNA0 EXPRESSION TAG
SEQADV 2RJQ ALA A 631 UNP Q9UNA0 EXPRESSION TAG
SEQADV 2RJQ TRP A 632 UNP Q9UNA0 EXPRESSION TAG
SEQADV 2RJQ SER A 633 UNP Q9UNA0 EXPRESSION TAG
SEQADV 2RJQ HIS A 634 UNP Q9UNA0 EXPRESSION TAG
SEQADV 2RJQ PRO A 635 UNP Q9UNA0 EXPRESSION TAG
SEQADV 2RJQ GLN A 636 UNP Q9UNA0 EXPRESSION TAG
SEQADV 2RJQ PHE A 637 UNP Q9UNA0 EXPRESSION TAG
SEQADV 2RJQ GLU A 638 UNP Q9UNA0 EXPRESSION TAG
SEQADV 2RJQ LYS A 639 UNP Q9UNA0 EXPRESSION TAG
SEQRES 1 A 378 SER ILE SER ARG ALA ARG GLN VAL GLU LEU LEU LEU VAL
SEQRES 2 A 378 ALA ASP ALA SER MET ALA ARG LEU TYR GLY ARG GLY LEU
SEQRES 3 A 378 GLN HIS TYR LEU LEU THR LEU ALA SER ILE ALA ASN ARG
SEQRES 4 A 378 LEU TYR SER HIS ALA SER ILE GLU ASN HIS ILE ARG LEU
SEQRES 5 A 378 ALA VAL VAL LYS VAL VAL VAL LEU GLY ASP LYS ASP LYS
SEQRES 6 A 378 SER LEU GLU VAL SER LYS ASN ALA ALA THR THR LEU LYS
SEQRES 7 A 378 ASN PHE CYS LYS TRP GLN HIS GLN HIS ASN GLN LEU GLY
SEQRES 8 A 378 ASP ASP HIS GLU GLU HIS TYR ASP ALA ALA ILE LEU PHE
SEQRES 9 A 378 THR ARG GLU ASP LEU CYS GLY HIS HIS SER CYS ASP THR
SEQRES 10 A 378 LEU GLY MET ALA ASP VAL GLY THR ILE CYS SER PRO GLU
SEQRES 11 A 378 ARG SER CYS ALA VAL ILE GLU ASP ASP GLY LEU HIS ALA
SEQRES 12 A 378 ALA PHE THR VAL ALA HIS GLU ILE GLY HIS LEU LEU GLY
SEQRES 13 A 378 LEU SER HIS ASP ASP SER LYS PHE CYS GLU GLU THR PHE
SEQRES 14 A 378 GLY SER THR GLU ASP LYS ARG LEU MET SER SER ILE LEU
SEQRES 15 A 378 THR SER ILE ASP ALA SER LYS PRO TRP SER LYS CYS THR
SEQRES 16 A 378 SER ALA THR ILE THR GLU PHE LEU ASP ASP GLY HIS GLY
SEQRES 17 A 378 ASN CYS LEU LEU ASP LEU PRO ARG LYS GLN ILE LEU GLY
SEQRES 18 A 378 PRO GLU GLU LEU PRO GLY GLN THR TYR ASP ALA THR GLN
SEQRES 19 A 378 GLN CYS ASN LEU THR PHE GLY PRO GLU TYR SER VAL CYS
SEQRES 20 A 378 PRO GLY MET ASP VAL CYS ALA ARG LEU TRP CYS ALA VAL
SEQRES 21 A 378 VAL ARG GLN GLY GLN MET VAL CYS LEU THR LYS LYS LEU
SEQRES 22 A 378 PRO ALA VAL GLU GLY THR PRO CYS GLY LYS GLY ARG ILE
SEQRES 23 A 378 CYS LEU GLN GLY LYS CYS VAL ASP LYS THR LYS LYS LYS
SEQRES 24 A 378 TYR TYR SER THR SER SER HIS GLY ASN TRP GLY SER TRP
SEQRES 25 A 378 GLY SER TRP GLY GLN CYS SER ARG SER CYS GLY GLY GLY
SEQRES 26 A 378 VAL GLN PHE ALA TYR ARG HIS CYS ASN ASN PRO ALA PRO
SEQRES 27 A 378 ARG ASN ASN GLY ARG TYR CYS THR GLY LYS ARG ALA ILE
SEQRES 28 A 378 TYR ARG SER CYS SER LEU MET PRO CYS PRO PRO ASN GLY
SEQRES 29 A 378 LYS SER PHE GLY SER ALA TRP SER HIS PRO GLN PHE GLU
SEQRES 30 A 378 LYS
MODRES 2RJQ ASN A 498 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET ZN A 1 1
HET ZN A 2 1
HET CL A 3 1
HET CL A 4 1
HET CA A 5 1
HET CA A 6 1
HET BAT A 559 32
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM CA CALCIUM ION
HETNAM BAT 4-(N-HYDROXYAMINO)-2R-ISOBUTYL-2S-(2-
HETNAM 2 BAT THIENYLTHIOMETHYL)SUCCINYL-L-PHENYLALANINE-N-
HETNAM 3 BAT METHYLAMIDE
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 BAT BATIMASTAT; BB94
FORMUL 2 NAG 2(C8 H15 N O6)
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 CL 2(CL 1-)
FORMUL 7 CA 2(CA 2+)
FORMUL 9 BAT C23 H31 N3 O4 S2
FORMUL 10 HOH *81(H2 O)
HELIX 1 1 ASP A 276 GLY A 284 1 9
HELIX 2 2 GLY A 286 SER A 303 1 18
HELIX 3 3 HIS A 304 GLU A 308 5 5
HELIX 4 4 ASN A 333 HIS A 348 1 16
HELIX 5 5 SER A 389 ARG A 392 5 4
HELIX 6 6 HIS A 403 LEU A 416 1 14
HELIX 7 7 SER A 423 PHE A 430 1 8
HELIX 8 8 SER A 453 ASP A 466 1 14
HELIX 9 9 GLY A 469 LEU A 473 5 5
HELIX 10 10 LEU A 486 TYR A 491 1 6
HELIX 11 11 ASP A 492 GLY A 502 1 11
SHEET 1 A 5 ILE A 311 VAL A 320 0
SHEET 2 A 5 ARG A 267 ALA A 275 1 N LEU A 271 O ALA A 314
SHEET 3 A 5 ALA A 361 THR A 366 1 O ILE A 363 N VAL A 274
SHEET 4 A 5 CYS A 394 GLU A 398 1 O ILE A 397 N LEU A 364
SHEET 5 A 5 GLY A 380 ALA A 382 -1 N MET A 381 O VAL A 396
SHEET 1 B 3 SER A 506 VAL A 507 0
SHEET 2 B 3 CYS A 519 ARG A 523 -1 O ALA A 520 N SER A 506
SHEET 3 B 3 GLN A 526 LEU A 530 -1 O LEU A 530 N CYS A 519
SHEET 1 C 2 ILE A 547 LEU A 549 0
SHEET 2 C 2 LYS A 552 VAL A 554 -1 O LYS A 552 N LEU A 549
SSBOND 1 CYS A 342 CYS A 394 1555 1555 2.04
SSBOND 2 CYS A 371 CYS A 376 1555 1555 2.05
SSBOND 3 CYS A 388 CYS A 471 1555 1555 2.04
SSBOND 4 CYS A 426 CYS A 455 1555 1555 2.04
SSBOND 5 CYS A 497 CYS A 519 1555 1555 2.04
SSBOND 6 CYS A 508 CYS A 529 1555 1555 2.04
SSBOND 7 CYS A 514 CYS A 548 1555 1555 2.04
SSBOND 8 CYS A 542 CYS A 553 1555 1555 2.04
LINK ND2 ASN A 498 C1 NAG B 1 1555 1555 1.44
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.45
LINK ZN ZN A 1 NE2 HIS A 410 1555 1555 1.99
LINK ZN ZN A 1 NE2 HIS A 414 1555 1555 2.13
LINK ZN ZN A 1 NE2 HIS A 420 1555 1555 2.14
LINK ZN ZN A 1 O1 BAT A 559 1555 1555 2.14
LINK ZN ZN A 1 O2 BAT A 559 1555 1555 2.33
LINK ZN ZN A 2 ND1 HIS A 374 1555 1555 2.02
LINK CA CA A 5 OE2 GLU A 270 1555 1555 2.30
LINK CA CA A 5 OD1 ASP A 360 1555 1555 2.34
LINK CA CA A 5 O CYS A 471 1555 1555 2.31
LINK CA CA A 5 OD1 ASP A 474 1555 1555 2.71
LINK CA CA A 5 O HOH A 578 1555 1555 2.32
LINK CA CA A 6 OD1 ASP A 369 1555 1555 2.32
LINK CA CA A 6 O LEU A 370 1555 1555 2.43
LINK CA CA A 6 O CYS A 376 1555 1555 2.38
LINK CA CA A 6 O THR A 378 1555 1555 2.38
LINK CA CA A 6 OE1 GLU A 398 1555 1555 2.38
CISPEP 1 ARG A 285 GLY A 286 0 -6.19
CRYST1 95.471 95.471 93.487 90.00 90.00 120.00 P 31 2 1 6
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 0.010474 0.006047 0.000000 0.00000
SCALE2 0.000000 0.012095 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010697 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
