HEADER STRUCTURAL PROTEIN 10-JUL-03 1PZ8
TITLE MODULATION OF AGRIN FUNCTION BY ALTERNATIVE SPLICING AND
TITLE 2 CA2+ BINDING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AGRIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 FRAGMENT: BASAL LAMINA DOMAIN;
SOURCE 3 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 4 ORGANISM_COMMON: CHICKEN;
SOURCE 5 ORGANISM_TAXID: 9031;
SOURCE 6 GENE: AGRN;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AGRIN, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.STETEFELD,A.T.ALEXANDRESCU,M.W.MACIEJEWSKI,M.JENNY,
AUTHOR 2 K.RATHGEB-SZABO,T.SCHULTHESS,R.LANDWEHR,S.FRANK,M.A.RUEGG,
AUTHOR 3 R.A.KAMMERER
REVDAT 2 24-FEB-09 1PZ8 1 VERSN
REVDAT 1 13-APR-04 1PZ8 0
JRNL AUTH J.STETEFELD,A.T.ALEXANDRESCU,M.W.MACIEJEWSKI,
JRNL AUTH 2 M.JENNY,K.RATHGEB-SZABO,T.SCHULTHESS,R.LANDWEHR,
JRNL AUTH 3 S.FRANK,M.A.RUEGG,R.A.KAMMERER
JRNL TITL MODULATION OF AGRIN FUNCTION BY ALTERNATIVE
JRNL TITL 2 SPLICING AND CA2+ BINDING.
JRNL REF STRUCTURE V. 12 503 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 15016366
JRNL DOI 10.1016/J.STR.2004.02.001
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 27706
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1479
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2078
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3320
REMARK 3 BIN FREE R VALUE SET COUNT : 91
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5485
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 569
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.55000
REMARK 3 B22 (A**2) : 0.26000
REMARK 3 B33 (A**2) : 1.30000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.689
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.291
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.309
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.738
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5601 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5080 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7599 ; 1.535 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11798 ; 0.829 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 700 ; 2.949 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 985 ;15.242 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 865 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6240 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1096 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1232 ; 0.247 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5137 ; 0.251 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 2 ; 0.049 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 487 ; 0.162 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 3 ; 0.014 ; 0.500
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.112 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 45 ; 0.167 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 132 ; 0.281 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.175 ; 0.500
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): 3500 ; 0.897 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5615 ; 1.650 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2101 ; 2.210 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1984 ; 3.731 ; 4.500
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 13 A 29
REMARK 3 RESIDUE RANGE : A 41 A 198
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6270 37.3590 37.6140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0884 T22: 0.0759
REMARK 3 T33: 0.0747 T12: -0.0179
REMARK 3 T13: 0.0365 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 1.7662 L22: 0.7782
REMARK 3 L33: 1.0873 L12: 0.2832
REMARK 3 L13: 1.0912 L23: 0.5995
REMARK 3 S TENSOR
REMARK 3 S11: -0.0178 S12: -0.0765 S13: -0.1167
REMARK 3 S21: -0.0131 S22: -0.0287 S23: 0.0649
REMARK 3 S31: -0.0514 S32: -0.0590 S33: 0.0465
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 13 B 30
REMARK 3 RESIDUE RANGE : B 41 B 198
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6930 7.4210 78.8820
REMARK 3 T TENSOR
REMARK 3 T11: 0.1010 T22: 0.0359
REMARK 3 T33: 0.0659 T12: -0.0142
REMARK 3 T13: 0.0094 T23: 0.0342
REMARK 3 L TENSOR
REMARK 3 L11: 2.7280 L22: 0.9199
REMARK 3 L33: 2.0292 L12: 0.2988
REMARK 3 L13: 0.6110 L23: 0.3507
REMARK 3 S TENSOR
REMARK 3 S11: 0.0187 S12: -0.0408 S13: 0.0025
REMARK 3 S21: 0.0699 S22: -0.0393 S23: 0.1165
REMARK 3 S31: -0.0436 S32: -0.1486 S33: 0.0206
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 13 C 29
REMARK 3 RESIDUE RANGE : C 41 C 198
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6870 -0.3610 37.1230
REMARK 3 T TENSOR
REMARK 3 T11: 0.0684 T22: 0.0431
REMARK 3 T33: 0.0417 T12: -0.0131
REMARK 3 T13: -0.0010 T23: -0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 2.1876 L22: 0.9216
REMARK 3 L33: 2.2816 L12: -0.0393
REMARK 3 L13: -0.4666 L23: -0.3465
REMARK 3 S TENSOR
REMARK 3 S11: -0.0221 S12: -0.0633 S13: -0.0235
REMARK 3 S21: 0.0662 S22: 0.0290 S23: -0.1279
REMARK 3 S31: 0.0278 S32: 0.1562 S33: -0.0069
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 13 D 29
REMARK 3 RESIDUE RANGE : D 41 D 198
REMARK 3 ORIGIN FOR THE GROUP (A): 55.8540 26.7230 78.9360
REMARK 3 T TENSOR
REMARK 3 T11: 0.0623 T22: 0.0481
REMARK 3 T33: 0.0607 T12: -0.0018
REMARK 3 T13: -0.0093 T23: -0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 2.3109 L22: 1.0824
REMARK 3 L33: 1.9525 L12: 0.3193
REMARK 3 L13: -0.4019 L23: -0.3482
REMARK 3 S TENSOR
REMARK 3 S11: 0.0167 S12: 0.0104 S13: -0.0760
REMARK 3 S21: 0.0675 S22: -0.0420 S23: -0.2131
REMARK 3 S31: 0.0143 S32: 0.1703 S33: 0.0253
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 1PZ8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-03.
REMARK 100 THE RCSB ID CODE IS RCSB019719.
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 : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : BW7B
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 : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29221
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 24.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 276K
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 28.27800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 GLU A 1
REMARK 465 LYS A 2
REMARK 465 VAL A 3
REMARK 465 ILE A 4
REMARK 465 ILE A 5
REMARK 465 GLU A 6
REMARK 465 LYS A 7
REMARK 465 ALA A 8
REMARK 465 ALA A 9
REMARK 465 GLY A 10
REMARK 465 ASP A 11
REMARK 465 ALA A 12
REMARK 465 THR A 30
REMARK 465 LYS A 31
REMARK 465 SER A 32
REMARK 465 HIS A 33
REMARK 465 LEU A 34
REMARK 465 SER A 35
REMARK 465 ASN A 36
REMARK 465 GLU A 37
REMARK 465 ILE A 38
REMARK 465 PRO A 39
REMARK 465 SER A 199
REMARK 465 ALA A 200
REMARK 465 LYS A 201
REMARK 465 GLU B 1
REMARK 465 LYS B 2
REMARK 465 VAL B 3
REMARK 465 ILE B 4
REMARK 465 ILE B 5
REMARK 465 GLU B 6
REMARK 465 LYS B 7
REMARK 465 ALA B 8
REMARK 465 ALA B 9
REMARK 465 GLY B 10
REMARK 465 LYS B 31
REMARK 465 SER B 32
REMARK 465 HIS B 33
REMARK 465 LEU B 34
REMARK 465 SER B 35
REMARK 465 ASN B 36
REMARK 465 GLU B 37
REMARK 465 ILE B 38
REMARK 465 PRO B 39
REMARK 465 SER B 199
REMARK 465 ALA B 200
REMARK 465 LYS B 201
REMARK 465 GLU C 1
REMARK 465 LYS C 2
REMARK 465 VAL C 3
REMARK 465 ILE C 4
REMARK 465 ILE C 5
REMARK 465 GLU C 6
REMARK 465 LYS C 7
REMARK 465 ALA C 8
REMARK 465 ALA C 9
REMARK 465 GLY C 10
REMARK 465 ASP C 11
REMARK 465 THR C 30
REMARK 465 LYS C 31
REMARK 465 SER C 32
REMARK 465 HIS C 33
REMARK 465 LEU C 34
REMARK 465 SER C 35
REMARK 465 ASN C 36
REMARK 465 GLU C 37
REMARK 465 ILE C 38
REMARK 465 PRO C 39
REMARK 465 ALA C 40
REMARK 465 SER C 199
REMARK 465 ALA C 200
REMARK 465 LYS C 201
REMARK 465 GLU D 1
REMARK 465 LYS D 2
REMARK 465 VAL D 3
REMARK 465 ILE D 4
REMARK 465 ILE D 5
REMARK 465 GLU D 6
REMARK 465 LYS D 7
REMARK 465 ALA D 8
REMARK 465 ALA D 9
REMARK 465 GLY D 10
REMARK 465 ASP D 11
REMARK 465 THR D 30
REMARK 465 LYS D 31
REMARK 465 SER D 32
REMARK 465 HIS D 33
REMARK 465 LEU D 34
REMARK 465 SER D 35
REMARK 465 ASN D 36
REMARK 465 GLU D 37
REMARK 465 ILE D 38
REMARK 465 PRO D 39
REMARK 465 SER D 199
REMARK 465 ALA D 200
REMARK 465 LYS D 201
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 OD1 ASN A 191 O HOH A 785 1.88
REMARK 500 NZ LYS A 160 O HOH A 778 1.99
REMARK 500 C ALA B 158 O HOH B 770 2.11
REMARK 500 NZ LYS D 160 O HOH D 763 2.11
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 ASP A 18 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 89 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 144 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 11 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 89 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP B 144 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP B 188 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP C 18 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP C 73 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP C 89 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP C 144 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ASP C 179 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASN D 27 N - CA - C ANGL. DEV. = 17.8 DEGREES
REMARK 500 ASP D 73 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP D 175 CB - CG - OD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ASP D 179 CB - CG - OD2 ANGL. DEV. = 5.4 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 ALA A 28 -156.04 -73.82
REMARK 500 LYS A 93 149.91 89.97
REMARK 500 ASN A 104 43.42 -89.43
REMARK 500 GLN A 117 -115.92 64.32
REMARK 500 LEU A 155 38.11 -93.38
REMARK 500 SER A 156 41.41 -65.58
REMARK 500 ARG A 180 -9.37 71.88
REMARK 500 ASN A 192 73.74 33.56
REMARK 500 ASN B 27 -144.83 -76.37
REMARK 500 ALA B 28 161.28 -34.49
REMARK 500 VAL B 29 -24.52 -179.31
REMARK 500 LYS B 93 156.25 92.13
REMARK 500 GLN B 117 -111.50 60.83
REMARK 500 LEU B 155 113.06 -177.60
REMARK 500 ALA B 158 37.50 -69.02
REMARK 500 HIS B 159 -12.16 177.42
REMARK 500 ARG B 180 -6.47 73.10
REMARK 500 ASN B 192 72.15 34.20
REMARK 500 ARG C 20 15.37 -142.90
REMARK 500 SER C 92 30.39 -140.14
REMARK 500 LYS C 93 150.21 91.42
REMARK 500 ASN C 104 42.07 -76.95
REMARK 500 GLN C 117 -113.11 57.09
REMARK 500 GLU C 153 -84.83 -51.65
REMARK 500 LEU C 155 118.53 -174.80
REMARK 500 ARG C 180 -18.57 81.05
REMARK 500 ASN C 192 70.92 44.63
REMARK 500 ASN D 27 162.48 -8.82
REMARK 500 ALA D 28 -172.36 15.47
REMARK 500 LYS D 93 148.70 92.57
REMARK 500 ASN D 104 47.11 -91.04
REMARK 500 GLN D 117 -116.76 54.79
REMARK 500 GLU D 153 -71.56 -30.36
REMARK 500 SER D 156 -25.28 -158.59
REMARK 500 ALA D 158 -49.88 -21.66
REMARK 500 ASN D 191 31.42 -76.22
REMARK 500 ASN D 192 81.22 23.20
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 717 DISTANCE = 5.54 ANGSTROMS
REMARK 525 HOH D 734 DISTANCE = 8.08 ANGSTROMS
REMARK 525 HOH A 750 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH C 757 DISTANCE = 8.41 ANGSTROMS
REMARK 525 HOH A 764 DISTANCE = 8.31 ANGSTROMS
REMARK 525 HOH B 767 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH A 769 DISTANCE = 8.58 ANGSTROMS
REMARK 525 HOH D 776 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH A 789 DISTANCE = 5.76 ANGSTROMS
REMARK 525 HOH B 792 DISTANCE = 8.02 ANGSTROMS
REMARK 525 HOH D 817 DISTANCE = 8.03 ANGSTROMS
REMARK 525 HOH D 823 DISTANCE = 10.81 ANGSTROMS
REMARK 525 HOH D 824 DISTANCE = 7.64 ANGSTROMS
REMARK 525 HOH D 825 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A 830 DISTANCE = 11.20 ANGSTROMS
REMARK 525 HOH C 832 DISTANCE = 8.17 ANGSTROMS
REMARK 525 HOH A 831 DISTANCE = 11.76 ANGSTROMS
REMARK 525 HOH C 833 DISTANCE = 14.67 ANGSTROMS
REMARK 525 HOH A 832 DISTANCE = 19.72 ANGSTROMS
REMARK 525 HOH A 833 DISTANCE = 10.29 ANGSTROMS
REMARK 525 HOH A 834 DISTANCE = 7.95 ANGSTROMS
REMARK 525 HOH C 836 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH B 838 DISTANCE = 5.67 ANGSTROMS
REMARK 525 HOH A 839 DISTANCE = 8.02 ANGSTROMS
REMARK 525 HOH A 840 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B 841 DISTANCE = 8.65 ANGSTROMS
REMARK 525 HOH A 841 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH A 843 DISTANCE = 6.40 ANGSTROMS
REMARK 525 HOH A 844 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH A 845 DISTANCE = 7.81 ANGSTROMS
REMARK 525 HOH B 846 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH A 847 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH B 848 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH A 848 DISTANCE = 6.77 ANGSTROMS
REMARK 525 HOH B 852 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A 852 DISTANCE = 6.01 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 CA A 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 142 OD1
REMARK 620 2 GLN A 140 O 75.8
REMARK 620 3 ASP A 73 OD1 84.4 94.3
REMARK 620 4 LEU A 90 O 162.2 88.2 89.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 702 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN B 140 O
REMARK 620 2 HOH B 710 O 79.9
REMARK 620 3 ASP B 73 OD1 81.1 157.8
REMARK 620 4 LEU B 90 O 82.3 82.3 83.9
REMARK 620 5 ASP B 142 OD2 99.5 109.0 85.4 168.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 703 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 142 OD2
REMARK 620 2 LEU C 90 O 148.9
REMARK 620 3 GLN C 140 O 115.0 93.8
REMARK 620 4 ASP C 73 OD1 87.6 80.2 91.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 704 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LEU D 90 O
REMARK 620 2 GLN D 140 O 91.9
REMARK 620 3 HOH D 764 O 87.2 71.7
REMARK 620 4 ASP D 142 OD2 161.8 104.5 105.2
REMARK 620 5 ASP D 73 OD1 87.3 91.9 162.5 84.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 701
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 702
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 703
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 704
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PZ7 RELATED DB: PDB
REMARK 900 G3 DOMAIN OF AGRIN WITH B11 INSERT AND CALCIUM
REMARK 900 RELATED ID: 1Q56 RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE B0 ISOFORM OF THE AGRIN G3 DOMAIN IN
REMARK 900 ITS CA2+ BOUND STATE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE C-TERMINAL AGRIN DOMAIN HAS ALTERNATIVE SPLICE
REMARK 999 VARIANTS, WE SOLVED THE STRUCTURE OF B11 (1PZ7) AND
REMARK 999 B8 WITH (1PZ8) AND WITHOUT (1PZ9) CALCIUM, THEREFORE
REMARK 999 THE SEQUENCE-FILE CONATINS EITHER 11 OR 8 RESIDUES
REMARK 999 MORE THAN THE SO CALLED B0-INSERT, THE INSERT STARTS
REMARK 999 AT TKS- AND ENDS AT EKA, B11:PDALDYPAEPS B8:HLSNEIPA
REMARK 999 HOWEVER, NOT ALL THE SPLICE-RESIDUES ARE DETECTABLE
REMARK 999 IN THE ELECTRON DENSITY MAP
DBREF 1PZ8 A 1 201 UNP P31696 AGRN_CHICK 1752 1955
DBREF 1PZ8 B 1 201 UNP P31696 AGRN_CHICK 1752 1955
DBREF 1PZ8 C 1 201 UNP P31696 AGRN_CHICK 1752 1955
DBREF 1PZ8 D 1 201 UNP P31696 AGRN_CHICK 1752 1955
SEQADV 1PZ8 HIS A 33 UNP P31696 PRO 1784 SEE REMARK 999
SEQADV 1PZ8 LEU A 34 UNP P31696 ASP 1785 SEE REMARK 999
SEQADV 1PZ8 SER A 35 UNP P31696 ALA 1786 SEE REMARK 999
SEQADV 1PZ8 ASN A 36 UNP P31696 LEU 1787 SEE REMARK 999
SEQADV 1PZ8 GLU A 37 UNP P31696 ASP 1788 SEE REMARK 999
SEQADV 1PZ8 ILE A 38 UNP P31696 TYR 1789 SEE REMARK 999
SEQADV 1PZ8 A 42 UNP P31696 PRO 1793 SEE REMARK 999
SEQADV 1PZ8 A 43 UNP P31696 SER 1794 SEE REMARK 999
SEQADV 1PZ8 A 44 UNP P31696 GLU 1795 SEE REMARK 999
SEQADV 1PZ8 HIS B 33 UNP P31696 PRO 1784 SEE REMARK 999
SEQADV 1PZ8 LEU B 34 UNP P31696 ASP 1785 SEE REMARK 999
SEQADV 1PZ8 SER B 35 UNP P31696 ALA 1786 SEE REMARK 999
SEQADV 1PZ8 ASN B 36 UNP P31696 LEU 1787 SEE REMARK 999
SEQADV 1PZ8 GLU B 37 UNP P31696 ASP 1788 SEE REMARK 999
SEQADV 1PZ8 ILE B 38 UNP P31696 TYR 1789 SEE REMARK 999
SEQADV 1PZ8 B 42 UNP P31696 PRO 1793 SEE REMARK 999
SEQADV 1PZ8 B 43 UNP P31696 SER 1794 SEE REMARK 999
SEQADV 1PZ8 B 44 UNP P31696 GLU 1795 SEE REMARK 999
SEQADV 1PZ8 HIS C 33 UNP P31696 PRO 1784 SEE REMARK 999
SEQADV 1PZ8 LEU C 34 UNP P31696 ASP 1785 SEE REMARK 999
SEQADV 1PZ8 SER C 35 UNP P31696 ALA 1786 SEE REMARK 999
SEQADV 1PZ8 ASN C 36 UNP P31696 LEU 1787 SEE REMARK 999
SEQADV 1PZ8 GLU C 37 UNP P31696 ASP 1788 SEE REMARK 999
SEQADV 1PZ8 ILE C 38 UNP P31696 TYR 1789 SEE REMARK 999
SEQADV 1PZ8 C 42 UNP P31696 PRO 1793 SEE REMARK 999
SEQADV 1PZ8 C 43 UNP P31696 SER 1794 SEE REMARK 999
SEQADV 1PZ8 C 44 UNP P31696 GLU 1795 SEE REMARK 999
SEQADV 1PZ8 HIS D 33 UNP P31696 PRO 1784 SEE REMARK 999
SEQADV 1PZ8 LEU D 34 UNP P31696 ASP 1785 SEE REMARK 999
SEQADV 1PZ8 SER D 35 UNP P31696 ALA 1786 SEE REMARK 999
SEQADV 1PZ8 ASN D 36 UNP P31696 LEU 1787 SEE REMARK 999
SEQADV 1PZ8 GLU D 37 UNP P31696 ASP 1788 SEE REMARK 999
SEQADV 1PZ8 ILE D 38 UNP P31696 TYR 1789 SEE REMARK 999
SEQADV 1PZ8 D 42 UNP P31696 PRO 1793 SEE REMARK 999
SEQADV 1PZ8 D 43 UNP P31696 SER 1794 SEE REMARK 999
SEQADV 1PZ8 D 44 UNP P31696 GLU 1795 SEE REMARK 999
SEQRES 1 A 201 GLU LYS VAL ILE ILE GLU LYS ALA ALA GLY ASP ALA GLU
SEQRES 2 A 201 ALA ILE ALA PHE ASP GLY ARG THR TYR MET GLU TYR HIS
SEQRES 3 A 201 ASN ALA VAL THR LYS SER HIS LEU SER ASN GLU ILE PRO
SEQRES 4 A 201 ALA GLU LYS ALA LEU GLN SER ASN HIS PHE GLU LEU SER
SEQRES 5 A 201 ILE LYS THR GLU ALA THR GLN GLY LEU ILE LEU TRP SER
SEQRES 6 A 201 GLY LYS GLY LEU GLU ARG SER ASP TYR ILE ALA LEU ALA
SEQRES 7 A 201 ILE VAL ASP GLY PHE VAL GLN MET MET TYR ASP LEU GLY
SEQRES 8 A 201 SER LYS PRO VAL VAL LEU ARG SER THR VAL PRO ILE ASN
SEQRES 9 A 201 THR ASN HIS TRP THR HIS ILE LYS ALA TYR ARG VAL GLN
SEQRES 10 A 201 ARG GLU GLY SER LEU GLN VAL GLY ASN GLU ALA PRO ILE
SEQRES 11 A 201 THR GLY SER SER PRO LEU GLY ALA THR GLN LEU ASP THR
SEQRES 12 A 201 ASP GLY ALA LEU TRP LEU GLY GLY MET GLU ARG LEU SER
SEQRES 13 A 201 VAL ALA HIS LYS LEU PRO LYS ALA TYR SER THR GLY PHE
SEQRES 14 A 201 ILE GLY CYS ILE ARG ASP VAL ILE VAL ASP ARG GLN GLU
SEQRES 15 A 201 LEU HIS LEU VAL GLU ASP ALA LEU ASN ASN PRO THR ILE
SEQRES 16 A 201 LEU HIS CYS SER ALA LYS
SEQRES 1 B 201 GLU LYS VAL ILE ILE GLU LYS ALA ALA GLY ASP ALA GLU
SEQRES 2 B 201 ALA ILE ALA PHE ASP GLY ARG THR TYR MET GLU TYR HIS
SEQRES 3 B 201 ASN ALA VAL THR LYS SER HIS LEU SER ASN GLU ILE PRO
SEQRES 4 B 201 ALA GLU LYS ALA LEU GLN SER ASN HIS PHE GLU LEU SER
SEQRES 5 B 201 ILE LYS THR GLU ALA THR GLN GLY LEU ILE LEU TRP SER
SEQRES 6 B 201 GLY LYS GLY LEU GLU ARG SER ASP TYR ILE ALA LEU ALA
SEQRES 7 B 201 ILE VAL ASP GLY PHE VAL GLN MET MET TYR ASP LEU GLY
SEQRES 8 B 201 SER LYS PRO VAL VAL LEU ARG SER THR VAL PRO ILE ASN
SEQRES 9 B 201 THR ASN HIS TRP THR HIS ILE LYS ALA TYR ARG VAL GLN
SEQRES 10 B 201 ARG GLU GLY SER LEU GLN VAL GLY ASN GLU ALA PRO ILE
SEQRES 11 B 201 THR GLY SER SER PRO LEU GLY ALA THR GLN LEU ASP THR
SEQRES 12 B 201 ASP GLY ALA LEU TRP LEU GLY GLY MET GLU ARG LEU SER
SEQRES 13 B 201 VAL ALA HIS LYS LEU PRO LYS ALA TYR SER THR GLY PHE
SEQRES 14 B 201 ILE GLY CYS ILE ARG ASP VAL ILE VAL ASP ARG GLN GLU
SEQRES 15 B 201 LEU HIS LEU VAL GLU ASP ALA LEU ASN ASN PRO THR ILE
SEQRES 16 B 201 LEU HIS CYS SER ALA LYS
SEQRES 1 C 201 GLU LYS VAL ILE ILE GLU LYS ALA ALA GLY ASP ALA GLU
SEQRES 2 C 201 ALA ILE ALA PHE ASP GLY ARG THR TYR MET GLU TYR HIS
SEQRES 3 C 201 ASN ALA VAL THR LYS SER HIS LEU SER ASN GLU ILE PRO
SEQRES 4 C 201 ALA GLU LYS ALA LEU GLN SER ASN HIS PHE GLU LEU SER
SEQRES 5 C 201 ILE LYS THR GLU ALA THR GLN GLY LEU ILE LEU TRP SER
SEQRES 6 C 201 GLY LYS GLY LEU GLU ARG SER ASP TYR ILE ALA LEU ALA
SEQRES 7 C 201 ILE VAL ASP GLY PHE VAL GLN MET MET TYR ASP LEU GLY
SEQRES 8 C 201 SER LYS PRO VAL VAL LEU ARG SER THR VAL PRO ILE ASN
SEQRES 9 C 201 THR ASN HIS TRP THR HIS ILE LYS ALA TYR ARG VAL GLN
SEQRES 10 C 201 ARG GLU GLY SER LEU GLN VAL GLY ASN GLU ALA PRO ILE
SEQRES 11 C 201 THR GLY SER SER PRO LEU GLY ALA THR GLN LEU ASP THR
SEQRES 12 C 201 ASP GLY ALA LEU TRP LEU GLY GLY MET GLU ARG LEU SER
SEQRES 13 C 201 VAL ALA HIS LYS LEU PRO LYS ALA TYR SER THR GLY PHE
SEQRES 14 C 201 ILE GLY CYS ILE ARG ASP VAL ILE VAL ASP ARG GLN GLU
SEQRES 15 C 201 LEU HIS LEU VAL GLU ASP ALA LEU ASN ASN PRO THR ILE
SEQRES 16 C 201 LEU HIS CYS SER ALA LYS
SEQRES 1 D 201 GLU LYS VAL ILE ILE GLU LYS ALA ALA GLY ASP ALA GLU
SEQRES 2 D 201 ALA ILE ALA PHE ASP GLY ARG THR TYR MET GLU TYR HIS
SEQRES 3 D 201 ASN ALA VAL THR LYS SER HIS LEU SER ASN GLU ILE PRO
SEQRES 4 D 201 ALA GLU LYS ALA LEU GLN SER ASN HIS PHE GLU LEU SER
SEQRES 5 D 201 ILE LYS THR GLU ALA THR GLN GLY LEU ILE LEU TRP SER
SEQRES 6 D 201 GLY LYS GLY LEU GLU ARG SER ASP TYR ILE ALA LEU ALA
SEQRES 7 D 201 ILE VAL ASP GLY PHE VAL GLN MET MET TYR ASP LEU GLY
SEQRES 8 D 201 SER LYS PRO VAL VAL LEU ARG SER THR VAL PRO ILE ASN
SEQRES 9 D 201 THR ASN HIS TRP THR HIS ILE LYS ALA TYR ARG VAL GLN
SEQRES 10 D 201 ARG GLU GLY SER LEU GLN VAL GLY ASN GLU ALA PRO ILE
SEQRES 11 D 201 THR GLY SER SER PRO LEU GLY ALA THR GLN LEU ASP THR
SEQRES 12 D 201 ASP GLY ALA LEU TRP LEU GLY GLY MET GLU ARG LEU SER
SEQRES 13 D 201 VAL ALA HIS LYS LEU PRO LYS ALA TYR SER THR GLY PHE
SEQRES 14 D 201 ILE GLY CYS ILE ARG ASP VAL ILE VAL ASP ARG GLN GLU
SEQRES 15 D 201 LEU HIS LEU VAL GLU ASP ALA LEU ASN ASN PRO THR ILE
SEQRES 16 D 201 LEU HIS CYS SER ALA LYS
HET CA A 701 1
HET CA B 702 1
HET CA C 703 1
HET CA D 704 1
HETNAM CA CALCIUM ION
FORMUL 5 CA 4(CA 2+)
FORMUL 9 HOH *569(H2 O)
HELIX 1 1 PRO A 162 THR A 167 5 6
HELIX 2 2 PRO B 162 THR B 167 5 6
HELIX 3 3 PRO C 162 THR C 167 5 6
HELIX 4 4 SER D 156 LEU D 161 1 6
HELIX 5 5 PRO D 162 THR D 167 5 6
SHEET 1 A 6 ILE A 15 ASP A 18 0
SHEET 2 A 6 ILE A 170 VAL A 178 -1 O ILE A 173 N ILE A 15
SHEET 3 A 6 SER A 46 THR A 55 -1 N LYS A 54 O CYS A 172
SHEET 4 A 6 THR A 109 VAL A 116 -1 O ALA A 113 N PHE A 49
SHEET 5 A 6 GLU A 119 VAL A 124 -1 O SER A 121 N TYR A 114
SHEET 6 A 6 ILE A 130 SER A 133 -1 O GLY A 132 N GLY A 120
SHEET 1 B 3 ILE A 15 ASP A 18 0
SHEET 2 B 3 ILE A 170 VAL A 178 -1 O ILE A 173 N ILE A 15
SHEET 3 B 3 GLN A 181 GLU A 182 -1 O GLN A 181 N VAL A 178
SHEET 1 C 6 MET A 23 HIS A 26 0
SHEET 2 C 6 ALA A 146 LEU A 149 -1 O LEU A 147 N TYR A 25
SHEET 3 C 6 GLY A 60 SER A 65 -1 N TRP A 64 O TRP A 148
SHEET 4 C 6 TYR A 74 VAL A 80 -1 O ILE A 79 N GLY A 60
SHEET 5 C 6 PHE A 83 ASP A 89 -1 O MET A 87 N ALA A 76
SHEET 6 C 6 VAL A 95 PRO A 102 -1 O LEU A 97 N MET A 86
SHEET 1 D 2 LYS A 42 LEU A 44 0
SHEET 2 D 2 LEU A 141 THR A 143 -1 O LEU A 141 N LEU A 44
SHEET 1 E 6 ILE B 15 ASP B 18 0
SHEET 2 E 6 ILE B 170 VAL B 178 -1 O GLY B 171 N PHE B 17
SHEET 3 E 6 SER B 46 THR B 55 -1 N GLU B 50 O ILE B 177
SHEET 4 E 6 THR B 109 VAL B 116 -1 O ALA B 113 N PHE B 49
SHEET 5 E 6 GLU B 119 VAL B 124 -1 O GLN B 123 N LYS B 112
SHEET 6 E 6 ILE B 130 SER B 133 -1 O ILE B 130 N LEU B 122
SHEET 1 F 3 ILE B 15 ASP B 18 0
SHEET 2 F 3 ILE B 170 VAL B 178 -1 O GLY B 171 N PHE B 17
SHEET 3 F 3 GLN B 181 GLU B 182 -1 O GLN B 181 N VAL B 178
SHEET 1 G 6 MET B 23 TYR B 25 0
SHEET 2 G 6 LEU B 147 LEU B 149 -1 O LEU B 149 N MET B 23
SHEET 3 G 6 GLY B 60 SER B 65 -1 N TRP B 64 O TRP B 148
SHEET 4 G 6 TYR B 74 VAL B 80 -1 O ILE B 79 N GLY B 60
SHEET 5 G 6 PHE B 83 ASP B 89 -1 O PHE B 83 N VAL B 80
SHEET 6 G 6 VAL B 95 PRO B 102 -1 O LEU B 97 N MET B 86
SHEET 1 H 2 LYS B 42 LEU B 44 0
SHEET 2 H 2 LEU B 141 THR B 143 -1 O LEU B 141 N LEU B 44
SHEET 1 I 6 ILE C 130 SER C 133 0
SHEET 2 I 6 GLU C 119 VAL C 124 -1 N GLY C 120 O GLY C 132
SHEET 3 I 6 THR C 109 VAL C 116 -1 N LYS C 112 O GLN C 123
SHEET 4 I 6 SER C 46 THR C 55 -1 N PHE C 49 O ALA C 113
SHEET 5 I 6 ILE C 170 VAL C 178 -1 O ILE C 177 N GLU C 50
SHEET 6 I 6 GLN C 181 GLU C 182 -1 O GLN C 181 N VAL C 178
SHEET 1 J 7 ILE C 130 SER C 133 0
SHEET 2 J 7 GLU C 119 VAL C 124 -1 N GLY C 120 O GLY C 132
SHEET 3 J 7 THR C 109 VAL C 116 -1 N LYS C 112 O GLN C 123
SHEET 4 J 7 SER C 46 THR C 55 -1 N PHE C 49 O ALA C 113
SHEET 5 J 7 ILE C 170 VAL C 178 -1 O ILE C 177 N GLU C 50
SHEET 6 J 7 ILE C 15 ASP C 18 -1 N PHE C 17 O GLY C 171
SHEET 7 J 7 LEU C 196 HIS C 197 -1 O LEU C 196 N ALA C 16
SHEET 1 K 6 MET C 23 HIS C 26 0
SHEET 2 K 6 ALA C 146 LEU C 149 -1 O LEU C 149 N MET C 23
SHEET 3 K 6 GLN C 59 SER C 65 -1 N TRP C 64 O TRP C 148
SHEET 4 K 6 TYR C 74 VAL C 80 -1 O ILE C 79 N GLY C 60
SHEET 5 K 6 PHE C 83 ASP C 89 -1 O MET C 87 N ALA C 76
SHEET 6 K 6 VAL C 95 PRO C 102 -1 O LEU C 97 N MET C 86
SHEET 1 L 2 LYS C 42 LEU C 44 0
SHEET 2 L 2 LEU C 141 THR C 143 -1 O THR C 143 N LYS C 42
SHEET 1 M 6 ILE D 15 ASP D 18 0
SHEET 2 M 6 ILE D 170 VAL D 178 -1 O ILE D 173 N ILE D 15
SHEET 3 M 6 SER D 46 THR D 55 -1 N GLU D 50 O ILE D 177
SHEET 4 M 6 THR D 109 VAL D 116 -1 O ILE D 111 N LEU D 51
SHEET 5 M 6 GLU D 119 VAL D 124 -1 O GLN D 123 N LYS D 112
SHEET 6 M 6 ILE D 130 SER D 133 -1 O GLY D 132 N GLY D 120
SHEET 1 N 3 ILE D 15 ASP D 18 0
SHEET 2 N 3 ILE D 170 VAL D 178 -1 O ILE D 173 N ILE D 15
SHEET 3 N 3 GLN D 181 GLU D 182 -1 O GLN D 181 N VAL D 178
SHEET 1 O 6 MET D 23 HIS D 26 0
SHEET 2 O 6 ALA D 146 LEU D 149 -1 O LEU D 147 N TYR D 25
SHEET 3 O 6 GLY D 60 SER D 65 -1 N TRP D 64 O TRP D 148
SHEET 4 O 6 TYR D 74 VAL D 80 -1 O ILE D 79 N GLY D 60
SHEET 5 O 6 PHE D 83 ASP D 89 -1 O PHE D 83 N VAL D 80
SHEET 6 O 6 PRO D 94 PRO D 102 -1 O LEU D 97 N MET D 86
SHEET 1 P 2 LYS D 42 LEU D 44 0
SHEET 2 P 2 LEU D 141 THR D 143 -1 O LEU D 141 N LEU D 44
SSBOND 1 CYS A 172 CYS A 198 1555 1555 2.06
SSBOND 2 CYS B 172 CYS B 198 1555 1555 2.04
SSBOND 3 CYS C 172 CYS C 198 1555 1555 2.07
SSBOND 4 CYS D 172 CYS D 198 1555 1555 2.07
LINK CA CA A 701 OD1 ASP A 142 1555 1555 3.05
LINK CA CA A 701 O GLN A 140 1555 1555 2.52
LINK CA CA A 701 OD1 ASP A 73 1555 1555 2.57
LINK CA CA A 701 O LEU A 90 1555 1555 2.51
LINK CA CA B 702 O GLN B 140 1555 1555 2.65
LINK CA CA B 702 O HOH B 710 1555 1555 3.12
LINK CA CA B 702 OD1 ASP B 73 1555 1555 2.56
LINK CA CA B 702 O LEU B 90 1555 1555 2.53
LINK CA CA B 702 OD2 ASP B 142 1555 1555 3.04
LINK CA CA C 703 OD2 ASP C 142 1555 1555 2.69
LINK CA CA C 703 O LEU C 90 1555 1555 2.50
LINK CA CA C 703 O GLN C 140 1555 1555 2.33
LINK CA CA C 703 OD1 ASP C 73 1555 1555 2.57
LINK CA CA D 704 O LEU D 90 1555 1555 2.54
LINK CA CA D 704 O GLN D 140 1555 1555 2.29
LINK CA CA D 704 O HOH D 764 1555 1555 3.00
LINK CA CA D 704 OD2 ASP D 142 1555 1555 2.75
LINK CA CA D 704 OD1 ASP D 73 1555 1555 2.60
SITE 1 AC1 4 ASP A 73 LEU A 90 GLN A 140 ASP A 142
SITE 1 AC2 4 ASP B 73 LEU B 90 GLN B 140 ASP B 142
SITE 1 AC3 4 ASP C 73 LEU C 90 GLN C 140 ASP C 142
SITE 1 AC4 5 ASP D 73 LEU D 90 GLN D 140 ASP D 142
SITE 2 AC4 5 HOH D 764
CRYST1 76.847 56.556 84.586 90.00 99.75 90.00 P 1 21 1 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 0.013013 0.000000 0.002236 0.00000
SCALE2 0.000000 0.017681 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011996 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
