HEADER TRANSFERASE 17-DEC-07 3BOF
TITLE COBALAMIN-DEPENDENT METHIONINE SYNTHASE (1-566) FROM THERMOTOGA
TITLE 2 MARITIMA COMPLEXED WITH ZN2+ AND HOMOCYSTEINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5-METHYLTETRAHYDROFOLATE S-HOMOCYSTEINE METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.1.1.13;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET29A
KEYWDS METH, TRANSFERASE, TIM BARREL, HOMOCYSTEINE, ZINC, ZINC INVERSION,
KEYWDS 2 METHYLTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KOUTMOS,J.L.SMITH,M.L.LUDWIG
REVDAT 5 03-APR-24 3BOF 1 HETSYN
REVDAT 4 21-FEB-24 3BOF 1 REMARK LINK
REVDAT 3 24-FEB-09 3BOF 1 VERSN
REVDAT 2 18-MAR-08 3BOF 1 JRNL
REVDAT 1 11-MAR-08 3BOF 0
JRNL AUTH M.KOUTMOS,R.PEJCHAL,T.M.BOMER,R.G.MATTHEWS,J.L.SMITH,
JRNL AUTH 2 M.L.LUDWIG
JRNL TITL METAL ACTIVE SITE ELASTICITY LINKED TO ACTIVATION OF
JRNL TITL 2 HOMOCYSTEINE IN METHIONINE SYNTHASES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 105 3286 2008
JRNL REFN ISSN 0027-8424
JRNL PMID 18296644
JRNL DOI 10.1073/PNAS.0709960105
REMARK 2
REMARK 2 RESOLUTION. 1.70 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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 136540
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6933
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9517
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE SET COUNT : 543
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8763
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 411
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.05000
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): 0.106
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.102
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.082
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8942 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12084 ; 1.419 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1113 ; 6.679 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 392 ;37.936 ;24.184
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1613 ;14.951 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;18.881 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1382 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6662 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4414 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6274 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 522 ; 0.128 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 7 ; 0.083 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 62 ; 0.240 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.192 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): 1 ; 0.043 ; 0.200
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): 5546 ; 0.864 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8971 ; 1.606 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3419 ; 2.483 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3113 ; 4.176 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3BOF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000045767.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-07
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : K-B PAIR OF BIOMORPH MIRRORS FOR
REMARK 200 VERTICAL AND HORIZONTAL FOCUSING
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 136540
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 46.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.32300
REMARK 200 R SYM FOR SHELL (I) : 0.39900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.360
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% 1,2-PROPANEDIOL, 10% GLYCEROL, 5%
REMARK 280 PEG 3000, 100 MM POTASIUM CITRATE PH 4.8, 1.5% 1,2,3-
REMARK 280 HEPTANETRIOL, 10 MM YCL3. SOAKING WITH 20% 1,2-PROPANEDIOL, 10%
REMARK 280 GLYCEROL, 5% PEG 3000, 100 MM TRIS PH 7, 1.5% 1,2,3-HEPTANETRIOL,
REMARK 280 AND 10MM HCY , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 43.15400
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2900 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 PRO A 561
REMARK 465 ARG A 562
REMARK 465 ALA A 563
REMARK 465 GLU A 564
REMARK 465 VAL A 565
REMARK 465 LYS A 566
REMARK 465 VAL B 240
REMARK 465 GLU B 241
REMARK 465 ASN B 242
REMARK 465 GLY B 243
REMARK 465 PRO B 561
REMARK 465 ARG B 562
REMARK 465 ALA B 563
REMARK 465 GLU B 564
REMARK 465 VAL B 565
REMARK 465 LYS B 566
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 LYS A 9 CG CD CE NZ
REMARK 470 GLU A 99 CG CD OE1 OE2
REMARK 470 GLN A 294 CG CD OE1 NE2
REMARK 470 LYS A 328 CG CD CE NZ
REMARK 470 LYS A 441 CB CG CD CE NZ
REMARK 470 ASP A 442 CB CG OD1 OD2
REMARK 470 LYS A 445 CG CD CE NZ
REMARK 470 LYS B 9 CG CD CE NZ
REMARK 470 GLU B 99 CG CD OE1 OE2
REMARK 470 LYS B 237 CG CD CE NZ
REMARK 470 ILE B 239 CG1 CG2 CD1
REMARK 470 LYS B 244 CG CD CE NZ
REMARK 470 THR B 245 OG1 CG2
REMARK 470 GLN B 294 CG CD OE1 NE2
REMARK 470 LYS B 328 CG CD CE NZ
REMARK 470 LYS B 441 CB CG CD CE NZ
REMARK 470 ASP B 442 CB CG OD1 OD2
REMARK 470 LYS B 445 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG A 14 OD1 ASN A 289 2.06
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 133 CB GLU A 133 CG -0.127
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 4 NE - CZ - NH1 ANGL. DEV. = -3.3 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 ALA A 42 63.99 -150.47
REMARK 500 THR A 147 30.44 70.41
REMARK 500 ASP A 199 49.08 -80.32
REMARK 500 CYS A 207 -175.56 70.82
REMARK 500 SER A 208 -41.61 67.47
REMARK 500 CYS A 272 -158.16 -104.24
REMARK 500 CYS A 273 129.65 -37.26
REMARK 500 LYS A 296 -88.97 -90.58
REMARK 500 LYS A 297 132.82 131.82
REMARK 500 ASN A 323 118.52 -160.32
REMARK 500 ASN A 384 -16.46 77.13
REMARK 500 ASN A 411 76.37 -108.98
REMARK 500 SER A 412 150.06 149.65
REMARK 500 GLU A 559 -156.07 61.82
REMARK 500 ALA B 42 61.53 -150.37
REMARK 500 CYS B 207 -172.67 69.22
REMARK 500 SER B 208 -39.16 67.92
REMARK 500 ALA B 235 31.10 -99.56
REMARK 500 THR B 245 -156.90 -64.20
REMARK 500 VAL B 246 106.16 16.95
REMARK 500 CYS B 272 -155.97 -111.96
REMARK 500 ASN B 323 115.45 -163.08
REMARK 500 ASN B 384 -15.67 79.05
REMARK 500 SER B 412 122.24 106.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 411 SER A 412 75.72
REMARK 500 LYS A 558 GLU A 559 149.56
REMARK 500 ASN B 411 SER B 412 136.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ASN A 411 15.15
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 K A 703 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 19 O
REMARK 620 2 ASP A 19 OD2 69.6
REMARK 620 3 GLY A 20 O 77.6 80.8
REMARK 620 4 GLU A 232 OE1 104.2 107.9 171.3
REMARK 620 5 GLY A 271 O 68.3 136.8 81.5 91.2
REMARK 620 6 HOH A 714 O 154.9 134.3 96.9 77.7 86.7
REMARK 620 N 1 2 3 4 5
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 CYS A 207 SG
REMARK 620 2 CYS A 272 SG 112.7
REMARK 620 3 CYS A 273 SG 106.9 118.5
REMARK 620 4 HCS A 711 SD 107.2 104.3 106.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 704 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 19 O
REMARK 620 2 ASP B 19 OD2 70.4
REMARK 620 3 GLY B 20 O 77.9 81.1
REMARK 620 4 GLU B 232 OE1 102.5 106.5 172.1
REMARK 620 5 GLY B 271 O 70.8 140.0 81.7 91.0
REMARK 620 6 HOH B 734 O 155.6 133.6 99.6 76.7 84.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 207 SG
REMARK 620 2 CYS B 272 SG 109.9
REMARK 620 3 CYS B 273 SG 105.6 118.9
REMARK 620 4 HCS B 712 SD 115.1 102.9 104.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HCS A 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HCS B 712
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Q8A RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEXED WOTH CD2+ INSTEAD OF ZN2+
REMARK 900 RELATED ID: 3BOL RELATED DB: PDB
REMARK 900 RELATED ID: 3BQ5 RELATED DB: PDB
REMARK 900 RELATED ID: 3BQ6 RELATED DB: PDB
DBREF 3BOF A 1 566 UNP Q9WYA5 Q9WYA5_THEMA 1 566
DBREF 3BOF B 1 566 UNP Q9WYA5 Q9WYA5_THEMA 1 566
SEQRES 1 A 566 MET ARG ASN ARG ARG GLU VAL SER LYS LEU LEU SER GLU
SEQRES 2 A 566 ARG VAL LEU LEU LEU ASP GLY ALA TYR GLY THR GLU PHE
SEQRES 3 A 566 MET LYS TYR GLY TYR ASP ASP LEU PRO GLU GLU LEU ASN
SEQRES 4 A 566 ILE LYS ALA PRO ASP VAL VAL LEU LYS VAL HIS ARG SER
SEQRES 5 A 566 TYR ILE GLU SER GLY SER ASP VAL ILE LEU THR ASN THR
SEQRES 6 A 566 PHE GLY ALA THR ARG MET LYS LEU ARG LYS HIS GLY LEU
SEQRES 7 A 566 GLU ASP LYS LEU ASP PRO ILE VAL ARG ASN ALA VAL ARG
SEQRES 8 A 566 ILE ALA ARG ARG ALA ALA GLY GLU LYS LEU VAL PHE GLY
SEQRES 9 A 566 ASP ILE GLY PRO THR GLY GLU LEU PRO TYR PRO LEU GLY
SEQRES 10 A 566 SER THR LEU PHE GLU GLU PHE TYR GLU ASN PHE ARG GLU
SEQRES 11 A 566 THR VAL GLU ILE MET VAL GLU GLU GLY VAL ASP GLY ILE
SEQRES 12 A 566 ILE PHE GLU THR PHE SER ASP ILE LEU GLU LEU LYS ALA
SEQRES 13 A 566 ALA VAL LEU ALA ALA ARG GLU VAL SER ARG ASP VAL PHE
SEQRES 14 A 566 LEU ILE ALA HIS MET THR PHE ASP GLU LYS GLY ARG SER
SEQRES 15 A 566 LEU THR GLY THR ASP PRO ALA ASN PHE ALA ILE THR PHE
SEQRES 16 A 566 ASP GLU LEU ASP ILE ASP ALA LEU GLY ILE ASN CYS SER
SEQRES 17 A 566 LEU GLY PRO GLU GLU ILE LEU PRO ILE PHE GLN GLU LEU
SEQRES 18 A 566 SER GLN TYR THR ASP LYS PHE LEU VAL VAL GLU PRO ASN
SEQRES 19 A 566 ALA GLY LYS PRO ILE VAL GLU ASN GLY LYS THR VAL TYR
SEQRES 20 A 566 PRO LEU LYS PRO HIS ASP PHE ALA VAL HIS ILE ASP SER
SEQRES 21 A 566 TYR TYR GLU LEU GLY VAL ASN ILE PHE GLY GLY CYS CYS
SEQRES 22 A 566 GLY THR THR PRO GLU HIS VAL LYS LEU PHE ARG LYS VAL
SEQRES 23 A 566 LEU GLY ASN ARG LYS PRO LEU GLN ARG LYS LYS LYS ARG
SEQRES 24 A 566 ILE PHE ALA VAL SER SER PRO SER LYS LEU VAL THR PHE
SEQRES 25 A 566 ASP HIS PHE VAL VAL ILE GLY GLU ARG ILE ASN PRO ALA
SEQRES 26 A 566 GLY ARG LYS LYS LEU TRP ALA GLU MET GLN LYS GLY ASN
SEQRES 27 A 566 GLU GLU ILE VAL ILE LYS GLU ALA LYS THR GLN VAL GLU
SEQRES 28 A 566 LYS GLY ALA GLU VAL LEU ASP VAL ASN PHE GLY ILE GLU
SEQRES 29 A 566 SER GLN ILE ASP VAL ARG TYR VAL GLU LYS ILE VAL GLN
SEQRES 30 A 566 THR LEU PRO TYR VAL SER ASN VAL PRO LEU SER LEU ASP
SEQRES 31 A 566 ILE GLN ASN VAL ASP LEU THR GLU ARG ALA LEU ARG ALA
SEQRES 32 A 566 TYR PRO GLY ARG SER LEU PHE ASN SER ALA LYS VAL ASP
SEQRES 33 A 566 GLU GLU GLU LEU GLU MET LYS ILE ASN LEU LEU LYS LYS
SEQRES 34 A 566 TYR GLY GLY THR LEU ILE VAL LEU LEU MET GLY LYS ASP
SEQRES 35 A 566 VAL PRO LYS SER PHE GLU GLU ARG LYS GLU TYR PHE GLU
SEQRES 36 A 566 LYS ALA LEU LYS ILE LEU GLU ARG HIS ASP PHE SER ASP
SEQRES 37 A 566 ARG VAL ILE PHE ASP PRO GLY VAL LEU PRO LEU GLY ALA
SEQRES 38 A 566 GLU GLY LYS PRO VAL GLU VAL LEU LYS THR ILE GLU PHE
SEQRES 39 A 566 ILE SER SER LYS GLY PHE ASN THR THR VAL GLY LEU SER
SEQRES 40 A 566 ASN LEU SER PHE GLY LEU PRO ASP ARG SER TYR TYR ASN
SEQRES 41 A 566 THR ALA PHE LEU VAL LEU GLY ILE SER LYS GLY LEU SER
SEQRES 42 A 566 SER ALA ILE MET ASN PRO LEU ASP GLU THR LEU MET LYS
SEQRES 43 A 566 THR LEU ASN ALA THR LEU VAL ILE LEU GLU LYS LYS GLU
SEQRES 44 A 566 LEU PRO ARG ALA GLU VAL LYS
SEQRES 1 B 566 MET ARG ASN ARG ARG GLU VAL SER LYS LEU LEU SER GLU
SEQRES 2 B 566 ARG VAL LEU LEU LEU ASP GLY ALA TYR GLY THR GLU PHE
SEQRES 3 B 566 MET LYS TYR GLY TYR ASP ASP LEU PRO GLU GLU LEU ASN
SEQRES 4 B 566 ILE LYS ALA PRO ASP VAL VAL LEU LYS VAL HIS ARG SER
SEQRES 5 B 566 TYR ILE GLU SER GLY SER ASP VAL ILE LEU THR ASN THR
SEQRES 6 B 566 PHE GLY ALA THR ARG MET LYS LEU ARG LYS HIS GLY LEU
SEQRES 7 B 566 GLU ASP LYS LEU ASP PRO ILE VAL ARG ASN ALA VAL ARG
SEQRES 8 B 566 ILE ALA ARG ARG ALA ALA GLY GLU LYS LEU VAL PHE GLY
SEQRES 9 B 566 ASP ILE GLY PRO THR GLY GLU LEU PRO TYR PRO LEU GLY
SEQRES 10 B 566 SER THR LEU PHE GLU GLU PHE TYR GLU ASN PHE ARG GLU
SEQRES 11 B 566 THR VAL GLU ILE MET VAL GLU GLU GLY VAL ASP GLY ILE
SEQRES 12 B 566 ILE PHE GLU THR PHE SER ASP ILE LEU GLU LEU LYS ALA
SEQRES 13 B 566 ALA VAL LEU ALA ALA ARG GLU VAL SER ARG ASP VAL PHE
SEQRES 14 B 566 LEU ILE ALA HIS MET THR PHE ASP GLU LYS GLY ARG SER
SEQRES 15 B 566 LEU THR GLY THR ASP PRO ALA ASN PHE ALA ILE THR PHE
SEQRES 16 B 566 ASP GLU LEU ASP ILE ASP ALA LEU GLY ILE ASN CYS SER
SEQRES 17 B 566 LEU GLY PRO GLU GLU ILE LEU PRO ILE PHE GLN GLU LEU
SEQRES 18 B 566 SER GLN TYR THR ASP LYS PHE LEU VAL VAL GLU PRO ASN
SEQRES 19 B 566 ALA GLY LYS PRO ILE VAL GLU ASN GLY LYS THR VAL TYR
SEQRES 20 B 566 PRO LEU LYS PRO HIS ASP PHE ALA VAL HIS ILE ASP SER
SEQRES 21 B 566 TYR TYR GLU LEU GLY VAL ASN ILE PHE GLY GLY CYS CYS
SEQRES 22 B 566 GLY THR THR PRO GLU HIS VAL LYS LEU PHE ARG LYS VAL
SEQRES 23 B 566 LEU GLY ASN ARG LYS PRO LEU GLN ARG LYS LYS LYS ARG
SEQRES 24 B 566 ILE PHE ALA VAL SER SER PRO SER LYS LEU VAL THR PHE
SEQRES 25 B 566 ASP HIS PHE VAL VAL ILE GLY GLU ARG ILE ASN PRO ALA
SEQRES 26 B 566 GLY ARG LYS LYS LEU TRP ALA GLU MET GLN LYS GLY ASN
SEQRES 27 B 566 GLU GLU ILE VAL ILE LYS GLU ALA LYS THR GLN VAL GLU
SEQRES 28 B 566 LYS GLY ALA GLU VAL LEU ASP VAL ASN PHE GLY ILE GLU
SEQRES 29 B 566 SER GLN ILE ASP VAL ARG TYR VAL GLU LYS ILE VAL GLN
SEQRES 30 B 566 THR LEU PRO TYR VAL SER ASN VAL PRO LEU SER LEU ASP
SEQRES 31 B 566 ILE GLN ASN VAL ASP LEU THR GLU ARG ALA LEU ARG ALA
SEQRES 32 B 566 TYR PRO GLY ARG SER LEU PHE ASN SER ALA LYS VAL ASP
SEQRES 33 B 566 GLU GLU GLU LEU GLU MET LYS ILE ASN LEU LEU LYS LYS
SEQRES 34 B 566 TYR GLY GLY THR LEU ILE VAL LEU LEU MET GLY LYS ASP
SEQRES 35 B 566 VAL PRO LYS SER PHE GLU GLU ARG LYS GLU TYR PHE GLU
SEQRES 36 B 566 LYS ALA LEU LYS ILE LEU GLU ARG HIS ASP PHE SER ASP
SEQRES 37 B 566 ARG VAL ILE PHE ASP PRO GLY VAL LEU PRO LEU GLY ALA
SEQRES 38 B 566 GLU GLY LYS PRO VAL GLU VAL LEU LYS THR ILE GLU PHE
SEQRES 39 B 566 ILE SER SER LYS GLY PHE ASN THR THR VAL GLY LEU SER
SEQRES 40 B 566 ASN LEU SER PHE GLY LEU PRO ASP ARG SER TYR TYR ASN
SEQRES 41 B 566 THR ALA PHE LEU VAL LEU GLY ILE SER LYS GLY LEU SER
SEQRES 42 B 566 SER ALA ILE MET ASN PRO LEU ASP GLU THR LEU MET LYS
SEQRES 43 B 566 THR LEU ASN ALA THR LEU VAL ILE LEU GLU LYS LYS GLU
SEQRES 44 B 566 LEU PRO ARG ALA GLU VAL LYS
HET ZN A 701 1
HET K A 703 1
HET YT3 A 705 1
HET HCS A 711 8
HET ZN B 702 1
HET K B 704 1
HET HCS B 712 8
HETNAM ZN ZINC ION
HETNAM K POTASSIUM ION
HETNAM YT3 YTTRIUM (III) ION
HETNAM HCS 2-AMINO-4-MERCAPTO-BUTYRIC ACID
HETSYN HCS L-HOMOCYSTEINE
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 K 2(K 1+)
FORMUL 5 YT3 Y 3+
FORMUL 6 HCS 2(C4 H9 N O2 S)
FORMUL 10 HOH *411(H2 O)
HELIX 1 1 ASN A 3 ARG A 14 1 12
HELIX 2 2 TYR A 22 MET A 27 1 6
HELIX 3 3 LYS A 28 GLY A 30 5 3
HELIX 4 4 LEU A 34 GLU A 36 5 3
HELIX 5 5 GLU A 37 ALA A 42 1 6
HELIX 6 6 ALA A 42 GLU A 55 1 14
HELIX 7 7 THR A 69 ARG A 74 1 6
HELIX 8 8 LYS A 75 GLY A 77 5 3
HELIX 9 9 LEU A 78 ASP A 80 5 3
HELIX 10 10 LYS A 81 GLY A 98 1 18
HELIX 11 11 LEU A 120 GLU A 138 1 19
HELIX 12 12 ASP A 150 SER A 165 1 16
HELIX 13 13 ASP A 187 GLU A 197 1 11
HELIX 14 14 GLY A 210 TYR A 224 1 15
HELIX 15 15 LYS A 250 VAL A 256 1 7
HELIX 16 16 HIS A 257 LEU A 264 1 8
HELIX 17 17 THR A 276 GLY A 288 1 13
HELIX 18 18 ARG A 327 LYS A 336 1 10
HELIX 19 19 GLU A 339 LYS A 352 1 14
HELIX 20 20 ILE A 363 ILE A 367 5 5
HELIX 21 21 ASP A 368 SER A 383 1 16
HELIX 22 22 ASN A 393 TYR A 404 1 12
HELIX 23 23 ASP A 416 GLY A 431 1 16
HELIX 24 24 SER A 446 HIS A 464 1 19
HELIX 25 25 PHE A 466 ASP A 468 5 3
HELIX 26 26 PRO A 478 GLU A 482 5 5
HELIX 27 27 LYS A 484 LYS A 498 1 15
HELIX 28 28 GLY A 505 PHE A 511 5 7
HELIX 29 29 ASP A 515 LYS A 530 1 16
HELIX 30 30 ASP A 541 LEU A 555 1 15
HELIX 31 31 ASN B 3 ARG B 14 1 12
HELIX 32 32 TYR B 22 TYR B 29 1 8
HELIX 33 33 LEU B 34 GLU B 36 5 3
HELIX 34 34 GLU B 37 ALA B 42 1 6
HELIX 35 35 ALA B 42 GLY B 57 1 16
HELIX 36 36 THR B 69 ARG B 74 1 6
HELIX 37 37 LYS B 75 GLY B 77 5 3
HELIX 38 38 LEU B 78 ASP B 80 5 3
HELIX 39 39 LYS B 81 GLY B 98 1 18
HELIX 40 40 LEU B 120 GLY B 139 1 20
HELIX 41 41 ASP B 150 SER B 165 1 16
HELIX 42 42 ASP B 187 GLU B 197 1 11
HELIX 43 43 GLY B 210 TYR B 224 1 15
HELIX 44 44 LYS B 250 VAL B 256 1 7
HELIX 45 45 HIS B 257 LEU B 264 1 8
HELIX 46 46 THR B 276 GLY B 288 1 13
HELIX 47 47 ARG B 327 LYS B 336 1 10
HELIX 48 48 GLU B 339 LYS B 352 1 14
HELIX 49 49 ILE B 363 ILE B 367 5 5
HELIX 50 50 ASP B 368 SER B 383 1 16
HELIX 51 51 ASN B 393 TYR B 404 1 12
HELIX 52 52 ASP B 416 GLY B 431 1 16
HELIX 53 53 SER B 446 HIS B 464 1 19
HELIX 54 54 PHE B 466 ASP B 468 5 3
HELIX 55 55 PRO B 478 GLU B 482 5 5
HELIX 56 56 LYS B 484 LYS B 498 1 15
HELIX 57 57 GLY B 505 PHE B 511 5 7
HELIX 58 58 ASP B 515 LYS B 530 1 16
HELIX 59 59 ASP B 541 LEU B 555 1 15
SHEET 1 A 8 LEU A 16 LEU A 17 0
SHEET 2 A 8 ILE A 268 PHE A 269 1 O PHE A 269 N LEU A 16
SHEET 3 A 8 PHE A 228 GLU A 232 1 N VAL A 231 O ILE A 268
SHEET 4 A 8 ALA A 202 ASN A 206 1 N LEU A 203 O PHE A 228
SHEET 5 A 8 LEU A 170 MET A 174 1 N ALA A 172 O ALA A 202
SHEET 6 A 8 GLY A 142 PHE A 148 1 N ILE A 143 O ILE A 171
SHEET 7 A 8 LEU A 101 ILE A 106 1 N GLY A 104 O GLY A 142
SHEET 8 A 8 VAL A 60 LEU A 62 1 N ILE A 61 O PHE A 103
SHEET 1 B 2 ILE A 239 GLU A 241 0
SHEET 2 B 2 LYS A 244 VAL A 246 -1 O VAL A 246 N ILE A 239
SHEET 1 C 2 ALA A 302 SER A 304 0
SHEET 2 C 2 LEU A 309 THR A 311 -1 O VAL A 310 N VAL A 303
SHEET 1 D 7 VAL A 470 ASP A 473 0
SHEET 2 D 7 THR A 433 LEU A 437 1 N VAL A 436 O ASP A 473
SHEET 3 D 7 LEU A 409 LYS A 414 1 N PHE A 410 O ILE A 435
SHEET 4 D 7 LEU A 387 ASP A 390 1 N LEU A 389 O ASN A 411
SHEET 5 D 7 VAL A 356 ASN A 360 1 N LEU A 357 O SER A 388
SHEET 6 D 7 VAL A 316 ILE A 322 1 N GLY A 319 O ASP A 358
SHEET 7 D 7 SER A 534 MET A 537 1 O ALA A 535 N ILE A 318
SHEET 1 E 8 LEU B 16 LEU B 17 0
SHEET 2 E 8 ILE B 268 PHE B 269 1 O PHE B 269 N LEU B 16
SHEET 3 E 8 PHE B 228 GLU B 232 1 N VAL B 231 O ILE B 268
SHEET 4 E 8 ALA B 202 ASN B 206 1 N LEU B 203 O PHE B 228
SHEET 5 E 8 LEU B 170 MET B 174 1 N ALA B 172 O ALA B 202
SHEET 6 E 8 ILE B 143 PHE B 148 1 N ILE B 143 O ILE B 171
SHEET 7 E 8 LEU B 101 ILE B 106 1 N GLY B 104 O ILE B 144
SHEET 8 E 8 VAL B 60 LEU B 62 1 N ILE B 61 O PHE B 103
SHEET 1 F 2 ALA B 302 SER B 304 0
SHEET 2 F 2 LEU B 309 THR B 311 -1 O VAL B 310 N VAL B 303
SHEET 1 G 8 ASN B 501 THR B 502 0
SHEET 2 G 8 VAL B 470 ASP B 473 1 N PHE B 472 O ASN B 501
SHEET 3 G 8 THR B 433 LEU B 437 1 N VAL B 436 O ILE B 471
SHEET 4 G 8 LEU B 409 LYS B 414 1 N PHE B 410 O THR B 433
SHEET 5 G 8 LEU B 387 ASP B 390 1 N LEU B 389 O ASN B 411
SHEET 6 G 8 VAL B 356 ASN B 360 1 N LEU B 357 O SER B 388
SHEET 7 G 8 VAL B 316 ILE B 322 1 N GLY B 319 O ASP B 358
SHEET 8 G 8 SER B 534 MET B 537 1 O ALA B 535 N ILE B 318
LINK O ASP A 19 K K A 703 1555 1555 2.88
LINK OD2 ASP A 19 K K A 703 1555 1555 2.80
LINK O GLY A 20 K K A 703 1555 1555 2.74
LINK SG CYS A 207 ZN ZN A 701 1555 1555 2.42
LINK OE1 GLU A 232 K K A 703 1555 1555 2.74
LINK O GLY A 271 K K A 703 1555 1555 2.72
LINK SG CYS A 272 ZN ZN A 701 1555 1555 2.30
LINK SG CYS A 273 ZN ZN A 701 1555 1555 2.37
LINK ZN ZN A 701 SD HCS A 711 1555 1555 2.34
LINK K K A 703 O HOH A 714 1555 1555 2.87
LINK O ASP B 19 K K B 704 1555 1555 2.84
LINK OD2 ASP B 19 K K B 704 1555 1555 2.78
LINK O GLY B 20 K K B 704 1555 1555 2.76
LINK SG CYS B 207 ZN ZN B 702 1555 1555 2.26
LINK OE1 GLU B 232 K K B 704 1555 1555 2.70
LINK O GLY B 271 K K B 704 1555 1555 2.62
LINK SG CYS B 272 ZN ZN B 702 1555 1555 2.33
LINK SG CYS B 273 ZN ZN B 702 1555 1555 2.45
LINK ZN ZN B 702 SD HCS B 712 1555 1555 2.32
LINK K K B 704 O HOH B 734 1555 1555 2.83
CISPEP 1 TYR A 114 PRO A 115 0 12.27
CISPEP 2 TYR B 114 PRO B 115 0 5.08
SITE 1 AC1 3 CYS A 207 CYS A 272 CYS A 273
SITE 1 AC2 3 CYS B 207 CYS B 272 CYS B 273
SITE 1 AC3 6 ASP A 19 GLY A 20 LEU A 62 GLU A 232
SITE 2 AC3 6 GLY A 271 HOH A 714
SITE 1 AC4 6 ASP B 19 GLY B 20 LEU B 62 GLU B 232
SITE 2 AC4 6 GLY B 271 HOH B 734
SITE 1 AC5 4 ASP A 253 GLU A 421 HOH A 908 HOH A 997
SITE 1 AC6 14 ALA A 21 TYR A 22 GLY A 23 LEU A 62
SITE 2 AC6 14 PHE A 66 ASP A 105 GLU A 146 THR A 147
SITE 3 AC6 14 CYS A 272 HOH A 714 HOH A 719 HOH A 724
SITE 4 AC6 14 HOH A 756 HOH A1121
SITE 1 AC7 12 ALA B 21 TYR B 22 GLY B 23 LEU B 62
SITE 2 AC7 12 ASP B 105 GLU B 146 THR B 147 CYS B 272
SITE 3 AC7 12 HOH B 734 HOH B 741 HOH B 769 HOH B 774
CRYST1 59.067 86.308 125.879 90.00 100.03 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 0.016930 0.000000 0.002995 0.00000
SCALE2 0.000000 0.011586 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008067 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
