HEADER OXIDOREDUCTASE 31-AUG-16 5T5V
TITLE LIPOXYGENASE-1 (SOYBEAN) AT 293K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEED LINOLEATE 13S-LIPOXYGENASE-1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LIPOXYGENASE-1,L-1;
COMPND 5 EC: 1.13.11.12;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GLYCINE MAX;
SOURCE 3 ORGANISM_COMMON: SOYBEAN;
SOURCE 4 ORGANISM_TAXID: 3847;
SOURCE 5 GENE: LOX1.1, LOX1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS LIPOXYGENASE, HYDROGEN TUNNELING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.M.POSS,J.S.FRASER
REVDAT 5 04-OCT-23 5T5V 1 LINK
REVDAT 4 25-DEC-19 5T5V 1 REMARK
REVDAT 3 24-JAN-18 5T5V 1 JRNL
REVDAT 2 27-SEP-17 5T5V 1 REMARK
REVDAT 1 06-SEP-17 5T5V 0
JRNL AUTH A.R.OFFENBACHER,S.HU,E.M.POSS,C.A.M.CARR,A.D.SCOURAS,
JRNL AUTH 2 D.M.PRIGOZHIN,A.T.IAVARONE,A.PALLA,T.ALBER,J.S.FRASER,
JRNL AUTH 3 J.P.KLINMAN
JRNL TITL HYDROGEN-DEUTERIUM EXCHANGE OF LIPOXYGENASE UNCOVERS A
JRNL TITL 2 RELATIONSHIP BETWEEN DISTAL, SOLVENT EXPOSED PROTEIN MOTIONS
JRNL TITL 3 AND THE THERMAL ACTIVATION BARRIER FOR CATALYTIC
JRNL TITL 4 PROTON-COUPLED ELECTRON TUNNELING.
JRNL REF ACS CENT SCI V. 3 570 2017
JRNL REFN ESSN 2374-7943
JRNL PMID 28691068
JRNL DOI 10.1021/ACSCENTSCI.7B00142
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.10PRE_2104
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 154489
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.135
REMARK 3 R VALUE (WORKING SET) : 0.134
REMARK 3 FREE R VALUE : 0.171
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.290
REMARK 3 FREE R VALUE TEST SET COUNT : 1994
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 91.4926 - 4.3381 0.99 11090 147 0.1095 0.1249
REMARK 3 2 4.3381 - 3.4432 1.00 11011 137 0.0949 0.1287
REMARK 3 3 3.4432 - 3.0080 1.00 11012 136 0.1213 0.1882
REMARK 3 4 3.0080 - 2.7329 1.00 10932 145 0.1285 0.1495
REMARK 3 5 2.7329 - 2.5370 1.00 10946 145 0.1264 0.1868
REMARK 3 6 2.5370 - 2.3874 0.99 10895 143 0.1238 0.1679
REMARK 3 7 2.3874 - 2.2679 0.99 10893 150 0.1240 0.1763
REMARK 3 8 2.2679 - 2.1691 0.99 10864 145 0.1371 0.1439
REMARK 3 9 2.1691 - 2.0856 0.99 10885 134 0.1539 0.2078
REMARK 3 10 2.0856 - 2.0136 0.99 10797 147 0.1682 0.2089
REMARK 3 11 2.0136 - 1.9507 0.99 10847 136 0.1817 0.2019
REMARK 3 12 1.9507 - 1.8949 0.99 10800 159 0.2088 0.2652
REMARK 3 13 1.8949 - 1.8450 0.99 10825 144 0.2397 0.2649
REMARK 3 14 1.8450 - 1.8000 0.98 10698 126 0.2774 0.3036
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 21600
REMARK 3 ANGLE : 1.030 30098
REMARK 3 CHIRALITY : 0.058 3432
REMARK 3 PLANARITY : 0.008 3946
REMARK 3 DIHEDRAL : 10.617 13905
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 6 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.3208 -44.0896 32.8865
REMARK 3 T TENSOR
REMARK 3 T11: 0.1301 T22: 0.1946
REMARK 3 T33: 0.2593 T12: -0.0033
REMARK 3 T13: -0.0026 T23: -0.0499
REMARK 3 L TENSOR
REMARK 3 L11: 0.1732 L22: 0.0697
REMARK 3 L33: 0.0662 L12: 0.0590
REMARK 3 L13: 0.0732 L23: -0.0206
REMARK 3 S TENSOR
REMARK 3 S11: 0.0394 S12: 0.1646 S13: -0.0625
REMARK 3 S21: 0.0112 S22: -0.0649 S23: 0.1297
REMARK 3 S31: 0.0519 S32: -0.1142 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 67 THROUGH 190 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0658 -41.7022 38.4676
REMARK 3 T TENSOR
REMARK 3 T11: 0.1031 T22: 0.1158
REMARK 3 T33: 0.1844 T12: 0.0015
REMARK 3 T13: 0.0046 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.5796 L22: 0.1010
REMARK 3 L33: 0.1052 L12: -0.0830
REMARK 3 L13: 0.0126 L23: -0.0235
REMARK 3 S TENSOR
REMARK 3 S11: 0.0144 S12: 0.0248 S13: 0.0120
REMARK 3 S21: 0.0192 S22: -0.0360 S23: 0.0888
REMARK 3 S31: 0.0111 S32: -0.0288 S33: -0.0003
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 191 THROUGH 496 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.3035 -48.0135 38.9033
REMARK 3 T TENSOR
REMARK 3 T11: 0.1061 T22: 0.1044
REMARK 3 T33: 0.0712 T12: -0.0146
REMARK 3 T13: 0.0032 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.7320 L22: 0.3058
REMARK 3 L33: 0.1271 L12: 0.2143
REMARK 3 L13: -0.0662 L23: -0.0153
REMARK 3 S TENSOR
REMARK 3 S11: 0.0011 S12: -0.0020 S13: -0.1111
REMARK 3 S21: -0.0167 S22: 0.0045 S23: -0.0441
REMARK 3 S31: 0.0040 S32: 0.0516 S33: 0.0363
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 497 THROUGH 839 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9395 -36.1467 38.3445
REMARK 3 T TENSOR
REMARK 3 T11: 0.0972 T22: 0.0760
REMARK 3 T33: 0.0807 T12: -0.0158
REMARK 3 T13: -0.0007 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.9530 L22: 0.3464
REMARK 3 L33: 0.1599 L12: 0.0974
REMARK 3 L13: -0.0779 L23: 0.0746
REMARK 3 S TENSOR
REMARK 3 S11: -0.0053 S12: 0.0414 S13: 0.1455
REMARK 3 S21: -0.0373 S22: 0.0090 S23: 0.0394
REMARK 3 S31: -0.0252 S32: 0.0362 S33: -0.0088
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 93 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.4720 -41.9154 80.6115
REMARK 3 T TENSOR
REMARK 3 T11: 0.1362 T22: 0.1913
REMARK 3 T33: 0.2142 T12: 0.0198
REMARK 3 T13: -0.0100 T23: -0.0247
REMARK 3 L TENSOR
REMARK 3 L11: 0.2275 L22: 0.1385
REMARK 3 L33: 0.0946 L12: 0.0775
REMARK 3 L13: 0.0793 L23: -0.0692
REMARK 3 S TENSOR
REMARK 3 S11: 0.0350 S12: 0.1674 S13: -0.0392
REMARK 3 S21: -0.0389 S22: -0.0562 S23: 0.1254
REMARK 3 S31: 0.0772 S32: -0.0570 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 94 THROUGH 221 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8796 -45.1498 93.7743
REMARK 3 T TENSOR
REMARK 3 T11: 0.1294 T22: 0.1355
REMARK 3 T33: 0.1405 T12: 0.0051
REMARK 3 T13: 0.0067 T23: 0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 0.6125 L22: 0.0894
REMARK 3 L33: 0.0816 L12: 0.2166
REMARK 3 L13: 0.1167 L23: 0.0754
REMARK 3 S TENSOR
REMARK 3 S11: 0.0496 S12: -0.1360 S13: -0.1020
REMARK 3 S21: 0.0379 S22: -0.0271 S23: 0.1226
REMARK 3 S31: 0.0166 S32: -0.0549 S33: -0.0026
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 222 THROUGH 409 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1557 -48.8108 85.1821
REMARK 3 T TENSOR
REMARK 3 T11: 0.1362 T22: 0.1089
REMARK 3 T33: 0.0749 T12: -0.0044
REMARK 3 T13: -0.0071 T23: 0.0006
REMARK 3 L TENSOR
REMARK 3 L11: 0.7766 L22: 0.1777
REMARK 3 L33: 0.0695 L12: -0.1097
REMARK 3 L13: -0.0062 L23: -0.0179
REMARK 3 S TENSOR
REMARK 3 S11: 0.0476 S12: -0.0083 S13: -0.1002
REMARK 3 S21: -0.0225 S22: -0.0353 S23: -0.0036
REMARK 3 S31: 0.0018 S32: 0.0259 S33: 0.0042
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 410 THROUGH 839 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1412 -37.7225 90.4819
REMARK 3 T TENSOR
REMARK 3 T11: 0.1153 T22: 0.0818
REMARK 3 T33: 0.0595 T12: 0.0044
REMARK 3 T13: 0.0005 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 1.0476 L22: 0.2752
REMARK 3 L33: 0.1775 L12: -0.0934
REMARK 3 L13: -0.0290 L23: 0.0772
REMARK 3 S TENSOR
REMARK 3 S11: 0.0451 S12: -0.0484 S13: 0.0785
REMARK 3 S21: -0.0163 S22: -0.0293 S23: -0.0053
REMARK 3 S31: -0.0263 S32: 0.0133 S33: 0.0107
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5T5V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1000223768.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 300
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8266
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 154694
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 92.754
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.88600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3PZW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-3350, SODIUM ACETATE, PH 5.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 46.37700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 PHE A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 GLY A 5
REMARK 465 ASN A 23
REMARK 465 PRO A 24
REMARK 465 ASP A 25
REMARK 465 GLY A 26
REMARK 465 SER A 27
REMARK 465 ALA A 28
REMARK 465 SER A 455
REMARK 465 ALA A 456
REMARK 465 GLY A 457
REMARK 465 ASP A 458
REMARK 465 LEU A 459
REMARK 465 SER A 460
REMARK 465 ALA A 461
REMARK 465 ALA A 462
REMARK 465 MET B 1
REMARK 465 PHE B 2
REMARK 465 SER B 3
REMARK 465 ALA B 4
REMARK 465 ASN B 23
REMARK 465 PRO B 24
REMARK 465 ASP B 25
REMARK 465 GLY B 26
REMARK 465 SER B 27
REMARK 465 ALA B 28
REMARK 465 VAL B 29
REMARK 465 ASP B 30
REMARK 465 SER B 455
REMARK 465 ALA B 456
REMARK 465 GLY B 457
REMARK 465 ASP B 458
REMARK 465 LEU B 459
REMARK 465 SER B 460
REMARK 465 ALA B 461
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 HH11 ARG B 301 OE1 GLN B 322 1.48
REMARK 500 OE2 GLU A 78 HZ3 LYS A 110 1.50
REMARK 500 HG SER B 519 O HOH B 1014 1.60
REMARK 500 OD2 ASP A 396 O HOH A 1002 2.07
REMARK 500 OG1 THR B 394 OD1 ASP B 396 2.14
REMARK 500 OD2 ASP B 396 O HOH B 1002 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 GLU A 565 CB GLU A 565 CG -0.126
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 B 203 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 432 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 432 NE - CZ - NH2 ANGL. DEV. = -3.8 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 ARG A 38 40.66 -105.97
REMARK 500 ARG A 38 40.73 -105.97
REMARK 500 ASP A 51 -168.46 -75.56
REMARK 500 SER A 70 42.51 -80.59
REMARK 500 SER A 70 41.02 -80.67
REMARK 500 ASN A 128 74.45 37.13
REMARK 500 GLU A 294 -84.14 -101.95
REMARK 500 VAL A 312 -55.56 76.31
REMARK 500 VAL A 312 -59.88 70.51
REMARK 500 ALA A 352 19.07 -147.25
REMARK 500 ALA A 447 145.62 -170.97
REMARK 500 MET A 497 -64.89 -100.49
REMARK 500 HIS A 499 -68.73 -96.96
REMARK 500 HIS A 499 -73.56 -96.96
REMARK 500 THR A 503 -82.53 -117.62
REMARK 500 SER A 519 152.07 -48.00
REMARK 500 SER A 560 -118.72 34.47
REMARK 500 SER A 560 -125.01 53.24
REMARK 500 ASP A 607 70.06 -101.58
REMARK 500 TYR A 608 103.23 -42.21
REMARK 500 LEU A 669 43.49 71.88
REMARK 500 SER A 687 -81.17 -109.37
REMARK 500 SER A 687 -81.17 -108.78
REMARK 500 ASN A 729 83.01 -150.87
REMARK 500 ASN A 729 84.04 -150.87
REMARK 500 HIS A 771 40.82 -108.83
REMARK 500 HIS B 6 60.29 35.47
REMARK 500 ARG B 38 41.93 -102.84
REMARK 500 ARG B 38 42.28 -105.50
REMARK 500 SER B 118 164.36 81.88
REMARK 500 SER B 118 164.69 80.81
REMARK 500 CYS B 127 -60.24 -107.92
REMARK 500 ALA B 145 -179.70 -59.25
REMARK 500 HIS B 147 170.64 -52.33
REMARK 500 ASP B 228 108.92 -162.08
REMARK 500 ILE B 265 -51.45 -121.46
REMARK 500 GLU B 294 -89.14 -96.29
REMARK 500 GLU B 294 -89.14 -109.42
REMARK 500 VAL B 312 -56.31 71.57
REMARK 500 VAL B 312 -58.01 72.22
REMARK 500 GLN B 322 -52.42 -131.75
REMARK 500 GLN B 322 -53.55 -131.75
REMARK 500 HIS B 323 -2.59 -140.03
REMARK 500 HIS B 323 -52.68 -127.82
REMARK 500 ALA B 352 15.84 -143.29
REMARK 500 MET B 497 -68.42 -103.05
REMARK 500 HIS B 499 -71.89 -96.79
REMARK 500 THR B 503 -81.95 -112.17
REMARK 500 SER B 560 -123.09 52.18
REMARK 500 SER B 560 -127.77 51.59
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
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 A 901 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 499 NE2
REMARK 620 2 HIS A 504 NE2 84.5
REMARK 620 3 HIS A 690 NE2 108.3 106.7
REMARK 620 4 ASN A 694 OD1 88.6 172.7 77.9
REMARK 620 5 ILE A 839 OXT 165.4 91.6 86.3 94.4
REMARK 620 6 HOH A1045 O 81.4 108.1 144.6 68.2 86.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 901 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 504 NE2
REMARK 620 2 HIS B 690 NE2 105.7
REMARK 620 3 ILE B 839 OXT 89.6 87.1
REMARK 620 4 HOH B1039 O 107.5 145.8 85.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE B 901
DBREF 5T5V A 1 839 UNP P08170 LOX1_SOYBN 1 839
DBREF 5T5V B 1 839 UNP P08170 LOX1_SOYBN 1 839
SEQADV 5T5V GLU A 160 UNP P08170 SER 160 CONFLICT
SEQADV 5T5V GLU B 160 UNP P08170 SER 160 CONFLICT
SEQRES 1 A 839 MET PHE SER ALA GLY HIS LYS ILE LYS GLY THR VAL VAL
SEQRES 2 A 839 LEU MET PRO LYS ASN GLU LEU GLU VAL ASN PRO ASP GLY
SEQRES 3 A 839 SER ALA VAL ASP ASN LEU ASN ALA PHE LEU GLY ARG SER
SEQRES 4 A 839 VAL SER LEU GLN LEU ILE SER ALA THR LYS ALA ASP ALA
SEQRES 5 A 839 HIS GLY LYS GLY LYS VAL GLY LYS ASP THR PHE LEU GLU
SEQRES 6 A 839 GLY ILE ASN THR SER LEU PRO THR LEU GLY ALA GLY GLU
SEQRES 7 A 839 SER ALA PHE ASN ILE HIS PHE GLU TRP ASP GLY SER MET
SEQRES 8 A 839 GLY ILE PRO GLY ALA PHE TYR ILE LYS ASN TYR MET GLN
SEQRES 9 A 839 VAL GLU PHE PHE LEU LYS SER LEU THR LEU GLU ALA ILE
SEQRES 10 A 839 SER ASN GLN GLY THR ILE ARG PHE VAL CYS ASN SER TRP
SEQRES 11 A 839 VAL TYR ASN THR LYS LEU TYR LYS SER VAL ARG ILE PHE
SEQRES 12 A 839 PHE ALA ASN HIS THR TYR VAL PRO SER GLU THR PRO ALA
SEQRES 13 A 839 PRO LEU VAL GLU TYR ARG GLU GLU GLU LEU LYS SER LEU
SEQRES 14 A 839 ARG GLY ASN GLY THR GLY GLU ARG LYS GLU TYR ASP ARG
SEQRES 15 A 839 ILE TYR ASP TYR ASP VAL TYR ASN ASP LEU GLY ASN PRO
SEQRES 16 A 839 ASP LYS SER GLU LYS LEU ALA ARG PRO VAL LEU GLY GLY
SEQRES 17 A 839 SER SER THR PHE PRO TYR PRO ARG ARG GLY ARG THR GLY
SEQRES 18 A 839 ARG GLY PRO THR VAL THR ASP PRO ASN THR GLU LYS GLN
SEQRES 19 A 839 GLY GLU VAL PHE TYR VAL PRO ARG ASP GLU ASN LEU GLY
SEQRES 20 A 839 HIS LEU LYS SER LYS ASP ALA LEU GLU ILE GLY THR LYS
SEQRES 21 A 839 SER LEU SER GLN ILE VAL GLN PRO ALA PHE GLU SER ALA
SEQRES 22 A 839 PHE ASP LEU LYS SER THR PRO ILE GLU PHE HIS SER PHE
SEQRES 23 A 839 GLN ASP VAL HIS ASP LEU TYR GLU GLY GLY ILE LYS LEU
SEQRES 24 A 839 PRO ARG ASP VAL ILE SER THR ILE ILE PRO LEU PRO VAL
SEQRES 25 A 839 ILE LYS GLU LEU TYR ARG THR ASP GLY GLN HIS ILE LEU
SEQRES 26 A 839 LYS PHE PRO GLN PRO HIS VAL VAL GLN VAL SER GLN SER
SEQRES 27 A 839 ALA TRP MET THR ASP GLU GLU PHE ALA ARG GLU MET ILE
SEQRES 28 A 839 ALA GLY VAL ASN PRO CYS VAL ILE ARG GLY LEU GLU GLU
SEQRES 29 A 839 PHE PRO PRO LYS SER ASN LEU ASP PRO ALA ILE TYR GLY
SEQRES 30 A 839 ASP GLN SER SER LYS ILE THR ALA ASP SER LEU ASP LEU
SEQRES 31 A 839 ASP GLY TYR THR MET ASP GLU ALA LEU GLY SER ARG ARG
SEQRES 32 A 839 LEU PHE MET LEU ASP TYR HIS ASP ILE PHE MET PRO TYR
SEQRES 33 A 839 VAL ARG GLN ILE ASN GLN LEU ASN SER ALA LYS THR TYR
SEQRES 34 A 839 ALA THR ARG THR ILE LEU PHE LEU ARG GLU ASP GLY THR
SEQRES 35 A 839 LEU LYS PRO VAL ALA ILE GLU LEU SER LEU PRO HIS SER
SEQRES 36 A 839 ALA GLY ASP LEU SER ALA ALA VAL SER GLN VAL VAL LEU
SEQRES 37 A 839 PRO ALA LYS GLU GLY VAL GLU SER THR ILE TRP LEU LEU
SEQRES 38 A 839 ALA LYS ALA TYR VAL ILE VAL ASN ASP SER CYS TYR HIS
SEQRES 39 A 839 GLN LEU MET SER HIS TRP LEU ASN THR HIS ALA ALA MET
SEQRES 40 A 839 GLU PRO PHE VAL ILE ALA THR HIS ARG HIS LEU SER VAL
SEQRES 41 A 839 LEU HIS PRO ILE TYR LYS LEU LEU THR PRO HIS TYR ARG
SEQRES 42 A 839 ASN ASN MET ASN ILE ASN ALA LEU ALA ARG GLN SER LEU
SEQRES 43 A 839 ILE ASN ALA ASN GLY ILE ILE GLU THR THR PHE LEU PRO
SEQRES 44 A 839 SER LYS TYR SER VAL GLU MET SER SER ALA VAL TYR LYS
SEQRES 45 A 839 ASN TRP VAL PHE THR ASP GLN ALA LEU PRO ALA ASP LEU
SEQRES 46 A 839 ILE LYS ARG GLY VAL ALA ILE LYS ASP PRO SER THR PRO
SEQRES 47 A 839 HIS GLY VAL ARG LEU LEU ILE GLU ASP TYR PRO TYR ALA
SEQRES 48 A 839 ALA ASP GLY LEU GLU ILE TRP ALA ALA ILE LYS THR TRP
SEQRES 49 A 839 VAL GLN GLU TYR VAL PRO LEU TYR TYR ALA ARG ASP ASP
SEQRES 50 A 839 ASP VAL LYS ASN ASP SER GLU LEU GLN HIS TRP TRP LYS
SEQRES 51 A 839 GLU ALA VAL GLU LYS GLY HIS GLY ASP LEU LYS ASP LYS
SEQRES 52 A 839 PRO TRP TRP PRO LYS LEU GLN THR LEU GLU ASP LEU VAL
SEQRES 53 A 839 GLU VAL CYS LEU ILE ILE ILE TRP ILE ALA SER ALA LEU
SEQRES 54 A 839 HIS ALA ALA VAL ASN PHE GLY GLN TYR PRO TYR GLY GLY
SEQRES 55 A 839 LEU ILE MET ASN ARG PRO THR ALA SER ARG ARG LEU LEU
SEQRES 56 A 839 PRO GLU LYS GLY THR PRO GLU TYR GLU GLU MET ILE ASN
SEQRES 57 A 839 ASN HIS GLU LYS ALA TYR LEU ARG THR ILE THR SER LYS
SEQRES 58 A 839 LEU PRO THR LEU ILE SER LEU SER VAL ILE GLU ILE LEU
SEQRES 59 A 839 SER THR HIS ALA SER ASP GLU VAL TYR LEU GLY GLN ARG
SEQRES 60 A 839 ASP ASN PRO HIS TRP THR SER ASP SER LYS ALA LEU GLN
SEQRES 61 A 839 ALA PHE GLN LYS PHE GLY ASN LYS LEU LYS GLU ILE GLU
SEQRES 62 A 839 GLU LYS LEU VAL ARG ARG ASN ASN ASP PRO SER LEU GLN
SEQRES 63 A 839 GLY ASN ARG LEU GLY PRO VAL GLN LEU PRO TYR THR LEU
SEQRES 64 A 839 LEU TYR PRO SER SER GLU GLU GLY LEU THR PHE ARG GLY
SEQRES 65 A 839 ILE PRO ASN SER ILE SER ILE
SEQRES 1 B 839 MET PHE SER ALA GLY HIS LYS ILE LYS GLY THR VAL VAL
SEQRES 2 B 839 LEU MET PRO LYS ASN GLU LEU GLU VAL ASN PRO ASP GLY
SEQRES 3 B 839 SER ALA VAL ASP ASN LEU ASN ALA PHE LEU GLY ARG SER
SEQRES 4 B 839 VAL SER LEU GLN LEU ILE SER ALA THR LYS ALA ASP ALA
SEQRES 5 B 839 HIS GLY LYS GLY LYS VAL GLY LYS ASP THR PHE LEU GLU
SEQRES 6 B 839 GLY ILE ASN THR SER LEU PRO THR LEU GLY ALA GLY GLU
SEQRES 7 B 839 SER ALA PHE ASN ILE HIS PHE GLU TRP ASP GLY SER MET
SEQRES 8 B 839 GLY ILE PRO GLY ALA PHE TYR ILE LYS ASN TYR MET GLN
SEQRES 9 B 839 VAL GLU PHE PHE LEU LYS SER LEU THR LEU GLU ALA ILE
SEQRES 10 B 839 SER ASN GLN GLY THR ILE ARG PHE VAL CYS ASN SER TRP
SEQRES 11 B 839 VAL TYR ASN THR LYS LEU TYR LYS SER VAL ARG ILE PHE
SEQRES 12 B 839 PHE ALA ASN HIS THR TYR VAL PRO SER GLU THR PRO ALA
SEQRES 13 B 839 PRO LEU VAL GLU TYR ARG GLU GLU GLU LEU LYS SER LEU
SEQRES 14 B 839 ARG GLY ASN GLY THR GLY GLU ARG LYS GLU TYR ASP ARG
SEQRES 15 B 839 ILE TYR ASP TYR ASP VAL TYR ASN ASP LEU GLY ASN PRO
SEQRES 16 B 839 ASP LYS SER GLU LYS LEU ALA ARG PRO VAL LEU GLY GLY
SEQRES 17 B 839 SER SER THR PHE PRO TYR PRO ARG ARG GLY ARG THR GLY
SEQRES 18 B 839 ARG GLY PRO THR VAL THR ASP PRO ASN THR GLU LYS GLN
SEQRES 19 B 839 GLY GLU VAL PHE TYR VAL PRO ARG ASP GLU ASN LEU GLY
SEQRES 20 B 839 HIS LEU LYS SER LYS ASP ALA LEU GLU ILE GLY THR LYS
SEQRES 21 B 839 SER LEU SER GLN ILE VAL GLN PRO ALA PHE GLU SER ALA
SEQRES 22 B 839 PHE ASP LEU LYS SER THR PRO ILE GLU PHE HIS SER PHE
SEQRES 23 B 839 GLN ASP VAL HIS ASP LEU TYR GLU GLY GLY ILE LYS LEU
SEQRES 24 B 839 PRO ARG ASP VAL ILE SER THR ILE ILE PRO LEU PRO VAL
SEQRES 25 B 839 ILE LYS GLU LEU TYR ARG THR ASP GLY GLN HIS ILE LEU
SEQRES 26 B 839 LYS PHE PRO GLN PRO HIS VAL VAL GLN VAL SER GLN SER
SEQRES 27 B 839 ALA TRP MET THR ASP GLU GLU PHE ALA ARG GLU MET ILE
SEQRES 28 B 839 ALA GLY VAL ASN PRO CYS VAL ILE ARG GLY LEU GLU GLU
SEQRES 29 B 839 PHE PRO PRO LYS SER ASN LEU ASP PRO ALA ILE TYR GLY
SEQRES 30 B 839 ASP GLN SER SER LYS ILE THR ALA ASP SER LEU ASP LEU
SEQRES 31 B 839 ASP GLY TYR THR MET ASP GLU ALA LEU GLY SER ARG ARG
SEQRES 32 B 839 LEU PHE MET LEU ASP TYR HIS ASP ILE PHE MET PRO TYR
SEQRES 33 B 839 VAL ARG GLN ILE ASN GLN LEU ASN SER ALA LYS THR TYR
SEQRES 34 B 839 ALA THR ARG THR ILE LEU PHE LEU ARG GLU ASP GLY THR
SEQRES 35 B 839 LEU LYS PRO VAL ALA ILE GLU LEU SER LEU PRO HIS SER
SEQRES 36 B 839 ALA GLY ASP LEU SER ALA ALA VAL SER GLN VAL VAL LEU
SEQRES 37 B 839 PRO ALA LYS GLU GLY VAL GLU SER THR ILE TRP LEU LEU
SEQRES 38 B 839 ALA LYS ALA TYR VAL ILE VAL ASN ASP SER CYS TYR HIS
SEQRES 39 B 839 GLN LEU MET SER HIS TRP LEU ASN THR HIS ALA ALA MET
SEQRES 40 B 839 GLU PRO PHE VAL ILE ALA THR HIS ARG HIS LEU SER VAL
SEQRES 41 B 839 LEU HIS PRO ILE TYR LYS LEU LEU THR PRO HIS TYR ARG
SEQRES 42 B 839 ASN ASN MET ASN ILE ASN ALA LEU ALA ARG GLN SER LEU
SEQRES 43 B 839 ILE ASN ALA ASN GLY ILE ILE GLU THR THR PHE LEU PRO
SEQRES 44 B 839 SER LYS TYR SER VAL GLU MET SER SER ALA VAL TYR LYS
SEQRES 45 B 839 ASN TRP VAL PHE THR ASP GLN ALA LEU PRO ALA ASP LEU
SEQRES 46 B 839 ILE LYS ARG GLY VAL ALA ILE LYS ASP PRO SER THR PRO
SEQRES 47 B 839 HIS GLY VAL ARG LEU LEU ILE GLU ASP TYR PRO TYR ALA
SEQRES 48 B 839 ALA ASP GLY LEU GLU ILE TRP ALA ALA ILE LYS THR TRP
SEQRES 49 B 839 VAL GLN GLU TYR VAL PRO LEU TYR TYR ALA ARG ASP ASP
SEQRES 50 B 839 ASP VAL LYS ASN ASP SER GLU LEU GLN HIS TRP TRP LYS
SEQRES 51 B 839 GLU ALA VAL GLU LYS GLY HIS GLY ASP LEU LYS ASP LYS
SEQRES 52 B 839 PRO TRP TRP PRO LYS LEU GLN THR LEU GLU ASP LEU VAL
SEQRES 53 B 839 GLU VAL CYS LEU ILE ILE ILE TRP ILE ALA SER ALA LEU
SEQRES 54 B 839 HIS ALA ALA VAL ASN PHE GLY GLN TYR PRO TYR GLY GLY
SEQRES 55 B 839 LEU ILE MET ASN ARG PRO THR ALA SER ARG ARG LEU LEU
SEQRES 56 B 839 PRO GLU LYS GLY THR PRO GLU TYR GLU GLU MET ILE ASN
SEQRES 57 B 839 ASN HIS GLU LYS ALA TYR LEU ARG THR ILE THR SER LYS
SEQRES 58 B 839 LEU PRO THR LEU ILE SER LEU SER VAL ILE GLU ILE LEU
SEQRES 59 B 839 SER THR HIS ALA SER ASP GLU VAL TYR LEU GLY GLN ARG
SEQRES 60 B 839 ASP ASN PRO HIS TRP THR SER ASP SER LYS ALA LEU GLN
SEQRES 61 B 839 ALA PHE GLN LYS PHE GLY ASN LYS LEU LYS GLU ILE GLU
SEQRES 62 B 839 GLU LYS LEU VAL ARG ARG ASN ASN ASP PRO SER LEU GLN
SEQRES 63 B 839 GLY ASN ARG LEU GLY PRO VAL GLN LEU PRO TYR THR LEU
SEQRES 64 B 839 LEU TYR PRO SER SER GLU GLU GLY LEU THR PHE ARG GLY
SEQRES 65 B 839 ILE PRO ASN SER ILE SER ILE
HET FE A 901 1
HET FE B 901 1
HETNAM FE FE (III) ION
FORMUL 3 FE 2(FE 3+)
FORMUL 5 HOH *996(H2 O)
HELIX 1 AA1 ASN A 18 GLU A 21 5 4
HELIX 2 AA2 ASN A 31 LEU A 36 5 6
HELIX 3 AA3 ASN A 133 TYR A 137 5 5
HELIX 4 AA4 PRO A 155 PRO A 157 5 3
HELIX 5 AA5 LEU A 158 GLY A 171 1 14
HELIX 6 AA6 SER A 198 ALA A 202 5 5
HELIX 7 AA7 PRO A 241 ASN A 245 5 5
HELIX 8 AA8 LYS A 250 ASP A 253 5 4
HELIX 9 AA9 ALA A 254 ILE A 265 1 12
HELIX 10 AB1 ILE A 265 LEU A 276 1 12
HELIX 11 AB2 SER A 285 ASP A 291 1 7
HELIX 12 AB3 LEU A 292 GLU A 294 5 3
HELIX 13 AB4 PRO A 300 ILE A 308 1 9
HELIX 14 AB5 VAL A 312 LEU A 316 5 5
HELIX 15 AB6 PRO A 330 GLN A 334 5 5
HELIX 16 AB7 SER A 338 MET A 341 5 4
HELIX 17 AB8 THR A 342 GLY A 353 1 12
HELIX 18 AB9 ASP A 372 GLY A 377 1 6
HELIX 19 AC1 THR A 384 LEU A 388 5 5
HELIX 20 AC2 THR A 394 SER A 401 1 8
HELIX 21 AC3 TYR A 409 GLN A 422 1 14
HELIX 22 AC4 GLY A 473 MET A 497 1 25
HELIX 23 AC5 THR A 503 LEU A 518 1 16
HELIX 24 AC6 HIS A 522 THR A 529 1 8
HELIX 25 AC7 PRO A 530 ARG A 533 5 4
HELIX 26 AC8 ASN A 534 LEU A 546 1 13
HELIX 27 AC9 GLY A 551 PHE A 557 1 7
HELIX 28 AD1 PRO A 559 LYS A 561 5 3
HELIX 29 AD2 TYR A 562 LYS A 572 1 11
HELIX 30 AD3 ASN A 573 TRP A 574 5 2
HELIX 31 AD4 VAL A 575 GLN A 579 5 5
HELIX 32 AD5 ALA A 580 ARG A 588 1 9
HELIX 33 AD6 TYR A 608 VAL A 629 1 22
HELIX 34 AD7 PRO A 630 TYR A 632 5 3
HELIX 35 AD8 ARG A 635 ASN A 641 1 7
HELIX 36 AD9 ASP A 642 LYS A 655 1 14
HELIX 37 AE1 HIS A 657 LYS A 661 5 5
HELIX 38 AE2 THR A 671 SER A 687 1 17
HELIX 39 AE3 SER A 687 PHE A 695 1 9
HELIX 40 AE4 GLY A 696 GLY A 702 1 7
HELIX 41 AE5 THR A 720 ASN A 729 1 10
HELIX 42 AE6 ASN A 729 ILE A 738 1 10
HELIX 43 AE7 SER A 740 SER A 755 1 16
HELIX 44 AE8 ASP A 775 ASP A 802 1 28
HELIX 45 AE9 LEU A 805 LEU A 810 1 6
HELIX 46 AF1 ASN B 18 GLU B 21 5 4
HELIX 47 AF2 ASN B 31 LEU B 36 5 6
HELIX 48 AF3 ASN B 133 TYR B 137 5 5
HELIX 49 AF4 PRO B 155 PRO B 157 5 3
HELIX 50 AF5 LEU B 158 GLY B 171 1 14
HELIX 51 AF6 SER B 198 ALA B 202 5 5
HELIX 52 AF7 PRO B 241 ASN B 245 5 5
HELIX 53 AF8 LYS B 250 ASP B 253 5 4
HELIX 54 AF9 ALA B 254 ILE B 265 1 12
HELIX 55 AG1 ILE B 265 LEU B 276 1 12
HELIX 56 AG2 SER B 285 ASP B 291 1 7
HELIX 57 AG3 PRO B 300 ILE B 308 1 9
HELIX 58 AG4 VAL B 312 LEU B 316 5 5
HELIX 59 AG5 PRO B 330 GLN B 334 5 5
HELIX 60 AG6 SER B 338 MET B 341 5 4
HELIX 61 AG7 THR B 342 GLY B 353 1 12
HELIX 62 AG8 ASP B 372 GLY B 377 1 6
HELIX 63 AG9 THR B 384 LEU B 388 5 5
HELIX 64 AH1 THR B 394 SER B 401 1 8
HELIX 65 AH2 TYR B 409 GLN B 422 1 14
HELIX 66 AH3 GLU B 472 MET B 497 1 26
HELIX 67 AH4 THR B 503 LEU B 518 1 16
HELIX 68 AH5 HIS B 522 THR B 529 1 8
HELIX 69 AH6 PRO B 530 ARG B 533 5 4
HELIX 70 AH7 ASN B 534 LEU B 546 1 13
HELIX 71 AH8 GLY B 551 PHE B 557 1 7
HELIX 72 AH9 PRO B 559 LYS B 561 5 3
HELIX 73 AI1 TYR B 562 LYS B 572 1 11
HELIX 74 AI2 ASN B 573 TRP B 574 5 2
HELIX 75 AI3 VAL B 575 GLN B 579 5 5
HELIX 76 AI4 ALA B 580 ARG B 588 1 9
HELIX 77 AI5 TYR B 608 TYR B 633 1 26
HELIX 78 AI6 ARG B 635 ASN B 641 1 7
HELIX 79 AI7 ASP B 642 LYS B 655 1 14
HELIX 80 AI8 HIS B 657 LYS B 661 5 5
HELIX 81 AI9 THR B 671 SER B 687 1 17
HELIX 82 AJ1 SER B 687 PHE B 695 1 9
HELIX 83 AJ2 GLY B 696 GLY B 702 1 7
HELIX 84 AJ3 THR B 720 ASN B 729 1 10
HELIX 85 AJ4 ASN B 729 ILE B 738 1 10
HELIX 86 AJ5 SER B 740 SER B 755 1 16
HELIX 87 AJ6 ASP B 775 ASN B 801 1 27
HELIX 88 AJ7 ASP B 802 SER B 804 5 3
HELIX 89 AJ8 LEU B 805 LEU B 810 1 6
SHEET 1 AA1 5 GLY A 66 ILE A 67 0
SHEET 2 AA1 5 SER A 79 GLU A 86 -1 O ASN A 82 N GLY A 66
SHEET 3 AA1 5 LYS A 7 PRO A 16 -1 N GLY A 10 O ILE A 83
SHEET 4 AA1 5 PHE A 107 LEU A 114 -1 O PHE A 108 N MET A 15
SHEET 5 AA1 5 ILE A 123 VAL A 131 -1 O SER A 129 N LEU A 109
SHEET 1 AA2 3 GLY A 56 VAL A 58 0
SHEET 2 AA2 3 VAL A 40 ALA A 50 -1 N SER A 46 O LYS A 57
SHEET 3 AA2 3 THR A 62 PHE A 63 -1 O THR A 62 N LEU A 42
SHEET 1 AA3 4 GLY A 56 VAL A 58 0
SHEET 2 AA3 4 VAL A 40 ALA A 50 -1 N SER A 46 O LYS A 57
SHEET 3 AA3 4 PRO A 94 ASN A 101 -1 O GLY A 95 N ILE A 45
SHEET 4 AA3 4 ARG A 141 PHE A 144 -1 O PHE A 143 N PHE A 97
SHEET 1 AA4 2 TYR A 186 ASP A 187 0
SHEET 2 AA4 2 ARG A 217 GLY A 218 -1 O ARG A 217 N ASP A 187
SHEET 1 AA5 3 ILE A 297 LYS A 298 0
SHEET 2 AA5 3 ILE A 324 LYS A 326 -1 O LEU A 325 N ILE A 297
SHEET 3 AA5 3 ARG A 318 THR A 319 -1 N ARG A 318 O LYS A 326
SHEET 1 AA6 5 ARG A 360 GLY A 361 0
SHEET 2 AA6 5 LEU A 404 ASP A 408 -1 O MET A 406 N ARG A 360
SHEET 3 AA6 5 ALA A 430 LEU A 437 -1 O LEU A 435 N PHE A 405
SHEET 4 AA6 5 LEU A 443 SER A 451 -1 O GLU A 449 N ARG A 432
SHEET 5 AA6 5 GLN A 465 VAL A 467 -1 O GLN A 465 N LEU A 450
SHEET 1 AA7 2 ALA A 591 LYS A 593 0
SHEET 2 AA7 2 VAL A 601 LEU A 603 -1 O ARG A 602 N ILE A 592
SHEET 1 AA8 5 GLY B 66 ASN B 68 0
SHEET 2 AA8 5 SER B 79 GLU B 86 -1 O ALA B 80 N ASN B 68
SHEET 3 AA8 5 LYS B 7 PRO B 16 -1 N GLY B 10 O ILE B 83
SHEET 4 AA8 5 PHE B 107 GLU B 115 -1 O PHE B 108 N MET B 15
SHEET 5 AA8 5 THR B 122 VAL B 131 -1 O SER B 129 N LEU B 109
SHEET 1 AA9 3 GLY B 56 VAL B 58 0
SHEET 2 AA9 3 VAL B 40 ALA B 50 -1 N SER B 46 O LYS B 57
SHEET 3 AA9 3 THR B 62 PHE B 63 -1 O THR B 62 N LEU B 42
SHEET 1 AB1 4 GLY B 56 VAL B 58 0
SHEET 2 AB1 4 VAL B 40 ALA B 50 -1 N SER B 46 O LYS B 57
SHEET 3 AB1 4 PRO B 94 ASN B 101 -1 O ALA B 96 N ILE B 45
SHEET 4 AB1 4 ARG B 141 PHE B 144 -1 O PHE B 143 N PHE B 97
SHEET 1 AB2 2 TYR B 186 ASP B 187 0
SHEET 2 AB2 2 ARG B 217 GLY B 218 -1 O ARG B 217 N ASP B 187
SHEET 1 AB3 2 ILE B 297 LYS B 298 0
SHEET 2 AB3 2 ILE B 324 LEU B 325 -1 O LEU B 325 N ILE B 297
SHEET 1 AB4 5 ARG B 360 GLY B 361 0
SHEET 2 AB4 5 LEU B 404 ASP B 408 -1 O MET B 406 N ARG B 360
SHEET 3 AB4 5 ALA B 430 LEU B 437 -1 O LEU B 435 N PHE B 405
SHEET 4 AB4 5 LEU B 443 LEU B 452 -1 O GLU B 449 N ARG B 432
SHEET 5 AB4 5 VAL B 463 VAL B 467 -1 O GLN B 465 N LEU B 450
SHEET 1 AB5 2 ALA B 591 LYS B 593 0
SHEET 2 AB5 2 VAL B 601 LEU B 603 -1 O ARG B 602 N ILE B 592
LINK NE2AHIS A 499 FE A FE A 901 1555 1555 2.21
LINK NE2AHIS A 504 FE A FE A 901 1555 1555 2.16
LINK NE2AHIS A 690 FE A FE A 901 1555 1555 2.21
LINK OD1AASN A 694 FE A FE A 901 1555 1555 2.56
LINK OXTAILE A 839 FE A FE A 901 1555 1555 2.14
LINK FE A FE A 901 O HOH A1045 1555 1555 1.98
LINK NE2AHIS B 504 FE A FE B 901 1555 1555 2.16
LINK NE2AHIS B 690 FE A FE B 901 1555 1555 2.28
LINK OXTAILE B 839 FE A FE B 901 1555 1555 2.23
LINK FE A FE B 901 O HOH B1039 1555 1555 2.05
CISPEP 1 PHE A 365 PRO A 366 0 3.33
CISPEP 2 PHE A 365 PRO A 366 0 0.15
CISPEP 3 PHE B 365 PRO B 366 0 2.31
CISPEP 4 PHE B 365 PRO B 366 0 1.38
SITE 1 AC1 6 HIS A 499 HIS A 504 HIS A 690 ASN A 694
SITE 2 AC1 6 ILE A 839 HOH A1045
SITE 1 AC2 6 HIS B 499 HIS B 504 HIS B 690 ASN B 694
SITE 2 AC2 6 ILE B 839 HOH B1039
CRYST1 91.572 92.754 100.919 90.00 93.76 90.00 P 1 21 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010920 0.000000 0.000718 0.00000
SCALE2 0.000000 0.010781 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009930 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
