HEADER IMMUNE SYSTEM 28-JAN-13 3ZL4
TITLE ANTIBODY STRUCTURAL ORGANIZATION: ROLE OF KAPPA - LAMBDA CHAIN
TITLE 2 CONSTANT DOMAIN SWITCH IN CATALYTIC FUNCTIONALITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: A17 ANTIBODY FAB FRAGMENT HEAVY CHAIN;
COMPND 3 CHAIN: H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: A17 ANTIBODY FAB FRAGMENT LAMBDA LIGHT CHAIN;
COMPND 7 CHAIN: L;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS GS115;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 644223;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PPICZALFA;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS GS115;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 644223;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PPICZALFA
KEYWDS IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR S.D.CHATZIEFTHIMIOU,N.A.PONOMARENKO,I.N.KURKOVA,A.V.SMIRNOV,
AUTHOR 2 I.V.SMIRNOV,V.S.LAMZIN,A.G.GABIBOV,M.WILMANNS
REVDAT 6 20-DEC-23 3ZL4 1 REMARK
REVDAT 5 07-MAR-18 3ZL4 1 SOURCE REMARK
REVDAT 4 17-DEC-14 3ZL4 1 REMARK
REVDAT 3 19-MAR-14 3ZL4 1 JRNL
REVDAT 2 12-MAR-14 3ZL4 1 JRNL
REVDAT 1 05-FEB-14 3ZL4 0
JRNL AUTH N.A.PONOMARENKO,S.D.CHATZIEFTHIMIOU,I.N.KURKOVA,
JRNL AUTH 2 Y.A.MOKRUSHINA,A.V.STEPANOVA,I.V.SMIRNOV,E.M.AVAKYAN,
JRNL AUTH 3 T.V.BOBIK,A.MAMEDOV,V.A.MITKEVICH,A.J.BELOGUROV,
JRNL AUTH 4 O.S.FEDOROVA,M.DUBINA,A.GOLOVIN,V.S.LAMZIN,A.FRIBOULET,
JRNL AUTH 5 A.A.MAKAROV,M.WILMANNS,A.G.GABIBOV
JRNL TITL ROLE OF KAPPA>LAMBDA LIGHT-CHAIN CONSTANT-DOMAIN SWITCH IN
JRNL TITL 2 THE STRUCTURE AND FUNCTIONALITY OF A17 REACTIBODY
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 708 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 24598740
JRNL DOI 10.1107/S1399004713032446
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 39271
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1971
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 24.4007 - 4.6895 1.00 2933 151 0.1751 0.2192
REMARK 3 2 4.6895 - 3.7265 1.00 2756 161 0.1661 0.1814
REMARK 3 3 3.7265 - 3.2567 1.00 2717 142 0.1989 0.2863
REMARK 3 4 3.2567 - 2.9595 1.00 2670 155 0.2117 0.2547
REMARK 3 5 2.9595 - 2.7477 1.00 2660 138 0.2324 0.2784
REMARK 3 6 2.7477 - 2.5858 1.00 2660 147 0.2310 0.3097
REMARK 3 7 2.5858 - 2.4565 1.00 2626 141 0.2242 0.2746
REMARK 3 8 2.4565 - 2.3496 1.00 2654 128 0.2197 0.2735
REMARK 3 9 2.3496 - 2.2592 1.00 2576 155 0.2215 0.3128
REMARK 3 10 2.2592 - 2.1813 1.00 2640 127 0.2300 0.2792
REMARK 3 11 2.1813 - 2.1132 1.00 2624 140 0.2408 0.3060
REMARK 3 12 2.1132 - 2.0528 1.00 2611 123 0.2387 0.2837
REMARK 3 13 2.0528 - 1.9988 0.99 2606 120 0.2571 0.3307
REMARK 3 14 1.9988 - 1.9500 1.00 2567 143 0.2778 0.3088
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.20
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 : 0.007 3430
REMARK 3 ANGLE : 1.118 4687
REMARK 3 CHIRALITY : 0.074 535
REMARK 3 PLANARITY : 0.006 597
REMARK 3 DIHEDRAL : 14.685 1216
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 3ZL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1290055656.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAY-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P14 (MX2)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2234
REMARK 200 MONOCHROMATOR : SI(III) CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39334
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.85000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2XZA
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5, 0.25 M AMMONIUM
REMARK 280 SULFATE, 20% W/V PEG 5000 MME
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 139.81950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.31550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.31550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 69.90975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.31550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.31550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 209.72925
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.31550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.31550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 69.90975
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.31550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.31550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 209.72925
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 139.81950
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: 4130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L
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 GLY H 232
REMARK 465 ASP H 233
REMARK 465 TYR H 234
REMARK 465 LYS H 235
REMARK 465 ASP H 236
REMARK 465 HIS H 237
REMARK 465 ASP H 238
REMARK 465 ILE H 239
REMARK 465 ASP H 240
REMARK 465 TYR H 241
REMARK 465 LYS H 242
REMARK 465 ASP H 243
REMARK 465 ASP H 244
REMARK 465 ASP H 245
REMARK 465 ASP H 246
REMARK 465 LYS H 247
REMARK 465 VAL H 248
REMARK 465 ASP H 249
REMARK 465 HIS H 250
REMARK 465 HIS H 251
REMARK 465 HIS H 252
REMARK 465 HIS H 253
REMARK 465 HIS H 254
REMARK 465 HIS H 255
REMARK 465 GLN L 1
REMARK 465 SER L 2
REMARK 465 ILE L 217
REMARK 465 ASP L 218
REMARK 465 ALA L 219
REMARK 465 ALA L 220
REMARK 465 ALA L 221
REMARK 465 ALA L 222
REMARK 465 ALA L 223
REMARK 465 SER L 224
REMARK 465 PHE L 225
REMARK 465 LEU L 226
REMARK 465 GLU L 227
REMARK 465 GLN L 228
REMARK 465 LYS L 229
REMARK 465 LEU L 230
REMARK 465 ILE L 231
REMARK 465 SER L 232
REMARK 465 GLU L 233
REMARK 465 GLU L 234
REMARK 465 ASP L 235
REMARK 465 LEU L 236
REMARK 465 ASN L 237
REMARK 465 SER L 238
REMARK 465 ALA L 239
REMARK 465 VAL L 240
REMARK 465 ASP L 241
REMARK 465 HIS L 242
REMARK 465 HIS L 243
REMARK 465 HIS L 244
REMARK 465 HIS L 245
REMARK 465 HIS L 246
REMARK 465 HIS L 247
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 CYS L 22 CA - CB - SG ANGL. DEV. = 6.6 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 SER H 15 -14.89 79.15
REMARK 500 TYR H 27 144.60 -173.74
REMARK 500 SER H 66 16.99 58.16
REMARK 500 ASP H 150 67.30 60.63
REMARK 500 THR H 166 -24.40 -140.24
REMARK 500 ASN H 210 68.53 -101.18
REMARK 500 ASN L 28 -87.50 -106.35
REMARK 500 ASN L 52 -47.18 72.63
REMARK 500 ASP L 154 -108.72 57.61
REMARK 500 ASN L 172 8.02 -65.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES L 1217
DBREF 3ZL4 H 1 255 PDB 3ZL4 3ZL4 1 255
DBREF 3ZL4 L 1 247 PDB 3ZL4 3ZL4 1 247
SEQRES 1 H 255 GLN VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS
SEQRES 2 H 255 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL SER GLY
SEQRES 3 H 255 TYR SER ILE SER SER GLY TYR TYR TRP GLY TRP ILE ARG
SEQRES 4 H 255 GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY SER ILE
SEQRES 5 H 255 TYR HIS SER GLY SER THR TYR TYR ASN PRO SER LEU LYS
SEQRES 6 H 255 SER ARG VAL THR ILE SER VAL ASP THR SER LYS ASN GLN
SEQRES 7 H 255 PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR
SEQRES 8 H 255 ALA VAL TYR TYR CYS ALA GLY LEU THR GLN SER SER HIS
SEQRES 9 H 255 ASN ASP ALA ASN TRP GLY GLN GLY THR LEU VAL THR VAL
SEQRES 10 H 255 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU
SEQRES 11 H 255 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA
SEQRES 12 H 255 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL
SEQRES 13 H 255 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL
SEQRES 14 H 255 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR
SEQRES 15 H 255 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU
SEQRES 16 H 255 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO
SEQRES 17 H 255 SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER
SEQRES 18 H 255 CYS LEU ALA MET ASP TYR LYS ASP HIS ASP GLY ASP TYR
SEQRES 19 H 255 LYS ASP HIS ASP ILE ASP TYR LYS ASP ASP ASP ASP LYS
SEQRES 20 H 255 VAL ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 L 247 GLN SER VAL LEU THR GLN PRO PRO SER VAL SER ALA ALA
SEQRES 2 L 247 PRO GLY GLN LYS VAL THR ILE SER CYS SER GLY SER SER
SEQRES 3 L 247 SER ASN ILE GLY ASN ASN TYR VAL SER TRP TYR GLN GLN
SEQRES 4 L 247 LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR ASP ASN
SEQRES 5 L 247 ASN LYS ARG PRO SER GLY ILE PRO ASP ARG PHE SER GLY
SEQRES 6 L 247 SER LYS SER GLY THR SER ALA THR LEU GLY ILE THR GLY
SEQRES 7 L 247 LEU GLN THR GLY ASP GLU ALA ASP TYR TYR CYS GLY THR
SEQRES 8 L 247 TRP ASP SER SER LEU ASN PRO VAL PHE GLY GLY GLY THR
SEQRES 9 L 247 LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO SER
SEQRES 10 L 247 VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN ALA
SEQRES 11 L 247 ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE TYR
SEQRES 12 L 247 PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER SER
SEQRES 13 L 247 PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER LYS
SEQRES 14 L 247 GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU SER
SEQRES 15 L 247 LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR SER
SEQRES 16 L 247 CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS THR
SEQRES 17 L 247 VAL ALA PRO THR GLU CYS SER GLY ILE ASP ALA ALA ALA
SEQRES 18 L 247 ALA ALA SER PHE LEU GLU GLN LYS LEU ILE SER GLU GLU
SEQRES 19 L 247 ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS HIS HIS
HET MES L1217 12
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
FORMUL 3 MES C6 H13 N O4 S
FORMUL 4 HOH *310(H2 O)
HELIX 1 1 SER H 28 GLY H 32 5 5
HELIX 2 2 PRO H 62 LYS H 65 5 4
HELIX 3 3 THR H 87 THR H 91 5 5
HELIX 4 4 SER H 162 ALA H 164 5 3
HELIX 5 5 SER H 193 THR H 197 5 5
HELIX 6 6 GLN L 80 GLU L 84 5 5
HELIX 7 7 SER L 124 ALA L 130 1 7
HELIX 8 8 THR L 184 LYS L 189 1 6
SHEET 1 HA 4 GLN H 3 SER H 7 0
SHEET 2 HA 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7
SHEET 3 HA 4 GLN H 78 LEU H 83 -1 O PHE H 79 N CYS H 22
SHEET 4 HA 4 VAL H 68 ASP H 73 -1 O THR H 69 N LYS H 82
SHEET 1 HB 4 LEU H 11 VAL H 12 0
SHEET 2 HB 4 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12
SHEET 3 HB 4 ALA H 92 LEU H 99 -1 O ALA H 92 N VAL H 115
SHEET 4 HB 4 ASN H 108 TRP H 109 -1 O ASN H 108 N GLY H 98
SHEET 1 HC 6 LEU H 11 VAL H 12 0
SHEET 2 HC 6 THR H 113 VAL H 117 1 O THR H 116 N VAL H 12
SHEET 3 HC 6 ALA H 92 LEU H 99 -1 O ALA H 92 N VAL H 115
SHEET 4 HC 6 TYR H 34 GLN H 40 -1 O TYR H 34 N LEU H 99
SHEET 5 HC 6 GLU H 47 TYR H 53 -1 O GLU H 47 N ARG H 39
SHEET 6 HC 6 THR H 58 TYR H 60 -1 O TYR H 59 N SER H 51
SHEET 1 HD 2 ASN H 108 TRP H 109 0
SHEET 2 HD 2 ALA H 92 LEU H 99 -1 O GLY H 98 N ASN H 108
SHEET 1 HE 2 SER H 126 LEU H 130 0
SHEET 2 HE 2 THR H 141 TYR H 151 -1 O GLY H 145 N LEU H 130
SHEET 1 HF 2 THR H 137 SER H 138 0
SHEET 2 HF 2 THR H 141 TYR H 151 -1 O THR H 141 N SER H 138
SHEET 1 HG 2 HIS H 170 THR H 171 0
SHEET 2 HG 2 TYR H 182 PRO H 191 -1 O VAL H 187 N HIS H 170
SHEET 1 HH 2 VAL H 175 LEU H 176 0
SHEET 2 HH 2 TYR H 182 PRO H 191 1 O SER H 183 N VAL H 175
SHEET 1 HI 3 THR H 157 TRP H 160 0
SHEET 2 HI 3 ILE H 201 HIS H 206 -1 O ASN H 203 N SER H 159
SHEET 3 HI 3 THR H 211 LYS H 216 -1 O THR H 211 N HIS H 206
SHEET 1 LA 4 SER L 9 ALA L 12 0
SHEET 2 LA 4 THR L 104 VAL L 108 1 O LYS L 105 N VAL L 10
SHEET 3 LA 4 ALA L 85 TRP L 92 -1 O ALA L 85 N LEU L 106
SHEET 4 LA 4 PRO L 98 PHE L 100 1 O VAL L 99 N THR L 91
SHEET 1 LB 5 SER L 9 ALA L 12 0
SHEET 2 LB 5 THR L 104 VAL L 108 1 O LYS L 105 N VAL L 10
SHEET 3 LB 5 ALA L 85 TRP L 92 -1 O ALA L 85 N LEU L 106
SHEET 4 LB 5 SER L 35 GLN L 39 -1 O SER L 35 N GLY L 90
SHEET 5 LB 5 LYS L 46 ILE L 49 -1 O LYS L 46 N GLN L 38
SHEET 1 LC 2 PRO L 98 PHE L 100 0
SHEET 2 LC 2 ALA L 85 TRP L 92 1 O THR L 91 N VAL L 99
SHEET 1 LD 3 VAL L 18 SER L 23 0
SHEET 2 LD 3 SER L 71 ILE L 76 -1 O ALA L 72 N CYS L 22
SHEET 3 LD 3 PHE L 63 SER L 68 -1 O SER L 64 N GLY L 75
SHEET 1 LE 4 SER L 117 PHE L 121 0
SHEET 2 LE 4 ALA L 133 PHE L 142 -1 O VAL L 136 N PHE L 121
SHEET 3 LE 4 TYR L 175 LEU L 183 -1 O TYR L 175 N ASP L 141
SHEET 4 LE 4 SER L 168 LYS L 169 1 O SER L 168 N ALA L 176
SHEET 1 LF 4 SER L 117 PHE L 121 0
SHEET 2 LF 4 ALA L 133 PHE L 142 -1 O VAL L 136 N PHE L 121
SHEET 3 LF 4 TYR L 175 LEU L 183 -1 O TYR L 175 N ASP L 141
SHEET 4 LF 4 VAL L 162 THR L 164 -1 O GLU L 163 N TYR L 180
SHEET 1 LG 2 SER L 168 LYS L 169 0
SHEET 2 LG 2 TYR L 175 LEU L 183 1 O ALA L 176 N SER L 168
SHEET 1 LH 4 SER L 156 VAL L 158 0
SHEET 2 LH 4 THR L 148 ALA L 153 -1 O TRP L 151 N VAL L 158
SHEET 3 LH 4 TYR L 194 HIS L 200 -1 O SER L 195 N LYS L 152
SHEET 4 LH 4 SER L 203 VAL L 209 -1 O SER L 203 N HIS L 200
SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.07
SSBOND 2 CYS H 146 CYS H 202 1555 1555 2.04
SSBOND 3 CYS H 222 CYS L 214 1555 1555 2.02
SSBOND 4 CYS L 22 CYS L 89 1555 1555 2.07
SSBOND 5 CYS L 137 CYS L 196 1555 1555 2.04
CISPEP 1 PHE H 152 PRO H 153 0 -4.77
CISPEP 2 GLU H 154 PRO H 155 0 1.72
CISPEP 3 TYR L 143 PRO L 144 0 3.60
SITE 1 AC1 8 LEU H 99 ASN H 105 ALA H 107 HOH H2127
SITE 2 AC1 8 HOH H2128 THR L 91 TRP L 92 PRO L 98
CRYST1 60.631 60.631 279.639 90.00 90.00 90.00 P 41 21 2 8
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 0.016493 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016493 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003576 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
