HEADER HYDROLASE 03-SEP-08 3EDI
TITLE CRYSTAL STRUCTURE OF TOLLOID-LIKE PROTEASE 1 (TLL-1)
TITLE 2 PROTEASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOLLOID-LIKE PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PROTEASE DOMAIN;
COMPND 5 SYNONYM: TLL-1;
COMPND 6 EC: 3.4.24.-;
COMPND 7 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: TLL1, TLL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS DISORDERED CYSTEINE-RICH LOOP, ALTERNATIVE SPLICING,
KEYWDS 2 CALCIUM, DEVELOPMENTAL PROTEIN, DIFFERENTIATION, EGF-LIKE
KEYWDS 3 DOMAIN, GLYCOPROTEIN, HYDROLASE, METAL-BINDING,
KEYWDS 4 METALLOPROTEASE, POLYMORPHISM, PROTEASE, SECRETED, ZINC,
KEYWDS 5 ZYMOGEN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.MAC SWEENEY
REVDAT 3 24-FEB-09 3EDI 1 VERSN
REVDAT 2 23-SEP-08 3EDI 1 AUTHOR JRNL
REVDAT 1 16-SEP-08 3EDI 0
JRNL AUTH A.MAC SWEENEY,S.G.PARRADO,D.VINZENZ,A.BERNARDI,
JRNL AUTH 2 A.HEIN,U.BODENDORF,P.ERBEL,C.LOGEL,B.GERHARTZ
JRNL TITL STRUCTURAL BASIS FOR THE SUBSTRATE SPECIFICITY OF
JRNL TITL 2 BONE MORPHOGENETIC PROTEIN 1/TOLLOID-LIKE
JRNL TITL 3 METALLOPROTEASES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 41791
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) : 0.155
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2090
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2237
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.69
REMARK 3 BIN R VALUE (WORKING SET) : 0.2070
REMARK 3 BIN FREE R VALUE SET COUNT : 118
REMARK 3 BIN FREE R VALUE : 0.2560
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1598
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 283
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.14000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.08000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.064
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.058
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.033
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.836
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1657 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2242 ; 1.473 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 201 ; 6.135 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;28.716 ;22.184
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 271 ;12.887 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;16.797 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 234 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1284 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 819 ; 0.288 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1138 ; 0.312 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 211 ; 0.256 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.034 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 45 ; 0.365 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 26 ; 0.591 ; 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): 1010 ; 1.843 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1592 ; 2.747 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 723 ; 4.873 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 644 ; 5.070 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 1733 ; 4.479 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 285 ; 7.680 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1620 ; 5.158 ; 3.000
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 : 1.40
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3EDI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-SEP-08.
REMARK 100 THE RCSB ID CODE IS RCSB049186.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41793
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 58.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : 0.04400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.66
REMARK 200 R MERGE FOR SHELL (I) : 0.47900
REMARK 200 R SYM FOR SHELL (I) : 0.32700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
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: 1DLE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 200MM LITHIUM
REMARK 280 SULPHATE, 100MM BIS-TRIS-HCL, PH 7.5, VAPOR DIFFUSION,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 29.46150
REMARK 290 SMTRY3 2 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 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 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 61
REMARK 465 CYS A 62
REMARK 465 GLY A 63
REMARK 465 CYS A 64
REMARK 465 GLY A 81
REMARK 465 LYS A 82
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TYR A 59 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 60 CG CD NE CZ NH1 NH2
REMARK 470 SER A 78 OG
REMARK 470 MET A 159 CG SD CE
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 HOH A 477 O HOH A 487 1.53
REMARK 500 O HOH A 483 O HOH A 487 1.66
REMARK 500 O HOH A 478 O HOH A 487 1.67
REMARK 500 O HOH A 495 O HOH A 496 1.76
REMARK 500 CE MET A 29 O HOH A 493 1.79
REMARK 500 O HOH A 409 O HOH A 486 1.93
REMARK 500 O HOH A 405 O HOH A 438 2.07
REMARK 500 O HOH A 243 O HOH A 494 2.07
REMARK 500 O HOH A 330 O HOH A 377 2.12
REMARK 500 SD MET A 29 O HOH A 493 2.13
REMARK 500 NH1 ARG A 170 O1 SO4 A 214 2.15
REMARK 500 O HOH A 405 O HOH A 475 2.17
REMARK 500 O HOH A 221 O HOH A 455 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 S DMS A 215 O HOH A 386 2546 0.77
REMARK 500 O HOH A 474 O HOH A 498 2555 1.68
REMARK 500 O HOH A 238 O HOH A 497 2556 1.70
REMARK 500 C2 DMS A 215 O HOH A 386 2546 1.77
REMARK 500 O HOH A 474 O HOH A 492 2555 1.81
REMARK 500 C1 DMS A 215 O HOH A 386 2546 2.08
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 49 -71.89 -110.69
REMARK 500 TYR A 59 8.83 -68.02
REMARK 500 CYS A 84 37.99 -91.54
REMARK 500 HIS A 112 -30.08 -131.56
REMARK 500 PHE A 160 -2.33 69.46
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 376 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH A 425 DISTANCE = 5.14 ANGSTROMS
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 210 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 65 SG
REMARK 620 2 HIS A 92 NE2 122.8
REMARK 620 3 HIS A 96 NE2 109.1 100.9
REMARK 620 4 HIS A 102 NE2 112.1 110.6 97.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 211 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN A 189 OE1
REMARK 620 2 ACE A 201 O 79.9
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE A 201
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 210
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 211
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 212
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 213
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 214
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 215
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EDG RELATED DB: PDB
REMARK 900 BMP-1
REMARK 900 RELATED ID: 3EDH RELATED DB: PDB
REMARK 900 DMSO
REMARK 900 RELATED ID: 1DLE RELATED DB: PDB
REMARK 900 ASTACIN
DBREF 3EDI A 1 200 UNP O43897 TLL1_HUMAN 148 348
SEQRES 1 A 201 ALA ALA THR SER ARG THR GLU ARG ILE TRP PRO GLY GLY
SEQRES 2 A 201 VAL ILE PRO TYR VAL ILE GLY GLY ASN PHE THR GLY SER
SEQRES 3 A 201 GLN ARG ALA MET PHE LYS GLN ALA MET ARG HIS TRP GLU
SEQRES 4 A 201 LYS HIS THR CYS VAL THR PHE ILE GLU ARG SER ASP GLU
SEQRES 5 A 201 GLU SER TYR ILE VAL PHE THR TYR ARG PRO CYS GLY CYS
SEQRES 6 A 201 CYS SER TYR VAL GLY ARG ARG GLY ASN GLY PRO GLN ALA
SEQRES 7 A 201 ILE SER ILE GLY LYS ASN CYS ASP LYS PHE GLY ILE VAL
SEQRES 8 A 201 VAL HIS GLU LEU GLY HIS VAL ILE GLY PHE TRP HIS GLU
SEQRES 9 A 201 HIS THR ARG PRO ASP ARG ASP ASN HIS VAL THR ILE ILE
SEQRES 10 A 201 ARG GLU ASN ILE GLN PRO GLY GLN GLU TYR ASN PHE LEU
SEQRES 11 A 201 LYS MET GLU PRO GLY GLU VAL ASN SER LEU GLY GLU ARG
SEQRES 12 A 201 TYR ASP PHE ASP SER ILE MET HIS TYR ALA ARG ASN THR
SEQRES 13 A 201 PHE SER ARG GLY MET PHE LEU ASP THR ILE LEU PRO SER
SEQRES 14 A 201 ARG ASP ASP ASN GLY ILE ARG PRO ALA ILE GLY GLN ARG
SEQRES 15 A 201 THR ARG LEU SER LYS GLY ASP ILE ALA GLN ALA ARG LYS
SEQRES 16 A 201 LEU TYR ARG CYS PRO ALA
HET ACE A 201 3
HET ZN A 210 1
HET ZN A 211 1
HET SO4 A 212 5
HET SO4 A 213 5
HET SO4 A 214 5
HET DMS A 215 4
HETNAM ACE ACETYL GROUP
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM DMS DIMETHYL SULFOXIDE
FORMUL 2 ACE C2 H4 O
FORMUL 3 ZN 2(ZN 2+)
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 8 DMS C2 H6 O S
FORMUL 9 HOH *283(H2 O)
HELIX 1 1 ARG A 5 ILE A 9 5 5
HELIX 2 2 TRP A 10 GLY A 12 5 3
HELIX 3 3 THR A 23 THR A 41 1 19
HELIX 4 4 LYS A 86 GLY A 99 1 14
HELIX 5 5 HIS A 102 ARG A 106 5 5
HELIX 6 6 ASP A 108 ASN A 111 5 4
HELIX 7 7 ARG A 117 ILE A 120 5 4
HELIX 8 8 GLN A 124 LEU A 129 5 6
HELIX 9 9 GLU A 132 VAL A 134 5 5
HELIX 10 10 SER A 183 TYR A 194 1 12
SHEET 1 A 4 THR A 44 GLU A 47 0
SHEET 2 A 4 VAL A 14 ILE A 19 1 N ILE A 15 O THR A 44
SHEET 3 A 4 ILE A 55 THR A 58 1 O ILE A 55 N PRO A 16
SHEET 4 A 4 GLN A 75 SER A 78 1 O ILE A 77 N VAL A 56
SHEET 1 B 2 VAL A 113 ILE A 115 0
SHEET 2 B 2 ILE A 164 PRO A 166 -1 O LEU A 165 N THR A 114
SSBOND 1 CYS A 42 CYS A 198 1555 1555 2.05
LINK N ALA A 1 C ACE A 201 1555 1555 1.42
LINK SG CYS A 65 ZN ZN A 210 1555 1555 2.26
LINK NE2 HIS A 92 ZN ZN A 210 1555 1555 2.04
LINK NE2 HIS A 96 ZN ZN A 210 1555 1555 2.08
LINK NE2 HIS A 102 ZN ZN A 210 1555 1555 2.02
LINK OE1 GLN A 189 ZN ZN A 211 1555 1555 2.40
LINK O ACE A 201 ZN ZN A 211 1555 1555 2.30
SITE 1 AC1 6 ALA A 1 ALA A 2 GLU A 103 ARG A 106
SITE 2 AC1 6 SER A 136 GLN A 189
SITE 1 AC2 4 CYS A 65 HIS A 92 HIS A 96 HIS A 102
SITE 1 AC3 5 GLU A 103 GLN A 189 HOH A 236 HOH A 240
SITE 2 AC3 5 HOH A 247
SITE 1 AC4 3 HIS A 36 LYS A 39 HIS A 40
SITE 1 AC5 8 SER A 4 ARG A 5 THR A 6 ARG A 151
SITE 2 AC5 8 HOH A 258 HOH A 287 HOH A 362 HOH A 370
SITE 1 AC6 5 SER A 167 ARG A 168 ARG A 170 HOH A 279
SITE 2 AC6 5 HOH A 437
SITE 1 AC7 6 TYR A 17 LYS A 31 ARG A 35 GLU A 38
SITE 2 AC7 6 PHE A 45 HOH A 414
CRYST1 41.281 58.923 47.444 90.00 104.62 90.00 P 1 21 1 2
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 0.024224 0.000000 0.006320 0.00000
SCALE2 0.000000 0.016971 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021783 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
