HEADER OXIDOREDUCTASE 01-DEC-06 2JB4
TITLE ISOPENICILLIN N SYNTHASE WITH A 2-THIABICYCLOHEPTAN-6-ONE PRODUCT
TITLE 2 ANALOGUE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOPENICILLIN N SYNTHETASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: IPNS, ISOPENICILLIN N SYNTHASE;
COMPND 5 EC: 1.21.3.1;
COMPND 6 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_PLASMID: PJB703
KEYWDS ANTIBIOTIC BIOSYNTHESIS, PENICILLIN BIOSYNTHESIS, IRON, OXYGENASE,
KEYWDS 2 VITAMIN C, METAL-BINDING, OXIDOREDUCTASE, B-LACTAM ANTIBIOTIC
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.STEWART,I.J.CLIFTON,R.M.ADLINGTON,J.E.BALDWIN,P.J.RUTLEDGE
REVDAT 3 13-DEC-23 2JB4 1 LINK
REVDAT 2 24-FEB-09 2JB4 1 VERSN
REVDAT 1 16-OCT-07 2JB4 0
JRNL AUTH A.C.STEWART,I.J.CLIFTON,R.M.ADLINGTON,J.E.BALDWIN,
JRNL AUTH 2 P.J.RUTLEDGE
JRNL TITL A CYCLOBUTANONE ANALOGUE MIMICS PENICILLIN IN BINDING TO
JRNL TITL 2 ISOPENICILLIN N SYNTHASE.
JRNL REF CHEMBIOCHEM V. 8 2003 2007
JRNL REFN ISSN 1439-4227
JRNL PMID 17907118
JRNL DOI 10.1002/CBIC.200700176
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.I.BURZLAFF,P.J.RUTLEDGE,I.J.CLIFTON,C.M.H.HENSGENS,
REMARK 1 AUTH 2 M.PICKFORD,R.M.ADLINGTON,P.L.ROACH,J.E.BALDWIN
REMARK 1 TITL THE REACTION CYCLE OF ISOPENICILLINN SYNTHASE OBSERVED BY
REMARK 1 TITL 2 X-RAY DIFFRACTION
REMARK 1 REF NATURE V. 401 721 1999
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 10537113
REMARK 1 DOI 10.1038/44400
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 76025
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) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4023
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) : 1.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3918
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE SET COUNT : 227
REMARK 3 BIN FREE R VALUE : 0.2650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2637
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 403
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 7.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : 0.45000
REMARK 3 B33 (A**2) : -0.29000
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): 0.045
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.048
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.029
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.366
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2767 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1830 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3765 ; 1.820 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4460 ; 1.758 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 328 ; 6.168 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 142 ;32.266 ;24.648
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 428 ;11.041 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;14.314 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 390 ; 0.132 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3099 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 566 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 516 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1891 ; 0.194 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1381 ; 0.193 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1421 ; 0.090 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 276 ; 0.193 ; 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): 9 ; 0.229 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 64 ; 0.259 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 32 ; 0.172 ; 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): 1743 ; 1.230 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2669 ; 1.670 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1252 ; 2.848 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1093 ; 4.009 ; 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 : 15
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 14
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2800 36.8110 -11.0120
REMARK 3 T TENSOR
REMARK 3 T11: -0.0018 T22: 0.0523
REMARK 3 T33: 0.0117 T12: 0.0177
REMARK 3 T13: -0.0490 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 7.1830 L22: 13.2747
REMARK 3 L33: 5.7866 L12: -8.3218
REMARK 3 L13: -4.8026 L23: 7.4159
REMARK 3 S TENSOR
REMARK 3 S11: -0.0470 S12: 0.0949 S13: -0.0774
REMARK 3 S21: -0.2144 S22: -0.2133 S23: 0.6201
REMARK 3 S31: -0.2591 S32: -0.4712 S33: 0.2602
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 15 A 49
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9500 31.6670 -17.2420
REMARK 3 T TENSOR
REMARK 3 T11: 0.0340 T22: 0.0423
REMARK 3 T33: 0.0104 T12: -0.0103
REMARK 3 T13: -0.0122 T23: 0.0030
REMARK 3 L TENSOR
REMARK 3 L11: 1.1201 L22: 0.9749
REMARK 3 L33: 2.1202 L12: 0.4108
REMARK 3 L13: -0.3978 L23: -0.5965
REMARK 3 S TENSOR
REMARK 3 S11: -0.0874 S12: 0.1448 S13: 0.0017
REMARK 3 S21: -0.1232 S22: 0.0394 S23: -0.0434
REMARK 3 S31: 0.0812 S32: -0.0910 S33: 0.0480
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 50 A 69
REMARK 3 ORIGIN FOR THE GROUP (A): 6.4220 21.4440 11.0510
REMARK 3 T TENSOR
REMARK 3 T11: 0.0185 T22: 0.0159
REMARK 3 T33: -0.0001 T12: -0.0084
REMARK 3 T13: 0.0091 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.6029 L22: 1.1298
REMARK 3 L33: 6.5072 L12: 0.5515
REMARK 3 L13: 1.9554 L23: 2.1105
REMARK 3 S TENSOR
REMARK 3 S11: 0.0633 S12: -0.1218 S13: -0.0586
REMARK 3 S21: 0.1494 S22: 0.0008 S23: -0.0115
REMARK 3 S31: 0.0919 S32: -0.2129 S33: -0.0641
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 70 A 86
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8020 34.1160 19.6680
REMARK 3 T TENSOR
REMARK 3 T11: 0.0089 T22: 0.0577
REMARK 3 T33: -0.0064 T12: 0.0036
REMARK 3 T13: -0.0045 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 2.6965 L22: 2.0727
REMARK 3 L33: 4.0342 L12: 0.1898
REMARK 3 L13: -0.1134 L23: 1.4045
REMARK 3 S TENSOR
REMARK 3 S11: 0.0347 S12: 0.0138 S13: 0.0976
REMARK 3 S21: 0.0104 S22: 0.0819 S23: -0.1115
REMARK 3 S31: -0.1174 S32: 0.3756 S33: -0.1165
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 87 A 119
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8440 31.5580 10.5120
REMARK 3 T TENSOR
REMARK 3 T11: 0.0268 T22: 0.0303
REMARK 3 T33: 0.0267 T12: 0.0044
REMARK 3 T13: -0.0212 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 1.4521 L22: 0.6870
REMARK 3 L33: 0.9416 L12: -0.2723
REMARK 3 L13: -0.3998 L23: 0.2439
REMARK 3 S TENSOR
REMARK 3 S11: -0.0017 S12: -0.1212 S13: 0.0753
REMARK 3 S21: 0.0504 S22: 0.0176 S23: -0.0413
REMARK 3 S31: -0.0240 S32: 0.0231 S33: -0.0159
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 120 A 143
REMARK 3 ORIGIN FOR THE GROUP (A): 19.6460 23.4220 10.3240
REMARK 3 T TENSOR
REMARK 3 T11: 0.0353 T22: 0.0296
REMARK 3 T33: 0.0241 T12: 0.0185
REMARK 3 T13: -0.0055 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.9506 L22: 1.7251
REMARK 3 L33: 1.0004 L12: 1.2521
REMARK 3 L13: -0.3674 L23: 0.0908
REMARK 3 S TENSOR
REMARK 3 S11: 0.0148 S12: -0.1455 S13: 0.0105
REMARK 3 S21: 0.1460 S22: -0.0237 S23: 0.0083
REMARK 3 S31: 0.0975 S32: 0.0583 S33: 0.0089
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 144 A 166
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5690 29.2410 -10.4670
REMARK 3 T TENSOR
REMARK 3 T11: 0.0227 T22: 0.0266
REMARK 3 T33: 0.0142 T12: -0.0062
REMARK 3 T13: -0.0016 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.1454 L22: 1.0462
REMARK 3 L33: 2.6235 L12: -0.1781
REMARK 3 L13: 0.4094 L23: -1.2875
REMARK 3 S TENSOR
REMARK 3 S11: -0.0479 S12: 0.0713 S13: 0.0181
REMARK 3 S21: -0.1093 S22: -0.0028 S23: -0.0573
REMARK 3 S31: 0.0598 S32: 0.0453 S33: 0.0508
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 167 A 179
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7560 31.9630 -12.6060
REMARK 3 T TENSOR
REMARK 3 T11: -0.0014 T22: 0.0427
REMARK 3 T33: -0.0036 T12: -0.0058
REMARK 3 T13: 0.0077 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 0.8149 L22: 2.5236
REMARK 3 L33: 3.9117 L12: -1.1878
REMARK 3 L13: 1.7075 L23: -2.3072
REMARK 3 S TENSOR
REMARK 3 S11: 0.0230 S12: 0.2032 S13: 0.0664
REMARK 3 S21: -0.2220 S22: -0.0847 S23: -0.0875
REMARK 3 S31: 0.1327 S32: 0.3078 S33: 0.0617
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 180 A 192
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4330 31.9540 8.5620
REMARK 3 T TENSOR
REMARK 3 T11: 0.0070 T22: 0.0316
REMARK 3 T33: 0.0193 T12: 0.0045
REMARK 3 T13: -0.0135 T23: -0.0127
REMARK 3 L TENSOR
REMARK 3 L11: 6.0193 L22: 0.5064
REMARK 3 L33: 3.0093 L12: -0.1998
REMARK 3 L13: -4.0325 L23: 0.0662
REMARK 3 S TENSOR
REMARK 3 S11: 0.0649 S12: -0.0351 S13: 0.0402
REMARK 3 S21: 0.0624 S22: -0.0504 S23: 0.0609
REMARK 3 S31: -0.0710 S32: -0.0738 S33: -0.0144
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 193 A 199
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6550 40.1860 19.2380
REMARK 3 T TENSOR
REMARK 3 T11: 0.1415 T22: 0.0341
REMARK 3 T33: -0.0017 T12: 0.0208
REMARK 3 T13: -0.0254 T23: -0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 2.8689 L22: 22.8239
REMARK 3 L33: 1.9474 L12: 0.9591
REMARK 3 L13: 0.5652 L23: -2.2274
REMARK 3 S TENSOR
REMARK 3 S11: -0.0601 S12: -0.1519 S13: 0.1953
REMARK 3 S21: 1.7458 S22: 0.0169 S23: 0.0078
REMARK 3 S31: -0.4690 S32: -0.3741 S33: 0.0432
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 200 A 227
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6050 41.4250 2.7680
REMARK 3 T TENSOR
REMARK 3 T11: 0.0126 T22: 0.0218
REMARK 3 T33: 0.0259 T12: 0.0064
REMARK 3 T13: -0.0110 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.9514 L22: 0.9670
REMARK 3 L33: 0.9790 L12: -0.4242
REMARK 3 L13: -0.7618 L23: 0.5044
REMARK 3 S TENSOR
REMARK 3 S11: 0.0340 S12: -0.0377 S13: 0.0931
REMARK 3 S21: 0.0317 S22: -0.0244 S23: 0.0985
REMARK 3 S31: -0.0735 S32: -0.0615 S33: -0.0096
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 228 A 244
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1610 42.7840 -3.1510
REMARK 3 T TENSOR
REMARK 3 T11: -0.0068 T22: 0.0406
REMARK 3 T33: 0.0311 T12: 0.0370
REMARK 3 T13: -0.0280 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 4.1044 L22: 8.2077
REMARK 3 L33: 2.5087 L12: 2.5899
REMARK 3 L13: -1.1717 L23: -1.3681
REMARK 3 S TENSOR
REMARK 3 S11: 0.0382 S12: 0.1316 S13: 0.2909
REMARK 3 S21: -0.2948 S22: -0.0806 S23: 0.2762
REMARK 3 S31: -0.0652 S32: -0.0704 S33: 0.0424
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 245 A 288
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5020 38.6410 -3.1320
REMARK 3 T TENSOR
REMARK 3 T11: 0.0161 T22: 0.0187
REMARK 3 T33: 0.0244 T12: 0.0033
REMARK 3 T13: -0.0144 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.7178 L22: 0.5139
REMARK 3 L33: 0.6196 L12: 0.0102
REMARK 3 L13: -0.3439 L23: 0.0367
REMARK 3 S TENSOR
REMARK 3 S11: 0.0175 S12: 0.0153 S13: 0.0635
REMARK 3 S21: -0.0577 S22: -0.0226 S23: 0.0325
REMARK 3 S31: -0.0548 S32: -0.0392 S33: 0.0051
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 289 A 304
REMARK 3 ORIGIN FOR THE GROUP (A): 22.5540 45.7270 -15.5190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0689 T22: 0.0163
REMARK 3 T33: 0.0077 T12: 0.0011
REMARK 3 T13: 0.0299 T23: 0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 2.5945 L22: 3.5807
REMARK 3 L33: 10.7494 L12: -2.0625
REMARK 3 L13: 4.1159 L23: -5.7785
REMARK 3 S TENSOR
REMARK 3 S11: -0.0181 S12: 0.2073 S13: 0.0915
REMARK 3 S21: -0.0133 S22: 0.0075 S23: -0.0907
REMARK 3 S31: -0.4857 S32: 0.1552 S33: 0.0106
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 305 A 331
REMARK 3 ORIGIN FOR THE GROUP (A): 19.5960 46.3480 0.2760
REMARK 3 T TENSOR
REMARK 3 T11: 0.0146 T22: -0.0211
REMARK 3 T33: 0.0400 T12: -0.0164
REMARK 3 T13: -0.0051 T23: -0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.9067 L22: 1.2705
REMARK 3 L33: 1.5939 L12: -0.2933
REMARK 3 L13: -0.3950 L23: 0.1684
REMARK 3 S TENSOR
REMARK 3 S11: -0.0039 S12: -0.1443 S13: 0.0595
REMARK 3 S21: 0.1044 S22: -0.0195 S23: -0.0126
REMARK 3 S31: -0.1358 S32: 0.0848 S33: 0.0234
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 : 1.20
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.ANISOTROPIC U FACTORS CALCULATED BY TLSANL FROM REFMAC
REMARK 3 TLS MODEL.
REMARK 4
REMARK 4 2JB4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1290030333.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93400
REMARK 200 MONOCHROMATOR : GE (2 2 0)
REMARK 200 OPTICS : RH COATED TOROIDAL MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80123
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC RIGID-BODY REFINEMENT
REMARK 200 STARTING MODEL: PDB ENTRY 1BK0
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M LITHIUM SULPHATE, 76MM TRIS/HCL,
REMARK 280 PH 8.5, 2.0MM FERROUS SULPHATE, 6.8 MM SUBSTRATE, 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 23.33850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.45300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.63650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.45300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.33850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.63650
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: PQS
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 ASP A 20 CG OD1 OD2
REMARK 470 LYS A 176 CE NZ
REMARK 470 LYS A 305 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 2182 O HOH A 2183 1.96
REMARK 500 O HOH A 2017 O HOH A 2042 1.99
REMARK 500 O HOH A 2100 O HOH A 2108 2.11
REMARK 500 O HOH A 2093 O HOH A 2201 2.16
REMARK 500 OD1 ASP A 131 O HOH A 2191 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 179 CB ASP A 179 CG -0.170
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 ARG A 87 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 VAL A 100 CG1 - CB - CG2 ANGL. DEV. = 13.4 DEGREES
REMARK 500 ASP A 179 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG A 271 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 300 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ASP A 38 -107.80 -100.52
REMARK 500 HIS A 82 61.43 -105.26
REMARK 500 LYS A 97 -43.64 -136.05
REMARK 500 THR A 123 -8.65 80.23
REMARK 500 ASN A 230 -28.86 -154.85
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 94.9
REMARK 620 3 HIS A 270 NE2 92.0 95.3
REMARK 620 4 HOH A2285 O 91.7 166.3 96.4
REMARK 620 5 HOH A2289 O 170.3 88.3 96.9 83.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A14 A1332
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A1333
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1334
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1335
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1336
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BK0 RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ACV-FE COMPLEX)
REMARK 900 RELATED ID: 1BLZ RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ACV-FE-NO
REMARK 900 COMPLEX)
REMARK 900 RELATED ID: 1HB1 RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ANAEROBIC ACOV
REMARK 900 FE COMPLEX)
REMARK 900 RELATED ID: 1HB2 RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (OXYGEN EXPOSED
REMARK 900 PRODUCT FROM ANAEROBIC ACOV FE COMPLEX)
REMARK 900 RELATED ID: 1HB3 RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (OXYGEN EXPOSED
REMARK 900 PRODUCT FROM ANAEROBIC ACOV FE COMPLEX)
REMARK 900 RELATED ID: 1HB4 RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (OXYGEN EXPOSED
REMARK 900 PRODUCT FROM ANAEROBIC ACOV FE COMPLEX)
REMARK 900 RELATED ID: 1IPS RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE
REMARK 900 COMPLEX)
REMARK 900 RELATED ID: 1OBN RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL -AMINOBUTYRATE-FE-
REMARK 900 NO COMPLEX
REMARK 900 RELATED ID: 1OC1 RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL -AMINOBUTYRATE-FE
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1ODM RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ANAEROBIC AC-
REMARK 900 VINYLGLYCINE FE COMPLEX )
REMARK 900 RELATED ID: 1ODN RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (OXYGEN-EXPOSED
REMARK 900 PRODUCT FROM ANAEROBIC AC-VINYLGLYCINE FE COMPLEX)
REMARK 900 RELATED ID: 1QIQ RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ACMC FE COMPLEX)
REMARK 900 RELATED ID: 1QJE RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (IPN - FE
REMARK 900 COMPLEX)
REMARK 900 RELATED ID: 1QJF RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MONOCYCLIC
REMARK 900 SULFOXIDE - FE COMPLEX)
REMARK 900 RELATED ID: 1UZW RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE WITH L-D-(A- AMINOADIPOYL)-L-CYSTEINYL-D-
REMARK 900 ISODEHYDROVALINE
REMARK 900 RELATED ID: 1W03 RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL -GLYCINE-FE COMPLEX
REMARK 900 RELATED ID: 1W04 RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL -GLYCINE-FE-NO
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1W05 RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL -ALANINE-FE COMPLEX
REMARK 900 RELATED ID: 1W06 RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL -ALANINE-FE NO
REMARK 900 COMPLEX
REMARK 900 RELATED ID: 1W3V RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE D-(L-A-AMINOADIPOYL )-(3R)-METHYL-L-
REMARK 900 CYSTEINE D-A- HYDROXYISOVALERYL ESTER COMPLEX (ANAEROBIC)
REMARK 900 RELATED ID: 1W3X RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE D-(L-A-AMINOADIPOYL )-(3R)-METHYL-L-
REMARK 900 CYSTEINE D-A- HYDROXYISOVALERYL ESTER COMPLEX (OXYGEN EXPOSED 5
REMARK 900 MINUTES 20 BAR)
REMARK 900 RELATED ID: 2BJS RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE C-TERMINAL TRUNCATION MUTANT
REMARK 900 RELATED ID: 2BU9 RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE COMPLEXED WITH L- AMINOADIPOYL-L-CYSTEINYL-
REMARK 900 L-HEXAFLUOROVALINE
REMARK 900 RELATED ID: 2IVI RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ANAEROBIC AC-
REMARK 900 METHYL-CYCLOPROPYLGLYCINE FE COMPLEX)
REMARK 900 RELATED ID: 2IVJ RELATED DB: PDB
REMARK 900 ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ANAEROBIC AC-
REMARK 900 CYCLOPROPYLGLYCINE FE COMPLEX)
DBREF 2JB4 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 A14 A1332 24
HET FE A1333 1
HET SO4 A1334 5
HET GOL A1335 6
HET SO4 A1336 5
HETNAM A14 (1S,4S,5S,7R)-7-{[(5S)-5-AMINO-5-
HETNAM 2 A14 CARBOXYPENTANOYL]AMINO}-3,3-DIMETHYL-6-OXO-2-
HETNAM 3 A14 THIABICYCLO[3.2.0]HEPTANE-4-CARBOXYLIC ACID
HETNAM FE FE (III) ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 A14 C15 H22 N2 O6 S
FORMUL 3 FE FE 3+
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 5 GOL C3 H8 O3
FORMUL 7 HOH *403(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 ALA A 74 1 9
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 TYR A 105 -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 2.11
LINK OD1 ASP A 216 FE FE A1333 1555 1555 2.11
LINK NE2 HIS A 270 FE FE A1333 1555 1555 2.16
LINK FE FE A1333 O HOH A2285 1555 1555 2.28
LINK FE FE A1333 O HOH A2289 1555 1555 2.09
CISPEP 1 ASP A 193 PRO A 194 0 3.51
SITE 1 AC1 16 ARG A 87 TYR A 91 SER A 183 ILE A 187
SITE 2 AC1 16 TYR A 189 PHE A 211 VAL A 272 SER A 281
SITE 3 AC1 16 FE A1333 HOH A2285 HOH A2349 HOH A2388
SITE 4 AC1 16 HOH A2389 HOH A2390 HOH A2391 HOH A2393
SITE 1 AC2 6 HIS A 214 ASP A 216 HIS A 270 A14 A1332
SITE 2 AC2 6 HOH A2285 HOH A2289
SITE 1 AC3 3 ARG A 27 LYS A 80 HOH A2394
SITE 1 AC4 8 ALA A 204 ASP A 205 GLY A 206 GLU A 215
SITE 2 AC4 8 ALA A 258 ARG A 308 HOH A2395 HOH A2396
SITE 1 AC5 11 ARG A 53 ASP A 140 PHE A 141 HOH A2203
SITE 2 AC5 11 HOH A2397 HOH A2398 HOH A2399 HOH A2400
SITE 3 AC5 11 HOH A2401 HOH A2402 HOH A2403
CRYST1 46.677 71.273 100.906 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 0.021424 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014031 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009910 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
