HEADER HYDROLASE 08-APR-05 2BO9
TITLE HUMAN CARBOXYPEPTIDASE A4 IN COMPLEX WITH HUMAN LATEXIN.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYPEPTIDASE A4;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: ALPHA/BETA-HYDROLASE DOMAIN, RESIDUES 114-421;
COMPND 5 SYNONYM: CARBOXYPEPTIDASE A3, UNQ694/PRO1339;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: N-GLYCOSYLATION AT ASN148 IN BOTH COPIES PRESENT.;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HUMAN LATEXIN;
COMPND 10 CHAIN: B, D;
COMPND 11 SYNONYM: MUM;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PPIC9;
SOURCE 8 OTHER_DETAILS: CDNA PROVIDED BY DRS.HUANG AND SMITH, MAYO CLINIC,
SOURCE 9 ROCHESTER, MN.;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_PLASMID: PGAT2
KEYWDS METALLOCARBOXYPEPTIDASE, X-RAY CRYSTAL STRUCTURE, ENDOGENOUS PROTEIN
KEYWDS 2 INHIBITOR, LATEXIN, METALLOPROTEASE CARBOXYPEPTIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.PALLARES,R.BONET,R.GARCIA-CASTELLANOS,S.VENTURA,F.X.AVILES,
AUTHOR 2 J.VENDRELL,F.X.GOMIS-RUETH
REVDAT 4 29-JUL-20 2BO9 1 COMPND REMARK HETNAM LINK
REVDAT 4 2 1 SITE
REVDAT 3 12-JUL-17 2BO9 1
REVDAT 2 24-FEB-09 2BO9 1 VERSN
REVDAT 1 15-APR-05 2BO9 0
SPRSDE 15-APR-05 2BO9 2BK7
JRNL AUTH I.PALLARES,R.BONET,R.GARCIA-CASTELLANOS,S.VENTURA,
JRNL AUTH 2 F.X.AVILES,J.VENDRELL,F.X.GOMIS-RUETH
JRNL TITL STRUCTURE OF HUMAN CARBOXYPEPTIDASE A4 WITH ITS ENDOGENOUS
JRNL TITL 2 PROTEIN INHIBITOR, LATEXIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 3978 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 15738388
JRNL DOI 10.1073/PNAS.0500678102
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.9999
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 178706
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.149
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.400
REMARK 3 FREE R VALUE TEST SET COUNT : 678
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13087
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1700
REMARK 3 BIN FREE R VALUE SET COUNT : 58
REMARK 3 BIN FREE R VALUE : 0.1900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8404
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 146
REMARK 3 SOLVENT ATOMS : 1153
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.98000
REMARK 3 B22 (A**2) : -1.36000
REMARK 3 B33 (A**2) : -0.71000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.063
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.467
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8811 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11984 ; 1.348 ; 1.933
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1044 ; 6.187 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 432 ;35.361 ;24.421
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1440 ;13.030 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 47 ;16.368 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1281 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6737 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4224 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 974 ; 0.125 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 59 ; 0.150 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 54 ; 0.106 ; 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): 5399 ; 0.884 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8532 ; 1.343 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3931 ; 2.126 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3452 ; 3.357 ; 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 : 10
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 3 A 308
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6159 43.9029 84.9449
REMARK 3 T TENSOR
REMARK 3 T11: -0.0666 T22: -0.0524
REMARK 3 T33: -0.0380 T12: -0.0013
REMARK 3 T13: -0.0001 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.2499 L22: 0.5623
REMARK 3 L33: 0.5673 L12: -0.1001
REMARK 3 L13: -0.1101 L23: 0.0561
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.0163 S13: -0.0001
REMARK 3 S21: -0.0075 S22: 0.0094 S23: -0.0121
REMARK 3 S31: 0.0169 S32: -0.0057 S33: -0.0080
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 : A 3 A 308
REMARK 3 RESIDUE RANGE : A 999 A 999
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6197 43.5913 85.0723
REMARK 3 T TENSOR
REMARK 3 T11: -0.0636 T22: -0.0488
REMARK 3 T33: -0.0367 T12: 0.0001
REMARK 3 T13: -0.0004 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.3371 L22: 0.6507
REMARK 3 L33: 0.6407 L12: -0.0840
REMARK 3 L13: -0.1451 L23: 0.0677
REMARK 3 S TENSOR
REMARK 3 S11: -0.0012 S12: 0.0168 S13: -0.0023
REMARK 3 S21: -0.0199 S22: 0.0033 S23: -0.0137
REMARK 3 S31: 0.0225 S32: -0.0036 S33: -0.0021
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 217
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0456 57.7595 94.4280
REMARK 3 T TENSOR
REMARK 3 T11: -0.0975 T22: -0.0001
REMARK 3 T33: -0.0041 T12: 0.0282
REMARK 3 T13: 0.0054 T23: -0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 1.1889 L22: 0.5016
REMARK 3 L33: 0.9643 L12: 0.0895
REMARK 3 L13: 0.1693 L23: -0.0230
REMARK 3 S TENSOR
REMARK 3 S11: -0.0125 S12: -0.0775 S13: 0.0823
REMARK 3 S21: 0.0057 S22: -0.0350 S23: 0.1493
REMARK 3 S31: -0.0698 S32: -0.2154 S33: 0.0475
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 217
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2845 57.6243 94.8258
REMARK 3 T TENSOR
REMARK 3 T11: -0.0989 T22: 0.0188
REMARK 3 T33: 0.0021 T12: 0.0295
REMARK 3 T13: 0.0044 T23: -0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 1.3526 L22: 0.7436
REMARK 3 L33: 1.2246 L12: -0.0020
REMARK 3 L13: 0.0755 L23: -0.0100
REMARK 3 S TENSOR
REMARK 3 S11: 0.0068 S12: -0.0816 S13: 0.0741
REMARK 3 S21: 0.0075 S22: -0.0389 S23: 0.1709
REMARK 3 S31: -0.0799 S32: -0.2666 S33: 0.0320
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 3 C 308
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0660 48.1154 40.2271
REMARK 3 T TENSOR
REMARK 3 T11: -0.0258 T22: -0.0549
REMARK 3 T33: -0.0456 T12: 0.0023
REMARK 3 T13: -0.0018 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 0.2262 L22: 0.4082
REMARK 3 L33: 0.8348 L12: -0.0962
REMARK 3 L13: -0.0299 L23: -0.1054
REMARK 3 S TENSOR
REMARK 3 S11: 0.0101 S12: 0.0286 S13: 0.0029
REMARK 3 S21: -0.0334 S22: 0.0040 S23: 0.0034
REMARK 3 S31: 0.0021 S32: 0.0311 S33: -0.0142
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 3 C 308
REMARK 3 RESIDUE RANGE : C 999 C 999
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0118 48.4309 40.3360
REMARK 3 T TENSOR
REMARK 3 T11: -0.0222 T22: -0.0504
REMARK 3 T33: -0.0409 T12: 0.0033
REMARK 3 T13: -0.0004 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.2823 L22: 0.4756
REMARK 3 L33: 0.9253 L12: -0.0501
REMARK 3 L13: 0.0272 L23: -0.1057
REMARK 3 S TENSOR
REMARK 3 S11: 0.0067 S12: 0.0330 S13: 0.0067
REMARK 3 S21: -0.0508 S22: 0.0027 S23: 0.0047
REMARK 3 S31: 0.0071 S32: 0.0341 S33: -0.0094
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 217
REMARK 3 ORIGIN FOR THE GROUP (A): 57.1516 34.5538 58.2159
REMARK 3 T TENSOR
REMARK 3 T11: -0.0330 T22: -0.0116
REMARK 3 T33: -0.0241 T12: 0.0526
REMARK 3 T13: -0.0024 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 1.4221 L22: 0.3717
REMARK 3 L33: 1.5927 L12: -0.0381
REMARK 3 L13: 0.2438 L23: 0.4224
REMARK 3 S TENSOR
REMARK 3 S11: 0.0747 S12: -0.0328 S13: -0.0434
REMARK 3 S21: -0.0633 S22: -0.0103 S23: -0.1554
REMARK 3 S31: 0.1656 S32: 0.2753 S33: -0.0644
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 217
REMARK 3 ORIGIN FOR THE GROUP (A): 57.2043 34.6354 58.6877
REMARK 3 T TENSOR
REMARK 3 T11: -0.0644 T22: 0.0470
REMARK 3 T33: -0.0013 T12: 0.0540
REMARK 3 T13: 0.0009 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 1.1573 L22: 0.6738
REMARK 3 L33: 1.7843 L12: 0.0167
REMARK 3 L13: 0.3440 L23: 0.2935
REMARK 3 S TENSOR
REMARK 3 S11: 0.0413 S12: -0.0386 S13: -0.0385
REMARK 3 S21: -0.0535 S22: 0.0096 S23: -0.1905
REMARK 3 S31: 0.1757 S32: 0.3696 S33: -0.0509
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 901 A 901
REMARK 3 RESIDUE RANGE : A 998 A 998
REMARK 3 RESIDUE RANGE : C 901 C 901
REMARK 3 RESIDUE RANGE : C 998 C 998
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5272 45.9936 58.9538
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: -0.0001
REMARK 3 T33: 0.0000 T12: -0.0002
REMARK 3 T13: 0.0001 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0502 L22: 1.0971
REMARK 3 L33: 6.1465 L12: -0.0644
REMARK 3 L13: -0.4542 L23: 2.0195
REMARK 3 S TENSOR
REMARK 3 S11: 0.0500 S12: 0.0325 S13: -0.0906
REMARK 3 S21: -0.2135 S22: -0.0639 S23: -0.0268
REMARK 3 S31: -0.3350 S32: -0.1214 S33: 0.0139
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 13
REMARK 3 RESIDUE RANGE : W 1 W 1153
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5694 45.6616 68.5770
REMARK 3 T TENSOR
REMARK 3 T11: 0.0012 T22: 0.0031
REMARK 3 T33: 0.0465 T12: -0.0009
REMARK 3 T13: -0.0128 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.1953 L22: 0.1673
REMARK 3 L33: 0.6996 L12: -0.0202
REMARK 3 L13: -0.1769 L23: 0.0190
REMARK 3 S TENSOR
REMARK 3 S11: -0.0034 S12: -0.0008 S13: 0.0007
REMARK 3 S21: -0.0238 S22: -0.0010 S23: 0.0094
REMARK 3 S31: 0.0166 S32: 0.0131 S33: 0.0044
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 RIDING
REMARK 3 POSITIONS. THERE IS NCS BETWEEN THE COMPLEX FORMED BY MOLECULES
REMARK 3 A-C AND COMPLEX B-D. IN MOLECULES B AND D, RESIDUES 218-222 ARE
REMARK 3 DISORDERED. THE COORDINATES OF HUMAN PROCARBOXYPEPTIDASE A4
REMARK 3 EMPLOYED FOR THE MR CORRESPOND TO PDB ENTRY 2BOA.
REMARK 4
REMARK 4 2BO9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1290023573.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0067
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 179401
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 48.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.26000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE, MLPHARE, SIGMAA, DM
REMARK 200 STARTING MODEL: CPA4 WITHIN PCPA4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% MPD; 0.1M BIS-TRIS PH 6.5, PH 6.50
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 48.32550
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 TYR A 309
REMARK 465 GLU B 218
REMARK 465 VAL B 219
REMARK 465 GLN B 220
REMARK 465 LEU B 221
REMARK 465 GLU B 222
REMARK 465 TYR C 309
REMARK 465 GLU D 218
REMARK 465 VAL D 219
REMARK 465 GLN D 220
REMARK 465 LEU D 221
REMARK 465 GLU D 222
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 OE1 GLU A 217 O HOH A 1001 1.95
REMARK 500 O ASN A 133 O SER A 136 2.02
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 23 CB - CG - OD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP B 44 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 155 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP C 23 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP D 179 CB - CG - OD2 ANGL. DEV. = 6.1 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 THR A 129 -173.68 -69.65
REMARK 500 SER A 199 -7.01 155.01
REMARK 500 GLN A 200 61.64 62.78
REMARK 500 SER A 234 12.69 -140.15
REMARK 500 TYR A 248 160.05 174.52
REMARK 500 ASP A 273 -147.51 -105.27
REMARK 500 LEU A 280 52.27 -91.11
REMARK 500 THR B 79 126.66 -36.15
REMARK 500 ASN B 121 67.18 60.56
REMARK 500 TRP B 157 73.87 -157.80
REMARK 500 ARG C 92 -51.99 -120.51
REMARK 500 THR C 121 -43.71 -130.26
REMARK 500 THR C 129 -174.24 -69.93
REMARK 500 SER C 199 -8.73 156.34
REMARK 500 GLN C 200 64.74 62.87
REMARK 500 TYR C 248 161.64 177.02
REMARK 500 ASP C 273 -149.88 -104.07
REMARK 500 LEU C 280 51.79 -90.81
REMARK 500 ARG D 48 -50.33 -124.46
REMARK 500 GLU D 82 53.27 -112.39
REMARK 500 ASN D 121 67.54 62.15
REMARK 500 TRP D 157 72.91 -157.38
REMARK 500 ASP D 173 -163.56 -100.58
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 902 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 69 ND1
REMARK 620 2 GLU A 72 OE1 118.0
REMARK 620 3 GLU A 72 OE2 95.5 57.9
REMARK 620 4 HIS A 196 ND1 101.2 92.4 150.2
REMARK 620 5 HOH A1003 O 109.4 124.2 91.1 106.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 69 ND1
REMARK 620 2 GLU C 72 OE1 119.2
REMARK 620 3 GLU C 72 OE2 93.0 57.1
REMARK 620 4 HIS C 196 ND1 103.1 92.9 150.0
REMARK 620 5 HOH C 503 O 109.1 122.6 93.1 104.9
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BOA RELATED DB: PDB
REMARK 900 HUMAN PROCARBOXYPEPTIDASE A4.
DBREF 2BO9 A 3 309 UNP Q9UI42 CBPA4_HUMAN 114 421
DBREF 2BO9 B 1 222 UNP Q9BS40 LXN_HUMAN 1 222
DBREF 2BO9 C 3 309 UNP Q9UI42 CBPA4_HUMAN 114 421
DBREF 2BO9 D 1 222 UNP Q9BS40 LXN_HUMAN 1 222
SEQRES 1 A 308 SER SER ASN ASN PHE ASN TYR GLY ALA TYR HIS SER LEU
SEQRES 2 A 308 GLU ALA ILE TYR HIS GLU MET ASP ASN ILE ALA ALA ASP
SEQRES 3 A 308 PHE PRO ASP LEU ALA ARG ARG VAL LYS ILE GLY HIS SER
SEQRES 4 A 308 PHE GLU ASN ARG PRO MET TYR VAL LEU LYS PHE SER THR
SEQRES 5 A 308 GLY LYS GLY VAL ARG ARG PRO ALA VAL TRP LEU ASN ALA
SEQRES 6 A 308 GLY ILE HIS SER ARG GLU TRP ILE SER GLN ALA THR ALA
SEQRES 7 A 308 ILE TRP THR ALA ARG LYS ILE VAL SER ASP TYR GLN ARG
SEQRES 8 A 308 ASP PRO ALA ILE THR SER ILE LEU GLU LYS MET ASP ILE
SEQRES 9 A 308 PHE LEU LEU PRO VAL ALA ASN PRO ASP GLY TYR VAL TYR
SEQRES 10 A 308 THR GLN THR GLN ASN ARG LEU TRP ARG LYS THR ARG SER
SEQRES 11 A 308 ARG ASN PRO GLY SER SER CYS ILE GLY ALA ASP PRO ASN
SEQRES 12 A 308 ARG ASN TRP ASN ALA SER PHE ALA GLY LYS GLY ALA SER
SEQRES 13 A 308 ASP ASN PRO CYS SER GLU VAL TYR HIS GLY PRO HIS ALA
SEQRES 14 A 308 ASN SER GLU VAL GLU VAL LYS SER VAL VAL ASP PHE ILE
SEQRES 15 A 308 GLN LYS HIS GLY ASN PHE LYS GLY PHE ILE ASP LEU HIS
SEQRES 16 A 308 SER TYR SER GLN LEU LEU MET TYR PRO TYR GLY TYR SER
SEQRES 17 A 308 VAL LYS LYS ALA PRO ASP ALA GLU GLU LEU ASP LYS VAL
SEQRES 18 A 308 ALA ARG LEU ALA ALA LYS ALA LEU ALA SER VAL SER GLY
SEQRES 19 A 308 THR GLU TYR GLN VAL GLY PRO THR CYS THR THR VAL TYR
SEQRES 20 A 308 PRO ALA SER GLY SER SER ILE ASP TRP ALA TYR ASP ASN
SEQRES 21 A 308 GLY ILE LYS PHE ALA PHE THR PHE GLU LEU ARG ASP THR
SEQRES 22 A 308 GLY THR TYR GLY PHE LEU LEU PRO ALA ASN GLN ILE ILE
SEQRES 23 A 308 PRO THR ALA GLU GLU THR TRP LEU GLY LEU LYS THR ILE
SEQRES 24 A 308 MET GLU HIS VAL ARG ASP ASN LEU TYR
SEQRES 1 B 222 MET GLU ILE PRO PRO THR ASN TYR PRO ALA SER ARG ALA
SEQRES 2 B 222 ALA LEU VAL ALA GLN ASN TYR ILE ASN TYR GLN GLN GLY
SEQRES 3 B 222 THR PRO HIS ARG VAL PHE GLU VAL GLN LYS VAL LYS GLN
SEQRES 4 B 222 ALA SER MET GLU ASP ILE PRO GLY ARG GLY HIS LYS TYR
SEQRES 5 B 222 ARG LEU LYS PHE ALA VAL GLU GLU ILE ILE GLN LYS GLN
SEQRES 6 B 222 VAL LYS VAL ASN CYS THR ALA GLU VAL LEU TYR PRO SER
SEQRES 7 B 222 THR GLY GLN GLU THR ALA PRO GLU VAL ASN PHE THR PHE
SEQRES 8 B 222 GLU GLY GLU THR GLY LYS ASN PRO ASP GLU GLU ASP ASN
SEQRES 9 B 222 THR PHE TYR GLN ARG LEU LYS SER MET LYS GLU PRO LEU
SEQRES 10 B 222 GLU ALA GLN ASN ILE PRO ASP ASN PHE GLY ASN VAL SER
SEQRES 11 B 222 PRO GLU MET THR LEU VAL LEU HIS LEU ALA TRP VAL ALA
SEQRES 12 B 222 CYS GLY TYR ILE ILE TRP GLN ASN SER THR GLU ASP THR
SEQRES 13 B 222 TRP TYR LYS MET VAL LYS ILE GLN THR VAL LYS GLN VAL
SEQRES 14 B 222 GLN ARG ASN ASP ASP PHE ILE GLU LEU ASP TYR THR ILE
SEQRES 15 B 222 LEU LEU HIS ASN ILE ALA SER GLN GLU ILE ILE PRO TRP
SEQRES 16 B 222 GLN MET GLN VAL LEU TRP HIS PRO GLN TYR GLY THR LYS
SEQRES 17 B 222 VAL LYS HIS ASN SER ARG LEU PRO LYS GLU VAL GLN LEU
SEQRES 18 B 222 GLU
SEQRES 1 C 308 SER SER ASN ASN PHE ASN TYR GLY ALA TYR HIS SER LEU
SEQRES 2 C 308 GLU ALA ILE TYR HIS GLU MET ASP ASN ILE ALA ALA ASP
SEQRES 3 C 308 PHE PRO ASP LEU ALA ARG ARG VAL LYS ILE GLY HIS SER
SEQRES 4 C 308 PHE GLU ASN ARG PRO MET TYR VAL LEU LYS PHE SER THR
SEQRES 5 C 308 GLY LYS GLY VAL ARG ARG PRO ALA VAL TRP LEU ASN ALA
SEQRES 6 C 308 GLY ILE HIS SER ARG GLU TRP ILE SER GLN ALA THR ALA
SEQRES 7 C 308 ILE TRP THR ALA ARG LYS ILE VAL SER ASP TYR GLN ARG
SEQRES 8 C 308 ASP PRO ALA ILE THR SER ILE LEU GLU LYS MET ASP ILE
SEQRES 9 C 308 PHE LEU LEU PRO VAL ALA ASN PRO ASP GLY TYR VAL TYR
SEQRES 10 C 308 THR GLN THR GLN ASN ARG LEU TRP ARG LYS THR ARG SER
SEQRES 11 C 308 ARG ASN PRO GLY SER SER CYS ILE GLY ALA ASP PRO ASN
SEQRES 12 C 308 ARG ASN TRP ASN ALA SER PHE ALA GLY LYS GLY ALA SER
SEQRES 13 C 308 ASP ASN PRO CYS SER GLU VAL TYR HIS GLY PRO HIS ALA
SEQRES 14 C 308 ASN SER GLU VAL GLU VAL LYS SER VAL VAL ASP PHE ILE
SEQRES 15 C 308 GLN LYS HIS GLY ASN PHE LYS GLY PHE ILE ASP LEU HIS
SEQRES 16 C 308 SER TYR SER GLN LEU LEU MET TYR PRO TYR GLY TYR SER
SEQRES 17 C 308 VAL LYS LYS ALA PRO ASP ALA GLU GLU LEU ASP LYS VAL
SEQRES 18 C 308 ALA ARG LEU ALA ALA LYS ALA LEU ALA SER VAL SER GLY
SEQRES 19 C 308 THR GLU TYR GLN VAL GLY PRO THR CYS THR THR VAL TYR
SEQRES 20 C 308 PRO ALA SER GLY SER SER ILE ASP TRP ALA TYR ASP ASN
SEQRES 21 C 308 GLY ILE LYS PHE ALA PHE THR PHE GLU LEU ARG ASP THR
SEQRES 22 C 308 GLY THR TYR GLY PHE LEU LEU PRO ALA ASN GLN ILE ILE
SEQRES 23 C 308 PRO THR ALA GLU GLU THR TRP LEU GLY LEU LYS THR ILE
SEQRES 24 C 308 MET GLU HIS VAL ARG ASP ASN LEU TYR
SEQRES 1 D 222 MET GLU ILE PRO PRO THR ASN TYR PRO ALA SER ARG ALA
SEQRES 2 D 222 ALA LEU VAL ALA GLN ASN TYR ILE ASN TYR GLN GLN GLY
SEQRES 3 D 222 THR PRO HIS ARG VAL PHE GLU VAL GLN LYS VAL LYS GLN
SEQRES 4 D 222 ALA SER MET GLU ASP ILE PRO GLY ARG GLY HIS LYS TYR
SEQRES 5 D 222 ARG LEU LYS PHE ALA VAL GLU GLU ILE ILE GLN LYS GLN
SEQRES 6 D 222 VAL LYS VAL ASN CYS THR ALA GLU VAL LEU TYR PRO SER
SEQRES 7 D 222 THR GLY GLN GLU THR ALA PRO GLU VAL ASN PHE THR PHE
SEQRES 8 D 222 GLU GLY GLU THR GLY LYS ASN PRO ASP GLU GLU ASP ASN
SEQRES 9 D 222 THR PHE TYR GLN ARG LEU LYS SER MET LYS GLU PRO LEU
SEQRES 10 D 222 GLU ALA GLN ASN ILE PRO ASP ASN PHE GLY ASN VAL SER
SEQRES 11 D 222 PRO GLU MET THR LEU VAL LEU HIS LEU ALA TRP VAL ALA
SEQRES 12 D 222 CYS GLY TYR ILE ILE TRP GLN ASN SER THR GLU ASP THR
SEQRES 13 D 222 TRP TYR LYS MET VAL LYS ILE GLN THR VAL LYS GLN VAL
SEQRES 14 D 222 GLN ARG ASN ASP ASP PHE ILE GLU LEU ASP TYR THR ILE
SEQRES 15 D 222 LEU LEU HIS ASN ILE ALA SER GLN GLU ILE ILE PRO TRP
SEQRES 16 D 222 GLN MET GLN VAL LEU TRP HIS PRO GLN TYR GLY THR LYS
SEQRES 17 D 222 VAL LYS HIS ASN SER ARG LEU PRO LYS GLU VAL GLN LEU
SEQRES 18 D 222 GLU
MODRES 2BO9 ASN A 148 ASN GLYCOSYLATION SITE
MODRES 2BO9 ASN C 148 ASN GLYCOSYLATION SITE
HET NAG A 901 14
HET ZN A 902 1
HET VAL A 903 8
HET MPD A 904 8
HET MPD A 905 8
HET MPD A 906 8
HET MPD B 301 8
HET MPD B 302 8
HET MPD B 303 8
HET MPD B 304 8
HET VAL C 401 8
HET NAG C 402 14
HET ZN C 403 1
HET MPD C 404 8
HET MPD D 301 8
HET MPD D 302 8
HET MPD D 303 8
HET MPD D 304 8
HET ACN D 305 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM ZN ZINC ION
HETNAM VAL VALINE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM ACN ACETONE
FORMUL 5 NAG 2(C8 H15 N O6)
FORMUL 6 ZN 2(ZN 2+)
FORMUL 7 VAL 2(C5 H11 N O2)
FORMUL 8 MPD 12(C6 H14 O2)
FORMUL 23 ACN C3 H6 O
FORMUL 24 HOH *1153(H2 O)
HELIX 1 1 SER A 14 PHE A 29 1 16
HELIX 2 2 GLU A 72 TYR A 90 1 19
HELIX 3 3 ASP A 93 MET A 103 1 11
HELIX 4 4 ASN A 112 GLN A 122 1 11
HELIX 5 5 ASP A 142 ASN A 146 5 5
HELIX 6 6 GLU A 173 GLY A 187 1 15
HELIX 7 7 ASP A 215 SER A 232 1 18
HELIX 8 8 THR A 243 VAL A 247 1 5
HELIX 9 9 SER A 253 ASN A 261 1 9
HELIX 10 10 PRO A 282 ASN A 284 5 3
HELIX 11 11 GLN A 285 ASP A 306 1 22
HELIX 12 12 ASN B 7 GLY B 26 1 20
HELIX 13 13 PRO B 99 MET B 113 1 15
HELIX 14 14 SER B 130 SER B 152 1 23
HELIX 15 15 SER C 14 PHE C 29 1 16
HELIX 16 16 GLU C 72 TYR C 90 1 19
HELIX 17 17 ASP C 93 MET C 103 1 11
HELIX 18 18 ASN C 112 GLN C 122 1 11
HELIX 19 19 ASP C 142 ASN C 146 5 5
HELIX 20 20 GLU C 173 GLY C 187 1 15
HELIX 21 21 ASP C 215 SER C 232 1 18
HELIX 22 22 THR C 243 VAL C 247 1 5
HELIX 23 23 SER C 253 ASN C 261 1 9
HELIX 24 24 PRO C 282 ASN C 284 5 3
HELIX 25 25 GLN C 285 ASP C 306 1 22
HELIX 26 26 ASN D 7 GLY D 26 1 20
HELIX 27 27 PRO D 99 SER D 112 1 14
HELIX 28 28 SER D 130 GLU D 132 5 3
HELIX 29 29 MET D 133 SER D 152 1 20
SHEET 1 AA 8 ALA A 33 HIS A 40 0
SHEET 2 AA 8 PRO A 46 PHE A 52 -1 O MET A 47 N ILE A 38
SHEET 3 AA 8 ASP A 104 LEU A 108 -1 O ILE A 105 N PHE A 52
SHEET 4 AA 8 ALA A 61 ALA A 66 1 O VAL A 62 N PHE A 106
SHEET 5 AA 8 PHE A 189 HIS A 196 1 N LYS A 190 O ALA A 61
SHEET 6 AA 8 PHE A 265 GLU A 270 1 O PHE A 265 N PHE A 192
SHEET 7 AA 8 LEU A 201 TYR A 204 -1 O LEU A 201 N GLU A 270
SHEET 8 AA 8 GLN A 239 PRO A 242 1 O GLN A 239 N LEU A 202
SHEET 1 BA 4 PHE B 32 ILE B 45 0
SHEET 2 BA 4 GLY B 49 GLU B 60 -1 O GLY B 49 N ILE B 45
SHEET 3 BA 4 LYS B 67 PRO B 77 -1 O VAL B 68 N VAL B 58
SHEET 4 BA 4 GLU B 86 PHE B 91 -1 O GLU B 86 N LEU B 75
SHEET 1 BB 5 GLU B 118 ILE B 122 0
SHEET 2 BB 5 TYR B 158 VAL B 169 -1 O ILE B 163 N ILE B 122
SHEET 3 BB 5 ILE B 176 ASN B 186 -1 O GLU B 177 N VAL B 169
SHEET 4 BB 5 ILE B 192 HIS B 202 -1 O ILE B 193 N LEU B 184
SHEET 5 BB 5 GLY B 206 ARG B 214 -1 O GLY B 206 N HIS B 202
SHEET 1 CA 8 ALA C 33 HIS C 40 0
SHEET 2 CA 8 PRO C 46 PHE C 52 -1 O MET C 47 N ILE C 38
SHEET 3 CA 8 ASP C 104 LEU C 108 -1 O ILE C 105 N PHE C 52
SHEET 4 CA 8 ALA C 61 ALA C 66 1 O VAL C 62 N PHE C 106
SHEET 5 CA 8 PHE C 189 HIS C 196 1 N LYS C 190 O ALA C 61
SHEET 6 CA 8 PHE C 265 GLU C 270 1 O PHE C 265 N PHE C 192
SHEET 7 CA 8 LEU C 201 TYR C 204 -1 O LEU C 201 N GLU C 270
SHEET 8 CA 8 GLN C 239 PRO C 242 1 O GLN C 239 N LEU C 202
SHEET 1 DA 4 PHE D 32 ILE D 45 0
SHEET 2 DA 4 GLY D 49 GLU D 60 -1 O GLY D 49 N ILE D 45
SHEET 3 DA 4 LYS D 67 PRO D 77 -1 O VAL D 68 N VAL D 58
SHEET 4 DA 4 GLU D 86 GLU D 92 -1 O GLU D 86 N LEU D 75
SHEET 1 DB 5 GLU D 118 ILE D 122 0
SHEET 2 DB 5 TYR D 158 VAL D 169 -1 O ILE D 163 N ILE D 122
SHEET 3 DB 5 ILE D 176 ASN D 186 -1 O GLU D 177 N VAL D 169
SHEET 4 DB 5 ILE D 192 TRP D 201 -1 O ILE D 193 N LEU D 184
SHEET 5 DB 5 THR D 207 ARG D 214 -1 O LYS D 208 N LEU D 200
SSBOND 1 CYS A 138 CYS A 161 1555 1555 2.04
SSBOND 2 CYS C 138 CYS C 161 1555 1555 2.03
LINK ND2 ASN A 148 C1 NAG A 901 1555 1555 1.45
LINK ND2 ASN C 148 C1 NAG C 402 1555 1555 1.45
LINK ND1 HIS A 69 ZN ZN A 902 1555 1555 2.03
LINK OE1 GLU A 72 ZN ZN A 902 1555 1555 2.29
LINK OE2 GLU A 72 ZN ZN A 902 1555 1555 2.27
LINK ND1 HIS A 196 ZN ZN A 902 1555 1555 2.03
LINK ZN ZN A 902 O HOH A1003 1555 1555 2.20
LINK ND1 HIS C 69 ZN ZN C 403 1555 1555 2.02
LINK OE1 GLU C 72 ZN ZN C 403 1555 1555 2.32
LINK OE2 GLU C 72 ZN ZN C 403 1555 1555 2.31
LINK ND1 HIS C 196 ZN ZN C 403 1555 1555 2.07
LINK ZN ZN C 403 O HOH C 503 1555 1555 2.24
CISPEP 1 SER A 197 TYR A 198 0 -2.55
CISPEP 2 PRO A 205 TYR A 206 0 3.59
CISPEP 3 ARG A 272 ASP A 273 0 -6.49
CISPEP 4 ILE B 122 PRO B 123 0 -5.37
CISPEP 5 SER C 197 TYR C 198 0 -3.04
CISPEP 6 PRO C 205 TYR C 206 0 1.89
CISPEP 7 ARG C 272 ASP C 273 0 -7.70
CISPEP 8 ILE D 122 PRO D 123 0 -6.81
CRYST1 78.922 96.651 92.358 90.00 99.60 90.00 P 1 21 1 4
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 0.012671 0.000000 0.002143 0.00000
SCALE2 0.000000 0.010347 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010981 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
