HEADER OXIDOREDUCTASE 21-FEB-13 3ZOI
TITLE ISOPENICILLIN N SYNTHASE WITH AC-O-METHYL-D-THREONINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOPENICILLIN N SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.21.3.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EMERICELLA NIDULANS;
SOURCE 3 ORGANISM_TAXID: 162425;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: NM554;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PJB703
KEYWDS OXIDOREDUCTASE, B-LACTAM ANTIBIOTIC, OXYGENASE, PENICILLIN
KEYWDS 2 BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.RUTLEDGE,I.J.CLIFTON,W.GE
REVDAT 4 20-DEC-23 3ZOI 1 REMARK LINK
REVDAT 3 05-JUL-17 3ZOI 1 REMARK
REVDAT 2 22-OCT-14 3ZOI 1 JRNL
REVDAT 1 26-JUN-13 3ZOI 0
SPRSDE 26-JUN-13 3ZOI 2Y86
JRNL AUTH I.J.CLIFTON,W.GE,R.M.ADLINGTON,J.E.BALDWIN,P.J.RUTLEDGE
JRNL TITL THE CRYSTAL STRUCTURE OF AN ISOPENICILLIN N SYNTHASE COMPLEX
JRNL TITL 2 WITH AN ETHEREAL SUBSTRATE ANALOGUE REVEALS WATER IN THE
JRNL TITL 3 OXYGEN BINDING SITE.
JRNL REF FEBS LETT. V. 587 2705 2013
JRNL REFN ISSN 0014-5793
JRNL PMID 23860486
JRNL DOI 10.1016/J.FEBSLET.2013.07.016
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 11.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 28870
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1181
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) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.86
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1960
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.83
REMARK 3 BIN R VALUE (WORKING SET) : 0.3160
REMARK 3 BIN FREE R VALUE SET COUNT : 86
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2640
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 233
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.38000
REMARK 3 B22 (A**2) : 1.88000
REMARK 3 B33 (A**2) : -1.50000
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): 0.124
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.120
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.802
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2802 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2532 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3826 ; 1.818 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5839 ; 0.924 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 341 ; 6.456 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 147 ;34.186 ;24.898
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 433 ;12.862 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ; 7.298 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 403 ; 0.243 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3252 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 676 ; 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): 1329 ; 0.901 ; 1.137
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1328 ; 0.900 ; 1.137
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1663 ; 1.315 ; 1.702
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1473 ; 1.662 ; 1.319
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): 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 : 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 3 A 8
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5730 42.8091 -6.9513
REMARK 3 T TENSOR
REMARK 3 T11: 0.1382 T22: 0.1983
REMARK 3 T33: 0.2303 T12: -0.0438
REMARK 3 T13: -0.0158 T23: -0.0848
REMARK 3 L TENSOR
REMARK 3 L11: 37.1978 L22: 21.8598
REMARK 3 L33: 33.1313 L12: -15.4897
REMARK 3 L13: -33.7788 L23: 13.7411
REMARK 3 S TENSOR
REMARK 3 S11: 0.2603 S12: 0.7728 S13: 0.1850
REMARK 3 S21: -0.2486 S22: -0.5219 S23: 0.8509
REMARK 3 S31: 0.1337 S32: -1.2353 S33: 0.2616
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 9 A 19
REMARK 3 ORIGIN FOR THE GROUP (A): 5.4320 27.8385 -15.6845
REMARK 3 T TENSOR
REMARK 3 T11: 0.0728 T22: 0.0827
REMARK 3 T33: 0.0435 T12: -0.0162
REMARK 3 T13: -0.0076 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 5.1840 L22: 4.7500
REMARK 3 L33: 2.3571 L12: -3.3866
REMARK 3 L13: -1.4077 L23: 0.6252
REMARK 3 S TENSOR
REMARK 3 S11: -0.2147 S12: -0.0978 S13: -0.1384
REMARK 3 S21: -0.0537 S22: 0.1633 S23: 0.0650
REMARK 3 S31: 0.1341 S32: -0.0046 S33: 0.0514
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 20 A 40
REMARK 3 ORIGIN FOR THE GROUP (A): 7.6177 34.2151 -20.8103
REMARK 3 T TENSOR
REMARK 3 T11: 0.0621 T22: 0.0926
REMARK 3 T33: 0.0409 T12: -0.0125
REMARK 3 T13: -0.0103 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 1.8863 L22: 5.0661
REMARK 3 L33: 3.5391 L12: -1.1424
REMARK 3 L13: -1.0402 L23: 2.0944
REMARK 3 S TENSOR
REMARK 3 S11: -0.0538 S12: 0.1183 S13: -0.0599
REMARK 3 S21: -0.0843 S22: -0.0285 S23: 0.0539
REMARK 3 S31: 0.0633 S32: -0.0359 S33: 0.0823
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 41 A 58
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2614 24.0366 -3.2854
REMARK 3 T TENSOR
REMARK 3 T11: 0.0674 T22: 0.0631
REMARK 3 T33: 0.0705 T12: -0.0107
REMARK 3 T13: 0.0014 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 0.2950 L22: 0.9890
REMARK 3 L33: 0.7770 L12: 0.0053
REMARK 3 L13: 0.2053 L23: -0.6790
REMARK 3 S TENSOR
REMARK 3 S11: -0.0125 S12: -0.0252 S13: -0.0175
REMARK 3 S21: -0.0235 S22: 0.0048 S23: 0.0151
REMARK 3 S31: 0.0594 S32: -0.0880 S33: 0.0077
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 59 A 71
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9166 24.3007 18.4498
REMARK 3 T TENSOR
REMARK 3 T11: 0.0635 T22: 0.0557
REMARK 3 T33: 0.0409 T12: 0.0133
REMARK 3 T13: 0.0024 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 2.4174 L22: 2.9091
REMARK 3 L33: 5.5889 L12: 1.7450
REMARK 3 L13: 2.3945 L23: 2.3456
REMARK 3 S TENSOR
REMARK 3 S11: 0.0133 S12: -0.0375 S13: -0.1646
REMARK 3 S21: 0.0302 S22: 0.0126 S23: 0.0293
REMARK 3 S31: 0.1321 S32: -0.2153 S33: -0.0259
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 72 A 81
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3363 34.4870 20.3146
REMARK 3 T TENSOR
REMARK 3 T11: 0.0533 T22: 0.0888
REMARK 3 T33: 0.0448 T12: 0.0055
REMARK 3 T13: 0.0046 T23: -0.0105
REMARK 3 L TENSOR
REMARK 3 L11: 6.8130 L22: 4.8382
REMARK 3 L33: 5.7042 L12: -1.6284
REMARK 3 L13: 1.1257 L23: -0.1865
REMARK 3 S TENSOR
REMARK 3 S11: -0.0149 S12: -0.0582 S13: 0.3367
REMARK 3 S21: 0.0747 S22: 0.0497 S23: -0.3248
REMARK 3 S31: -0.2616 S32: 0.2437 S33: -0.0348
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 82 A 114
REMARK 3 ORIGIN FOR THE GROUP (A): 17.5433 31.7837 12.2601
REMARK 3 T TENSOR
REMARK 3 T11: 0.0589 T22: 0.0585
REMARK 3 T33: 0.0452 T12: 0.0012
REMARK 3 T13: -0.0129 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.0561 L22: 0.4976
REMARK 3 L33: 1.3450 L12: -0.2210
REMARK 3 L13: -0.8962 L23: 0.3557
REMARK 3 S TENSOR
REMARK 3 S11: 0.0036 S12: -0.1416 S13: 0.0692
REMARK 3 S21: 0.0353 S22: 0.0281 S23: -0.0452
REMARK 3 S31: -0.0265 S32: 0.0609 S33: -0.0317
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 115 A 134
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4636 27.5153 9.9859
REMARK 3 T TENSOR
REMARK 3 T11: 0.0857 T22: 0.1009
REMARK 3 T33: 0.0670 T12: 0.0098
REMARK 3 T13: -0.0140 T23: -0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 3.1689 L22: 2.8851
REMARK 3 L33: 1.1870 L12: 2.0037
REMARK 3 L13: -0.7970 L23: -0.6982
REMARK 3 S TENSOR
REMARK 3 S11: 0.0278 S12: -0.1429 S13: -0.0030
REMARK 3 S21: 0.1573 S22: -0.0344 S23: -0.1042
REMARK 3 S31: -0.0417 S32: 0.0172 S33: 0.0067
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 135 A 165
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0663 25.3096 -4.2577
REMARK 3 T TENSOR
REMARK 3 T11: 0.0538 T22: 0.0513
REMARK 3 T33: 0.0655 T12: 0.0001
REMARK 3 T13: -0.0021 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 0.4158 L22: 1.3034
REMARK 3 L33: 2.5718 L12: 0.0439
REMARK 3 L13: -0.0374 L23: -1.3336
REMARK 3 S TENSOR
REMARK 3 S11: 0.0092 S12: -0.0063 S13: -0.0175
REMARK 3 S21: -0.0030 S22: 0.0132 S23: 0.0304
REMARK 3 S31: 0.0729 S32: 0.0414 S33: -0.0223
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 166 A 176
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5580 33.3386 -15.1919
REMARK 3 T TENSOR
REMARK 3 T11: 0.0325 T22: 0.1381
REMARK 3 T33: 0.1423 T12: -0.0079
REMARK 3 T13: 0.0585 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.3967 L22: 0.3414
REMARK 3 L33: 10.0801 L12: -0.3187
REMARK 3 L13: 1.8133 L23: -1.8411
REMARK 3 S TENSOR
REMARK 3 S11: -0.0605 S12: 0.1666 S13: -0.0372
REMARK 3 S21: 0.0038 S22: -0.1270 S23: -0.0627
REMARK 3 S31: -0.0848 S32: 0.6195 S33: 0.1875
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 177 A 182
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1403 29.6393 -2.5971
REMARK 3 T TENSOR
REMARK 3 T11: 0.0596 T22: 0.0597
REMARK 3 T33: 0.0535 T12: -0.0033
REMARK 3 T13: 0.0114 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 5.1055 L22: 12.0423
REMARK 3 L33: 5.0694 L12: -5.6386
REMARK 3 L13: -3.1997 L23: 6.1040
REMARK 3 S TENSOR
REMARK 3 S11: 0.0547 S12: 0.0773 S13: 0.2657
REMARK 3 S21: -0.2014 S22: 0.0413 S23: -0.4831
REMARK 3 S31: 0.0955 S32: 0.1132 S33: -0.0960
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 183 A 195
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3699 32.7409 12.8977
REMARK 3 T TENSOR
REMARK 3 T11: 0.0615 T22: 0.0617
REMARK 3 T33: 0.0414 T12: 0.0087
REMARK 3 T13: 0.0041 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 2.3581 L22: 1.1449
REMARK 3 L33: 1.2962 L12: -1.0068
REMARK 3 L13: -1.0748 L23: 0.6159
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: -0.0578 S13: -0.0504
REMARK 3 S21: 0.1331 S22: -0.0263 S23: 0.1379
REMARK 3 S31: -0.0885 S32: -0.1217 S33: 0.0342
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 196 A 208
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6842 47.0959 12.0200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0776 T22: 0.0334
REMARK 3 T33: 0.0991 T12: 0.0172
REMARK 3 T13: 0.0114 T23: -0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 1.8391 L22: 6.3712
REMARK 3 L33: 13.6598 L12: -0.8648
REMARK 3 L13: 3.3354 L23: -7.3153
REMARK 3 S TENSOR
REMARK 3 S11: 0.0569 S12: -0.1325 S13: -0.0225
REMARK 3 S21: 0.3336 S22: 0.0492 S23: -0.1313
REMARK 3 S31: -0.0989 S32: -0.0922 S33: -0.1061
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 209 A 239
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2355 40.8593 -0.3975
REMARK 3 T TENSOR
REMARK 3 T11: 0.0592 T22: 0.0722
REMARK 3 T33: 0.0537 T12: 0.0083
REMARK 3 T13: -0.0125 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 2.0668 L22: 1.3670
REMARK 3 L33: 0.7257 L12: -0.1446
REMARK 3 L13: -0.7413 L23: 0.6247
REMARK 3 S TENSOR
REMARK 3 S11: 0.0841 S12: 0.0304 S13: 0.1438
REMARK 3 S21: -0.0600 S22: -0.0811 S23: 0.1421
REMARK 3 S31: -0.0935 S32: -0.1019 S33: -0.0031
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 240 A 246
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2991 35.5189 -4.2590
REMARK 3 T TENSOR
REMARK 3 T11: 0.0552 T22: 0.1294
REMARK 3 T33: 0.0727 T12: -0.0120
REMARK 3 T13: -0.0077 T23: -0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 3.0177 L22: 20.7276
REMARK 3 L33: 0.5979 L12: -5.6291
REMARK 3 L13: 0.4218 L23: 0.7021
REMARK 3 S TENSOR
REMARK 3 S11: 0.1524 S12: 0.1750 S13: -0.1366
REMARK 3 S21: -0.5938 S22: -0.2379 S23: 0.7087
REMARK 3 S31: 0.0541 S32: -0.1338 S33: 0.0855
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 247 A 266
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7732 41.4031 -10.1629
REMARK 3 T TENSOR
REMARK 3 T11: 0.0656 T22: 0.0645
REMARK 3 T33: 0.0540 T12: 0.0133
REMARK 3 T13: -0.0081 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 1.7986 L22: 1.6346
REMARK 3 L33: 1.0497 L12: 0.9236
REMARK 3 L13: -0.4984 L23: -0.1699
REMARK 3 S TENSOR
REMARK 3 S11: 0.0412 S12: 0.0769 S13: 0.1597
REMARK 3 S21: -0.1131 S22: -0.0099 S23: 0.0344
REMARK 3 S31: -0.1494 S32: -0.0345 S33: -0.0313
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 267 A 293
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5142 37.0787 1.8121
REMARK 3 T TENSOR
REMARK 3 T11: 0.0640 T22: 0.0572
REMARK 3 T33: 0.0624 T12: -0.0036
REMARK 3 T13: -0.0086 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.6283 L22: 0.4412
REMARK 3 L33: 0.6547 L12: -0.2303
REMARK 3 L13: -0.1809 L23: -0.0672
REMARK 3 S TENSOR
REMARK 3 S11: 0.0180 S12: 0.0363 S13: 0.0610
REMARK 3 S21: 0.0027 S22: -0.0245 S23: 0.0078
REMARK 3 S31: -0.0445 S32: -0.0359 S33: 0.0065
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 294 A 305
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6470 48.4223 -20.1181
REMARK 3 T TENSOR
REMARK 3 T11: 0.1501 T22: 0.0598
REMARK 3 T33: 0.0804 T12: 0.0163
REMARK 3 T13: 0.0031 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 4.4512 L22: 2.8548
REMARK 3 L33: 11.8338 L12: 0.9491
REMARK 3 L13: 5.4259 L23: -2.5444
REMARK 3 S TENSOR
REMARK 3 S11: -0.1873 S12: 0.3053 S13: 0.0356
REMARK 3 S21: 0.0046 S22: 0.1031 S23: 0.0165
REMARK 3 S31: -0.3807 S32: 0.3134 S33: 0.0842
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 306 A 319
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8081 46.6058 -5.2589
REMARK 3 T TENSOR
REMARK 3 T11: 0.0915 T22: 0.0401
REMARK 3 T33: 0.0785 T12: -0.0075
REMARK 3 T13: 0.0229 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.9732 L22: 3.1855
REMARK 3 L33: 3.3748 L12: 0.1346
REMARK 3 L13: 1.5375 L23: -1.0445
REMARK 3 S TENSOR
REMARK 3 S11: -0.0127 S12: 0.0932 S13: 0.0766
REMARK 3 S21: -0.0500 S22: -0.1343 S23: -0.2675
REMARK 3 S31: -0.1946 S32: 0.2367 S33: 0.1470
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 320 A 331
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8722 45.4938 8.8055
REMARK 3 T TENSOR
REMARK 3 T11: 0.1166 T22: 0.0327
REMARK 3 T33: 0.0646 T12: -0.0328
REMARK 3 T13: 0.0015 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 2.7184 L22: 3.5527
REMARK 3 L33: 1.4626 L12: 0.5293
REMARK 3 L13: -0.2846 L23: -1.4771
REMARK 3 S TENSOR
REMARK 3 S11: -0.0145 S12: 0.0513 S13: 0.2269
REMARK 3 S21: 0.0277 S22: 0.1125 S23: 0.0240
REMARK 3 S31: -0.3016 S32: 0.0468 S33: -0.0980
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.
REMARK 4
REMARK 4 3ZOI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1290055896.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30904
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.810
REMARK 200 RESOLUTION RANGE LOW (A) : 21.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.81
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.80
REMARK 200 R MERGE FOR SHELL (I) : 0.34000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1BK0
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M LITHIUM SULPHATE, 76MM TRIS/HCL,
REMARK 280 PH 8.5, 2.0MM FERROUS SULPHATE, 2.6MG/ML TRIPEPTIDE, 25MG/ML IPNS
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 23.24000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.25500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.39500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.25500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.24000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.39500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLY A 2
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 ALA A 237 CB
REMARK 470 LYS A 305 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2082 O HOH A 2117 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O1 GOL A 2235 O HOH A 2015 2565 1.35
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 113 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 271 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 279 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 300 NE - CZ - NH2 ANGL. DEV. = -3.2 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 ASP A 38 -111.21 -93.30
REMARK 500 HIS A 82 63.98 -106.15
REMARK 500 LYS A 97 -43.31 -131.48
REMARK 500 ASN A 107 117.75 -39.12
REMARK 500 THR A 123 -9.34 79.61
REMARK 500 ASN A 230 -30.99 -151.38
REMARK 500 ASP A 307 33.59 -96.09
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 FE A1333 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 214 NE2
REMARK 620 2 ASP A 216 OD1 95.9
REMARK 620 3 HIS A 270 NE2 85.6 85.3
REMARK 620 4 M2W A1332 S37 92.5 87.6 172.5
REMARK 620 5 HOH A2173 O 87.0 174.3 89.9 97.2
REMARK 620 6 HOH A2178 O 172.1 87.1 87.4 94.9 89.5
REMARK 620 N 1 2 3 4 5
REMARK 630
REMARK 630 MOLECULE TYPE: NULL
REMARK 630 MOLECULE NAME: DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL-O-METHYL-D-
REMARK 630 THREONINE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 M2W A 1332
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: UN1 CYS XDT
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M2W A 1332
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 1333
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1334
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1335
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2234
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2235
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2236
DBREF 3ZOI A 1 331 UNP P05326 IPNS_EMENI 1 331
SEQRES 1 A 331 MET GLY SER VAL SER LYS ALA ASN VAL PRO LYS ILE ASP
SEQRES 2 A 331 VAL SER PRO LEU PHE GLY ASP ASP GLN ALA ALA LYS MET
SEQRES 3 A 331 ARG VAL ALA GLN GLN ILE ASP ALA ALA SER ARG ASP THR
SEQRES 4 A 331 GLY PHE PHE TYR ALA VAL ASN HIS GLY ILE ASN VAL GLN
SEQRES 5 A 331 ARG LEU SER GLN LYS THR LYS GLU PHE HIS MET SER ILE
SEQRES 6 A 331 THR PRO GLU GLU LYS TRP ASP LEU ALA ILE ARG ALA TYR
SEQRES 7 A 331 ASN LYS GLU HIS GLN ASP GLN VAL ARG ALA GLY TYR TYR
SEQRES 8 A 331 LEU SER ILE PRO GLY LYS LYS ALA VAL GLU SER PHE CYS
SEQRES 9 A 331 TYR LEU ASN PRO ASN PHE THR PRO ASP HIS PRO ARG ILE
SEQRES 10 A 331 GLN ALA LYS THR PRO THR HIS GLU VAL ASN VAL TRP PRO
SEQRES 11 A 331 ASP GLU THR LYS HIS PRO GLY PHE GLN ASP PHE ALA GLU
SEQRES 12 A 331 GLN TYR TYR TRP ASP VAL PHE GLY LEU SER SER ALA LEU
SEQRES 13 A 331 LEU LYS GLY TYR ALA LEU ALA LEU GLY LYS GLU GLU ASN
SEQRES 14 A 331 PHE PHE ALA ARG HIS PHE LYS PRO ASP ASP THR LEU ALA
SEQRES 15 A 331 SER VAL VAL LEU ILE ARG TYR PRO TYR LEU ASP PRO TYR
SEQRES 16 A 331 PRO GLU ALA ALA ILE LYS THR ALA ALA ASP GLY THR LYS
SEQRES 17 A 331 LEU SER PHE GLU TRP HIS GLU ASP VAL SER LEU ILE THR
SEQRES 18 A 331 VAL LEU TYR GLN SER ASN VAL GLN ASN LEU GLN VAL GLU
SEQRES 19 A 331 THR ALA ALA GLY TYR GLN ASP ILE GLU ALA ASP ASP THR
SEQRES 20 A 331 GLY TYR LEU ILE ASN CYS GLY SER TYR MET ALA HIS LEU
SEQRES 21 A 331 THR ASN ASN TYR TYR LYS ALA PRO ILE HIS ARG VAL LYS
SEQRES 22 A 331 TRP VAL ASN ALA GLU ARG GLN SER LEU PRO PHE PHE VAL
SEQRES 23 A 331 ASN LEU GLY TYR ASP SER VAL ILE ASP PRO PHE ASP PRO
SEQRES 24 A 331 ARG GLU PRO ASN GLY LYS SER ASP ARG GLU PRO LEU SER
SEQRES 25 A 331 TYR GLY ASP TYR LEU GLN ASN GLY LEU VAL SER LEU ILE
SEQRES 26 A 331 ASN LYS ASN GLY GLN THR
HET M2W A1332 25
HET FE A1333 1
HET SO4 A1334 5
HET SO4 A1335 5
HET SO4 A2234 5
HET GOL A2235 6
HET SO4 A2236 5
HETNAM M2W DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL-O-METHYL-D-
HETNAM 2 M2W THREONINE
HETNAM FE FE (III) ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 M2W C14 H25 N3 O7 S
FORMUL 3 FE FE 3+
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 7 GOL C3 H8 O3
FORMUL 9 HOH *233(H2 O)
HELIX 1 1 SER A 15 GLY A 19 5 5
HELIX 2 2 ASP A 21 ASP A 38 1 18
HELIX 3 3 ASN A 50 ILE A 65 1 16
HELIX 4 4 THR A 66 LEU A 73 1 8
HELIX 5 5 HIS A 114 ALA A 119 1 6
HELIX 6 6 GLY A 137 LEU A 164 1 28
HELIX 7 7 PHE A 171 PHE A 175 5 5
HELIX 8 8 PRO A 196 ILE A 200 5 5
HELIX 9 9 GLY A 254 THR A 261 1 8
HELIX 10 10 SER A 312 GLY A 329 1 18
SHEET 1 AA 8 LYS A 11 ASP A 13 0
SHEET 2 AA 8 PHE A 41 VAL A 45 1 O TYR A 43 N ILE A 12
SHEET 3 AA 8 TYR A 249 CYS A 253 -1 O TYR A 249 N ALA A 44
SHEET 4 AA 8 ILE A 220 GLN A 225 -1 O THR A 221 N ASN A 252
SHEET 5 AA 8 ARG A 279 VAL A 286 -1 O LEU A 282 N TYR A 224
SHEET 6 AA 8 SER A 183 TYR A 189 -1 O SER A 183 N PHE A 285
SHEET 7 AA 8 GLU A 101 LEU A 106 -1 O GLU A 101 N ARG A 188
SHEET 8 AA 8 GLY A 89 TYR A 91 -1 O GLY A 89 N CYS A 104
SHEET 1 AB 5 LYS A 201 THR A 202 0
SHEET 2 AB 5 LYS A 208 HIS A 214 -1 O LEU A 209 N LYS A 201
SHEET 3 AB 5 HIS A 270 LYS A 273 -1 O HIS A 270 N HIS A 214
SHEET 4 AB 5 LEU A 231 THR A 235 -1 O GLN A 232 N ARG A 271
SHEET 5 AB 5 GLY A 238 ASP A 241 -1 O GLY A 238 N THR A 235
LINK NE2 HIS A 214 FE FE A1333 1555 1555 2.22
LINK OD1 ASP A 216 FE FE A1333 1555 1555 2.12
LINK NE2 HIS A 270 FE FE A1333 1555 1555 2.25
LINK S37 M2W A1332 FE FE A1333 1555 1555 2.38
LINK FE FE A1333 O HOH A2173 1555 1555 2.36
LINK FE FE A1333 O HOH A2178 1555 1555 2.14
CISPEP 1 ASP A 193 PRO A 194 0 -0.83
SITE 1 AC1 22 ARG A 87 TYR A 91 SER A 183 ILE A 187
SITE 2 AC1 22 TYR A 189 PHE A 211 HIS A 214 ASP A 216
SITE 3 AC1 22 LEU A 223 LEU A 231 SER A 281 PRO A 283
SITE 4 AC1 22 PHE A 285 LEU A 324 FE A1333 HOH A2173
SITE 5 AC1 22 HOH A2182 HOH A2210 HOH A2229 HOH A2230
SITE 6 AC1 22 HOH A2231 HOH A2232
SITE 1 AC2 6 HIS A 214 ASP A 216 HIS A 270 M2W A1332
SITE 2 AC2 6 HOH A2173 HOH A2178
SITE 1 AC3 9 ARG A 53 ASP A 140 PHE A 141 GLN A 144
SITE 2 AC3 9 HOH A2127 HOH A2130 HOH A2132 HOH A2135
SITE 3 AC3 9 HOH A2233
SITE 1 AC4 6 ARG A 116 THR A 121 PRO A 122 LYS A 273
SITE 2 AC4 6 HOH A2111 HOH A2212
SITE 1 AC5 4 ASN A 46 HIS A 47 GLY A 48 HOH A2037
SITE 1 AC6 4 ALA A 24 ARG A 27 LYS A 80 HOH A2015
SITE 1 AC7 3 ARG A 188 HOH A2064 HOH A2065
CRYST1 46.480 70.790 100.510 90.00 90.00 90.00 P 21 21 21 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 0.021515 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014126 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009949 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
