HEADER HYDROLASE/INHIBITOR 23-APR-12 4ARF
TITLE CRYSTAL STRUCTURE OF THE PEPTIDASE DOMAIN OF COLLAGENASE H FROM
TITLE 2 CLOSTRIDIUM HISTOLYTICUM IN COMPLEX WITH THE PEPTIDIC INHIBITOR
TITLE 3 ISOAMYLPHOSPHONYL-GLY-PRO-ALA AT 1.77 ANGSTROM RESOLUTION.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COLH PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PEPTIDASE DOMAIN, RESIDUES 331-721;
COMPND 5 SYNONYM: COLLAGENASE;
COMPND 6 EC: 3.4.24.3;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ISOAMYLPHOSPHONYL-GLY-PRO-ALA;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM HISTOLYTICUM;
SOURCE 3 ORGANISM_TAXID: 1498;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PET-15B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 12 ORGANISM_TAXID: 32630
KEYWDS HYDROLASE-INHIBITOR COMPLEX, COLLAGENOLYSIS, HYDROLYSE,
KEYWDS 2 METALLOPROTEASE, HEXXH
EXPDTA X-RAY DIFFRACTION
AUTHOR U.ECKHARD,H.BRANDSTETTER
REVDAT 5 20-DEC-23 4ARF 1 LINK ATOM
REVDAT 4 07-FEB-18 4ARF 1 REMARK HELIX SHEET LINK
REVDAT 4 2 1 SITE ATOM
REVDAT 3 08-FEB-17 4ARF 1 SOURCE
REVDAT 2 31-JUL-13 4ARF 1 JRNL
REVDAT 1 05-JUN-13 4ARF 0
JRNL AUTH U.ECKHARD,E.SCHONAUER,H.BRANDSTETTER
JRNL TITL STRUCTURAL BASIS FOR ACTIVITY REGULATION AND SUBSTRATE
JRNL TITL 2 PREFERENCE OF CLOSTRIDIAL COLLAGENASES G, H, AND T.
JRNL REF J.BIOL.CHEM. V. 288 20184 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23703618
JRNL DOI 10.1074/JBC.M112.448548
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 40273
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) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2150
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) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2292
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 117
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3105
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 267
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.30000
REMARK 3 B22 (A**2) : 1.50000
REMARK 3 B33 (A**2) : -1.81000
REMARK 3 B12 (A**2) : 0.00000
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): 0.160
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.105
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.073
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.339
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3190 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2167 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4304 ; 1.147 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5220 ; 0.823 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 379 ; 5.397 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 166 ;31.689 ;24.337
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 525 ;11.928 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;20.279 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 445 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3595 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 695 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 5357 ; 2.961 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 85 ;23.143 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5463 ;13.040 ; 5.000
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 : 20
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 342 A 356
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9980 14.7608 -28.5202
REMARK 3 T TENSOR
REMARK 3 T11: 0.0168 T22: 0.0653
REMARK 3 T33: 0.0345 T12: -0.0033
REMARK 3 T13: -0.0093 T23: 0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 2.1288 L22: 3.3866
REMARK 3 L33: 2.2718 L12: 2.0724
REMARK 3 L13: -1.7506 L23: -1.6843
REMARK 3 S TENSOR
REMARK 3 S11: -0.0234 S12: -0.1249 S13: -0.1443
REMARK 3 S21: -0.0472 S22: -0.0161 S23: -0.0976
REMARK 3 S31: 0.0744 S32: -0.0442 S33: 0.0394
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 357 A 372
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8268 15.5684 -21.8204
REMARK 3 T TENSOR
REMARK 3 T11: 0.0555 T22: 0.0859
REMARK 3 T33: 0.0403 T12: -0.0189
REMARK 3 T13: 0.0039 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.0286 L22: 5.8735
REMARK 3 L33: 0.2119 L12: -0.2519
REMARK 3 L13: -0.0643 L23: 1.0295
REMARK 3 S TENSOR
REMARK 3 S11: -0.0199 S12: 0.0037 S13: -0.0297
REMARK 3 S21: -0.0236 S22: -0.0509 S23: 0.3276
REMARK 3 S31: 0.0320 S32: -0.0361 S33: 0.0708
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 : A 373 A 412
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8007 18.5219 -18.8348
REMARK 3 T TENSOR
REMARK 3 T11: 0.0393 T22: 0.0590
REMARK 3 T33: 0.0355 T12: 0.0012
REMARK 3 T13: -0.0124 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 0.2410 L22: 0.1683
REMARK 3 L33: 0.2927 L12: -0.0616
REMARK 3 L13: -0.0539 L23: 0.2190
REMARK 3 S TENSOR
REMARK 3 S11: 0.0055 S12: -0.0292 S13: -0.0082
REMARK 3 S21: 0.0072 S22: -0.0046 S23: -0.0099
REMARK 3 S31: 0.0011 S32: -0.0124 S33: -0.0009
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 : A 413 A 419
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4681 -2.0062 -19.2159
REMARK 3 T TENSOR
REMARK 3 T11: 0.1236 T22: 0.2435
REMARK 3 T33: 0.2635 T12: 0.0126
REMARK 3 T13: 0.0644 T23: -0.0696
REMARK 3 L TENSOR
REMARK 3 L11: 23.0189 L22: 12.1256
REMARK 3 L33: 1.6628 L12: 0.3358
REMARK 3 L13: 6.1715 L23: -0.2248
REMARK 3 S TENSOR
REMARK 3 S11: 0.6745 S12: -0.3007 S13: 2.4223
REMARK 3 S21: 0.4313 S22: -1.2591 S23: 0.2490
REMARK 3 S31: 0.1870 S32: -0.0482 S33: 0.5846
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 : A 420 A 427
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5493 1.6723 -12.2576
REMARK 3 T TENSOR
REMARK 3 T11: 0.1156 T22: 0.1016
REMARK 3 T33: 0.1548 T12: 0.0659
REMARK 3 T13: 0.0469 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 1.3600 L22: 19.2883
REMARK 3 L33: 3.6360 L12: 1.1689
REMARK 3 L13: 0.4372 L23: 2.8178
REMARK 3 S TENSOR
REMARK 3 S11: -0.1538 S12: -0.0351 S13: -0.3275
REMARK 3 S21: 0.5087 S22: 0.0926 S23: -1.2030
REMARK 3 S31: 0.5210 S32: 0.3141 S33: 0.0613
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 428 A 445
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5523 8.1862 -15.7892
REMARK 3 T TENSOR
REMARK 3 T11: 0.0637 T22: 0.0864
REMARK 3 T33: 0.0250 T12: 0.0164
REMARK 3 T13: -0.0113 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 3.4920 L22: 1.2732
REMARK 3 L33: 1.3260 L12: 1.1037
REMARK 3 L13: -1.6576 L23: 0.1102
REMARK 3 S TENSOR
REMARK 3 S11: -0.0962 S12: -0.0129 S13: -0.2064
REMARK 3 S21: 0.0604 S22: -0.0390 S23: -0.0401
REMARK 3 S31: 0.0377 S32: -0.0709 S33: 0.1351
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 : A 446 A 469
REMARK 3 ORIGIN FOR THE GROUP (A): -6.7316 16.8135 -13.8895
REMARK 3 T TENSOR
REMARK 3 T11: 0.0540 T22: 0.0648
REMARK 3 T33: 0.0118 T12: 0.0056
REMARK 3 T13: -0.0168 T23: 0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.7323 L22: 0.3673
REMARK 3 L33: 0.0948 L12: 0.1990
REMARK 3 L13: 0.0280 L23: 0.1744
REMARK 3 S TENSOR
REMARK 3 S11: -0.0022 S12: -0.0161 S13: 0.0398
REMARK 3 S21: 0.0397 S22: 0.0005 S23: 0.0001
REMARK 3 S31: 0.0063 S32: -0.0029 S33: 0.0018
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 : A 470 A 477
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1340 10.2915 -14.3460
REMARK 3 T TENSOR
REMARK 3 T11: 0.0516 T22: 0.0426
REMARK 3 T33: 0.0493 T12: -0.0186
REMARK 3 T13: -0.0102 T23: 0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 3.7402 L22: 3.6278
REMARK 3 L33: 7.6564 L12: 0.0294
REMARK 3 L13: 2.9036 L23: 3.0091
REMARK 3 S TENSOR
REMARK 3 S11: -0.0089 S12: 0.1122 S13: -0.1991
REMARK 3 S21: 0.2276 S22: 0.0976 S23: 0.2214
REMARK 3 S31: 0.3318 S32: 0.2673 S33: -0.0887
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 478 A 487
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9120 12.8602 -5.5268
REMARK 3 T TENSOR
REMARK 3 T11: 0.0247 T22: 0.0907
REMARK 3 T33: 0.0219 T12: -0.0116
REMARK 3 T13: -0.0047 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 1.5113 L22: 0.3337
REMARK 3 L33: 1.7072 L12: 0.6572
REMARK 3 L13: -1.0372 L23: -0.2326
REMARK 3 S TENSOR
REMARK 3 S11: -0.0833 S12: 0.0534 S13: -0.0786
REMARK 3 S21: -0.0447 S22: 0.0639 S23: -0.0421
REMARK 3 S31: 0.0200 S32: 0.1476 S33: 0.0194
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 488 A 517
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5364 20.5016 -0.5684
REMARK 3 T TENSOR
REMARK 3 T11: 0.0464 T22: 0.0591
REMARK 3 T33: 0.0303 T12: 0.0085
REMARK 3 T13: -0.0166 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.2220 L22: 0.5602
REMARK 3 L33: 1.1990 L12: 0.3457
REMARK 3 L13: -0.3722 L23: -0.4688
REMARK 3 S TENSOR
REMARK 3 S11: -0.0068 S12: 0.0172 S13: 0.0117
REMARK 3 S21: 0.0076 S22: 0.0236 S23: 0.0176
REMARK 3 S31: 0.0583 S32: -0.0228 S33: -0.0168
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 518 A 547
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4346 13.0706 3.5524
REMARK 3 T TENSOR
REMARK 3 T11: 0.0316 T22: 0.0531
REMARK 3 T33: 0.0237 T12: 0.0065
REMARK 3 T13: 0.0007 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 0.5906 L22: 0.7170
REMARK 3 L33: 1.3425 L12: 0.1569
REMARK 3 L13: -0.1151 L23: 0.6694
REMARK 3 S TENSOR
REMARK 3 S11: 0.0026 S12: -0.0279 S13: -0.0383
REMARK 3 S21: -0.0219 S22: -0.0069 S23: 0.0036
REMARK 3 S31: 0.0876 S32: 0.0992 S33: 0.0043
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 548 A 574
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9823 24.5009 -4.0794
REMARK 3 T TENSOR
REMARK 3 T11: 0.0397 T22: 0.0697
REMARK 3 T33: 0.0582 T12: -0.0133
REMARK 3 T13: 0.0041 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 1.6648 L22: 0.7949
REMARK 3 L33: 0.6613 L12: -0.9335
REMARK 3 L13: -0.9225 L23: 0.6899
REMARK 3 S TENSOR
REMARK 3 S11: 0.0087 S12: -0.0877 S13: 0.0766
REMARK 3 S21: -0.0603 S22: 0.0597 S23: -0.0073
REMARK 3 S31: -0.0503 S32: 0.0680 S33: -0.0684
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 575 A 584
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9967 20.6671 7.7092
REMARK 3 T TENSOR
REMARK 3 T11: 0.0131 T22: 0.1083
REMARK 3 T33: 0.0216 T12: -0.0050
REMARK 3 T13: -0.0007 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 5.9325 L22: 6.2068
REMARK 3 L33: 17.2498 L12: -5.2517
REMARK 3 L13: -9.0790 L23: 7.7193
REMARK 3 S TENSOR
REMARK 3 S11: -0.0071 S12: -0.3100 S13: 0.0780
REMARK 3 S21: -0.0027 S22: 0.1537 S23: -0.0456
REMARK 3 S31: 0.1934 S32: 0.6644 S33: -0.1466
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 585 A 605
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0089 22.5010 7.6496
REMARK 3 T TENSOR
REMARK 3 T11: 0.0423 T22: 0.0467
REMARK 3 T33: 0.0358 T12: -0.0121
REMARK 3 T13: -0.0143 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 1.2946 L22: 0.1022
REMARK 3 L33: 2.0873 L12: -0.2810
REMARK 3 L13: 1.1128 L23: -0.3155
REMARK 3 S TENSOR
REMARK 3 S11: 0.0155 S12: 0.0085 S13: 0.0473
REMARK 3 S21: -0.0346 S22: 0.0258 S23: 0.0096
REMARK 3 S31: -0.0602 S32: -0.0723 S33: -0.0413
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 606 A 615
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7252 27.0199 -18.5463
REMARK 3 T TENSOR
REMARK 3 T11: 0.0547 T22: 0.0703
REMARK 3 T33: 0.0158 T12: 0.0209
REMARK 3 T13: -0.0093 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 5.2505 L22: 2.6942
REMARK 3 L33: 4.8245 L12: -1.8278
REMARK 3 L13: 4.6912 L23: -2.7716
REMARK 3 S TENSOR
REMARK 3 S11: -0.0153 S12: -0.2157 S13: -0.0804
REMARK 3 S21: -0.0232 S22: 0.1329 S23: 0.0884
REMARK 3 S31: 0.0175 S32: -0.2172 S33: -0.1176
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 616 A 636
REMARK 3 ORIGIN FOR THE GROUP (A): -14.5438 43.8463 -24.9842
REMARK 3 T TENSOR
REMARK 3 T11: 0.0264 T22: 0.0425
REMARK 3 T33: 0.1678 T12: -0.0290
REMARK 3 T13: -0.0162 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 1.4551 L22: 1.3311
REMARK 3 L33: 0.0416 L12: 1.0808
REMARK 3 L13: 0.2451 L23: 0.1738
REMARK 3 S TENSOR
REMARK 3 S11: -0.1014 S12: 0.0946 S13: 0.3112
REMARK 3 S21: -0.0677 S22: 0.0441 S23: 0.0058
REMARK 3 S31: -0.0157 S32: 0.0149 S33: 0.0573
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 637 A 665
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9319 35.8299 -20.7734
REMARK 3 T TENSOR
REMARK 3 T11: 0.0460 T22: 0.0574
REMARK 3 T33: 0.0435 T12: -0.0141
REMARK 3 T13: 0.0073 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.1480 L22: 0.4976
REMARK 3 L33: 1.4968 L12: 0.1734
REMARK 3 L13: 1.0149 L23: 0.6830
REMARK 3 S TENSOR
REMARK 3 S11: -0.0062 S12: 0.0013 S13: -0.0395
REMARK 3 S21: 0.0433 S22: 0.0470 S23: -0.0225
REMARK 3 S31: 0.0370 S32: 0.0600 S33: -0.0408
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 666 A 685
REMARK 3 ORIGIN FOR THE GROUP (A): -12.0593 40.6985 -10.3413
REMARK 3 T TENSOR
REMARK 3 T11: 0.0429 T22: 0.0486
REMARK 3 T33: 0.0740 T12: -0.0068
REMARK 3 T13: -0.0186 T23: -0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 7.4915 L22: 0.0597
REMARK 3 L33: 1.7769 L12: 0.0425
REMARK 3 L13: 2.4692 L23: 0.2401
REMARK 3 S TENSOR
REMARK 3 S11: -0.0756 S12: -0.1808 S13: 0.1778
REMARK 3 S21: 0.0115 S22: -0.0216 S23: -0.0101
REMARK 3 S31: 0.0002 S32: -0.1547 S33: 0.0972
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 686 A 715
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7137 39.3054 -16.4664
REMARK 3 T TENSOR
REMARK 3 T11: 0.0305 T22: 0.0496
REMARK 3 T33: 0.0546 T12: -0.0153
REMARK 3 T13: 0.0021 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 1.7789 L22: 0.4613
REMARK 3 L33: 0.9949 L12: 0.3794
REMARK 3 L13: 0.8614 L23: 0.6507
REMARK 3 S TENSOR
REMARK 3 S11: -0.0277 S12: 0.0695 S13: 0.0664
REMARK 3 S21: 0.0078 S22: 0.0476 S23: -0.0410
REMARK 3 S31: 0.0091 S32: 0.0645 S33: -0.0199
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 716 A 721
REMARK 3 ORIGIN FOR THE GROUP (A): -20.4970 33.4497 -31.8078
REMARK 3 T TENSOR
REMARK 3 T11: 0.0775 T22: 0.0838
REMARK 3 T33: 0.0636 T12: 0.0133
REMARK 3 T13: 0.0485 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 9.8626 L22: 0.9012
REMARK 3 L33: 18.1945 L12: -0.2944
REMARK 3 L13: 8.5561 L23: -3.3502
REMARK 3 S TENSOR
REMARK 3 S11: -0.1651 S12: 0.3651 S13: -0.0527
REMARK 3 S21: -0.0778 S22: 0.1400 S23: -0.0345
REMARK 3 S31: 0.1055 S32: -0.2334 S33: 0.0252
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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. U VALUES WITH TLS ADDED
REMARK 4
REMARK 4 4ARF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1290052157.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.25
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8856
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42481
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.770
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 2Y3U
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG3350, 0.15M SODIUM FORMATE,
REMARK 280 PH 7.25
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 39.93500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 53.39000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.93500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 53.39000
REMARK 290 SMTRY3 4 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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1130 LIES ON A SPECIAL POSITION.
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 GLY A 328
REMARK 465 GLY A 329
REMARK 465 THR A 330
REMARK 465 LEU A 331
REMARK 465 ASP A 332
REMARK 465 LYS A 333
REMARK 465 PHE A 334
REMARK 465 LYS A 335
REMARK 465 LYS A 336
REMARK 465 GLU A 337
REMARK 465 GLY A 338
REMARK 465 LYS A 339
REMARK 465 GLU A 340
REMARK 465 LYS A 341
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 342 CE1 CZ OH
REMARK 470 LYS A 345 CE NZ
REMARK 470 GLU A 365 CD OE1 OE2
REMARK 470 GLU A 409 CD OE1 OE2
REMARK 470 LYS A 412 CD CE NZ
REMARK 470 VAL A 416 CG1 CG2
REMARK 470 LEU A 417 CD1
REMARK 470 TYR A 418 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR A 420 CE1 CE2 CZ OH
REMARK 470 ASP A 421 OD1 OD2
REMARK 470 ASN A 423 OD1 ND2
REMARK 470 LYS A 475 CE NZ
REMARK 470 ARG A 576 NE CZ NH1 NH2
REMARK 470 GLU A 629 CD OE1 OE2
REMARK 470 LYS A 634 NZ
REMARK 470 LYS A 637 CE NZ
REMARK 470 LYS A 642 CE NZ
REMARK 470 LYS A 668 NZ
REMARK 470 LYS A 680 CE NZ
REMARK 470 LYS A 700 CE NZ
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 O HOH A 1132 O HOH A 1132 2565 0.49
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 ASP A 388 27.41 -143.55
REMARK 500 ASP A 397 4.70 -69.41
REMARK 500 ASP A 552 59.52 -157.29
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 A1164 DISTANCE = 6.00 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 802 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 430 OE2
REMARK 620 2 GLY A 463 O 80.0
REMARK 620 3 VAL A 467 O 156.2 89.1
REMARK 620 4 GLY A 469 O 93.2 167.6 100.9
REMARK 620 5 HOH A 945 O 78.2 101.8 83.5 86.8
REMARK 620 6 HOH A 974 O 104.9 82.0 94.3 89.9 175.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 455 NE2
REMARK 620 2 HIS A 459 NE2 103.3
REMARK 620 3 GLU A 487 OE1 102.9 103.5
REMARK 620 4 IP8 B 1 O2 107.6 136.2 99.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4AR1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PEPTIDASE DOMAIN OF COLLAGENASE H FROM
REMARK 900 CLOSTRIDIUM HISTOLYTICUM AT 2.01 ANGSTROM RESOLUTION.
DBREF 4ARF A 331 721 UNP Q46085 Q46085_CLOHI 331 721
DBREF 4ARF B 1 4 PDB 4ARF 4ARF 1 4
SEQADV 4ARF GLY A 328 UNP Q46085 EXPRESSION TAG
SEQADV 4ARF GLY A 329 UNP Q46085 EXPRESSION TAG
SEQADV 4ARF THR A 330 UNP Q46085 EXPRESSION TAG
SEQADV 4ARF HIS A 582 UNP Q46085 TYR 582 VARIANT
SEQADV 4ARF VAL A 659 UNP Q46085 ALA 659 VARIANT
SEQADV 4ARF LYS A 706 UNP Q46085 ARG 706 VARIANT
SEQRES 1 A 394 GLY GLY THR LEU ASP LYS PHE LYS LYS GLU GLY LYS GLU
SEQRES 2 A 394 LYS TYR CYS PRO LYS THR TYR THR PHE ASP ASP GLY LYS
SEQRES 3 A 394 VAL ILE ILE LYS ALA GLY ALA ARG VAL GLU GLU GLU LYS
SEQRES 4 A 394 VAL LYS ARG LEU TYR TRP ALA SER LYS GLU VAL ASN SER
SEQRES 5 A 394 GLN PHE PHE ARG VAL TYR GLY ILE ASP LYS PRO LEU GLU
SEQRES 6 A 394 GLU GLY ASN PRO ASP ASP ILE LEU THR MET VAL ILE TYR
SEQRES 7 A 394 ASN SER PRO GLU GLU TYR LYS LEU ASN SER VAL LEU TYR
SEQRES 8 A 394 GLY TYR ASP THR ASN ASN GLY GLY MET TYR ILE GLU PRO
SEQRES 9 A 394 GLU GLY THR PHE PHE THR TYR GLU ARG GLU ALA GLN GLU
SEQRES 10 A 394 SER THR TYR THR LEU GLU GLU LEU PHE ARG HIS GLU TYR
SEQRES 11 A 394 THR HIS TYR LEU GLN GLY ARG TYR ALA VAL PRO GLY GLN
SEQRES 12 A 394 TRP GLY ARG THR LYS LEU TYR ASP ASN ASP ARG LEU THR
SEQRES 13 A 394 TRP TYR GLU GLU GLY GLY ALA GLU LEU PHE ALA GLY SER
SEQRES 14 A 394 THR ARG THR SER GLY ILE LEU PRO ARG LYS SER ILE VAL
SEQRES 15 A 394 SER ASN ILE HIS ASN THR THR ARG ASN ASN ARG TYR LYS
SEQRES 16 A 394 LEU SER ASP THR VAL HIS SER LYS TYR GLY ALA SER PHE
SEQRES 17 A 394 GLU PHE TYR ASN TYR ALA CYS MET PHE MET ASP TYR MET
SEQRES 18 A 394 TYR ASN LYS ASP MET GLY ILE LEU ASN LYS LEU ASN ASP
SEQRES 19 A 394 LEU ALA LYS ASN ASN ASP VAL ASP GLY TYR ASP ASN TYR
SEQRES 20 A 394 ILE ARG ASP LEU SER SER ASN HIS ALA LEU ASN ASP LYS
SEQRES 21 A 394 TYR GLN ASP HIS MET GLN GLU ARG ILE ASP ASN TYR GLU
SEQRES 22 A 394 ASN LEU THR VAL PRO PHE VAL ALA ASP ASP TYR LEU VAL
SEQRES 23 A 394 ARG HIS ALA TYR LYS ASN PRO ASN GLU ILE TYR SER GLU
SEQRES 24 A 394 ILE SER GLU VAL ALA LYS LEU LYS ASP ALA LYS SER GLU
SEQRES 25 A 394 VAL LYS LYS SER GLN TYR PHE SER THR PHE THR LEU ARG
SEQRES 26 A 394 GLY SER TYR THR GLY GLY VAL SER LYS GLY LYS LEU GLU
SEQRES 27 A 394 ASP GLN LYS ALA MET ASN LYS PHE ILE ASP ASP SER LEU
SEQRES 28 A 394 LYS LYS LEU ASP THR TYR SER TRP SER GLY TYR LYS THR
SEQRES 29 A 394 LEU THR ALA TYR PHE THR ASN TYR LYS VAL ASP SER SER
SEQRES 30 A 394 ASN LYS VAL THR TYR ASP VAL VAL PHE HIS GLY TYR LEU
SEQRES 31 A 394 PRO ASN GLU GLY
SEQRES 1 B 4 IP8 GLY PRO ALA
HET IP8 B 1 9
HET ZN A 801 1
HET CA A 802 1
HETNAM IP8 ISOPENTENYL PHOSPHATE
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETSYN IP8 3-METHYLBUT-3-EN-1-YL DIHYDROGEN PHOSPHATE
FORMUL 2 IP8 C5 H11 O4 P
FORMUL 3 ZN ZN 2+
FORMUL 4 CA CA 2+
FORMUL 5 HOH *267(H2 O)
HELIX 1 AA1 GLU A 363 GLY A 386 1 24
HELIX 2 AA2 ASN A 395 ILE A 399 5 5
HELIX 3 AA3 SER A 407 SER A 415 1 9
HELIX 4 AA4 GLU A 430 GLU A 432 5 3
HELIX 5 AA5 GLU A 441 SER A 445 5 5
HELIX 6 AA6 THR A 448 ALA A 466 1 19
HELIX 7 AA7 THR A 474 ARG A 481 5 8
HELIX 8 AA8 LEU A 482 ALA A 494 1 13
HELIX 9 AA9 ARG A 505 SER A 510 1 6
HELIX 10 AB1 THR A 516 ARG A 520 5 5
HELIX 11 AB2 LYS A 522 VAL A 527 1 6
HELIX 12 AB3 PHE A 535 ASP A 552 1 18
HELIX 13 AB4 ASP A 552 ASN A 565 1 14
HELIX 14 AB5 ASP A 567 SER A 580 1 14
HELIX 15 AB6 ASN A 581 ASN A 598 1 18
HELIX 16 AB7 TYR A 599 LEU A 602 5 4
HELIX 17 AB8 ALA A 608 VAL A 613 5 6
HELIX 18 AB9 ASN A 619 ALA A 631 1 13
HELIX 19 AC1 GLY A 662 ASP A 682 1 21
HELIX 20 AC2 TRP A 686 LEU A 692 5 7
SHEET 1 AA1 5 LYS A 345 PHE A 349 0
SHEET 2 AA1 5 VAL A 354 ALA A 358 -1 O ILE A 356 N TYR A 347
SHEET 3 AA1 5 LEU A 400 TYR A 405 1 O MET A 402 N ILE A 355
SHEET 4 AA1 5 THR A 434 TYR A 438 1 O PHE A 435 N VAL A 403
SHEET 5 AA1 5 GLY A 426 ILE A 429 -1 N ILE A 429 O THR A 434
SHEET 1 AA2 4 LYS A 634 LYS A 642 0
SHEET 2 AA2 4 SER A 647 VAL A 659 -1 O SER A 654 N LYS A 634
SHEET 3 AA2 4 LYS A 706 LEU A 717 -1 O VAL A 707 N GLY A 657
SHEET 4 AA2 4 THR A 693 VAL A 701 -1 N THR A 697 O ASP A 710
LINK P1 IP8 B 1 N GLY B 2 1555 1555 1.73
LINK OE2 GLU A 430 CA CA A 802 1555 1555 2.34
LINK NE2 HIS A 455 ZN ZN A 801 1555 1555 2.06
LINK NE2 HIS A 459 ZN ZN A 801 1555 1555 2.03
LINK O GLY A 463 CA CA A 802 1555 1555 2.32
LINK O VAL A 467 CA CA A 802 1555 1555 2.31
LINK O GLY A 469 CA CA A 802 1555 1555 2.31
LINK OE1 GLU A 487 ZN ZN A 801 1555 1555 2.00
LINK ZN ZN A 801 O2 IP8 B 1 1555 1555 1.98
LINK CA CA A 802 O HOH A 945 1555 1555 2.41
LINK CA CA A 802 O HOH A 974 1555 1555 2.36
SITE 1 AC1 4 HIS A 455 HIS A 459 GLU A 487 IP8 B 1
SITE 1 AC2 6 GLU A 430 GLY A 463 VAL A 467 GLY A 469
SITE 2 AC2 6 HOH A 945 HOH A 974
CRYST1 79.870 106.780 51.350 90.00 90.00 90.00 P 21 21 2 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 0.012520 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009365 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019474 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
