HEADER CYTOKINE 28-AUG-03 1QVN
TITLE STRUCTURE OF SP4160 BOUND TO IL-2 V69A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: IL-2, T-CELL GROWTH FACTOR, TCGF, ALDESLEUKIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: IL2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS IL-2 SMALL MOLECULE HOT SPOT, CYTOKINE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.D.THANOS,W.L.DELANO,J.A.WELLS
REVDAT 4 27-OCT-21 1QVN 1 REMARK SEQADV LINK
REVDAT 3 09-JAN-13 1QVN 1 JRNL VERSN
REVDAT 2 24-FEB-09 1QVN 1 VERSN
REVDAT 1 05-APR-05 1QVN 0
JRNL AUTH C.D.THANOS,W.L.DELANO,J.A.WELLS
JRNL TITL HOT-SPOT MIMICRY OF A CYTOKINE RECEPTOR BY A SMALL MOLECULE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 103 15422 2006
JRNL REFN ISSN 0027-8424
JRNL PMID 17032757
JRNL DOI 10.1073/PNAS.0607058103
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 14582
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) : 0.261
REMARK 3 R VALUE (WORKING SET) : 0.258
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 771
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1036
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE SET COUNT : 54
REMARK 3 BIN FREE R VALUE : 0.4490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3916
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 192
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.24000
REMARK 3 B22 (A**2) : 3.41000
REMARK 3 B33 (A**2) : -0.17000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.453
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.383
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.871
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.889
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.860
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4130 ; 1.888 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5569 ;14.789 ; 2.024
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 480 ; 3.436 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 670 ; 7.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2948 ; 0.069 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 4 ; 0.471 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2264 ; 0.658 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 67 ; 0.217 ; 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): 78 ; 0.165 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.106 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2448 ; 1.296 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3967 ; 2.383 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1682 ; 4.506 ; 2.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1602 ; 4.891 ; 5.000
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 : 12
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 4 A 132
REMARK 3 ORIGIN FOR THE GROUP (A): 33.1322 15.4072 85.9276
REMARK 3 T TENSOR
REMARK 3 T11: 0.5165 T22: 0.3919
REMARK 3 T33: 0.4445 T12: -0.0394
REMARK 3 T13: -0.0155 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 7.1697 L22: 0.8132
REMARK 3 L33: 1.9866 L12: 0.3494
REMARK 3 L13: 1.4582 L23: 0.3190
REMARK 3 S TENSOR
REMARK 3 S11: 0.0595 S12: -0.0030 S13: -0.1514
REMARK 3 S21: -0.0633 S22: -0.0097 S23: 0.0421
REMARK 3 S31: 0.2319 S32: -0.1754 S33: -0.0499
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 : B 4 B 132
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7656 23.1715 9.2933
REMARK 3 T TENSOR
REMARK 3 T11: 0.4356 T22: 0.4335
REMARK 3 T33: 0.4692 T12: -0.0158
REMARK 3 T13: 0.0091 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 2.7124 L22: 1.3139
REMARK 3 L33: 1.0533 L12: -1.2627
REMARK 3 L13: -0.7400 L23: -0.0371
REMARK 3 S TENSOR
REMARK 3 S11: 0.1474 S12: -0.0793 S13: 0.2831
REMARK 3 S21: -0.0036 S22: 0.0366 S23: -0.0002
REMARK 3 S31: -0.1948 S32: 0.1255 S33: -0.1840
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 : C 4 C 132
REMARK 3 ORIGIN FOR THE GROUP (A): 0.2130 25.5488 69.4215
REMARK 3 T TENSOR
REMARK 3 T11: 0.4486 T22: 0.4428
REMARK 3 T33: 0.3834 T12: -0.0193
REMARK 3 T13: -0.0046 T23: 0.0113
REMARK 3 L TENSOR
REMARK 3 L11: 3.8009 L22: 2.6124
REMARK 3 L33: 1.0658 L12: -1.6890
REMARK 3 L13: -0.1349 L23: 0.2990
REMARK 3 S TENSOR
REMARK 3 S11: -0.0333 S12: -0.0146 S13: 0.1962
REMARK 3 S21: -0.1021 S22: -0.0095 S23: -0.0538
REMARK 3 S31: -0.1197 S32: -0.1059 S33: 0.0428
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 : D 4 D 132
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0589 8.8739 22.1264
REMARK 3 T TENSOR
REMARK 3 T11: 0.4661 T22: 0.4312
REMARK 3 T33: 0.4349 T12: -0.0087
REMARK 3 T13: 0.0219 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 2.5673 L22: 1.4162
REMARK 3 L33: 1.7450 L12: -1.5677
REMARK 3 L13: 0.5633 L23: -0.7013
REMARK 3 S TENSOR
REMARK 3 S11: 0.0152 S12: 0.0664 S13: -0.1214
REMARK 3 S21: 0.0046 S22: -0.0425 S23: 0.1060
REMARK 3 S31: 0.1041 S32: 0.2166 S33: 0.0272
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 201 A 201
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4280 16.9814 80.4671
REMARK 3 T TENSOR
REMARK 3 T11: 0.7471 T22: 0.7563
REMARK 3 T33: 0.8829 T12: -0.1136
REMARK 3 T13: -0.0908 T23: -0.0527
REMARK 3 L TENSOR
REMARK 3 L11: 7.6531 L22: -4.0229
REMARK 3 L33: -11.0453 L12: -16.0323
REMARK 3 L13: -1.5130 L23: 26.4964
REMARK 3 S TENSOR
REMARK 3 S11: 0.1081 S12: -0.3583 S13: 0.8265
REMARK 3 S21: -0.5663 S22: -1.3990 S23: -0.6514
REMARK 3 S31: -2.9060 S32: 1.0207 S33: 1.2908
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 : B 301 B 301
REMARK 3 ORIGIN FOR THE GROUP (A): 51.2878 13.6878 0.2049
REMARK 3 T TENSOR
REMARK 3 T11: 0.4027 T22: 0.4411
REMARK 3 T33: 0.4412 T12: -0.0229
REMARK 3 T13: -0.0259 T23: -0.0385
REMARK 3 L TENSOR
REMARK 3 L11: 19.0518 L22: 54.2059
REMARK 3 L33: 11.4864 L12: 0.5352
REMARK 3 L13: 3.7682 L23: 12.9499
REMARK 3 S TENSOR
REMARK 3 S11: 0.0820 S12: -0.2239 S13: -1.1010
REMARK 3 S21: -1.1334 S22: 0.0509 S23: -3.7147
REMARK 3 S31: 0.5078 S32: 0.3231 S33: -0.1329
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 : C 401 C 401
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4841 13.6985 63.5567
REMARK 3 T TENSOR
REMARK 3 T11: 0.4772 T22: 0.5577
REMARK 3 T33: 0.3953 T12: 0.0711
REMARK 3 T13: -0.0253 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 11.0615 L22: -14.8383
REMARK 3 L33: 3.9421 L12: 2.0928
REMARK 3 L13: -3.7663 L23: 22.5272
REMARK 3 S TENSOR
REMARK 3 S11: -0.0497 S12: 0.2561 S13: -0.8059
REMARK 3 S21: -0.1313 S22: -0.3984 S23: -1.0032
REMARK 3 S31: 1.4414 S32: 1.4661 S33: 0.4481
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 501 D 501
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0389 11.9282 17.7677
REMARK 3 T TENSOR
REMARK 3 T11: 0.5739 T22: 0.8223
REMARK 3 T33: 0.6038 T12: -0.1011
REMARK 3 T13: -0.0722 T23: -0.1401
REMARK 3 L TENSOR
REMARK 3 L11: 5.4964 L22: -27.0564
REMARK 3 L33: 3.9528 L12: -4.0689
REMARK 3 L13: -6.6832 L23: 25.2624
REMARK 3 S TENSOR
REMARK 3 S11: 0.0547 S12: -0.2341 S13: -0.5205
REMARK 3 S21: -1.2186 S22: -0.1044 S23: 0.8647
REMARK 3 S31: -0.6448 S32: -1.2376 S33: 0.0497
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 : B 601 B 601
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5745 14.3648 11.6986
REMARK 3 T TENSOR
REMARK 3 T11: 1.0176 T22: 0.5493
REMARK 3 T33: 1.0641 T12: 0.1192
REMARK 3 T13: -0.0545 T23: 0.5139
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 701 A 701
REMARK 3 ORIGIN FOR THE GROUP (A): 41.7107 17.8687 75.4306
REMARK 3 T TENSOR
REMARK 3 T11: 1.2416 T22: 0.4799
REMARK 3 T33: 0.6694 T12: 0.1635
REMARK 3 T13: -0.5673 T23: 0.0660
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 : B 801 B 801
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0338 17.3557 -5.8098
REMARK 3 T TENSOR
REMARK 3 T11: 0.7117 T22: 0.3006
REMARK 3 T33: 0.6014 T12: 0.0454
REMARK 3 T13: 0.3453 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
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 : C 901 C 901
REMARK 3 ORIGIN FOR THE GROUP (A): 8.6901 16.0237 56.5732
REMARK 3 T TENSOR
REMARK 3 T11: 0.5016 T22: 0.4580
REMARK 3 T33: 0.7412 T12: 0.1079
REMARK 3 T13: 0.1792 T23: 0.1754
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QVN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-03.
REMARK 100 THE DEPOSITION ID IS D_1000020123.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JAN-03
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.08
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14582
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M ZINC ACETATE, 0.075 M MAGNESIUM
REMARK 280 CHLORIDE, 18% (W/V) POLYETHYLENE GLYCOL 10K, 0.1M SODIUM
REMARK 280 CACODYLATE, PH 5.9. , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 26.75700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.07050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.56700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.07050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.75700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.56700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -90.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -186.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 -1.000000 0.000000 0.000000 80.27100
REMARK 350 BIOMT2 1 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 -61.07050
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 26.75700
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 -61.07050
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -93.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 53.51400
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 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 ALA A 1
REMARK 465 PRO A 2
REMARK 465 THR A 3
REMARK 465 SER A 75
REMARK 465 LYS A 76
REMARK 465 ASN A 77
REMARK 465 PHE A 78
REMARK 465 HIS A 79
REMARK 465 LEU A 80
REMARK 465 ALA B 1
REMARK 465 PRO B 2
REMARK 465 THR B 3
REMARK 465 SER B 75
REMARK 465 LYS B 76
REMARK 465 ASN B 77
REMARK 465 PHE B 78
REMARK 465 HIS B 79
REMARK 465 LEU B 80
REMARK 465 SER B 99
REMARK 465 ALA C 1
REMARK 465 PRO C 2
REMARK 465 THR C 3
REMARK 465 SER C 75
REMARK 465 LYS C 76
REMARK 465 ASN C 77
REMARK 465 PHE C 78
REMARK 465 HIS C 79
REMARK 465 LEU C 80
REMARK 465 SER C 99
REMARK 465 ALA D 1
REMARK 465 PRO D 2
REMARK 465 THR D 3
REMARK 465 SER D 75
REMARK 465 LYS D 76
REMARK 465 ASN D 77
REMARK 465 PHE D 78
REMARK 465 HIS D 79
REMARK 465 LEU D 80
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 GLN A 74 CG CD OE1 NE2
REMARK 470 ARG A 81 CG CD NE CZ NH1 NH2
REMARK 470 SER B 5 OG
REMARK 470 ASN B 30 CG OD1 ND2
REMARK 470 LYS B 48 CG CD CE NZ
REMARK 470 GLN B 74 CG CD OE1 NE2
REMARK 470 ARG B 81 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 100 CG CD OE1 OE2
REMARK 470 SER C 5 OG
REMARK 470 ASN C 30 CG OD1 ND2
REMARK 470 LYS C 48 CG CD CE NZ
REMARK 470 GLN C 74 CG CD OE1 NE2
REMARK 470 ARG C 81 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 100 CG CD OE1 OE2
REMARK 470 SER D 5 OG
REMARK 470 ASN D 30 CG OD1 ND2
REMARK 470 LYS D 48 CG CD CE NZ
REMARK 470 GLN D 74 CG CD OE1 NE2
REMARK 470 ARG D 81 CG CD NE CZ NH1 NH2
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 SER A 99 -158.27 51.55
REMARK 500 ALA C 73 74.73 -113.25
REMARK 500 THR C 101 -75.82 -120.15
REMARK 500 GLU D 100 -26.04 72.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 16 NE2
REMARK 620 2 HIS C 16 NE2 103.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 68 OE2
REMARK 620 2 GLU B 95 OE2 92.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU C 68 OE1
REMARK 620 2 GLU C 95 OE2 106.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FRI A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FRI B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FRI C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FRI D 501
DBREF 1QVN A 1 132 UNP P60568 IL2_HUMAN 21 152
DBREF 1QVN B 1 132 UNP P60568 IL2_HUMAN 21 152
DBREF 1QVN C 1 132 UNP P60568 IL2_HUMAN 21 152
DBREF 1QVN D 1 132 UNP P60568 IL2_HUMAN 21 152
SEQADV 1QVN ALA A 69 UNP P60568 VAL 89 ENGINEERED MUTATION
SEQADV 1QVN ALA B 69 UNP P60568 VAL 89 ENGINEERED MUTATION
SEQADV 1QVN ALA C 69 UNP P60568 VAL 89 ENGINEERED MUTATION
SEQADV 1QVN ALA D 69 UNP P60568 VAL 89 ENGINEERED MUTATION
SEQRES 1 A 132 ALA PRO THR SER SER SER THR LYS LYS THR GLN LEU GLN
SEQRES 2 A 132 LEU GLU HIS LEU LEU LEU ASP LEU GLN MET ILE LEU ASN
SEQRES 3 A 132 GLY ILE ASN ASN TYR LYS ASN PRO LYS LEU THR ARG MET
SEQRES 4 A 132 LEU THR PHE LYS PHE TYR MET PRO LYS LYS ALA THR GLU
SEQRES 5 A 132 LEU LYS HIS LEU GLN CYS LEU GLU GLU GLU LEU LYS PRO
SEQRES 6 A 132 LEU GLU GLU ALA LEU ASN LEU ALA GLN SER LYS ASN PHE
SEQRES 7 A 132 HIS LEU ARG PRO ARG ASP LEU ILE SER ASN ILE ASN VAL
SEQRES 8 A 132 ILE VAL LEU GLU LEU LYS GLY SER GLU THR THR PHE MET
SEQRES 9 A 132 CYS GLU TYR ALA ASP GLU THR ALA THR ILE VAL GLU PHE
SEQRES 10 A 132 LEU ASN ARG TRP ILE THR PHE CYS GLN SER ILE ILE SER
SEQRES 11 A 132 THR LEU
SEQRES 1 B 132 ALA PRO THR SER SER SER THR LYS LYS THR GLN LEU GLN
SEQRES 2 B 132 LEU GLU HIS LEU LEU LEU ASP LEU GLN MET ILE LEU ASN
SEQRES 3 B 132 GLY ILE ASN ASN TYR LYS ASN PRO LYS LEU THR ARG MET
SEQRES 4 B 132 LEU THR PHE LYS PHE TYR MET PRO LYS LYS ALA THR GLU
SEQRES 5 B 132 LEU LYS HIS LEU GLN CYS LEU GLU GLU GLU LEU LYS PRO
SEQRES 6 B 132 LEU GLU GLU ALA LEU ASN LEU ALA GLN SER LYS ASN PHE
SEQRES 7 B 132 HIS LEU ARG PRO ARG ASP LEU ILE SER ASN ILE ASN VAL
SEQRES 8 B 132 ILE VAL LEU GLU LEU LYS GLY SER GLU THR THR PHE MET
SEQRES 9 B 132 CYS GLU TYR ALA ASP GLU THR ALA THR ILE VAL GLU PHE
SEQRES 10 B 132 LEU ASN ARG TRP ILE THR PHE CYS GLN SER ILE ILE SER
SEQRES 11 B 132 THR LEU
SEQRES 1 C 132 ALA PRO THR SER SER SER THR LYS LYS THR GLN LEU GLN
SEQRES 2 C 132 LEU GLU HIS LEU LEU LEU ASP LEU GLN MET ILE LEU ASN
SEQRES 3 C 132 GLY ILE ASN ASN TYR LYS ASN PRO LYS LEU THR ARG MET
SEQRES 4 C 132 LEU THR PHE LYS PHE TYR MET PRO LYS LYS ALA THR GLU
SEQRES 5 C 132 LEU LYS HIS LEU GLN CYS LEU GLU GLU GLU LEU LYS PRO
SEQRES 6 C 132 LEU GLU GLU ALA LEU ASN LEU ALA GLN SER LYS ASN PHE
SEQRES 7 C 132 HIS LEU ARG PRO ARG ASP LEU ILE SER ASN ILE ASN VAL
SEQRES 8 C 132 ILE VAL LEU GLU LEU LYS GLY SER GLU THR THR PHE MET
SEQRES 9 C 132 CYS GLU TYR ALA ASP GLU THR ALA THR ILE VAL GLU PHE
SEQRES 10 C 132 LEU ASN ARG TRP ILE THR PHE CYS GLN SER ILE ILE SER
SEQRES 11 C 132 THR LEU
SEQRES 1 D 132 ALA PRO THR SER SER SER THR LYS LYS THR GLN LEU GLN
SEQRES 2 D 132 LEU GLU HIS LEU LEU LEU ASP LEU GLN MET ILE LEU ASN
SEQRES 3 D 132 GLY ILE ASN ASN TYR LYS ASN PRO LYS LEU THR ARG MET
SEQRES 4 D 132 LEU THR PHE LYS PHE TYR MET PRO LYS LYS ALA THR GLU
SEQRES 5 D 132 LEU LYS HIS LEU GLN CYS LEU GLU GLU GLU LEU LYS PRO
SEQRES 6 D 132 LEU GLU GLU ALA LEU ASN LEU ALA GLN SER LYS ASN PHE
SEQRES 7 D 132 HIS LEU ARG PRO ARG ASP LEU ILE SER ASN ILE ASN VAL
SEQRES 8 D 132 ILE VAL LEU GLU LEU LYS GLY SER GLU THR THR PHE MET
SEQRES 9 D 132 CYS GLU TYR ALA ASP GLU THR ALA THR ILE VAL GLU PHE
SEQRES 10 D 132 LEU ASN ARG TRP ILE THR PHE CYS GLN SER ILE ILE SER
SEQRES 11 D 132 THR LEU
HET ZN A 701 1
HET FRI A 201 47
HET ZN B 601 1
HET ZN B 801 1
HET FRI B 301 47
HET ZN C 901 1
HET FRI C 401 47
HET FRI D 501 47
HETNAM ZN ZINC ION
HETNAM FRI 2-GUANIDINO-4-METHYL-PENTANOIC ACID [2-(4-{5-[4-(4-
HETNAM 2 FRI ACETYLAMINO-BENZYLOXY)-2,3-DICHLORO-PHENYL]-2-METHYL-
HETNAM 3 FRI 2H-PYRAZOL-3-YL}-PIPERIDIN-1-YL)-2-OXO-ETHYL]-AMIDE
HETSYN FRI SP4160
FORMUL 5 ZN 4(ZN 2+)
FORMUL 6 FRI 4(C33 H42 CL2 N8 O4)
HELIX 1 1 SER A 4 ASN A 30 1 27
HELIX 2 2 LYS A 32 LEU A 40 1 9
HELIX 3 3 GLU A 52 HIS A 55 5 4
HELIX 4 4 LEU A 56 GLU A 61 1 6
HELIX 5 5 GLU A 62 ALA A 73 1 12
HELIX 6 6 ARG A 81 LYS A 97 1 17
HELIX 7 7 THR A 113 SER A 130 1 18
HELIX 8 8 SER B 4 ASN B 30 1 27
HELIX 9 9 LYS B 32 LEU B 40 1 9
HELIX 10 10 GLU B 52 HIS B 55 5 4
HELIX 11 11 LEU B 56 GLU B 62 1 7
HELIX 12 12 GLU B 62 LEU B 72 1 11
HELIX 13 13 ARG B 81 GLY B 98 1 18
HELIX 14 14 THR B 113 THR B 131 1 19
HELIX 15 15 SER C 4 ASN C 29 1 26
HELIX 16 16 LYS C 32 LEU C 40 1 9
HELIX 17 17 GLU C 52 HIS C 55 5 4
HELIX 18 18 LEU C 56 GLU C 61 1 6
HELIX 19 19 GLU C 62 ALA C 73 1 12
HELIX 20 20 ARG C 81 GLY C 98 1 18
HELIX 21 21 THR C 113 LEU C 132 1 20
HELIX 22 22 SER D 4 ASN D 30 1 27
HELIX 23 23 LYS D 32 LEU D 40 1 9
HELIX 24 24 GLU D 52 HIS D 55 5 4
HELIX 25 25 LEU D 56 GLU D 62 1 7
HELIX 26 26 GLU D 62 ALA D 73 1 12
HELIX 27 27 ARG D 81 LYS D 97 1 17
HELIX 28 28 THR D 113 LEU D 132 1 20
SSBOND 1 CYS A 58 CYS A 105 1555 1555 2.04
SSBOND 2 CYS B 58 CYS B 105 1555 1555 2.03
SSBOND 3 CYS C 58 CYS C 105 1555 1555 2.03
SSBOND 4 CYS D 58 CYS D 105 1555 1555 2.03
LINK NE2 HIS A 16 ZN ZN A 701 1555 1555 2.06
LINK ZN ZN A 701 NE2 HIS C 16 1555 1655 2.43
LINK OE2 GLU B 68 ZN ZN B 801 1555 1555 2.25
LINK OE2 GLU B 95 ZN ZN B 801 4555 1555 1.95
LINK ZN ZN B 601 NE2 HIS D 16 1555 1555 2.71
LINK OE1 GLU C 68 ZN ZN C 901 1555 1555 2.36
LINK OE2 GLU C 95 ZN ZN C 901 4556 1555 1.85
SITE 1 AC1 3 HIS B 16 ASP B 20 HIS D 16
SITE 1 AC2 2 HIS A 16 HIS C 16
SITE 1 AC3 2 GLU B 68 GLU B 95
SITE 1 AC4 2 GLU C 68 GLU C 95
SITE 1 AC5 14 PRO A 34 LYS A 35 ARG A 38 MET A 39
SITE 2 AC5 14 THR A 41 PHE A 42 LYS A 43 TYR A 45
SITE 3 AC5 14 GLU A 62 LEU A 72 ALA A 73 ASN C 29
SITE 4 AC5 14 THR C 113 GLU C 116
SITE 1 AC6 17 LYS B 35 ARG B 38 MET B 39 THR B 41
SITE 2 AC6 17 PHE B 42 LYS B 43 PHE B 44 TYR B 45
SITE 3 AC6 17 GLU B 62 PRO B 65 LEU B 72 ALA B 73
SITE 4 AC6 17 ASN B 88 VAL B 91 LEU B 94 GLU B 95
SITE 5 AC6 17 GLU B 100
SITE 1 AC7 13 LYS C 35 ARG C 38 MET C 39 THR C 41
SITE 2 AC7 13 PHE C 42 LYS C 43 TYR C 45 GLU C 62
SITE 3 AC7 13 PRO C 65 LEU C 72 ALA C 73 LEU C 94
SITE 4 AC7 13 LYS D 64
SITE 1 AC8 16 ASN B 29 LEU B 40 THR B 113 VAL B 115
SITE 2 AC8 16 GLU B 116 PRO D 34 LYS D 35 ARG D 38
SITE 3 AC8 16 MET D 39 THR D 41 PHE D 42 LYS D 43
SITE 4 AC8 16 TYR D 45 GLU D 62 PRO D 65 LEU D 72
CRYST1 53.514 85.134 122.141 90.00 90.00 90.00 P 21 21 21 16
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 0.018687 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011746 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008187 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
